PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
2687272-5	1989	The results demonstrated that only the species that consist of the regions encoded by exons 2 and 4, joined by five disulfide bonds, are capable of binding IL-2 and that the presence of semi-sensitive cleavage sites within the two homologous domains had no apparent effect on IL-2 binding.	Disulfides	116-125	interleukin 2	Homo sapiens	156-160
2592374-3	1989	The arrangement of the three disulfide bonds in recombinant sCD4 was also established by mass spectrometry and comparative high performance liquid chromatography mapping and shown to be identical to that expected from previous studies of intrachain disulfide bonding in T4 antigens derived from sheep and mouse.	Disulfides	29-38	stearoyl-coenzyme A desaturase 4	Mus musculus	60-64
2592374-3	1989	The arrangement of the three disulfide bonds in recombinant sCD4 was also established by mass spectrometry and comparative high performance liquid chromatography mapping and shown to be identical to that expected from previous studies of intrachain disulfide bonding in T4 antigens derived from sheep and mouse.	Disulfides	249-258	stearoyl-coenzyme A desaturase 4	Mus musculus	60-64
2611257-9	1989	However, IAN treatment of the alpha beta heterodimeric IGF-1 receptors inhibited the IGF-1-dependent covalent formation of the disulfide-linked alpha 2 beta 2 heterotetrameric complex.	Disulfides	127-136	insulin like growth factor 1	Homo sapiens	55-60
2532155-2	1989	The major form of C4BP is composed of 7 identical, disulfide-linked 70 kDa subunits (alpha-chains), the arrangement of which gives the C4BP molecule a spider-like appearance.	Disulfides	51-60	complement component 4 binding protein alpha	Homo sapiens	18-22
2532155-2	1989	The major form of C4BP is composed of 7 identical, disulfide-linked 70 kDa subunits (alpha-chains), the arrangement of which gives the C4BP molecule a spider-like appearance.	Disulfides	51-60	complement component 4 binding protein alpha	Homo sapiens	135-139
2611257-9	1989	However, IAN treatment of the alpha beta heterodimeric IGF-1 receptors inhibited the IGF-1-dependent covalent formation of the disulfide-linked alpha 2 beta 2 heterotetrameric complex.	Disulfides	127-136	insulin like growth factor 1	Homo sapiens	85-90
2483822-1	1989	The effects of phosphorylation, ribosylation of proteins and formation of protein-mixed disulfides on substance P degradation under the action of synaptosomal plasma membranes were studied.	Disulfides	88-98	tachykinin precursor 1	Homo sapiens	102-113
2611257-10	1989	These data indicate that IGF-1 induces the covalent association of isolated alpha beta heterodimeric IGF-1 receptor complexes into a disulfide-linked alpha 2 beta 2 heterotetrameric state whereas Mn/MgATP induces a noncovalent association.	Disulfides	133-142	insulin like growth factor 1	Homo sapiens	25-30
2611257-10	1989	These data indicate that IGF-1 induces the covalent association of isolated alpha beta heterodimeric IGF-1 receptor complexes into a disulfide-linked alpha 2 beta 2 heterotetrameric state whereas Mn/MgATP induces a noncovalent association.	Disulfides	133-142	insulin like growth factor 1	Homo sapiens	101-106
2692717-9	1989	The differences between proinsulin and mini-proinsulin suggest a structural mechanism for the observation that the fully reduced B29-A1 analogue folds more efficiently than proinsulin to form the correct pattern of disulfide bonds.	Disulfides	215-224	insulin	Homo sapiens	24-34
2692717-9	1989	The differences between proinsulin and mini-proinsulin suggest a structural mechanism for the observation that the fully reduced B29-A1 analogue folds more efficiently than proinsulin to form the correct pattern of disulfide bonds.	Disulfides	215-224	insulin	Homo sapiens	44-54
2692717-9	1989	The differences between proinsulin and mini-proinsulin suggest a structural mechanism for the observation that the fully reduced B29-A1 analogue folds more efficiently than proinsulin to form the correct pattern of disulfide bonds.	Disulfides	215-224	insulin	Homo sapiens	44-54
2684974-3	1989	The major peptides are portions of the insulin molecule, with the amino ends of the A and B chains or the carboxyl ends of the A and B chains still connected by disulfide bonds.	Disulfides	161-170	insulin	Homo sapiens	39-46
2684978-13	1989	These data suggest that the disulfide bond joining the heavy and light chains of cathepsin L is essential for enzymatic activity.	Disulfides	28-37	cathepsin L	Homo sapiens	81-92
2531187-1	1989	The high affinity receptor for IgE (Fc epsilon RI) is a tetrameric structure consisting of a single IgE-binding alpha subunit, a single beta subunit, and two disulfide-linked gamma subunits.	Disulfides	158-167	Fc receptor, IgE, high affinity I, gamma polypeptide	Mus musculus	36-49
2635691-5	1989	In most cases loss or change in length of one of the disulfide rings eliminates paralytic activity except with compound 17, which is weakly active, IC50 = 7.0 x 10(-5) M. Replacement of the Cys1-Cys6 disulfide bond with an amide bond (compound 9) greatly lowers paralytic activity, IC50 = 3.7 x 10(-5) M.	Disulfides	200-209	cystin 1	Mus musculus	190-194
2628430-0	1989	Direct identification of disulfide bond linkages in human insulin-like growth factor I (IGF-I) by chemical synthesis.	Disulfides	25-34	insulin like growth factor 1	Homo sapiens	58-86
2628430-0	1989	Direct identification of disulfide bond linkages in human insulin-like growth factor I (IGF-I) by chemical synthesis.	Disulfides	25-34	insulin like growth factor 1	Homo sapiens	88-93
2628430-1	1989	The primary structure of human IGF-I, except for the disulfide bond system, has been reported by Rinderknecht and Humbel.	Disulfides	53-62	insulin like growth factor 1	Homo sapiens	31-36
2628430-4	1989	The disulfide bond system of IGF-I was unequivocally determined to be the Type II form along with Cys18-Cys61.	Disulfides	4-13	insulin like growth factor 1	Homo sapiens	29-34
2628430-5	1989	Interestingly, the Type I system was included in the disulfide bond isomer produced as the main by-product in the refolding step on IGF-I synthesis by the recombinant DNA method.	Disulfides	53-62	insulin like growth factor 1	Homo sapiens	132-137
2584205-4	1989	hVPF was purified from serum-free conditioned medium of the human histiocytic lymphoma cell line U937 as a disulfide-linked dimeric 40-kDa protein that promoted dermal blood vessel leakage in guinea pigs at a dose of 20 ng (3 x 10(-9) M) and promoted in vitro endothelial cell growth at concentrations as low as 50 PM.	Disulfides	107-116	vascular endothelial growth factor A	Homo sapiens	0-4
2513572-4	1989	By the use of affinity chromatography followed by two-dimensional diagonal gel electrophoresis, we have identified a Mr 43,000 disulfide-bonded heterodimer copurifying with CD4.	Disulfides	127-136	CD4 molecule	Homo sapiens	173-176
2556142-0	1989	Neurotensin receptors on circular smooth muscle of canine small intestine: role of disulfide bridges.	Disulfides	83-92	neurotensin	Canis lupus familiaris	0-11
2556142-6	1989	The implications of the role of disulfide bridges in the neurotensin response is discussed.	Disulfides	32-41	neurotensin	Canis lupus familiaris	57-68
2690069-5	1989	The sequences of the genes for amylin and the calcitonin gene-related peptides (CGRPs) show strong similarity, especially over their 5" coding regions, where both peptides have a conserved intramolecular disulfide bridge, and also over their 3" coding regions, where the presence of a glycine codon strongly suggests that the carboxyl-terminal residue of amylin, like that of CGRP, is amidated.	Disulfides	204-213	calcitonin related polypeptide alpha	Homo sapiens	80-84
2590229-2	1989	Using high performance liquid chromatography and other protein isolation techniques we have demonstrated that a glycosylated prolactin species is linked to immunoglobulin by disulfide bonds in amniotic fluid.	Disulfides	174-183	prolactin	Homo sapiens	125-134
2613682-4	1989	From the sequence, it was concluded that three disulfide bridges in RNase A were conserved in the bullfrog RNase, that a disulfide bridge in RNase A [Cys65-Cys126 (RNase A numbering)] was deleted, and that a new disulfide bridge was created in the C-terminal part of the enzyme.	Disulfides	47-56	ribonuclease pancreatic	Bos taurus	68-75
2478554-2	1989	Human transforming growth factor alpha (TGF alpha) is a 50-residue mitogenic peptide with a compact structure restrained by three disulfide bonds.	Disulfides	130-139	tumor necrosis factor	Homo sapiens	6-38
2613682-4	1989	From the sequence, it was concluded that three disulfide bridges in RNase A were conserved in the bullfrog RNase, that a disulfide bridge in RNase A [Cys65-Cys126 (RNase A numbering)] was deleted, and that a new disulfide bridge was created in the C-terminal part of the enzyme.	Disulfides	121-130	ribonuclease pancreatic	Bos taurus	68-75
2553933-4	1989	The high affinity of the analogs [Cys(ACM)2.7]hCGRP and cyclo2.7 [Asp2, Lys7]hCGRP indicates that the disulfide bridge between positions 2 and 7 is not essential for the binding of the ligand to the CGRP receptor.	Disulfides	102-111	calcitonin related polypeptide alpha	Homo sapiens	46-51
2613682-4	1989	From the sequence, it was concluded that three disulfide bridges in RNase A were conserved in the bullfrog RNase, that a disulfide bridge in RNase A [Cys65-Cys126 (RNase A numbering)] was deleted, and that a new disulfide bridge was created in the C-terminal part of the enzyme.	Disulfides	121-130	ribonuclease pancreatic	Bos taurus	141-148
2613682-4	1989	From the sequence, it was concluded that three disulfide bridges in RNase A were conserved in the bullfrog RNase, that a disulfide bridge in RNase A [Cys65-Cys126 (RNase A numbering)] was deleted, and that a new disulfide bridge was created in the C-terminal part of the enzyme.	Disulfides	121-130	ribonuclease pancreatic	Bos taurus	141-148
2613682-4	1989	From the sequence, it was concluded that three disulfide bridges in RNase A were conserved in the bullfrog RNase, that a disulfide bridge in RNase A [Cys65-Cys126 (RNase A numbering)] was deleted, and that a new disulfide bridge was created in the C-terminal part of the enzyme.	Disulfides	121-130	ribonuclease pancreatic	Bos taurus	68-75
2613682-4	1989	From the sequence, it was concluded that three disulfide bridges in RNase A were conserved in the bullfrog RNase, that a disulfide bridge in RNase A [Cys65-Cys126 (RNase A numbering)] was deleted, and that a new disulfide bridge was created in the C-terminal part of the enzyme.	Disulfides	121-130	ribonuclease pancreatic	Bos taurus	141-148
2613682-4	1989	From the sequence, it was concluded that three disulfide bridges in RNase A were conserved in the bullfrog RNase, that a disulfide bridge in RNase A [Cys65-Cys126 (RNase A numbering)] was deleted, and that a new disulfide bridge was created in the C-terminal part of the enzyme.	Disulfides	121-130	ribonuclease pancreatic	Bos taurus	141-148
2553933-4	1989	The high affinity of the analogs [Cys(ACM)2.7]hCGRP and cyclo2.7 [Asp2, Lys7]hCGRP indicates that the disulfide bridge between positions 2 and 7 is not essential for the binding of the ligand to the CGRP receptor.	Disulfides	102-111	calcitonin related polypeptide alpha	Homo sapiens	77-82
2553933-4	1989	The high affinity of the analogs [Cys(ACM)2.7]hCGRP and cyclo2.7 [Asp2, Lys7]hCGRP indicates that the disulfide bridge between positions 2 and 7 is not essential for the binding of the ligand to the CGRP receptor.	Disulfides	102-111	calcitonin related polypeptide alpha	Homo sapiens	47-51
2608054-2	1989	This unique pair of cysteine residues may be responsible for the extreme tendency of hamster PL-II, compared to other members of the GH-PRL-PL family, to form disulfide-bonded hormone-serum protein complexes.	Disulfides	159-168	prolactin family 3, subfamily B, member 1	Rattus norvegicus	93-98
2677399-4	1989	In r-p16 particles, disulfide bonds linked the truncated polypeptides in dimers, assembled in the particle by noncovalent interactions.	Disulfides	20-29	cyclin dependent kinase inhibitor 2A	Homo sapiens	5-8
2790045-0	1989	Sulfhydryl groups in glycolipid transfer protein: formation of an intramolecular disulfide bond and oligomers by Cu2+-catalyzed oxidation.	Disulfides	81-90	LOC100624001	Sus scrofa	21-48
2529261-3	1989	These patterns suggest that GPIIIa contains a large disulfide-bonded loop of at least 325 amino acids that is susceptible to proteolytic cleavage, and that the 4 cysteine residues between residues 177 and 273 bond with each other.	Disulfides	52-61	integrin subunit beta 3	Homo sapiens	28-34
2550456-4	1989	2) Fluorescence measurements and iodoacetate trapping of free sulfhydryls show that the disulfide bonds of MetSO-RNase A, in which the 4 methionine residues are oxidized to the sulfoxide, are reduced by 2 mM dithiothreitol (DTT) in standard Ub conjugation assays so that this derivative also is unfolded.	Disulfides	88-97	ribonuclease pancreatic	Bos taurus	113-120
2790045-15	1989	A value of 2.2 mol sulfhydryl groups per mol of GLTP was found in the presence of 0.5% SDS and one sulfhydryl group in a GLTP molecule was very rapidly oxidized in the native state, from which it is assumed that the slower component contains three sulfhydryl groups per GLTP molecule and the faster component contains one sulfhydryl group and one disulfide bond per GLTP molecule.	Disulfides	347-356	LOC100624001	Sus scrofa	48-52
2698041-6	1989	Data suggest direct interaction between the alkaline phosphatase and insulin molecules, involving either disulfide cross linkages or the metal chelating activity of insulin.	Disulfides	105-114	insulin	Homo sapiens	69-76
2790045-15	1989	A value of 2.2 mol sulfhydryl groups per mol of GLTP was found in the presence of 0.5% SDS and one sulfhydryl group in a GLTP molecule was very rapidly oxidized in the native state, from which it is assumed that the slower component contains three sulfhydryl groups per GLTP molecule and the faster component contains one sulfhydryl group and one disulfide bond per GLTP molecule.	Disulfides	347-356	LOC100624001	Sus scrofa	121-125
2790045-15	1989	A value of 2.2 mol sulfhydryl groups per mol of GLTP was found in the presence of 0.5% SDS and one sulfhydryl group in a GLTP molecule was very rapidly oxidized in the native state, from which it is assumed that the slower component contains three sulfhydryl groups per GLTP molecule and the faster component contains one sulfhydryl group and one disulfide bond per GLTP molecule.	Disulfides	347-356	LOC100624001	Sus scrofa	121-125
2790045-15	1989	A value of 2.2 mol sulfhydryl groups per mol of GLTP was found in the presence of 0.5% SDS and one sulfhydryl group in a GLTP molecule was very rapidly oxidized in the native state, from which it is assumed that the slower component contains three sulfhydryl groups per GLTP molecule and the faster component contains one sulfhydryl group and one disulfide bond per GLTP molecule.	Disulfides	347-356	LOC100624001	Sus scrofa	121-125
2482065-6	1989	alpha-Thrombin-serpin complexes but not Xa-serpin complexes formed disulfide-bonded complexes with vitronectin.	Disulfides	67-76	coagulation factor II, thrombin	Homo sapiens	6-14
2531072-3	1989	The predicted polypeptide of preproinsulin from sponge contains two disulfide bridges which link the A- to the B-chain.	Disulfides	68-77	insulin	Homo sapiens	29-42
2508091-11	1989	Each of the 11 IgA-f isotypes was shown to bind SC by a disulfide linkage, whereas the single IgA-g isotype appeared to bind SC through noncovalent interactions only.	Disulfides	56-65	CD79a molecule	Homo sapiens	15-18
2676475-1	1989	A cleaved form of rat PRL (cldPRL), which resolves after reduction of the disulfide bonds into two fragments of 16K and 8K mol wt, has been reported in the pituitary gland.	Disulfides	74-83	prolactin	Rattus norvegicus	22-25
2813340-4	1989	Active human transforming growth factor-alpha (TGF-alpha), a 50 amino acid long protein with three disulfide bonds, has been synthesized and purified in multiple tens of mg amounts in less than 7 days.	Disulfides	99-108	tumor necrosis factor	Homo sapiens	13-45
2781534-1	1989	Thrombin, a serine proteinase comprised of two disulfide-linked subunits (A chain and B chain), induces clotting by releasing fibrinopeptide A from fibrinogen and then influences the character of the resulting fibrin by releasing fibrinopeptide B and by activating factor XIII.	Disulfides	47-56	coagulation factor II, thrombin	Homo sapiens	0-8
2529137-3	1989	Action of purified granulocyte elastase on pro-uPA generated enzymatically inactive two-chain uPA linked by disulfide bridges which was indistinguishable by SDS-PAGE from plasmin-generated HMW-uPA.	Disulfides	108-117	plasminogen activator, urokinase	Homo sapiens	47-50
2529137-3	1989	Action of purified granulocyte elastase on pro-uPA generated enzymatically inactive two-chain uPA linked by disulfide bridges which was indistinguishable by SDS-PAGE from plasmin-generated HMW-uPA.	Disulfides	108-117	plasminogen activator, urokinase	Homo sapiens	94-97
2529137-3	1989	Action of purified granulocyte elastase on pro-uPA generated enzymatically inactive two-chain uPA linked by disulfide bridges which was indistinguishable by SDS-PAGE from plasmin-generated HMW-uPA.	Disulfides	108-117	plasminogen activator, urokinase	Homo sapiens	94-97
2760061-0	1989	The arrangement of disulfide loops in human alpha 2-HS glycoprotein.	Disulfides	19-28	alpha 2-HS glycoprotein	Homo sapiens	44-67
2760061-17	1989	The particular arrangement of disulfide loops in alpha 2-HS glycoprotein is similar to the patterns of linearly arranged and tandemly repeated disulfide loops of cysteine proteinase inhibitors, i.e. the cystatins and the kininogens.	Disulfides	30-39	alpha 2-HS glycoprotein	Homo sapiens	49-72
2760061-2	1989	The complete disulfide loop structure of human alpha 2-HS glycoprotein has been elucidated.	Disulfides	13-22	alpha 2-HS glycoprotein	Homo sapiens	47-70
2760061-17	1989	The particular arrangement of disulfide loops in alpha 2-HS glycoprotein is similar to the patterns of linearly arranged and tandemly repeated disulfide loops of cysteine proteinase inhibitors, i.e. the cystatins and the kininogens.	Disulfides	143-152	alpha 2-HS glycoprotein	Homo sapiens	49-72
2788160-2	1989	Large von Willebrand factor (vWf) multimers are assembled by the formation of disulfide bonds between dimers in trans Golgi and post-Golgi compartments.	Disulfides	78-87	von Willebrand factor	Homo sapiens	6-27
2474534-6	1989	8, 4162-4168) with purified recombinant TGF-beta 1 (rTGF-beta 1) precursor produced by Chinese hamster ovary (CHO) cells revealed that Cys-33 can form a disulfide bond with at least 1 cysteine residue in mature TGF-beta 1, contributing to the formation of a 90-110-kDa protein.	Disulfides	153-162	transforming growth factor, beta 1	Rattus norvegicus	52-63
2788160-2	1989	Large von Willebrand factor (vWf) multimers are assembled by the formation of disulfide bonds between dimers in trans Golgi and post-Golgi compartments.	Disulfides	78-87	von Willebrand factor	Homo sapiens	29-32
2557141-6	1989	The disulfide reducing agent, dithiothreitol, caused a decrease in specific binding of radiolabeled VIP.	Disulfides	4-13	vasoactive intestinal peptide	Homo sapiens	100-103
2557141-8	1989	These results suggest that disulfide bonds are important for ligand binding to vascular VIP receptors.	Disulfides	27-36	vasoactive intestinal peptide	Homo sapiens	88-91
2507316-1	1989	The human transferrin receptor is expressed as a disulfide-linked dimer at the cell surface.	Disulfides	49-58	transferrin	Homo sapiens	10-21
2807563-4	1989	It could be shown that these polymers or aggregates are formed by disulfide bonds between albumin and the small amounts of denatured impurity globulins (haptoglobin, transferrin) during the pasteurization step.	Disulfides	66-75	haptoglobin	Homo sapiens	153-164
2792756-3	1989	Individual Notch polypeptide chains appear to be associated with one another by disulfide bonds, suggesting that homotypic interaction of these proteins is required for function.	Disulfides	80-89	Notch	Drosophila melanogaster	11-16
2473036-4	1989	Composition and sequence determinations revealed that GNCP-1 and GNCP-2 are each single polypeptides containing 31 amino acid residues and three intramolecular disulfide bonds.	Disulfides	160-169	neutrophil cationic peptide 1 type A	Cavia porcellus	65-71
2790008-1	1989	The reaction of 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB) with S1 and tryptic S1 has been examined to identify the sites of mixed and intramolecular disulfides formed in the initial and final stages of the reaction in these two forms of S1.	Disulfides	150-160	proteasome 26S subunit, non-ATPase 1	Homo sapiens	64-81
2477003-3	1989	Our effort to further characterize the immunological and structural nature of Ro/SS-A suggests that the native human Ro/SS-A molecule is not glycosylated and consists of two disulfide linked domains.	Disulfides	174-183	tripartite motif containing 21	Homo sapiens	78-85
2477003-3	1989	Our effort to further characterize the immunological and structural nature of Ro/SS-A suggests that the native human Ro/SS-A molecule is not glycosylated and consists of two disulfide linked domains.	Disulfides	174-183	tripartite motif containing 21	Homo sapiens	117-124
2472117-0	1989	Disulfide structures of human interleukin-6 are similar to those of human granulocyte colony stimulating factor.	Disulfides	0-9	interleukin 6	Homo sapiens	30-43
2472117-3	1989	Labeling experiments of recombinant interleukin-6 with tritiated iodoacetate confirmed that the molecule forms two intramolecular disulfide bonds and contains no detectable level of free sulfhydryls.	Disulfides	130-139	interleukin 6	Homo sapiens	36-49
2472117-4	1989	By isolation and characterization of tryptic and subtilytic peptides obtained from different proteolytic digestions, the disulfide bonds of the IL-6 molecule were assigned to Cys44-Cys50 and Cys73-Cys83.	Disulfides	121-130	interleukin 6	Homo sapiens	144-148
2776731-6	1989	This procedure revealed that all apolipoprotein E monomers in CSF, which are synthesized in astrocytes, are linked by disulfide bonds.	Disulfides	118-127	apolipoprotein E	Homo sapiens	33-49
2679533-12	1989	Because the Raji C1qR reveals two components when analyzed by two dimensional SDS-PAGE, the possibility that the C1qR may be a doublet of two apparent 70 kDa molecules only one of which contains relatively more intrachain disulfide bonds is being raised.	Disulfides	222-231	CD93 molecule	Homo sapiens	113-117
2742583-2	1989	In contrast to human alpha atrial natriuretic peptide/cardiodilatin (ANP/CDD) showing a single major cleavage within the disulfide-linked loop between Cys and Phe in position 7 and 8, pBNP-26 is cleaved at several sites.	Disulfides	121-130	natriuretic peptide A	Homo sapiens	69-72
2792501-3	1989	The chicken transferrin receptor was shown to be a 190,000 dalton cell surface membrane molecule consisting of two similar disulfide-bonded subunits of approximately 95,000 daltons.	Disulfides	123-132	transferrin	Homo sapiens	12-23
2602354-1	1989	The properties of a previously isolated disulfide form of pituitary porcine prolactin (pPRL) were studied.	Disulfides	40-49	prolactin	Homo sapiens	76-85
2654942-8	1989	Radioiodination of CTL surface proteins followed by immunoprecipitation with anti-TNF antibodies confirmed the presence of a TNF-related cytokine in the plasma membranes of CTLs that migrated with an apparent molecular mass of 50-60 kDa under disulfide-reducing conditions.	Disulfides	243-252	tumor necrosis factor	Mus musculus	125-128
2550652-1	1989	SDS-polyacrylamide gel electrophoresis and immunoblotting were used to investigate inter- and intramolecular disulfide bonds to connexin 43 (the cardiac gap junctional protein) in isolated rat heart gap junctions and in whole heart fractions.	Disulfides	109-118	gap junction protein, alpha 1	Rattus norvegicus	128-139
2550652-2	1989	In gap junctions isolated in the absence of alkylating agent, connexin 43 molecules are cross-linked by disulfide bonds.	Disulfides	104-113	gap junction protein, alpha 1	Rattus norvegicus	62-73
2540333-1	1989	Analogues of atriopeptin(103-125)amide were prepared having a disulfide bridge at positions different from that found in the natural product.	Disulfides	62-71	natriuretic peptide A	Homo sapiens	13-24
2669962-0	1989	Disulfide bonds are localized within the short consensus repeat units of complement regulatory proteins: C4b-binding protein.	Disulfides	0-9	complement component 4 binding protein alpha	Homo sapiens	105-124
2669962-6	1989	This pattern of disulfides may confer to C4BP (and to other structurally related proteins) a conformation which apparently allows the assembly of the SCR units (4-30) in a tandem fashion.	Disulfides	16-26	complement component 4 binding protein alpha	Homo sapiens	41-45
28305778-4	1989	Upon reduction, the electrophoretic mobility of P110 is decreased, indicating the presence of internal disulfide bonds.	Disulfides	103-112	TBP-associated factor 4	Drosophila melanogaster	48-52
2708329-0	1989	Direct evidence for intra- and intermolecular disulfide bond formation in the human glucocorticoid receptor.	Disulfides	46-55	nuclear receptor subfamily 3 group C member 1	Homo sapiens	84-107
2653312-3	1989	The geometric criteria are applied to the serine protease, subtilisin, to model stereochemically favorable disulfide mutants without altering the active site geometry, implying conservation of native biological activity.	Disulfides	107-116	coagulation factor II, thrombin	Homo sapiens	42-57
2708329-2	1989	We have investigated the potential for the steroid affinity-labeled human glucocorticoid receptor to form both intramolecular and intermolecular disulfide bonds.	Disulfides	145-154	nuclear receptor subfamily 3 group C member 1	Homo sapiens	74-97
2564860-2	1989	The IT was a rat IgG2c mAb recognizing the Thy-1 Ag, disulfide-linked to a ribosome-inactivating protein isolated from the seeds of the plant Saponaria officinalis (soapwort).	Disulfides	53-62	Thy-1 cell surface antigen	Rattus norvegicus	43-48
2651524-1	1989	Activation of the Hageman factor-dependent pathways in human plasma leads to the cleavage of high molecular weight kininogen (HMWK) into a disulfide-linked two-chain (heavy and light chain) molecule and release of bradykinin, a vasoactive peptide.	Disulfides	139-148	kininogen 1	Homo sapiens	93-124
2651524-1	1989	Activation of the Hageman factor-dependent pathways in human plasma leads to the cleavage of high molecular weight kininogen (HMWK) into a disulfide-linked two-chain (heavy and light chain) molecule and release of bradykinin, a vasoactive peptide.	Disulfides	139-148	kininogen 1	Homo sapiens	126-130
2647502-3	1989	The latter contains disulfide bonds, which in vitro are reduced by the thioredoxin system, i.e. thioredoxin, thioredoxin reductase and NADPH.	Disulfides	20-29	thioredoxin 1	Rattus norvegicus	71-82
2466831-12	1989	These findings indicate that "F" alpha 2M interacts with IL-1 beta through a thiol-disulfide exchange reaction.	Disulfides	83-92	interleukin 1 beta	Homo sapiens	57-66
2758067-1	1989	The A- and B-chains have been isolated from the non-covalent complex of human thrombin A- and B-chains, using selective reduction of the interchain disulfide bridge.	Disulfides	148-157	coagulation factor II, thrombin	Homo sapiens	78-86
2494662-0	1989	Molecular heterogeneity of gamma delta T-cell antigen receptors expressed by CD4- CD8- T-cell clones from normal donors: both disulfide- and non-disulfide-linked receptors are delta TCS1+.	Disulfides	126-135	CD4 molecule	Homo sapiens	77-80
2494995-4	1989	The alpha-alpha subunit disulfide bonds result in the inhibition of transducin activation by bleached rhodopsin which is restored by reducing the disulfides with dithiothreitol.	Disulfides	24-33	rhodopsin	Homo sapiens	102-111
2494995-4	1989	The alpha-alpha subunit disulfide bonds result in the inhibition of transducin activation by bleached rhodopsin which is restored by reducing the disulfides with dithiothreitol.	Disulfides	146-156	rhodopsin	Homo sapiens	102-111
2501158-6	1989	Bovine pancreatic RNase A contains four disulfide bonds and the proper formation of these bonds is required for activity.	Disulfides	40-49	ribonuclease pancreatic	Bos taurus	18-25
2753599-0	1989	Contribution of disulfide bonds to stability of the folding intermediate of alpha-lactalbumin.	Disulfides	16-25	lactalbumin alpha	Homo sapiens	76-93
2753599-1	1989	The secondary structure formed in disulfide reduced alpha-lactalbumin is investigated by CD spectrum and is compared with that of the folding intermediate of the disulfide intact protein.	Disulfides	34-43	lactalbumin alpha	Homo sapiens	52-69
2648400-8	1989	Two disulfide-linked polypeptides, of Mr 48,000 and 40,000, were associated with the CD3 complex on the TCR3 cells.	Disulfides	4-13	CD3d molecule	Gallus gallus	85-88
2745634-0	1989	Determination of a disulfide-containing octapeptide antagonist of vasopressin in human plasma utilizing high-performance liquid chromatography with fluorescence detection.	Disulfides	19-28	arginine vasopressin	Homo sapiens	66-77
2466666-10	1989	The epitope for monoclonal antibody A5 is located within residues 1-393, and its recognition of antithrombin III or antithrombin-III-thrombin is strongly dependent on the integrity of the disulfide bonds.	Disulfides	188-197	coagulation factor II, thrombin	Homo sapiens	100-108
2647502-3	1989	The latter contains disulfide bonds, which in vitro are reduced by the thioredoxin system, i.e. thioredoxin, thioredoxin reductase and NADPH.	Disulfides	20-29	thioredoxin 1	Rattus norvegicus	96-107
2647502-3	1989	The latter contains disulfide bonds, which in vitro are reduced by the thioredoxin system, i.e. thioredoxin, thioredoxin reductase and NADPH.	Disulfides	20-29	thioredoxin 1	Rattus norvegicus	96-107
2645941-0	1989	The position of the disulfide bonds in human plasma alpha 2 HS-glycoprotein and the repeating double disulfide bonds in the domain structure.	Disulfides	20-29	alpha 2-HS glycoprotein	Homo sapiens	52-75
2784474-1	1989	Von Willebrand factor (vWf) is an adhesive glycoprotein composed of identical subunits linked by disulfide bonds to form multimers of varying sizes.	Disulfides	97-106	von Willebrand factor	Homo sapiens	23-26
2645941-5	1989	The location of the intra-disulfide bonds revealed that the A-chain of alpha 2 HS-glycoprotein is composed of three domains.	Disulfides	26-35	alpha 2-HS glycoprotein	Homo sapiens	71-94
2784474-1	1989	Von Willebrand factor (vWf) is an adhesive glycoprotein composed of identical subunits linked by disulfide bonds to form multimers of varying sizes.	Disulfides	97-106	von Willebrand factor	Homo sapiens	0-21
2498645-6	1989	vWF was properly processed and secreted to yield disulfide-bonded high-molecular-weight multimers similar to those observed in vWF secreted from human endothelial cells.	Disulfides	49-58	von Willebrand factor	Homo sapiens	0-3
2498645-6	1989	vWF was properly processed and secreted to yield disulfide-bonded high-molecular-weight multimers similar to those observed in vWF secreted from human endothelial cells.	Disulfides	49-58	von Willebrand factor	Homo sapiens	127-130
2648385-6	1989	Thus, GDCF and MDNCF have a similar gross secondary structure because of the loops formed by the clustered disulfides, and their different leukocyte specificities are most likely determined by the large differences in primary sequence.	Disulfides	107-117	C-X-C motif chemokine ligand 8	Homo sapiens	15-20
2647146-2	1989	A disulfide derivative of phosphatidylethanolamine containing a reactive N-hydroxysuccinimide ester group is synthesized, and the derivative is reacted with serum transferrin in deoxycholate-containing buffer.	Disulfides	2-11	transferrin	Homo sapiens	163-174
2645941-1	1989	The positions of the inter- and intra-chain disulfide bonds of human plasma alpha 2 HS-glycoprotein were determined.	Disulfides	44-53	alpha 2-HS glycoprotein	Homo sapiens	76-99
2647146-3	1989	Disulfide-linked transferrin-phosphatidylethanolamine conjugates containing up to 6 mol phospholipid/mol protein are prepared.	Disulfides	0-9	transferrin	Homo sapiens	17-28
2647146-7	1989	Using the disulfide linker to release transferrin from the liposomes, evidence is presented for a function of the phosphatidylethanolamine as an anchor-molecule into the liposomal lipid.	Disulfides	10-19	transferrin	Homo sapiens	38-49
2469470-6	1989	The interchain disulfide bond present in the human alpha 2M carboxyl-terminal 20-kDa fragment was conserved in bovine alpha 2M and rat alpha 1I3, but not in rat alpha 1M.	Disulfides	15-24	alpha-2-macroglobulin	Bos taurus	118-126
2463905-7	1989	The transition of p beta 1 to uncombined p beta 2 involves the formation of at least one intramolecular disulfide bond coincident with the conformational shift of the p beta molecule.	Disulfides	104-113	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	20-26
2463905-9	1989	This peptide presumably contains one of the two crucial cysteine residues that participate in forming the disulfide bond that distinguishes p beta 1 from the p beta 2 forms.	Disulfides	106-115	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	142-148
2912972-1	1989	Laminin, a major component of basement membranes, is a large glycoprotein consisting of three disulfide-bonded subunits, A, B1, and B2.	Disulfides	94-103	Laminin A	Drosophila melanogaster	0-7
2540806-2	1989	In the presence of Mn/MgATP, insulin binding to the isolated alpha beta heterodimeric insulin receptor was found to induce the formation of a covalent disulfide-linked alpha 2 beta 2 heterotetrameric complex.	Disulfides	151-160	insulin	Homo sapiens	29-36
2540806-2	1989	In the presence of Mn/MgATP, insulin binding to the isolated alpha beta heterodimeric insulin receptor was found to induce the formation of a covalent disulfide-linked alpha 2 beta 2 heterotetrameric complex.	Disulfides	151-160	insulin	Homo sapiens	86-93
2558637-5	1989	Altogether the results indicated that Cys402, probably by participating in a disulfide bridge, is essential for (i) the CD4-binding ability of env gene products and for (ii) the physical stability of gp 120.	Disulfides	77-86	CD4 molecule	Homo sapiens	120-123
2784109-7	1989	G1 mAb reacted with 5 clones, that were also stained by the previously described BB3 mAb (recognizing the disulfide-linked form of TcR gamma/delta).	Disulfides	106-115	B.burgdorferi-associated arthritis 3	Mus musculus	81-84
2523232-0	1989	Fast atom bombardment mass spectrometric investigation of in vitro degradation within the disulfide-linked core of atrial natriuretic factor.	Disulfides	90-99	natriuretic peptide A	Homo sapiens	115-140
2523232-3	1989	These truncated analogs were selected to investigate metabolism within the disulfide-linked core of ANF, particularly at the Cys7-Phe8 bond.	Disulfides	75-84	natriuretic peptide A	Homo sapiens	100-103
2785950-6	1989	Reduced and nonreduced two-dimensional electrophoresis analysis further revealed that Lyb-2 molecules are present on the B cell surface in two forms, a disulfide-bonded heterodimer of 45 kDa and 105 kDa chains and a 45 kDa homatrimer.	Disulfides	152-161	CD72 antigen	Mus musculus	86-91
2561638-0	1989	Selective inhibition of thrombin- and plasmin-induced platelet aggregation by a synthetic peptide disulfide.	Disulfides	98-107	coagulation factor II, thrombin	Homo sapiens	24-32
2473333-2	1989	The disulfide structures of ET-3 and sarafotoxin S6b were found to be identical with that of ET-1 (type A) but distinct from that of apamin (type B).	Disulfides	4-13	endothelin 1	Homo sapiens	93-97
2473333-6	1989	The opening of any disulfide bond in the ET-1 molecule extremely decreased the activity, while oxidation of the Met residue did not alter it.	Disulfides	19-28	endothelin 1	Homo sapiens	41-45
2473333-9	1989	The other disulfide analogues (type B and C) of ET-1 showed markedly lower activity than the parent molecule (type A).	Disulfides	10-19	endothelin 1	Homo sapiens	48-52
2561638-2	1989	A synthetic peptide disulfide, Gln-Val-Val-Cys(NpyS)-Gly-NH2 (P1) inhibited thrombin and plasmin-induced platelet aggregation and cleavage of aggregin.	Disulfides	20-29	coagulation factor II, thrombin	Homo sapiens	76-84
3264160-0	1988	Characterization of a recombinant murine interleukin-6: assignment of disulfide bonds.	Disulfides	70-79	interleukin 6	Mus musculus	41-54
2974038-1	1988	Fibronectin is organized into disulfide cross-linked, insoluble pericellular matrix fibrils by fibroblasts in vitro.	Disulfides	30-39	fibronectin 1	Homo sapiens	0-11
3245844-1	1988	Rabbit serum transferrin is isolated by a procedure designed to preserve its conformation and disulfide linkages.	Disulfides	94-103	transferrin	Homo sapiens	13-24
2846575-10	1988	Thus, the soluble form of the VIP receptor was probably a multimeric complex in which disulfide bonds may play an important role to hold the receptor in an active configuration.	Disulfides	86-95	vasoactive intestinal peptide	Homo sapiens	30-33
2975600-4	1988	Performing the electrophoretic run under reducing conditions completely abrogated the signal on the blot, indicating that the type I IFN receptor contains a disulfide bond essential for IFN binding.	Disulfides	157-166	interferon alpha 1	Homo sapiens	133-136
2975600-4	1988	Performing the electrophoretic run under reducing conditions completely abrogated the signal on the blot, indicating that the type I IFN receptor contains a disulfide bond essential for IFN binding.	Disulfides	157-166	interferon alpha 1	Homo sapiens	186-189
3264160-4	1988	The two disulfide bridges in mIL-6 have been identified by Staphylococcus aureus V8 protease peptide mapping and Edman degradation of cystine-containing peptides.	Disulfides	8-17	interleukin 6	Mus musculus	29-34
3221877-9	1988	These data show that POMC processing generates a COOH terminally amidated hJP predominantly secreted as a homodimer, probably through disulfide bonding between the single Cys9 residue of two molecules.	Disulfides	134-143	proopiomelanocortin	Homo sapiens	21-25
3179320-1	1988	Synthetic peptides cyclized via disulfide linkages have been synthesized as conformationally restricted analogs of a novel class of antithrombotic peptides that inhibit fibrinogen cleavage by binding to a non-enzymatic site on thrombin.	Disulfides	32-41	coagulation factor II, thrombin	Homo sapiens	227-235
2468359-9	1988	We suggest that the formation of the disulfide bridge between apo B and apo(a) in Lp(a) alters the system of disulfide bonds present in apo B and thereby modifies apo B structure.	Disulfides	37-46	apolipoprotein B	Homo sapiens	62-67
2468359-9	1988	We suggest that the formation of the disulfide bridge between apo B and apo(a) in Lp(a) alters the system of disulfide bonds present in apo B and thereby modifies apo B structure.	Disulfides	37-46	apolipoprotein B	Homo sapiens	136-141
2468359-9	1988	We suggest that the formation of the disulfide bridge between apo B and apo(a) in Lp(a) alters the system of disulfide bonds present in apo B and thereby modifies apo B structure.	Disulfides	37-46	apolipoprotein B	Homo sapiens	136-141
2468359-9	1988	We suggest that the formation of the disulfide bridge between apo B and apo(a) in Lp(a) alters the system of disulfide bonds present in apo B and thereby modifies apo B structure.	Disulfides	109-118	apolipoprotein B	Homo sapiens	62-67
2468359-9	1988	We suggest that the formation of the disulfide bridge between apo B and apo(a) in Lp(a) alters the system of disulfide bonds present in apo B and thereby modifies apo B structure.	Disulfides	109-118	apolipoprotein B	Homo sapiens	136-141
2468359-9	1988	We suggest that the formation of the disulfide bridge between apo B and apo(a) in Lp(a) alters the system of disulfide bonds present in apo B and thereby modifies apo B structure.	Disulfides	109-118	apolipoprotein B	Homo sapiens	136-141
3241126-5	1988	In human apoB this domain contains two regions enriched in positively charged amino acids flanking two disulfide-linked cysteine residues.	Disulfides	103-112	apolipoprotein B	Homo sapiens	9-13
3241126-10	1988	Also, the two disulfide-linked cysteine residues found near the proposed apoB binding domain were not conserved in the pig.	Disulfides	14-23	apolipoprotein B	Homo sapiens	73-77
3263644-5	1988	This shows that in IL-3 a single disulfide bridge, between cysteines 17 and 80, is required for biological activity that approximates physiological levels.	Disulfides	33-42	interleukin 3	Mus musculus	19-23
3263644-0	1988	Role of disulfide bridges in determining the biological activity of interleukin 3.	Disulfides	8-17	interleukin 3	Mus musculus	68-81
3263644-1	1988	Total chemical synthesis of analog proteins was used to examine the requirement for specific disulfide bridges for the biological activity of interleukin 3 (IL-3), a growth factor that stimulates multiple lineages of hemopoietic cells.	Disulfides	93-102	interleukin 3	Mus musculus	142-161
3196704-5	1988	In other experiments, the 17 through 27 synthetic peptide of the human fibrinogen A alpha chain was not an inhibitor of alpha-thrombin, while the NH2-terminal disulfide knot (NDSK) fragment was a simple competitive inhibitor of alpha-thrombin with a Ki approximately 3 microM (0.15 M NaCl, pH 7.3, approximately 23 degrees C).	Disulfides	159-168	coagulation factor II, thrombin	Homo sapiens	234-242
3255377-0	1988	Effect of oxidative sulfitolysis of disulfide bonds of bovine serum albumin on its structural properties: a physiochemical study.	Disulfides	36-45	albumin	Homo sapiens	62-75
2970465-3	1988	It has been demonstrated that C4BP consists of seven disulfide-linked, identical 70-kDa subunits, which are arranged to give the molecule a spider-like structure.	Disulfides	53-62	complement component 4 binding protein alpha	Homo sapiens	30-34
2970465-9	1988	The new subunit was demonstrated to be a disulfide-linked component of the central core of C4BP.	Disulfides	41-50	complement component 4 binding protein alpha	Homo sapiens	91-95
3047122-8	1988	About 30% of human transferrin receptors made in insect cells do not form intermolecular disulfide bonds, but are recognized by the anti-transferrin receptor antibody, B3/25, and bind specifically to a human transferrin-Sepharose column.	Disulfides	89-98	transferrin	Homo sapiens	19-30
3045123-5	1988	The amino acid sequences of the two proteinase-sensitive regions are mutually homologous; they are further characterized by the presence of a single copy each of the consensus tetrapeptide Cys-X-Gly-Cys known to form a narrow disulfide loop (Kellermann, J., Thelen, C., Lottspeich, F., Henschen, A., Vogel, R., and Muller-Esterl, W. (1987) Biochem.	Disulfides	226-235	endogenous retrovirus group K member 25	Homo sapiens	36-46
3266476-2	1988	Synthesis of chicken calcitonin-gene-related peptide (cCGRP) by application of sulfoxide-directed disulfide-bond-forming reaction.	Disulfides	98-107	calcitonin	Gallus gallus	21-52
2458152-9	1988	Both non-disulfide-bonded and disulfide-bonded vitronectin bound to antibody-Sepharose from a mixture of vitronectin and thrombin-antithrombin III.	Disulfides	30-39	coagulation factor II, thrombin	Homo sapiens	121-129
3403518-11	1988	Eight of the nine pairs of cysteines involved in disulfide bonds in RfBP are conserved in folate-binding protein, as are all of the tryptophan residues.	Disulfides	49-58	riboflavin binding protein	Gallus gallus	68-72
2457625-11	1988	These results indicate that hydrophobic forces and disulfide bonds may be involved in the association of P17 and P18 in serum and that HBeAg/2 activity depends upon association of HBeAg-polypeptides but that HBeAg/1 activity does not.	Disulfides	51-60	family with sequence similarity 72 member B	Homo sapiens	105-108
2457625-11	1988	These results indicate that hydrophobic forces and disulfide bonds may be involved in the association of P17 and P18 in serum and that HBeAg/2 activity depends upon association of HBeAg-polypeptides but that HBeAg/1 activity does not.	Disulfides	51-60	H3 histone pseudogene 12	Homo sapiens	113-116
3260917-6	1988	One heterodimer, composed of disulfide-linked 41- to 45-kDa protein (including a V gamma/C gamma 4 component), is expressed on a T cell hybridoma, DN-1.21, which was derived from fused splenic CD3+, CD4-, CD8- T cells.	Disulfides	29-38	CD247 antigen	Mus musculus	193-196
3044830-3	1988	MDNCF forms two loops via a neighboring pair of disulfide bridges, the probable locations of which are residues 7-34 and 9-50.	Disulfides	48-57	C-X-C motif chemokine ligand 8	Homo sapiens	0-5
3134521-9	1988	Treatment with dithiothreitol inhibited VPF activity, indicating the presence of at least one essential disulfide bond in this molecule.	Disulfides	104-113	vascular endothelial growth factor A	Homo sapiens	40-43
2847785-2	1988	Toward this end, C1-s was digested with trypsin in the presence of Ca2+, a treatment that rapidly degraded the B chain, leaving a 56-kDa fragment comprised of a complete A chain disulfide linked to a small (less than 4-kDa) residual piece of the B chain.	Disulfides	178-187	complement C1s	Homo sapiens	17-21
2899081-2	1988	Type beta transforming growth factors (TGF) are disulfide-linked homo- and heterodimers of two related polypeptide chains, beta 1 and beta 2.	Disulfides	48-57	transforming growth factor, beta 1	Rattus norvegicus	39-42
3181166-5	1988	In particular, the enrichment of thioredoxin and thioredoxin reductase to the endoplasmic reticulum is consistent with functions in protein processing, secretion and the formation of nascent protein disulfides.	Disulfides	199-209	thioredoxin 1	Rattus norvegicus	33-44
3181166-5	1988	In particular, the enrichment of thioredoxin and thioredoxin reductase to the endoplasmic reticulum is consistent with functions in protein processing, secretion and the formation of nascent protein disulfides.	Disulfides	199-209	peroxiredoxin 5	Rattus norvegicus	49-70
3056519-1	1988	A two-chain, disulfide linked, insulin-like compound embodying the A-domain of insulin-like growth factor I (IGF-I) and the B-chain of insulin has been synthesized and characterized with respect to insulin-like biological activity and growth-promoting potency.	Disulfides	13-22	insulin	Homo sapiens	31-38
3056519-1	1988	A two-chain, disulfide linked, insulin-like compound embodying the A-domain of insulin-like growth factor I (IGF-I) and the B-chain of insulin has been synthesized and characterized with respect to insulin-like biological activity and growth-promoting potency.	Disulfides	13-22	insulin like growth factor 1	Homo sapiens	79-107
3056519-1	1988	A two-chain, disulfide linked, insulin-like compound embodying the A-domain of insulin-like growth factor I (IGF-I) and the B-chain of insulin has been synthesized and characterized with respect to insulin-like biological activity and growth-promoting potency.	Disulfides	13-22	insulin like growth factor 1	Homo sapiens	109-114
3056519-1	1988	A two-chain, disulfide linked, insulin-like compound embodying the A-domain of insulin-like growth factor I (IGF-I) and the B-chain of insulin has been synthesized and characterized with respect to insulin-like biological activity and growth-promoting potency.	Disulfides	13-22	insulin	Homo sapiens	79-86
3056519-1	1988	A two-chain, disulfide linked, insulin-like compound embodying the A-domain of insulin-like growth factor I (IGF-I) and the B-chain of insulin has been synthesized and characterized with respect to insulin-like biological activity and growth-promoting potency.	Disulfides	13-22	insulin	Homo sapiens	79-86
2899077-2	1988	In the absence of added Factor XIIIa, fibronectin binds to cultured fibroblast cell layers and is assembled into disulfide-bonded multimers of the extracellular matrix.	Disulfides	113-122	fibronectin 1	Homo sapiens	38-49
2899077-9	1988	Thus, Factor XIIIa-mediated fibronectin cross-linking complements disulfide-bonded multimer formation in the stabilization of assembling fibronectin molecules and thus enhances the formation of extracellular matrix.	Disulfides	66-75	coagulation factor XIII A chain	Homo sapiens	6-18
3179268-6	1988	The disulfide-linked dimer of oncomodulin appears to be more similar to calmodulin than oncomodulin since the dimer displayed "calmodulin-like" affinity for the amphiphilic peptide melittin.	Disulfides	4-13	calmodulin 1	Homo sapiens	127-137
3134887-6	1988	Based on assignment of the disulfide bonds, a structural model of the interleukin-2 receptor for interleukin-2 binding is proposed.	Disulfides	27-36	interleukin 2	Homo sapiens	70-83
3179277-7	1988	The location of the 19 disulfide bridges is described, and their possible structural roles are discussed in relation to the transferrin family of proteins.	Disulfides	23-32	transferrin	Homo sapiens	124-135
2899077-9	1988	Thus, Factor XIIIa-mediated fibronectin cross-linking complements disulfide-bonded multimer formation in the stabilization of assembling fibronectin molecules and thus enhances the formation of extracellular matrix.	Disulfides	66-75	fibronectin 1	Homo sapiens	137-148
3134887-6	1988	Based on assignment of the disulfide bonds, a structural model of the interleukin-2 receptor for interleukin-2 binding is proposed.	Disulfides	27-36	interleukin 2	Homo sapiens	97-110
3220478-4	1988	Sequence comparisons between the extracellular domains of CEA and NCA show that the N-terminal and adjacent loop domains of each apoprotein have high homology (85-90%) to each other, while comparison of loop-domain regions reveals a possible nonrandom distribution of base changes and altered amino acids near certain cysteine residues that are inferred to be involved in forming disulfide loops.	Disulfides	380-389	CEA cell adhesion molecule 3	Homo sapiens	58-61
3286642-0	1988	Insulin-dependent covalent reassociation of isolated alpha beta heterodimeric insulin receptors into an alpha 2 beta 2 heterotetrameric disulfide-linked complex.	Disulfides	136-145	insulin	Homo sapiens	78-85
3390172-3	1988	The four cysteine residues detected in the NCA-50 molecule form disulfide bonds.	Disulfides	64-73	CEA cell adhesion molecule 4	Homo sapiens	43-46
2453925-3	1988	All of the seven epitopes that were located reside within two immunoglobulin-like disulfide loops situated between residues 1 and 168 of the CD4 protein.	Disulfides	82-91	CD4 molecule	Homo sapiens	141-144
3286642-0	1988	Insulin-dependent covalent reassociation of isolated alpha beta heterodimeric insulin receptors into an alpha 2 beta 2 heterotetrameric disulfide-linked complex.	Disulfides	136-145	insulin	Homo sapiens	0-7
3286642-4	1988	Comparison by reducing and nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the insulin-dependent covalent reassociation to an alpha 2 beta 2 heterotetrameric complex was due to the formation of a disulfide linkage(s) between the alpha beta heterodimers.	Disulfides	232-241	insulin	Homo sapiens	115-122
3417115-4	1988	Yellow tail growth hormone exhibits a typical structural feature as growth hormone, including four cysteine residues to form two disulfide bonds and other identical amino acids with other vertebrate GHs.	Disulfides	129-138	growth hormone 1	Homo sapiens	12-26
3165289-0	1988	Conformation of the second disulfide loop in human transforming growth factor-alpha studied by two-dimensional NMR spectroscopy.	Disulfides	27-36	tumor necrosis factor	Homo sapiens	51-83
3417115-4	1988	Yellow tail growth hormone exhibits a typical structural feature as growth hormone, including four cysteine residues to form two disulfide bonds and other identical amino acids with other vertebrate GHs.	Disulfides	129-138	growth hormone 1	Homo sapiens	68-82
2835858-3	1988	In analogy to PDGF, the gp200sis protein backbone is shown here to consist of disulfide-linked polypeptide chains.	Disulfides	78-87	podocalyxin like	Homo sapiens	24-29
3162913-4	1988	The 13-kDa subunit was part of a disulfide-bonded dimer and was identified by amino acid sequencing as TGF-beta 1.	Disulfides	33-42	transforming growth factor beta 1	Homo sapiens	103-113
3288200-0	1988	Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae.	Disulfides	8-17	lysozyme	Homo sapiens	58-66
3288200-2	1988	Our results have revealed that the formation of the disulfide bond Cys6/Cys128 in human lysozyme is a prerequisite for correct folding in vivo in yeast.	Disulfides	52-61	lysozyme	Homo sapiens	88-96
3288200-5	1988	These are the first findings that the individual disulfide bonds of human lysozyme have different functions in folding and secretion in vivo.	Disulfides	49-58	lysozyme	Homo sapiens	74-82
3130094-1	1988	Tissue plasminogen activator (tPA) was covalently linked by disulfide bonds to a monoclonal antibody specific for the amino terminus of the beta chain of fibrin (antibody 59D8).	Disulfides	60-69	plasminogen activator, tissue type	Homo sapiens	0-34
3144290-0	1988	Identification of the second (buried) cysteine residue and of the C-terminal disulfide bridge of bovine spleen cathepsin B.	Disulfides	77-86	cathepsin B	Bos taurus	111-122
3144290-2	1988	The intra- and interchain thiol-disulfide exchange reactions accompanying the denaturation of cathepsin B were investigated by polyacrylamide gel electrophoresis in SDS and by gel filtration experiments.	Disulfides	32-41	cathepsin B	Bos taurus	94-105
3144290-4	1988	After conditions preventing thiol-disulfide exchange reactions, had been developed, the second SH-group (Cys240) was demonstrated independently in carboxymethylated cathepsin B by labeling with 4-(dimethylamino)azobenzene-4"-iodoacetamide and by selective isolation of the SH-peptide containing Cys240 on thiopropyl-Sepharose.	Disulfides	34-43	cathepsin B	Bos taurus	165-176
2835654-0	1988	Identification of nonessential disulfide bonds and altered conformations in the v-sis protein, a homolog of the B chain of platelet-derived growth factor.	Disulfides	31-40	hypothetical protein	Woolly monkey sarcoma virus	80-85
2835654-3	1988	Both native PDGF and the v-sis protein occur as disulfide-bonded dimers, probably containing both intramolecular and intermolecular disulfide bonds.	Disulfides	48-57	hypothetical protein	Woolly monkey sarcoma virus	25-30
2835654-3	1988	Both native PDGF and the v-sis protein occur as disulfide-bonded dimers, probably containing both intramolecular and intermolecular disulfide bonds.	Disulfides	132-141	hypothetical protein	Woolly monkey sarcoma virus	25-30
2835654-11	1988	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis indicated that the v-sis proteins encoded by some of the biologically active mutants exhibited an altered conformation when compared with the wild-type v-sis protein, and suggested that Cys-154 and Cys-163 participate in a nonessential disulfide bond.	Disulfides	303-312	hypothetical protein	Woolly monkey sarcoma virus	86-91
3258329-3	1988	The CT8 antibody precipitated a molecule of Mr 63,000 under non-reducing conditions and polypeptide chains of Mr 34,000 under reducing conditions, suggesting that the CT8 molecule is a disulfide-linked homodimer.	Disulfides	185-194	leucine zipper protein 4	Homo sapiens	4-7
3258329-3	1988	The CT8 antibody precipitated a molecule of Mr 63,000 under non-reducing conditions and polypeptide chains of Mr 34,000 under reducing conditions, suggesting that the CT8 molecule is a disulfide-linked homodimer.	Disulfides	185-194	leucine zipper protein 4	Homo sapiens	167-170
2831901-4	1988	The substitution of the residues at these positions, especially at position 88, reduced the heterogeneity recognized as several peaks of bFGF eluted from a heparin affinity column, even after oxidation with hydrogen peroxide, suggesting that the cysteines at these positions are exposed to the surface of the molecule to form disulfide bonds that induce heterologous conformations.	Disulfides	326-335	fibroblast growth factor 2	Homo sapiens	137-141
2449439-14	1988	These results demonstrate that: 1) disulfide bonds are required for the activity of PSP-A, 2) disruption of disulfides does not prevent the formation of oligomeric forms of PSP-A, 3) the oligosaccharide moiety is not essential for biological activity, and 4) monoclonal antibodies can be used to map the epitopes responsible for biological activity.	Disulfides	35-44	surfactant protein A1	Rattus norvegicus	84-92
2449439-14	1988	These results demonstrate that: 1) disulfide bonds are required for the activity of PSP-A, 2) disruption of disulfides does not prevent the formation of oligomeric forms of PSP-A, 3) the oligosaccharide moiety is not essential for biological activity, and 4) monoclonal antibodies can be used to map the epitopes responsible for biological activity.	Disulfides	108-118	surfactant protein A1	Rattus norvegicus	84-92
3338452-1	1988	Hepatic-type fatty-acid-binding protein (hFABP) from the cytosol of bovine liver is a 14.4-kDa neutral protein with a blocked N-terminus and a disulfide system located on the surface of the protein.	Disulfides	143-152	fatty acid binding protein 3	Homo sapiens	41-46
3276306-0	1988	Monensin is obligatory for the cytotoxic action of a disulfide linked methotrexate-anti-transferrin receptor conjugate.	Disulfides	53-62	transferrin	Homo sapiens	88-99
3276306-1	1988	Methotrexate (MTX) in the form of a gamma-cysteinylglycine derivative was disulfide linked to a monoclonal antibody reactive with the human transferrin receptor to give an antibody-MTX conjugate (anti-TfR-MTX).	Disulfides	74-83	transferrin	Homo sapiens	140-151
2450565-7	1988	This suggests that the epitope is conformationally dependent and that a disulfide bridge linking cysteines-217 and -221 is present in the native structure of human renin.	Disulfides	72-81	renin	Homo sapiens	164-169
3367540-8	1988	The proposed model of circulating transferrin receptor may be the nicked dimers of 55,000 daltons in which inter- and intra-disulfide bridges were present.	Disulfides	124-133	transferrin	Homo sapiens	34-45
2448168-2	1988	Most likely, the two proteins diverged after the primary duplication of a single cystatin domain as the two cystatin domains of alpha-2-HS-glycoprotein are more similar, especially in disulfide bonding, to the corresponding domains of kininogen than to each other.	Disulfides	184-193	alpha 2-HS glycoprotein	Homo sapiens	128-151
3338452-6	1988	His was excluded, as 1H-NMR analysis of His-C2 and His-C4 protons indicated that binding of oleic acid shifts the pK of His from 6.9 to 7.1 only in hFABP with the disulfide system in the oxidized state; acylation of His with diethylpyrocarbonate does not affect the binding of the fatty acid.	Disulfides	163-172	fatty acid binding protein 3	Homo sapiens	148-153
2452045-5	1988	The results suggested that some disulfide linkages of AFP could be reduced.	Disulfides	32-41	alpha fetoprotein	Homo sapiens	54-57
3248239-2	1988	Six conformationally restricted analogues of angiotensin II containing one disulfide bridge were synthesized by the solid-phase method.	Disulfides	75-84	angiotensinogen	Rattus norvegicus	45-59
2835273-10	1988	In response to insulin, activation of protein phosphatase type-1 occurs with a stable conformational change that may involve rearrangement of disulfide bonds.	Disulfides	142-151	insulin	Homo sapiens	15-22
3069640-9	1988	Plasma vWF consists of a heterogenous series of multimers, composed of an apparently single-type glycoprotein subunit, linked together by disulfide bonds.	Disulfides	138-147	von Willebrand factor	Homo sapiens	7-10
2447882-1	1987	Two synthetic insulin-like compounds consisting of the B-chain of insulin linked via disulfide bonds to A chains corresponding to the A-domain or the A- and D-domains of insulin-like growth factor I (IGF-I) have been evaluated for mitogenic activity and for binding to IGF receptors and IGF carrier proteins.	Disulfides	85-94	insulin	Gallus gallus	14-21
3356297-2	1988	Human haptoglobin (Hp) type 2-1 was subjected to the sulfanilazo-modification of tyrosine and histidine residues, the removal of sialic acid, and the reduction of disulfide bonds (isolation of alpha 2, alpha 1, beta subunits), respectively.	Disulfides	163-172	haptoglobin	Homo sapiens	6-17
2961806-5	1988	Electrophoresis under reducing and nonreducing conditions suggested that CD22 and CD21 may have similarities in intra-chain disulfide bond formation.	Disulfides	124-133	CD22 molecule	Homo sapiens	73-77
2961806-5	1988	Electrophoresis under reducing and nonreducing conditions suggested that CD22 and CD21 may have similarities in intra-chain disulfide bond formation.	Disulfides	124-133	complement C3d receptor 2	Homo sapiens	82-86
2451704-10	1988	However, it could also be that the binding of the [a]antigen to apoB via disulfide bridges causes profound conformational changes of the apoB region exposed to the surface.	Disulfides	73-82	apolipoprotein B	Homo sapiens	64-68
2451704-10	1988	However, it could also be that the binding of the [a]antigen to apoB via disulfide bridges causes profound conformational changes of the apoB region exposed to the surface.	Disulfides	73-82	apolipoprotein B	Homo sapiens	137-141
2450560-6	1987	Translation of these sequences showed that the FNR alpha, the VnR alpha, and GP IIb are composed of disulfide-linked large (858-871 amino acids) and small (137-158 amino acids) chains that are posttranslationally processed from a single mRNA.	Disulfides	100-109	integrin subunit alpha 5	Homo sapiens	47-56
3316225-8	1987	These data demonstrate that the isolated alpha beta heterodimeric insulin receptor complex is fully capable of expressing insulin-dependent activation of the beta subunit protein kinase domain with the covalent reassociation of the alpha beta heterodimeric complex into an alpha 2 beta 2 heterotetrameric disulfide-linked state.	Disulfides	305-314	insulin	Homo sapiens	66-73
3502076-0	1987	Identification of disulfide-bridged substructures within human von Willebrand factor.	Disulfides	18-27	von Willebrand factor	Homo sapiens	63-84
3316225-8	1987	These data demonstrate that the isolated alpha beta heterodimeric insulin receptor complex is fully capable of expressing insulin-dependent activation of the beta subunit protein kinase domain with the covalent reassociation of the alpha beta heterodimeric complex into an alpha 2 beta 2 heterotetrameric disulfide-linked state.	Disulfides	305-314	insulin	Homo sapiens	122-129
3122318-4	1987	vWF is composed of identical subunits linked together by disulfide bridges.	Disulfides	57-66	von Willebrand factor	Homo sapiens	0-3
3425722-6	1987	Thus, enzymatic cleavage of AVP by luminal and lysosomal peptidases in proximal tubules could involve disulfide bond, C-terminal, and N-terminal loci.	Disulfides	102-111	arginine vasopressin	Homo sapiens	28-31
3498719-3	1987	The larger Fragment III, a disulfide-linked homodimer, extends between residues 1 and 1365 of the 2050-residue vWF subunit and comprises the sequence of all the others.	Disulfides	27-36	von Willebrand factor	Homo sapiens	111-114
3122823-5	1987	RMCP I has six half-cystine residues at the same positions as in RMCP II, cathepsin G, and the two lymphocyte proteases, suggesting disulfide pairs identical with those reported for RMCP II.	Disulfides	132-141	mast cell protease 1-like 1	Rattus norvegicus	0-6
3675570-6	1987	Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) has been identified as the protein undergoing thiol/disulfide redox status and enzymic activity changes.	Disulfides	107-116	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	0-40
3119602-3	1987	Drosophila laminin is a disulfide-linked molecule consisting of three chains with apparent molecular masses of 400, 215, and 185 kD.	Disulfides	24-33	Laminin A	Drosophila melanogaster	11-18
3500356-1	1987	An immunoconjugate was prepared containing a disulfide linker between a murine monoclonal antibody (5E9), which recognized the human transferrin receptor, and the ribosome-inactivating protein gelonin.	Disulfides	45-54	transferrin	Homo sapiens	133-144
3500472-1	1987	The monoclonal antibody 1F5 recognizes human B-cell surface protein CD20 and can activate resting B cells; with this antibody we found CD20 to be a 35/37-kDa non-disulfide-linked protein.	Disulfides	162-171	keratin 20	Homo sapiens	135-139
3667599-2	1987	After trypsin digestion of the type I procollagen, a portion of the alpha 1 (I) chains was recovered as disulfide-linked dimers.	Disulfides	104-113	collagen type I alpha 2 chain	Homo sapiens	31-49
3116546-6	1987	These revealed a 65-kDa heavy chain-t-PA fusion protein that is secreted in association with the 59D8 light chain in the form of a 170-kDa disulfide-linked dimer.	Disulfides	139-148	plasminogen activator, tissue type	Homo sapiens	36-40
3624271-9	1987	The pre-beta 1 form has a t1/2 of about 4 min and has a precursor-product relationship with a more completely disulfide-bonded form, termed pre-beta 2, which does combine with the alpha subunit to form a dimer.	Disulfides	110-119	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	8-14
3654604-0	1987	Role of single disulfide in recombinant human tumor necrosis factor-alpha.	Disulfides	15-24	tumor necrosis factor	Homo sapiens	46-73
3654604-6	1987	The cytolytic, macrophage activation, and lipogenic activities decreased in the order of the natural sequence TNF-alpha greater than the alanine analog greater than the leucine analog, suggesting that the surface involving the disulfide bond plays a role in these biological functions and the introduced modifications decrease the activity.	Disulfides	227-236	tumor necrosis factor	Homo sapiens	110-119
3038177-0	1987	Characterization of disulfide bonds in recombinant proteins: reduced human interleukin 2 in inclusion bodies and its oxidative refolding.	Disulfides	20-29	interleukin 2	Homo sapiens	75-88
3040761-8	1987	P24 co-migrated with GP Ib beta on reduced gels (Mr = 24,000) and also on nonreduced gels (when GP Ib beta is disulfide-linked to GP Ib alpha and migrates with Mr = 170,000).	Disulfides	110-119	transmembrane p24 trafficking protein 2	Homo sapiens	0-3
3115179-0	1987	Importance of disulfide linkage for constructing the biologically active human interleukin-2.	Disulfides	14-23	interleukin 2	Homo sapiens	79-92
3115179-1	1987	Recombinant human interleukin-2 (rIL-2) produced in Escherichia coli possesses a free thiol group at Cys-125 and a disulfide linkage between Cys-58 and Cys-105, as in the case for natural human interleukin-2.	Disulfides	115-124	interleukin 2	Homo sapiens	18-31
3115179-7	1987	These results strongly demonstrate that the Cys-58-Cys-105 disulfide linkage in the IL-2 molecule is essential for constructing a rigid and biologically active form of IL-2.	Disulfides	59-68	interleukin 2	Homo sapiens	84-88
3115179-7	1987	These results strongly demonstrate that the Cys-58-Cys-105 disulfide linkage in the IL-2 molecule is essential for constructing a rigid and biologically active form of IL-2.	Disulfides	59-68	interleukin 2	Homo sapiens	168-172
3304287-0	1987	Non-enzymatic formation of insulin-glutathione mixed disulfides: evidence for a transient species by plasma desorption mass spectrometry.	Disulfides	53-63	insulin	Homo sapiens	27-34
3304287-1	1987	Formation of insulin-glutathione mixed disulfides takes place under the conditions of 0.1 M ammonium acetate, neutral pH and without the presence of any enzyme.	Disulfides	39-49	insulin	Homo sapiens	13-20
3304287-2	1987	Using a SH-free glutathione-agarose column it is demonstrated that the interaction of insulin with glutathione is specific, and increasing the incubation time between these two peptides results in the reduction of insulin disulfide bonds and the production of A and B chains.	Disulfides	222-231	insulin	Homo sapiens	86-93
3304287-2	1987	Using a SH-free glutathione-agarose column it is demonstrated that the interaction of insulin with glutathione is specific, and increasing the incubation time between these two peptides results in the reduction of insulin disulfide bonds and the production of A and B chains.	Disulfides	222-231	insulin	Homo sapiens	214-221
2885839-4	1987	Two Thy-1+ DEC lines expressed a disulfide-linked 70-kDa molecule that could be precipitated with an anti-gamma-chain antiserum and could be coprecipitated with an antiserum to the T3 delta chain; the molecule appeared as a single 34-kDa band under reducing conditions.	Disulfides	33-42	thymus cell antigen 1, theta	Mus musculus	4-9
3597378-9	1987	Reduction of the intrachain disulfide bonds in this part of the alpha subunit leads to a loss of insulin binding.	Disulfides	28-37	insulin	Homo sapiens	97-104
3038177-2	1987	Human IL-2 has three Cys residues, namely, Cys-58, Cys-105, and Cys-125, and native IL-2 has an intramolecular disulfide bond between Cys-58 and Cys-105.	Disulfides	111-120	interleukin 2	Homo sapiens	84-88
2436912-4	1987	It disappeared upon reduction of disulfide bridges and also after thrombin of chymotrypsin cleavage of protein S. Thrombin cleaves protein S close to the calcium-binding region containing gamma-carboxyglutamic acid (Gla).	Disulfides	33-42	coagulation factor II, thrombin	Homo sapiens	114-122
2822674-0	1987	Formation of mixed disulfide of cystatin-beta in cultured macrophages treated with various oxidants.	Disulfides	19-28	cystatin B	Homo sapiens	32-45
3616572-1	1987	The assembly of fibronectin into fibrils was monitored by high voltage electron microscopy using 18 nm colloidal gold beads bound to fibronectin (Au18-fibronectin) or an amino terminal 70 kd fragment of fibronectin (Au18-70 kd) that blocks the incorporation of fibronectin into disulfide bonded fibrils.	Disulfides	278-287	fibronectin 1	Homo sapiens	16-27
2436691-3	1987	With trypsinized, labeled platelets, AK 1, SZ 1, and FMC 25 (epitope on GP IX) immunoprecipitated a membrane-bound proteolytic fragment of the GP Ib-IX complex consisting of GP IX and an congruent to 25,000 mol wt remnant of the alpha-chain of GP lb disulfide-linked to the beta-subunit.	Disulfides	250-259	adenylate kinase 1	Homo sapiens	37-41
3571267-8	1987	Rat hydroxyindole-O-methyltransferase is also inactivated in the absence of added disulfides and dissolved O2.	Disulfides	82-92	acetylserotonin O-methyltransferase	Rattus norvegicus	4-37
3571267-12	1987	Together these observations indicate that rat pineal hydroxyindole-O-methyltransferase can be inactivated by a protein thiol:disulfide exchange mechanism.	Disulfides	125-134	acetylserotonin O-methyltransferase	Rattus norvegicus	53-86
3571267-0	1987	Inactivation of rat pineal hydroxyindole-O-methyltransferase by disulfide-containing compounds.	Disulfides	64-73	acetylserotonin O-methyltransferase	Rattus norvegicus	27-60
3571267-1	1987	Rat pineal hydroxyindole-O-methyltransferase activity in crude homogenates is reduced by treatment with disulfides.	Disulfides	104-114	acetylserotonin O-methyltransferase	Rattus norvegicus	11-44
3605592-0	1987	Preparation of homogeneous pig liver thioltransferase by a thiol:disulfide mediated pI shift.	Disulfides	65-74	glutaredoxin-1	Sus scrofa	37-53
2443487-11	1987	By analogy with human alpha 2M, the 35 kDa subunit would be located at the C-terminal end of murine alpha 2M, disulfide-bonded to the major 165 kDa subunit.	Disulfides	110-119	PZP, alpha-2-macroglobulin like	Mus musculus	100-108
2435722-6	1987	It was shown that in the medium of [35S]methionine-labeled hepatocytes the two subunits of alpha 1-macroglobulin are linked by disulfide bridges.	Disulfides	127-136	pregnancy-zone protein	Rattus norvegicus	91-112
3472206-1	1987	Apolipoprotein(a) [apo(a)] is a glycoprotein with Mr approximately equal to 280,000 that is disulfide linked to apolipoprotein B in lipoprotein(a) particles.	Disulfides	92-101	apolipoprotein B	Homo sapiens	112-128
3030446-7	1987	We also identified a novel disulfide-bonded collagen-binding glycoprotein (CBP2; Mr = 45,000, reduced).	Disulfides	27-36	serpin family H member 1	Rattus norvegicus	75-79
3037720-2	1987	Fully formed fibrinogen is a six chain, disulfide-linked, dimeric molecule with a molecular weight of 340kDa.	Disulfides	40-49	fibrinogen beta chain	Homo sapiens	13-23
2950941-3	1987	The samples were treated with cyanogen bromide (CNBr), and the total amount of fibrinogen and fibrin-derived protein was determined as NDSK, the NH2-terminal disulfide knot of fibrinogen.	Disulfides	158-167	fibrinogen beta chain	Homo sapiens	79-89
3593791-1	1987	Copolymerization of fibrinogen with desAB- and desA-fibrin NH2-terminal disulfide knots (tN-DSK and rN-DSK, respectively) caused by interdomain D-E-binding was compared.	Disulfides	72-81	fibrinogen beta chain	Homo sapiens	20-30
3605592-1	1987	An enzyme catalyzing thiol-disulfide exchange, thioltransferase, was purified to homogeneity from pig liver.	Disulfides	27-36	glutaredoxin-1	Sus scrofa	47-63
2435170-7	1987	Thus the high-affinity VIP receptor on pancreatic acinar cell membranes consists of a single major polypeptide of Mr 45,000, and this polypeptide is not a subunit of a larger disulfide-linked structure.	Disulfides	175-184	vasoactive intestinal peptide	Rattus norvegicus	23-26
3817157-0	1987	Identification of disulfide bonds in carboxy-terminal propeptides of human type I procollagen.	Disulfides	18-27	collagen type I alpha 2 chain	Homo sapiens	75-93
3029090-1	1987	Botulinum neurotoxin (NT) is synthesized by Clostridium botulinum in any of seven antigenically distinct forms called types A-G. NT, when fully active, is a dichain protein, composed of two polypeptides, a heavy (H) and a light (L) chain (approximately 100,000 and approximately 50,000 Da, respectively) that are held together by noncovalent bonds and at least one disulfide bond.	Disulfides	365-374	neurotoxin	Clostridium botulinum	10-20
3101765-4	1987	The NH2-terminal fragment (FI), mol wt approximately 18,000, was disulfide-linked to the thrombin A chain.	Disulfides	65-74	coagulation factor II, thrombin	Homo sapiens	89-97
3104900-5	1987	CD4 domains 2 and 4 contain disulfide bonds but seem like truncated immunoglobulin domains, whereas domain 3 may have a pattern of beta-strands like an immunoglobulin variable domain, but without the disulfide bond.	Disulfides	28-37	CD4 molecule	Homo sapiens	0-3
3817157-1	1987	Intra-chain and inter-chain disulfide bonds within the carboxy-terminal propeptides of human type I procollagen were studied using cyanogen bromide cleavage of the propeptides and electrophoresis on SDS-polyacrylamide/glycerol gels.	Disulfides	28-37	collagen type I alpha 2 chain	Homo sapiens	93-111
3582362-0	1987	Identification of the intermolecular disulfide bonds of the human transferrin receptor and its lipid-attachment site.	Disulfides	37-46	transferrin	Homo sapiens	66-77
3582362-1	1987	Structural studies of the human transferrin receptor have shown that the molecule is a disulfide-bonded dimer consisting of two identical subunits (Mr = 95,000) which are post-translationally modified by the addition of a fatty acyl moiety.	Disulfides	87-96	transferrin	Homo sapiens	32-43
3558694-0	1987	Quantitative liquid chromatographic determination of disulfide-containing peptide analogues of vasopressin with dual Hg/Au electrochemical detection.	Disulfides	53-62	arginine vasopressin	Homo sapiens	95-106
3558694-1	1987	Quantitative methodology was developed for the analysis of disulfide-containing peptide analogues of vasopressin in biologic media.	Disulfides	59-68	arginine vasopressin	Homo sapiens	101-112
3466649-12	1987	Tetrathionate modification of rhodanese may proceed through the formation of sulfenylthiosulfate intermediates at sulfhydryl groups, close to but not identical with the active-site sulfhydryl group, which then can react further with the active-site sulfhydryl group to form disulfide bridges.	Disulfides	274-283	thiosulfate sulfurtransferase	Bos taurus	30-39
3804996-5	1987	The ternary complex, DNA X HMG1 X 1, seemed to represent a specific structure, since its formation depeNded on the reduced sulfhydryl state of HMG1; the disulfide form of HMG1, which was shown by circular dichroism to contain more random coil than did the reduced form, had no effect on the circular dichroic spectrum of the DNA X H1 complex.	Disulfides	153-162	high mobility group box 1 pseudogene 5	Homo sapiens	27-31
3804996-5	1987	The ternary complex, DNA X HMG1 X 1, seemed to represent a specific structure, since its formation depeNded on the reduced sulfhydryl state of HMG1; the disulfide form of HMG1, which was shown by circular dichroism to contain more random coil than did the reduced form, had no effect on the circular dichroic spectrum of the DNA X H1 complex.	Disulfides	153-162	high mobility group box 1 pseudogene 5	Homo sapiens	143-147
3804996-5	1987	The ternary complex, DNA X HMG1 X 1, seemed to represent a specific structure, since its formation depeNded on the reduced sulfhydryl state of HMG1; the disulfide form of HMG1, which was shown by circular dichroism to contain more random coil than did the reduced form, had no effect on the circular dichroic spectrum of the DNA X H1 complex.	Disulfides	153-162	high mobility group box 1 pseudogene 5	Homo sapiens	143-147
2432067-4	1987	alpha 1M, and (alpha beta)4-tetramer in native solution, separated in the second sodium dodecyl sulfate-containing electrophoretic dimension as a disulfide-linked (alpha beta)2-dimer with an approximate Mr of 360 kDa.	Disulfides	146-155	pregnancy-zone protein	Rattus norvegicus	0-8
3327411-1	1987	Ricin A chain, a potent ribosomal poison, was disulfide linked either to the iron transport protein, transferrin, or to anti-transferrin receptor antibodies to produce highly specific derivative toxins, Tf-A and TfR-A, respectively.	Disulfides	46-55	transferrin	Homo sapiens	101-112
3812684-7	1987	After taking into account the molecular weight of 125I-gastrin2(-17), our results suggest that the gastrin receptor on parietal cells is a single protein of Mr 74,000 without disulfide-linked subunits.	Disulfides	175-184	gastrin	Canis lupus familiaris	99-106
3496151-1	1987	Anti-carcinoembryonic antigen (CEA) immunotoxins constructed with multiple anti-CEA antibodies (goat and baboon polyclonal, and three murine monoclonal antibodies) by covalently linking them to the A chain of ricin via a disulfide bond all function as potent and specific toxins for CEA-bearing cells, suggesting that the CEA molecule is capable of directing productive internalization of ricin A chain.	Disulfides	221-230	CEA cell adhesion molecule 3	Homo sapiens	31-34
3496157-0	1987	The antileukemic efficacy of an immunotoxin composed of a monoclonal anti-Thy-1 antibody disulfide linked to the ribosome-inactivating protein gelonin.	Disulfides	89-98	thymus cell antigen 1, theta	Mus musculus	74-79
3539228-0	1987	Topology and order of formation of interchain disulfide bonds in von Willebrand factor.	Disulfides	46-55	von Willebrand factor	Homo sapiens	65-86
3539228-1	1987	Interchain disulfide bonds between the subunits in von Willebrand factor (vWf) dimers and in vWf multimers have been studied using some unique features of the cultured human umbilical vein endothelial cell system.	Disulfides	11-20	von Willebrand factor	Homo sapiens	51-72
3539228-1	1987	Interchain disulfide bonds between the subunits in von Willebrand factor (vWf) dimers and in vWf multimers have been studied using some unique features of the cultured human umbilical vein endothelial cell system.	Disulfides	11-20	von Willebrand factor	Homo sapiens	74-77
3539228-1	1987	Interchain disulfide bonds between the subunits in von Willebrand factor (vWf) dimers and in vWf multimers have been studied using some unique features of the cultured human umbilical vein endothelial cell system.	Disulfides	11-20	von Willebrand factor	Homo sapiens	93-96
3102228-1	1986	The human interleukin-2 (IL-2) receptor was quantitatively cleaved into two large disulfide-bonded fragments by either trypsin or endoproteinase lys-C (endo lys-C).	Disulfides	82-91	interleukin 2	Homo sapiens	10-23
3021744-10	1986	Both beta 1- and beta 2-receptors displayed this same shift in electrophoretic mobility observed in the presence as compared to the absence of disulfide bridge-reducing agents, as detected both by autoradiography of the radiolabeled receptors and by immunoblotting of native receptors.	Disulfides	143-152	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	5-11
3536910-4	1986	The resulting two major fragments, which were purified by affinity and hydrophobic interaction chromatography and by glycerol-gradient ultracentrifugation, are disulfide-linked homodimers of these domains (i.e. RR and GG) and are morphologically identical to the alternating RR and GG domains of intact vWF.	Disulfides	160-169	von Willebrand factor	Homo sapiens	303-306
3572088-3	1986	Based on analysis of IFN-alpha 2, IFN-alpha 1 contains two disulfide bridges between cysteine residues 29 and 139 and cysteine residues 1 and 99.	Disulfides	59-68	interferon alpha 1	Homo sapiens	34-45
2946674-0	1986	Thiol/disulfide redox equilibrium between glutathione and glycogen debranching enzyme (amylo-1,6-glucosidase/4-alpha-glucanotransferase) from rabbit muscle.	Disulfides	6-15	glycogen debranching enzyme	Oryctolagus cuniculus	87-135
3778971-0	1986	[Effect of reduction of the interchain disulfide bridge of human thrombin on its enzymatic activity and structure].	Disulfides	39-48	coagulation factor II, thrombin	Homo sapiens	65-73
3534892-6	1986	Preliminary analysis indicated that, unlike the human receptor, the plasmodial transferrin receptor is not a disulfide linked dimer but a single polypeptide acylated via 1,2-diacyl-sn-glycerol.	Disulfides	109-118	transferrin	Homo sapiens	79-90
3021167-9	1986	A model is proposed wherein DSF and serum albumin rapidly form a noncovalent adduct and, subsequently, in a slow unimolecular process, DSF is reduced to one mole of free DDC and one mole of the serum albumin-DDC mixed disulfide.	Disulfides	218-227	albumin	Homo sapiens	36-49
3021167-9	1986	A model is proposed wherein DSF and serum albumin rapidly form a noncovalent adduct and, subsequently, in a slow unimolecular process, DSF is reduced to one mole of free DDC and one mole of the serum albumin-DDC mixed disulfide.	Disulfides	218-227	albumin	Homo sapiens	194-207
3778971-1	1986	It was shown that selective hydrolysis of the disulfide bridge between the A- and B-chains of human thrombin in the absence of denaturating agents decrease its proteolytic (e.g., fibrinogen-binding), esterase and amidase activities.	Disulfides	46-55	coagulation factor II, thrombin	Homo sapiens	100-108
2874135-3	1986	Type I TGF beta receptors include the 280-kilodalton labeled receptor form previously found to be the subunit of a disulfide-linked TGF beta receptor complex.	Disulfides	115-124	transforming growth factor beta 1	Homo sapiens	7-15
3021210-1	1986	Limited cleavages of human C1r by extrinsic proteases of various specificity (plasmin, elastase, chymotrypsin, thermolysin) yield dimeric associations of two globular domains, each comprised of the intact B chain disulfide linked to gamma, the C-terminal fragment of the A chain.	Disulfides	213-222	complement C1r	Homo sapiens	27-30
3781575-1	1986	Selective cleavage of the interchain disulfide bonds present in the two IgG1-kappa monoclonal cryoglobulins Ger and Muk results in a partial loss of cryoprecipitability of the parent proteins at 0 degree C. The progressive loss of cryoprecipitability which occurs as a function of increasing reductant concentration parallels the successive cleavage of interheavy-light and interheavy-heavy chain disulfides.	Disulfides	37-46	mitogen-activated protein kinase kinase kinase 12	Homo sapiens	116-119
3781575-1	1986	Selective cleavage of the interchain disulfide bonds present in the two IgG1-kappa monoclonal cryoglobulins Ger and Muk results in a partial loss of cryoprecipitability of the parent proteins at 0 degree C. The progressive loss of cryoprecipitability which occurs as a function of increasing reductant concentration parallels the successive cleavage of interheavy-light and interheavy-heavy chain disulfides.	Disulfides	397-407	mitogen-activated protein kinase kinase kinase 12	Homo sapiens	116-119
3461443-3	1986	The largest clone identified contains an open reading frame that encodes the amino-terminal heparin binding domain of TSP and part of the immediately adjacent collagen binding domain, a region of TSP that includes the site of disulfide crosslinking responsible for trimer formation.	Disulfides	226-235	thrombospondin 1	Homo sapiens	196-199
3461443-7	1986	In contrast, 80 residues beyond the start of the collagen binding domain, a cluster of 10 cysteine residues occurs within 40 amino acids corresponding to the point of interchain disulfide crosslinking in the TSP trimer.	Disulfides	178-187	thrombospondin 1	Homo sapiens	208-211
2877688-4	1986	Proteolytic digestion of [14C]putrescine-labeled TSP with trypsin or thrombin yielded a labeled disulfide-bonded core of 90 or 120-130 kilodalton (kDa) subunits, labeled fragments of less than 10 kDa, and an unlabeled 30-kDa heparin-binding fragment, indicating the presence of multiple factor XIIIa reactive glutaminyl residues located in several domains of the molecule.	Disulfides	96-105	thrombospondin 1	Homo sapiens	49-52
2877688-4	1986	Proteolytic digestion of [14C]putrescine-labeled TSP with trypsin or thrombin yielded a labeled disulfide-bonded core of 90 or 120-130 kilodalton (kDa) subunits, labeled fragments of less than 10 kDa, and an unlabeled 30-kDa heparin-binding fragment, indicating the presence of multiple factor XIIIa reactive glutaminyl residues located in several domains of the molecule.	Disulfides	96-105	coagulation factor II, thrombin	Homo sapiens	69-77
2877688-6	1986	The disulfide-bonded core of TSP formed upon thrombin digestion copolymerized with fibrin as efficiently as intact TSP.	Disulfides	4-13	thrombospondin 1	Homo sapiens	29-32
2877688-6	1986	The disulfide-bonded core of TSP formed upon thrombin digestion copolymerized with fibrin as efficiently as intact TSP.	Disulfides	4-13	coagulation factor II, thrombin	Homo sapiens	45-53
3016176-0	1986	Disulfide bond formation between nerve growth factor and the nerve growth factor receptor from embryonic sensory neurons.	Disulfides	0-9	nerve growth factor	Gallus gallus	33-52
3016176-2	1986	This complex is between the nerve growth factor and the high-affinity (type I) receptor and occurs through the formation of a disulfide bond.	Disulfides	126-135	nerve growth factor	Gallus gallus	28-47
3019388-0	1986	Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor.	Disulfides	29-39	insulin	Homo sapiens	43-50
3019388-0	1986	Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor.	Disulfides	29-39	insulin	Homo sapiens	70-77
3019388-0	1986	Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor.	Disulfides	29-39	insulin	Homo sapiens	70-77
2874135-3	1986	Type I TGF beta receptors include the 280-kilodalton labeled receptor form previously found to be the subunit of a disulfide-linked TGF beta receptor complex.	Disulfides	115-124	transforming growth factor beta 1	Homo sapiens	132-140
3739028-0	1986	[Mechanism of functioning of specific sites of interdomain D-E binding of fibrin molecules: interaction of fibrinogen with the N-terminal disulfide node of fibrin].	Disulfides	138-147	fibrinogen beta chain	Homo sapiens	107-117
3722204-0	1986	Disulfide-bonded polymerization of plasma fibronectin in the presence of metal ions.	Disulfides	0-9	fibronectin 1	Homo sapiens	42-53
3722204-1	1986	Incubation of human plasma fibronectin in the presence of low concentrations of FeCl3 or CuSO4 led to the formation of disulfide-bonded multimers as revealed by analysis in sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing or reducing conditions.	Disulfides	119-128	fibronectin 1	Homo sapiens	27-38
3722204-5	1986	When incubated in the presence of FeCl3, the Mr 30,000 NH2-terminal, Mr 40,000 gelatin-binding, and the Mr 120,000-140,000 COOH-terminal fragments of fibronectin formed disulfide-bonded polymers, whereas only the Mr 140,000 fragment was polymerized in the presence of CuSO4.	Disulfides	169-178	fibronectin 1	Homo sapiens	150-161
3722204-6	1986	Disulfide-bonded polymers were also formed in the presence of FeCl3 but not CuSO4 when the free sulfhydryl groups of fibronectin were blocked by N-ethylmaleimide.	Disulfides	0-9	fibronectin 1	Homo sapiens	117-128
3722204-7	1986	The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules.	Disulfides	51-60	fibronectin 1	Homo sapiens	86-97
3722204-7	1986	The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules.	Disulfides	51-60	fibronectin 1	Homo sapiens	270-281
3722204-7	1986	The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules.	Disulfides	210-220	fibronectin 1	Homo sapiens	86-97
3722204-7	1986	The results suggest that in the presence of CuSO4, disulfide-bonded polymerization of fibronectin may involve predominantly the free sulfhydryl groups, whereas in the presence of FeCl3, also the intramolecular disulfides may exchange to form disulfides between separate fibronectin molecules.	Disulfides	242-252	fibronectin 1	Homo sapiens	86-97
3722204-8	1986	Thus, under different conditions, different parts of fibronectin may be susceptible to disulfide-bonded polymerization.	Disulfides	87-96	fibronectin 1	Homo sapiens	53-64
3704648-1	1986	Arginine vasopressin consists of a 20-membered, disulfide-linked macrocyclic ring system called pressinoic acid to which is attached a COOH-terminal tripeptide.	Disulfides	48-57	arginine vasopressin	Homo sapiens	9-20
3759334-4	1986	Refolding under reducing conditions almost completely inhibited the regeneration of hydrophobic binding regions, suggesting that the formation of disulfide bonds plays an important role in the refolding of serum albumin.	Disulfides	146-155	albumin	Homo sapiens	206-219
3015199-2	1986	vWF is composed of a number of glycoprotein subunits that are linked together by disulfide bonds to form a series of multimers.	Disulfides	81-90	von Willebrand factor	Homo sapiens	0-3
3748012-6	1986	In contrast, the anti-pre-S(2)/GP33-GP36 antibodies and the anti-pre-S(1)/P39-GP42 antibodies can be easily detected in WIBA, providing these antibodies recognize the disulfide-bond independent pre-S determinants on the denatured env proteins.	Disulfides	167-176	cyclin dependent kinase 5 regulatory subunit 2	Homo sapiens	74-77
3701066-2	1986	These alpha-chain fragments are linked to the parent C4 molecule through disulfide bonds.	Disulfides	73-82	Fc gamma receptor and transporter	Homo sapiens	6-17
3701066-7	1986	Based on the identification of fragments liberated, the kinetics of their appearance, their sulfhydryl content, and the reported primary structure of human C4, a model of the interchain disulfide bonds is proposed in which the amino terminal portion of the alpha-chain is disulfide-linked to both the beta- and gamma-chains, whereas the carboxyl terminal portion of the alpha-chain is disulfide-linked to only the gamma-chain.	Disulfides	186-195	Fc gamma receptor and transporter	Homo sapiens	257-268
3701066-7	1986	Based on the identification of fragments liberated, the kinetics of their appearance, their sulfhydryl content, and the reported primary structure of human C4, a model of the interchain disulfide bonds is proposed in which the amino terminal portion of the alpha-chain is disulfide-linked to both the beta- and gamma-chains, whereas the carboxyl terminal portion of the alpha-chain is disulfide-linked to only the gamma-chain.	Disulfides	186-195	Fc gamma receptor and transporter	Homo sapiens	370-381
3701066-7	1986	Based on the identification of fragments liberated, the kinetics of their appearance, their sulfhydryl content, and the reported primary structure of human C4, a model of the interchain disulfide bonds is proposed in which the amino terminal portion of the alpha-chain is disulfide-linked to both the beta- and gamma-chains, whereas the carboxyl terminal portion of the alpha-chain is disulfide-linked to only the gamma-chain.	Disulfides	272-281	Fc gamma receptor and transporter	Homo sapiens	257-268
3701066-7	1986	Based on the identification of fragments liberated, the kinetics of their appearance, their sulfhydryl content, and the reported primary structure of human C4, a model of the interchain disulfide bonds is proposed in which the amino terminal portion of the alpha-chain is disulfide-linked to both the beta- and gamma-chains, whereas the carboxyl terminal portion of the alpha-chain is disulfide-linked to only the gamma-chain.	Disulfides	272-281	Fc gamma receptor and transporter	Homo sapiens	257-268
3487260-0	1986	Disulfide scrambling of interleukin-2: HPLC resolution of the three possible isomers.	Disulfides	0-9	interleukin 2	Homo sapiens	24-37
3487260-1	1986	Native interleukin-2 (IL-2) contains three cysteines; two exist in a disulfide bridge (Cys-58 and Cys-105) and the third Cys-125 is a free sulfhydryl.	Disulfides	69-78	interleukin 2	Homo sapiens	7-20
3487260-1	1986	Native interleukin-2 (IL-2) contains three cysteines; two exist in a disulfide bridge (Cys-58 and Cys-105) and the third Cys-125 is a free sulfhydryl.	Disulfides	69-78	interleukin 2	Homo sapiens	22-26
3698895-1	1986	We investigated the possibility that thiol-disulfide interchange mechanisms are involved in depletion-transformation (loss of tissue PRL detectability) and release of PRL from adenohypophyses (AP) of lactating rats.	Disulfides	43-52	prolactin	Rattus norvegicus	133-136
3698895-1	1986	We investigated the possibility that thiol-disulfide interchange mechanisms are involved in depletion-transformation (loss of tissue PRL detectability) and release of PRL from adenohypophyses (AP) of lactating rats.	Disulfides	43-52	prolactin	Rattus norvegicus	167-170
3698895-12	1986	Thus, thiols and aminothiols may preferentially lead to depletion-transformation of PRL, whereas disulfides may inhibit depletion and facilitate PRL release.	Disulfides	97-107	prolactin	Rattus norvegicus	145-148
3698895-13	1986	Although in some experiments increased depletion was dissociated from increased release, nonetheless the data support the concept that shifts in PRL detectability during depletion-transformation, repletion, and release involve thiol-disulfide interchange mechanisms.	Disulfides	233-242	prolactin	Rattus norvegicus	145-148
3698896-2	1986	The present studies were designed to determine whether thiol-disulfide interchange mechanisms may be involved in PRL transformation and release by the pituitary of the lactating rat.	Disulfides	61-70	prolactin	Rattus norvegicus	113-116
3007145-12	1986	The sequence data and homology to two-chain serine proteases indicate a single interchain disulfide bond in C1s.	Disulfides	90-99	complement C1s	Homo sapiens	108-111
3008761-0	1986	Effect of disulfide-bond reducing agents on the specific binding of growth hormone to microsomal membrane preparations from rabbit liver.	Disulfides	10-19	somatotropin	Oryctolagus cuniculus	68-82
3008761-1	1986	The effect of the disulfide-bond reducing agents, mercaptoethanol (ME) and dithiothreitol (DTT), on the specific binding of 125I-labeled human growth hormone (hGH) to microsomal membrane preparations from rabbit liver was investigated.	Disulfides	18-27	growth hormone 1	Homo sapiens	143-157
3081501-1	1986	Two-chain tissue-type plasminogen activator (t-PA), which consists of a heavy chain (Mr congruent to 38,000) and a light chain (Mr congruent to 31,000) connected by a disulfide bridge, was reduced with 2-mercaptoethanol and then air-reoxidized at a low protein concentration and carboxamidomethylated.	Disulfides	167-176	plasminogen activator, tissue type	Homo sapiens	10-43
3005300-7	1986	These findings indicate that intact class I disulfides are required for insulin binding but are not necessary for maintenance of the preactivated kinase.	Disulfides	44-54	insulin	Homo sapiens	72-79
3005300-9	1986	Thus disulfide bonds appear to have multiple roles in the function of the insulin receptor/kinase.	Disulfides	5-14	insulin	Homo sapiens	74-81
3753883-0	1986	Interaction of pantetheinase with sulfhydryl reagents and disulfides.	Disulfides	58-68	vanin 1	Homo sapiens	15-28
3081501-1	1986	Two-chain tissue-type plasminogen activator (t-PA), which consists of a heavy chain (Mr congruent to 38,000) and a light chain (Mr congruent to 31,000) connected by a disulfide bridge, was reduced with 2-mercaptoethanol and then air-reoxidized at a low protein concentration and carboxamidomethylated.	Disulfides	167-176	plasminogen activator, tissue type	Homo sapiens	45-49
3509954-0	1986	[Effect of peptides--structural analogs of NH2-terminal sites of fibrin alpha- and beta-chains--on specific binding of the NH2-terminal disulfide bond of fibrin with fibrinogen].	Disulfides	136-145	fibrinogen beta chain	Homo sapiens	166-176
3519485-0	1986	Reinvestigation of the disulfide bridge arrangement in human pro-opiomelanocortin N-terminal segment (hNT 1-76).	Disulfides	23-32	proopiomelanocortin	Homo sapiens	61-81
2419904-8	1986	Conservation of disulfide bridges and of amino acids thought to compose the iron binding pockets suggests that p97 is also related to transferrin in tertiary structure and function.	Disulfides	16-25	transferrin	Homo sapiens	134-145
2416632-5	1985	It possess three disulfide bonds and 2 tryptophan residues which is also characteristic of many species of PRL.	Disulfides	17-26	prolactin	Homo sapiens	107-110
2418018-10	1986	A6.1 reacts with the 70-kDa fragment generated by chymotrypsin in EDTA which contains the interchain disulfide bonds of TSP and the binding site(s) for type V collagen (Mumby, S. M., Raugi, G. J., and Bornstein, P. (1984) J.	Disulfides	101-110	thrombospondin 1	Homo sapiens	120-123
3484479-1	1986	Human interleukin-2 (IL-2) has 3 cysteine residues; cysteines 58 and 105 form an intramolecular disulfide bridge, whereas cysteine 125 has a free sulfhydryl group.	Disulfides	96-105	interleukin 2	Homo sapiens	6-19
3484479-1	1986	Human interleukin-2 (IL-2) has 3 cysteine residues; cysteines 58 and 105 form an intramolecular disulfide bridge, whereas cysteine 125 has a free sulfhydryl group.	Disulfides	96-105	interleukin 2	Homo sapiens	21-25
3492399-3	1986	Reduction-carboxymethylation and reduction-mercuration resulted in complete loss of Meg-CSF and Epo activities, suggesting that one of the essential chemical groups of Meg-CSF and Epo is a disulfide bond.	Disulfides	189-198	thrombopoietin	Homo sapiens	84-91
3492399-3	1986	Reduction-carboxymethylation and reduction-mercuration resulted in complete loss of Meg-CSF and Epo activities, suggesting that one of the essential chemical groups of Meg-CSF and Epo is a disulfide bond.	Disulfides	189-198	erythropoietin	Homo sapiens	96-99
3492399-3	1986	Reduction-carboxymethylation and reduction-mercuration resulted in complete loss of Meg-CSF and Epo activities, suggesting that one of the essential chemical groups of Meg-CSF and Epo is a disulfide bond.	Disulfides	189-198	erythropoietin	Homo sapiens	180-183
3492399-4	1986	Reduction of disulfide bonds at neutral pH revealed that Meg-CSF is less susceptible to reduction than Epo.	Disulfides	13-22	thrombopoietin	Homo sapiens	57-64
3492399-4	1986	Reduction of disulfide bonds at neutral pH revealed that Meg-CSF is less susceptible to reduction than Epo.	Disulfides	13-22	erythropoietin	Homo sapiens	103-106
3837613-6	1985	The enthalpy of activation values of 8.0 kcal.mol-1 an 17.4 kcal.mol-1 obtained, from the Arrhenius plot, for the "fast" and "slow" rate disulfide reduction, respectively, are indicative that a strong conformational strain of S--S bonds in the closed ring structure is maintained.	Disulfides	137-146	thiamine thiazole synthase	Saccharomyces cerevisiae S288C	46-51
3837613-6	1985	The enthalpy of activation values of 8.0 kcal.mol-1 an 17.4 kcal.mol-1 obtained, from the Arrhenius plot, for the "fast" and "slow" rate disulfide reduction, respectively, are indicative that a strong conformational strain of S--S bonds in the closed ring structure is maintained.	Disulfides	137-146	thiamine thiazole synthase	Saccharomyces cerevisiae S288C	65-70
3510133-2	1986	In contrast to a recent report, we found the erythrocyte insulin receptor to be similar in structure to that in classic target tissues for insulin, consisting of at least three species of molecular weight approximately 295,000, 265,000, and 245,000, containing disulfide-linked subunits of molecular weight approximately 130,000 and 95,000.	Disulfides	261-270	insulin	Homo sapiens	57-64
2944811-4	1986	They are structurally homologous to insulin receptors, containing disulfide-linked a-subunits that bind the peptides and beta-subunits that have intrinsic tyrosine-specific kinase activity.	Disulfides	66-75	insulin	Homo sapiens	36-43
2415977-6	1985	Of particular interest is a conserved pattern of disulfide bridges that form the triple-domain structures in albumin, alpha-fetoprotein, and Gc.	Disulfides	49-58	alpha fetoprotein	Homo sapiens	118-135
3877057-8	1985	Rapidity of disulfide bond formation in rough microsomes was evident from the presence of only 1.3 cysteine thiols/molecule of rough microsomal transferrin (total of 19 cystines) and the absence of mixed disulfides.	Disulfides	12-21	transferrin	Rattus norvegicus	144-155
2417623-11	1985	Cathepsin D digestion produced an 83K heparin-binding, monoclonal antibody reactive fragment that contains the interchain disulfide bond(s) linking the two fibronectin chains at their C-termini.	Disulfides	122-131	fibronectin 1	Homo sapiens	156-167
4063070-0	1985	Different susceptibility of inter- and intra-chain disulfide bonds to reductive cleavage in native fibronectin and effect of their cleavage on conformation.	Disulfides	51-60	fibronectin 1	Homo sapiens	99-110
2999280-9	1985	These studies suggest that Lp(a) is, in essence, an LDL-particle to which the protein (a) is attached through disulfide bonds to apoB.	Disulfides	110-119	apolipoprotein B	Homo sapiens	129-133
3002432-0	1985	Fat cell beta 1-adrenergic receptor: structural evidence for existence of disulfide bridges essential for ligand binding.	Disulfides	74-83	adrenoceptor beta 1	Rattus norvegicus	9-35
2413033-7	1985	Formation of the disulfide-linked complexes requires 125I-FSH, specifically bound to the hormone receptor and cross-linking, and can be prevented with an excess of native FSH but not human choriogonadotropin.	Disulfides	17-26	nuclear receptor subfamily 4 group A member 1	Homo sapiens	89-105
4063070-1	1985	The two thread-like subunits (Mr approximately equal to 250 000) of the multidomain protein fibronectin are connected by a pair of inter-chain disulfide bridges in their C-terminal regions.	Disulfides	143-152	fibronectin 1	Homo sapiens	92-103
4063070-4	1985	The susceptibility of inter-chain disulfide bonds to 10mM 1,4-dithiothreitol at pH 7.8 as quantitated by the rate of reductive cleavage of fibronectin into its subunits was found to be only 8-fold larger than that of the intra-chain bonds.	Disulfides	34-43	fibronectin 1	Homo sapiens	139-150
4063070-6	1985	The rate of inter-chain disulfide cleavage was found to be identical for fibronectin and a 140-kDa fragment comprising the C-terminal portions of the two subunits.	Disulfides	24-33	fibronectin 1	Homo sapiens	73-84
4063070-8	1985	Changes of circular dichroism and thermal transition profiles for fibronectin and its C-terminal 140-kDa fragment indicated that already partial reduction of the intra-chain disulfide bonds alters the conformations of type I and II domains without affecting the type III domains.	Disulfides	174-183	fibronectin 1	Homo sapiens	66-77
3863100-11	1985	The NH2-terminal one-third of PSAP-32 probably contains the cysteine involved in interchain disulfide bonds.	Disulfides	92-101	prosaposin	Canis lupus familiaris	30-34
2932468-2	1985	vWf multimers, which appear as flexible strands varying in length up to 2 micron, consist of dimeric units (protomers) polymerized linearly in an end-to-end fashion through disulfide bonds.	Disulfides	173-182	von Willebrand factor	Homo sapiens	0-3
2932468-7	1985	Two subunits are disulfide-linked, probably near their carboxyl termini, to form the protomer; disulfide bonds in the amino-terminal globular ends link promoters to form vWf multimers.	Disulfides	95-104	von Willebrand factor	Homo sapiens	170-173
3840195-10	1985	The predicted amino acid sequence of TL products indicates that TL and H-2 are similar in domain structure and disulfide bonds, but differ in glycosylation sites and in cytoplasmic domain sequences.	Disulfides	111-120	histocompatibility-2, MHC	Mus musculus	71-74
3897219-5	1985	The mass spectra of the digests of the two interleukin-2 preparations and synthetic peptides with sequences from 117 to 128 and 121 to 128 predicted from the nucleotide sequence of cDNA for a human interleukin-2 indicated that Cys residues at positions 58 and 105 are linked by a disulfide bond and that the Cys residue at position 125 is free.	Disulfides	280-289	interleukin 2	Homo sapiens	198-211
3161885-7	1985	Platelet GP IIb and GP IIIa and the related membrane proteins on both HUVE and BAE cells showed similar changes in electrophoretic mobility upon disulfide reduction.	Disulfides	145-154	integrin subunit beta 3	Homo sapiens	20-27
4074791-0	1985	[Effect of partial reduction of disulfide bonds on the enzymatic activity of thrombin].	Disulfides	32-41	coagulation factor II, thrombin	Homo sapiens	77-85
3926767-5	1985	Binding of 125I-TSP was inhibited by unlabeled TSP, by low pH, and by reduction of intersubunit disulfide bonds with dithiothreitol.	Disulfides	96-105	thrombospondin 1	Homo sapiens	16-19
4074791-1	1985	It was demonstrated that partial reduction of disulfide bonds in thrombin by dithiothreitol in the absence of denaturating agents leads to a decrease of enzymatic activity with respect to fibrinogen coagulation and tosylarginine methyl ester hydrolysis.	Disulfides	46-55	coagulation factor II, thrombin	Homo sapiens	65-73
4008606-4	1985	With reduction of disulfide bonds, there was a shift of the peak I PRL to smaller mol wt peptides.	Disulfides	18-27	prolactin	Homo sapiens	67-70
3876847-2	1985	At concentrations of vWF found in plasma (approximately 16 micrograms/mL), disulfide bond reduction with 50 mM 2-mercaptoethanol (2-ME) markedly reduced both vWF activity, as measured by ristocetin-dependent platelet agglutination, and average polymer size (Rh, the mean hydrodynamic radius) in solution, as determined by quasi-elastic light scattering (QLS) and by gel filtration chromatography.	Disulfides	75-84	von Willebrand factor	Homo sapiens	21-24
3876847-2	1985	At concentrations of vWF found in plasma (approximately 16 micrograms/mL), disulfide bond reduction with 50 mM 2-mercaptoethanol (2-ME) markedly reduced both vWF activity, as measured by ristocetin-dependent platelet agglutination, and average polymer size (Rh, the mean hydrodynamic radius) in solution, as determined by quasi-elastic light scattering (QLS) and by gel filtration chromatography.	Disulfides	75-84	von Willebrand factor	Homo sapiens	158-161
3925269-5	1985	These results suggest that HMW-angiotensinogen is probably a complex of LMW-angiotensinogen and other protein(s) which might be bound by disulfide bond.	Disulfides	137-146	angiotensinogen	Homo sapiens	31-46
3876847-3	1985	With increasing vWF concentration, activity and Rh increased despite reduction of interprotomer disulfide bonds.	Disulfides	96-105	von Willebrand factor	Homo sapiens	16-19
3925269-5	1985	These results suggest that HMW-angiotensinogen is probably a complex of LMW-angiotensinogen and other protein(s) which might be bound by disulfide bond.	Disulfides	137-146	angiotensinogen	Homo sapiens	76-91
3876847-7	1985	These data show that disulfide bonds are necessary to maintain vWF polymer size and activity at plasma concentrations but that noncovalent forces of association can maintain vWF polymer size and activity at higher concentrations.	Disulfides	21-30	von Willebrand factor	Homo sapiens	63-66
3896577-6	1985	Fragmentation occurs by proteolysis of the albumin molecule both at sites within and outside disulfide loops.	Disulfides	93-102	albumin	Homo sapiens	43-50
18640546-4	1985	The apparent molecular weights of P81, P53, and P49 changed significantly according to the composition of the lysis buffer used, suggesting that the differences in their molecular weights were due to conformational changes produced by reduction of their intramolecular disulfide bonds.	Disulfides	269-278	DNA primase subunit 1	Homo sapiens	48-51
3896577-7	1985	The predominant cleavage site appears to be approximately two-fifths of the distance from one end of the albumin molecule to produce disulfide-linked fragments of about 45 000 and 30 000 molecular weight.	Disulfides	133-142	albumin	Homo sapiens	105-112
3896810-8	1985	The distribution of thioredoxin and thioredoxin reductase is compatible with function in thiol-disulfide interchange reaction related to protein synthesis, intracellular transport and different forms of secretion.	Disulfides	95-104	thioredoxin 1	Rattus norvegicus	20-31
3936216-3	1985	Small molecular forms of FVIII/vWF from normal and variant type II plasma, and those derived by disulfide reduction of high-molecular weight FVIII/vWF, showed remarkably decreased reactivity in ristocetin-, botrocetin- and latex-assay.	Disulfides	96-105	von Willebrand factor	Homo sapiens	147-150
3896810-8	1985	The distribution of thioredoxin and thioredoxin reductase is compatible with function in thiol-disulfide interchange reaction related to protein synthesis, intracellular transport and different forms of secretion.	Disulfides	95-104	peroxiredoxin 5	Rattus norvegicus	36-57
4027236-6	1985	Reduction of the disulfide bonds within the TSP molecule inhibits its platelet agglutinating activity.	Disulfides	17-26	thrombospondin 1	Homo sapiens	44-47
3160727-10	1985	Analysis of plasmin-digested vWF allowed deduction of a model for the native vWF structure, including the approximate location of the interprotomer disulfide bond(s).	Disulfides	148-157	von Willebrand factor	Homo sapiens	77-80
3859688-1	1985	The ribosome-inactivating protein saporin, from Saponaria officinalis, was coupled by a disulfide bond to monoclonal anti-Thy 1.1 antibody (OX7) and to its F(ab")2 fragment.	Disulfides	88-97	thymus cell antigen 1, theta	Mus musculus	122-129
2989825-2	1985	At the monomeric level, both C1r and C1s comprised two globular domains, a smaller interaction domain (corresponding to the NH2-terminal half of the A chain, alpha, and responsible for calcium binding and C1r-C1s interaction) and a larger catalytic domain (corresponding to the COOH-terminal part of the A chain, gamma, disulfide-linked to the B chain and bearing the serine protease active site).	Disulfides	320-329	complement C1r	Homo sapiens	29-32
2989825-2	1985	At the monomeric level, both C1r and C1s comprised two globular domains, a smaller interaction domain (corresponding to the NH2-terminal half of the A chain, alpha, and responsible for calcium binding and C1r-C1s interaction) and a larger catalytic domain (corresponding to the COOH-terminal part of the A chain, gamma, disulfide-linked to the B chain and bearing the serine protease active site).	Disulfides	320-329	complement C1s	Homo sapiens	37-40
2992579-3	1985	Formation of the disulfide radical in ribonuclease is slower than the reaction between protein and CO2-; formation of the flavin semiquinone in the riboflavin binding protein is slower than the protein-CO2- reaction.	Disulfides	17-26	riboflavin binding protein	Gallus gallus	148-174
2992579-4	1985	We conclude for both proteins that CO2- must reduce an as yet unidentified group or groups, which in turn reduce(s) the disulfide of RNase or the flavin of riboflavin binding protein.	Disulfides	120-129	riboflavin binding protein	Gallus gallus	156-182
2992579-6	1985	The CO2--initiated reductions of the disulfide in ribonuclease and the flavin in the riboflavin binding protein are mixed first- and second-order processes.	Disulfides	37-46	riboflavin binding protein	Gallus gallus	85-111
3973587-9	1985	Limited digestion of DS-AChE with proteinase K led to isolation of an enzyme that no longer bound detergents and lacked the intersubunit disulfide bridges.	Disulfides	137-146	acetylcholinesterase (Cartwright blood group)	Homo sapiens	24-28
2991034-4	1985	Studies covalently crosslinking 125I-CCK to its receptor have revealed a binding glycoprotein subunit of Mr = 76,000 attached by a disulfide bridge to a Mr = 40,000 nonbinding subunit.	Disulfides	131-140	cholecystokinin	Homo sapiens	37-40
3986759-1	1985	Monoclonal antibodies against human T-cell antigen 3A1, human transferrin receptor, and mouse Thy 1.1 antigen were linked to pokeweed antiviral protein (PAP) by a disulfide bond.	Disulfides	163-172	thymus cell antigen 1, theta	Mus musculus	94-101
3972830-1	1985	The soluble form of dopamine beta-hydroxylase from bovine adrenal medulla has previously been shown to exist as a tetrameric species of Mr = 290,000 composed of two disulfide-linked dimers.	Disulfides	165-174	dopamine beta-hydroxylase	Bos taurus	20-45
2860016-7	1985	Most likely, CSH acts by interacting with the disulfide bonds of PRL, thus rendering the molecule both immunologically and biologically inactive.	Disulfides	46-55	prolactin	Rattus norvegicus	65-68
3994396-0	1985	Preparation of functionally intact monomers by limited disulfide reduction of human plasma fibronectin dimers.	Disulfides	55-64	fibronectin 1	Homo sapiens	91-102
3994396-1	1985	Most (90 to 95%) human plasma fibronectin (PFn) molecules exist as 450-kDa disulfide-rich dimers comprised of two major types of subunits (A, 220 kDa; B, 215 kDa) that are joined near the COOH terminus by two disulfide bonds.	Disulfides	75-84	fibronectin 1	Homo sapiens	30-41
3994396-1	1985	Most (90 to 95%) human plasma fibronectin (PFn) molecules exist as 450-kDa disulfide-rich dimers comprised of two major types of subunits (A, 220 kDa; B, 215 kDa) that are joined near the COOH terminus by two disulfide bonds.	Disulfides	209-218	fibronectin 1	Homo sapiens	30-41
2984291-7	1985	Comparison of the sequence with that of the human transferrin receptor shows a high degree of conservation of the sequences surrounding and penetrating the membrane, including cysteine residues that may be involved in interchain disulfide bonding and/or covalent attachment of lipid.	Disulfides	229-238	transferrin	Homo sapiens	50-61
3884381-1	1985	The insulin disulfide reducing thioredoxin system from E. coli was used to investigate a possible mechanism of degradation for the two somatomedins, insulin-like growth factor I and II (IGF-I and -II).	Disulfides	12-21	insulin	Homo sapiens	4-11
3884381-1	1985	The insulin disulfide reducing thioredoxin system from E. coli was used to investigate a possible mechanism of degradation for the two somatomedins, insulin-like growth factor I and II (IGF-I and -II).	Disulfides	12-21	insulin	Homo sapiens	149-156
3884381-1	1985	The insulin disulfide reducing thioredoxin system from E. coli was used to investigate a possible mechanism of degradation for the two somatomedins, insulin-like growth factor I and II (IGF-I and -II).	Disulfides	12-21	insulin like growth factor 1	Homo sapiens	186-199
3884381-3	1985	The results show that both IGF-I and -II were as sensitive to disulfide reduction as insulin.	Disulfides	62-71	insulin like growth factor 1	Homo sapiens	27-40
3979399-6	1985	GPIIIa was also cleaved within a loop structure formed by disulfide bond(s).	Disulfides	58-67	integrin subunit beta 3	Homo sapiens	0-6
3965488-1	1985	A form of PRL that is cleaved in its large disulfide loop has been reported in rat and mouse pituitary glands, but it is not known whether it exists in the human pituitary gland and whether it circulates in blood.	Disulfides	43-52	prolactin	Rattus norvegicus	10-13
2984068-1	1985	The disulfide bonds of two lactogenic hormones, ovine prolactin (oPRL) and human growth hormone (hGH), were reduced with dithiothreitol under denaturing conditions and alkylated with iodoacetic acid.	Disulfides	4-13	prolactin	Homo sapiens	54-63
2984068-1	1985	The disulfide bonds of two lactogenic hormones, ovine prolactin (oPRL) and human growth hormone (hGH), were reduced with dithiothreitol under denaturing conditions and alkylated with iodoacetic acid.	Disulfides	4-13	growth hormone 1	Homo sapiens	81-95
6437445-11	1984	It is concluded that glycoprotein G (thrombin-sensitive protein, thrombospondin) and thrombin form a dissociable complex that leads to a covalent complex by thiol-disulfide exchange of a thiol group on glycoprotein G and a disulfide on thrombin.	Disulfides	163-172	coagulation factor II, thrombin	Homo sapiens	37-45
3918033-3	1985	Like C3-1, C3-2 consists of two disulfide-linked polypeptide chains (128,000 alpha and 72,000 beta) and retains the unique thiol ester site in the alpha-chain.	Disulfides	32-41	c3-1	Oncorhynchus mykiss	5-15
2995938-5	1985	Thiol reagents reduced receptor binding activity, suggesting that an intrachain disulfide bond might be an important constituent of the VIP binding site.	Disulfides	80-89	vasoactive intestinal peptide	Rattus norvegicus	136-139
3976012-0	1985	[Complexes of the N-terminal disulfide branch point of fibrin with fibrinogen].	Disulfides	29-38	fibrinogen beta chain	Homo sapiens	67-77
6510521-1	1984	Cyanogen bromide digestion of hemopexin at its 6 methionine residues results in 7 fragments (CB1-CB7) partially connected by disulfide bridges.	Disulfides	125-134	cannabinoid receptor 1	Homo sapiens	93-100
6525362-6	1984	A disulfide dimeric form of prolactin with Mr of about 50 000 was isolated and characterized.	Disulfides	2-11	prolactin	Homo sapiens	28-37
6091760-6	1984	The disulfide-linked conjugate inhibited protein synthesis in the human breast tumor cell line MCF-7, whereas anti-transferrin receptor, pokeweed antiviral protein II, or an immunotoxin composed of an irrelevant antiserum and pokeweed antiviral protein II, were nontoxic.	Disulfides	4-13	annexin A4	Homo sapiens	245-255
6437445-0	1984	Formation of a stable complex of thrombin and the secreted platelet protein glycoprotein G (thrombin-sensitive protein, thrombospondin) by thiol-disulfide exchange.	Disulfides	145-154	coagulation factor II, thrombin	Homo sapiens	33-41
6437445-0	1984	Formation of a stable complex of thrombin and the secreted platelet protein glycoprotein G (thrombin-sensitive protein, thrombospondin) by thiol-disulfide exchange.	Disulfides	145-154	coagulation factor II, thrombin	Homo sapiens	92-100
3965054-1	1985	Thrombospondin, one of the major glycoproteins released from alpha-granules of thrombin-stimulated platelets, is a disulfide-linked trimer of 160,000-dalton subunits.	Disulfides	115-124	coagulation factor II	Mus musculus	79-87
2578194-8	1985	We suggest that (i) gC1 and gC2 arise by proteolytic cleavage from the same precursor molecule and stay joined via disulfide bridges and (ii) gC0 is an uncleaved precursor.	Disulfides	115-124	solute carrier family 25 member 18	Homo sapiens	28-31
6437459-3	1984	Normal human fibrinogen, which consists of three pairs of disulfide-bonded peptide chains, (A alpha, B beta, gamma)2, is heterogeneous with respect to sialic acid content and also contains a small proportion of molecules with a variant gamma chain (designated gamma"), elongated by a peptide extension at the COOH-terminus of the normal gamma chain.	Disulfides	58-67	fibrinogen beta chain	Homo sapiens	13-23
6397077-0	1984	Cleaving of disulfide bridges and apparent molecular weight of human prolactin variants as revealed by immunoperoxidase electrophoresis.	Disulfides	12-21	prolactin	Homo sapiens	69-78
6480605-0	1984	Mechanism of formation of disulfide-bonded multimers of plasma fibronectin in cell layers of cultured human fibroblasts.	Disulfides	26-35	fibronectin 1	Homo sapiens	63-74
6480605-4	1984	Matrix-bound 125I-fCam-fibronectin, like matrix-bound 125I-fibronectin, was present as disulfide-bonded multimers as well as disulfide-bonded dimers.	Disulfides	87-96	fibronectin 1	Homo sapiens	23-34
6480605-4	1984	Matrix-bound 125I-fCam-fibronectin, like matrix-bound 125I-fibronectin, was present as disulfide-bonded multimers as well as disulfide-bonded dimers.	Disulfides	125-134	fibronectin 1	Homo sapiens	23-34
6480605-5	1984	These results indicate that the mechanism of formation of disulfide-bonded fibronectin multimers does not involve oxidation of free sulfhydryls.	Disulfides	58-67	fibronectin 1	Homo sapiens	75-86
6480605-8	1984	Thus, fibronectin multimer formation probably occurs by disulfide exchange in the amino-terminal portion of the molecule.	Disulfides	56-65	fibronectin 1	Homo sapiens	6-17
6437445-11	1984	It is concluded that glycoprotein G (thrombin-sensitive protein, thrombospondin) and thrombin form a dissociable complex that leads to a covalent complex by thiol-disulfide exchange of a thiol group on glycoprotein G and a disulfide on thrombin.	Disulfides	163-172	coagulation factor II, thrombin	Homo sapiens	85-93
6437445-11	1984	It is concluded that glycoprotein G (thrombin-sensitive protein, thrombospondin) and thrombin form a dissociable complex that leads to a covalent complex by thiol-disulfide exchange of a thiol group on glycoprotein G and a disulfide on thrombin.	Disulfides	163-172	coagulation factor II, thrombin	Homo sapiens	85-93
6437445-11	1984	It is concluded that glycoprotein G (thrombin-sensitive protein, thrombospondin) and thrombin form a dissociable complex that leads to a covalent complex by thiol-disulfide exchange of a thiol group on glycoprotein G and a disulfide on thrombin.	Disulfides	223-232	coagulation factor II, thrombin	Homo sapiens	37-45
6437445-11	1984	It is concluded that glycoprotein G (thrombin-sensitive protein, thrombospondin) and thrombin form a dissociable complex that leads to a covalent complex by thiol-disulfide exchange of a thiol group on glycoprotein G and a disulfide on thrombin.	Disulfides	223-232	coagulation factor II, thrombin	Homo sapiens	85-93
6437445-11	1984	It is concluded that glycoprotein G (thrombin-sensitive protein, thrombospondin) and thrombin form a dissociable complex that leads to a covalent complex by thiol-disulfide exchange of a thiol group on glycoprotein G and a disulfide on thrombin.	Disulfides	223-232	coagulation factor II, thrombin	Homo sapiens	85-93
6393990-1	1984	The reduction of insulin by tri-n-butylphosphine followed by air oxidation in dilute solution at pH 9.1 yields A- and B-chain disulfides.	Disulfides	126-136	insulin	Homo sapiens	17-24
6438823-2	1984	Limited reduction of disulfide bonds in this complex by NADPH, thioredoxin reductase and thioredoxin leads to partial disaggregation of the multimeric VIII:vWF with concomitant loss of its platelet agglutinating activity in the presence of ristocetin, and with dissociation of factor VIII:C from the complex.	Disulfides	21-30	von Willebrand factor	Homo sapiens	156-159
6393990-5	1984	The kinetics of reduction and reoxidation of insulin disulfide bonds are discussed.	Disulfides	53-62	insulin	Homo sapiens	45-52
6208037-2	1984	Thymus Ly-2/3 consists of similar amounts of two types of disulfide-linked heterodimer, alpha beta and alpha" beta (Mr alpha = 38000, Mr alpha" = 35000, Mr beta = 30000).	Disulfides	58-67	CD8b molecule	Homo sapiens	7-13
6236225-5	1984	In addition, there was heterogeneity in the size of apoprotein (a) (apo(a] which was found to be linked to apoprotein B (apo-B) through disulfide bonds.	Disulfides	136-145	apolipoprotein B	Homo sapiens	107-119
6236225-5	1984	In addition, there was heterogeneity in the size of apoprotein (a) (apo(a] which was found to be linked to apoprotein B (apo-B) through disulfide bonds.	Disulfides	136-145	apolipoprotein B	Homo sapiens	121-126
6479100-9	1984	These data suggest that the mechanism by which CySH causes PRL depletion is mediated by granule disulfides and the -SH of CySH.	Disulfides	96-106	prolactin	Bos taurus	59-62
6479100-10	1984	The regulation of thiol:disulfide equilibria appears to be an important determinant of the detectability of PRL storage forms and of their secretion.	Disulfides	24-33	prolactin	Bos taurus	108-111
6479101-4	1984	We suggest that cysteamine alters PRL structure in secretory granules, probably by interacting with the disulfide bonds of PRL, thereby altering bioactivity and immunoreactivity.	Disulfides	104-113	prolactin	Rattus norvegicus	34-37
6479101-4	1984	We suggest that cysteamine alters PRL structure in secretory granules, probably by interacting with the disulfide bonds of PRL, thereby altering bioactivity and immunoreactivity.	Disulfides	104-113	prolactin	Rattus norvegicus	123-126
6333684-4	1984	The entire primary sequence of interleukin 2, including the location of the intramolecular disulfide bridge, was determined by a combination of peptide mapping and protein sequencing.	Disulfides	91-100	interleukin 2	Homo sapiens	31-44
6427925-4	1984	Substitution of serine for cysteine residues at either position 58 or 105 of the IL-2 protein substantially reduced biological activity, indicating that the cysteines at these positions are necessary for maintenance of the biologically active conformation and may therefore be linked by a disulfide bridge.	Disulfides	289-298	interleukin 2	Homo sapiens	81-85
6503992-1	1984	Fibronectin is a recently characterized 4.4 X 10(5) dalton glycoprotein consisting of two probably identical 2.2 X 10(5) dalton subunits held together by disulfide linkages.	Disulfides	154-163	fibronectin 1	Homo sapiens	0-11
6088505-9	1984	Later other A alpha and gamma chains are added by ordered disulfide interaction, leading to the eventual formation of dimeric fibrinogen.	Disulfides	58-67	fibrinogen beta chain	Homo sapiens	126-136
6333249-7	1984	This study shows that (1) disulfide reduction and carboxamidation cause significant conformational changes in vWF, (2) vWF may contain discrete, ordered, conformational domains linked by regions of random polypeptide chain, and (3) specific tertiary structural domains within vWF are not affected by disulfide reduction and carboxamidation.	Disulfides	26-35	von Willebrand factor	Homo sapiens	110-113
6333249-7	1984	This study shows that (1) disulfide reduction and carboxamidation cause significant conformational changes in vWF, (2) vWF may contain discrete, ordered, conformational domains linked by regions of random polypeptide chain, and (3) specific tertiary structural domains within vWF are not affected by disulfide reduction and carboxamidation.	Disulfides	300-309	von Willebrand factor	Homo sapiens	110-113
6333249-7	1984	This study shows that (1) disulfide reduction and carboxamidation cause significant conformational changes in vWF, (2) vWF may contain discrete, ordered, conformational domains linked by regions of random polypeptide chain, and (3) specific tertiary structural domains within vWF are not affected by disulfide reduction and carboxamidation.	Disulfides	300-309	von Willebrand factor	Homo sapiens	119-122
6333249-7	1984	This study shows that (1) disulfide reduction and carboxamidation cause significant conformational changes in vWF, (2) vWF may contain discrete, ordered, conformational domains linked by regions of random polypeptide chain, and (3) specific tertiary structural domains within vWF are not affected by disulfide reduction and carboxamidation.	Disulfides	300-309	von Willebrand factor	Homo sapiens	119-122
6736123-4	1984	Analysis of the sequence of events in assembly of GP140 and fibronectin in the extracellular matrix detected the following: (a) fibronectin was first to appear in the extracellular matrix; (b) GP140 accumulated in the cytoplasm, then deposited in the extracellular matrix and co-aligned with the established fibronectin; and (c) maturation of the extracellular matrix proceeded by continued intermolecular disulfide bonding.	Disulfides	406-415	fibronectin 1	Homo sapiens	60-71
6736123-6	1984	Precipitation of the biotinylated matrix from extracts of the cultures using avidin indicated: (a) disulfide bonding of radioactive GP140 and fibronectin into the exogenous biotinylated matrix required cell contact with the matrix.	Disulfides	99-108	fibronectin 1	Homo sapiens	142-153
6508858-2	1984	With the aid of thiol-disulfide exchange chromatography and SDS polyacrylamide gel electrophoresis the F1 and F2 fragments of the modified cytochrome P-450 were isolated.	Disulfides	22-31	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	139-155
6086661-4	1984	Transferrin receptors from uninduced and differentiating cells were partially purified by affinity chromatography on transferrin-Sepharose and shown to be disulfide-bridged homodimers of a polypeptide with an apparent molecular weight of approximately 90,000.	Disulfides	155-164	transferrin	Homo sapiens	0-11
6429132-6	1984	After reduction, labeled PSF had a slightly higher Mr of 32,000, although reduction resulted in loss of 98% of PSF activity, thus suggesting that the integrity of internal disulfide bond(s) was required for activity.	Disulfides	172-181	interleukin 3	Mus musculus	25-28
6089874-3	1984	This behavior, unusual for disulfide-containing proteins, was studied by using a thiosulfonate derivative of subtype A of human alpha interferon (IFN-alpha A).	Disulfides	27-36	interferon alpha 1	Homo sapiens	128-155
6466597-5	1984	Equimolar mixtures of IFNs 24-81 and 111-166 formed a noncovalent complex that was resistant to the formation of the Cys29-Cys139 disulfide bond found in native interferon alpha 1.	Disulfides	130-139	interferon alpha 1	Homo sapiens	161-179
6209020-1	1984	Epidermal growth factor (EGF) was derivatized at the amino terminus with N-succinimidyl 3-(2-pyridyldithio)propionate and then cross-linked to the cysteinyl residues of alpha 2-macroglobulin (alpha 2M) via disulfide bonds.	Disulfides	206-215	alpha-2-macroglobulin	Mus musculus	169-190
6723574-1	1984	A form of rat PRL with a clip in its large disulfide loop, the so-called cleaved PRL, has been reported to have a greater mammogenic activity than the intact molecule.	Disulfides	43-52	prolactin	Rattus norvegicus	14-17
6723574-1	1984	A form of rat PRL with a clip in its large disulfide loop, the so-called cleaved PRL, has been reported to have a greater mammogenic activity than the intact molecule.	Disulfides	43-52	prolactin	Rattus norvegicus	81-84
6089874-4	1984	The disulfide-free thiosulfonate formed at 25 degrees C has essentially no antiviral activity, while maintaining a conformation related to that of native IFN-alpha A.	Disulfides	4-13	interferon alpha 1	Homo sapiens	154-163
6089874-7	1984	These results explain the difficulty in obtaining, under native conditions, a reduced species that regains activity upon oxidation; complete reduction of IFN-alpha A in 100 mM 2-mercaptoethanol requires 37 degrees C, a temperature that promotes conformational decay of the disulfide-free form.	Disulfides	273-282	interferon alpha 1	Homo sapiens	154-163
6732781-0	1984	Primary structure of human plasma fibronectin--characterization of the 6,000 dalton C-terminal fragment containing the interchain disulfide bridges.	Disulfides	130-139	fibronectin 1	Homo sapiens	34-45
6725253-4	1984	Rainbow trout C3-1 is a beta-globulin of Mr = 190,000 composed of two polypeptide chains (Mr = 128,000 alpha-chain and Mr = 74,000 beta-chain) linked by disulfide bonds.	Disulfides	153-162	c3-1	Oncorhynchus mykiss	14-18
6746411-6	1984	These results show that arginine esterase of dog seminal plasma is a serine protease composed of two different chains linked by disulfide bridges.	Disulfides	128-137	arginine esterase	Canis lupus familiaris	24-41
6429073-9	1984	The initial acid-catalyzed deamidation occurs in and around the 65-72 disulfide loop giving rise to at least three distinct monodeamidated derivatives of RNase A without an appreciable change in the catalytic activity and conformation of the ribonuclease molecule.	Disulfides	70-79	ribonuclease pancreatic	Bos taurus	154-161
6609141-8	1984	The radiation-induced broadening of the serum albumin peak is interpreted as being a result of intramolecular disulfide exchange.	Disulfides	110-119	albumin	Homo sapiens	40-53
6142765-0	1984	Prevention of growth of leukemia cells in mice by monoclonal antibodies directed against Thy 1.1 antigen disulfide linked to two ribosomal inhibitors:pokeweed antiviral protein or ricin A chain.	Disulfides	105-114	thymus cell antigen 1, theta	Mus musculus	89-96
6142765-2	1984	Immunotoxins were prepared by linking monoclonal anti-Thy 1.1 antibodies to PAP and ricin A chain through a disulfide bond.	Disulfides	108-117	thymus cell antigen 1, theta	Mus musculus	54-61
6584430-8	1984	The results show that purified cholesterol 7 alpha-hydroxylase can be regulated by a mechanism involving disulfide bonds in the cytochrome P-450 molecule.	Disulfides	105-114	cytochrome P450 family 7 subfamily A member 1	Rattus norvegicus	31-62
6584430-8	1984	The results show that purified cholesterol 7 alpha-hydroxylase can be regulated by a mechanism involving disulfide bonds in the cytochrome P-450 molecule.	Disulfides	105-114	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	128-144
6712666-4	1984	Examination by SDS-PAGE under both reducing and nonreducing conditions reveals that the fibrinogen-binding domain is derived from the region of the thrombospondin molecule containing the interchain disulfide bonds.	Disulfides	198-207	fibrinogen beta chain	Homo sapiens	88-98
6319379-1	1984	The toxic A chain of ricin was linked to human transferrin via a disulfide bond and the resulting conjugate was shown to bind to cell membrane transferrin receptors.	Disulfides	65-74	transferrin	Homo sapiens	47-58
6714942-4	1984	Further, by end-group determination and sequencing of the unreduced core of des-Arg omega-C5a the position of its three disulfide bridges has been determined, now allowing insight into the tertiary structure of des-Arg omega-C5a.	Disulfides	120-129	complement C5a receptor 1	Homo sapiens	90-93
6198530-4	1984	Several aspects of the disulfide interactions of the two gp70s were conserved; in both cases the carboxy-terminal fragments were disulfide bonded to p15(E), there were no disulfide bonds between amino- and carboxy-terminal fragments, and the amino-terminal fragments exhibited a significant increase in mobility upon analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing conditions.	Disulfides	23-32	cyclin dependent kinase inhibitor 2B	Homo sapiens	149-152
6714942-0	1984	Amino-acid sequence and disulfide linkages of the anaphylatoxin, des-Arg omega-C5a, from porcine serum.	Disulfides	24-33	complement C5a receptor 1	Homo sapiens	79-82
6319379-1	1984	The toxic A chain of ricin was linked to human transferrin via a disulfide bond and the resulting conjugate was shown to bind to cell membrane transferrin receptors.	Disulfides	65-74	transferrin	Homo sapiens	143-154
6653778-2	1983	C4bp, a regulator of the classical pathway of complement system, is composed of 6-8 disulfide-linked subunit chains of 75 kDa.	Disulfides	84-93	complement component 4 binding protein alpha	Homo sapiens	0-4
6330376-6	1984	The covalent 125I-beta nerve growth factor-receptor complex is dissociated in 50 mM dithiothreitol indicating that disulfide linkages are involved.	Disulfides	115-124	nerve growth factor	Homo sapiens	18-42
6197991-8	1983	Mass map analysis of hAFP correlates with the subdomains organized by disulfide bridges.	Disulfides	70-79	alpha fetoprotein	Homo sapiens	21-25
6229271-1	1983	Plasma fibronectin is one of the largest plasma proteins (Mr approximately 440 000), comprising two approximately equal polypeptide chains which are held together by a disulfide linkage near the C-terminal end of the molecule.	Disulfides	168-177	fibronectin 1	Homo sapiens	7-18
6607731-3	1983	Matrix Gla protein is a 15,000 dalton protein whose amino acid composition includes a single disulfide bond.	Disulfides	93-102	matrix Gla protein	Bos taurus	0-18
6607069-7	1983	Analysis of the purified polypeptide by electrophoresis on sodium dodecyl sulfate-polyacrylamide gels indicates that TGF-beta is composed of two closely related polypeptide chains cross-linked by disulfide bonds.	Disulfides	196-205	transforming growth factor, beta 1	Rattus norvegicus	117-125
6653778-3	1983	Upon incubation with chymotrypsin, C4bp was rapidly cleaved into a nicked C4bp, composed of disulfide-linked 48 kDa and 27 kDa fragments.	Disulfides	92-101	complement component 4 binding protein alpha	Homo sapiens	35-39
6653778-3	1983	Upon incubation with chymotrypsin, C4bp was rapidly cleaved into a nicked C4bp, composed of disulfide-linked 48 kDa and 27 kDa fragments.	Disulfides	92-101	complement component 4 binding protein alpha	Homo sapiens	74-78
6417659-3	1983	In HUT-102B2 cells, the TCGF receptor is a Mr 50,000 glycoprotein with internal disulfide bond(s) and a pI of 5.5-6.0, and it represents approximately equal to 0.05% of total cellular de novo protein synthesis.	Disulfides	80-89	interleukin 2	Homo sapiens	24-28
6139811-4	1983	Over the next 12 hr, a slow intracellular process removes a dipeptide near the carboxyl terminus, converting the one-chain renin into two chains joined by a single disulfide bond.	Disulfides	164-173	renin	Homo sapiens	123-128
6194153-0	1983	Disulfide exchange between insulin and its receptor.	Disulfides	0-9	insulin	Homo sapiens	27-34
6194153-2	1983	A fraction of the insulin specifically bound to adipocytes undergoes a disulfide interchange with its receptor (Clark, S., and Harrison, L. C. (1982) J. Biol.	Disulfides	71-80	insulin	Homo sapiens	18-25
6194153-5	1983	In order to test the hypothesis that this covalent modification is a relevant step in insulin action, we have examined the relationship between disulfide binding of insulin and several insulin bioeffects, using sulfhydryl group blocking reagents as probes.	Disulfides	144-153	insulin	Homo sapiens	165-172
6194153-5	1983	In order to test the hypothesis that this covalent modification is a relevant step in insulin action, we have examined the relationship between disulfide binding of insulin and several insulin bioeffects, using sulfhydryl group blocking reagents as probes.	Disulfides	144-153	insulin	Homo sapiens	165-172
6351858-1	1983	Liver plasma membranes bind insulin in a complex fashion via three prominent disulfide-linked insulin receptor structures of 360K, 300K, and 260K molecular weight.	Disulfides	77-86	insulin	Homo sapiens	28-35
6658711-0	1983	Enzymic activity of thrombin with partially reduced disulfide bonds.	Disulfides	52-61	coagulation factor II, thrombin	Homo sapiens	20-28
6658711-3	1983	As a result of the reaction with dithiothreitol, two disulfide bonds are cleaved in thrombin molecule inducing a small decrease of beta-sheets in the secondary structure of thrombin.	Disulfides	53-62	coagulation factor II, thrombin	Homo sapiens	84-92
6658711-3	1983	As a result of the reaction with dithiothreitol, two disulfide bonds are cleaved in thrombin molecule inducing a small decrease of beta-sheets in the secondary structure of thrombin.	Disulfides	53-62	coagulation factor II, thrombin	Homo sapiens	173-181
6313762-1	1983	Insulin receptors and Type I insulinlike growth factor (IGF) receptors have a similar structure with a major binding subunit of Mr approximately 130,000 linked by disulfide bonds to other membrane proteins to form a Mr greater than 300,000 complex.	Disulfides	163-172	insulin	Homo sapiens	0-7
6684689-1	1983	Previous studies have shown that 6-thiopurine is metabolically activated by hepatic cytochrome P-450 to an intermediate capable of binding to proteins by a mixed disulfide linkage.	Disulfides	162-171	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	84-100
6615818-1	1983	Reduction of the chicken egg white riboflavin binding protein by the hydrated electron results in competitive formation of both a disulfide-electron adduct and an anionic flavin semiquinone bound to the protein.	Disulfides	130-139	riboflavin binding protein	Gallus gallus	35-61
6362479-6	1983	Electrophoresis on the mixed disulfide-polyacrylamide gel proved to be a rapid and sensitive technique to detect very small amounts of enzyme (approximately 0.02 fmol acetylcholinesterase) and should have wide application for detecting other enzymes that hydrolyze thiol substrates.	Disulfides	29-38	acetylcholinesterase (Cartwright blood group)	Homo sapiens	167-187
6874690-4	1983	The third proteoglycan, PG-Lt, differs from the other two in containing disulfide-bonded collagenous polypeptides (Noro, A., Kimata, K., Oike, Y., Shinomura, T., Maeda, N., Yano, S., Takahashi, N., and Suzuki, S. (1983) J. Biol.	Disulfides	72-81	versican	Gallus gallus	10-22
6351858-1	1983	Liver plasma membranes bind insulin in a complex fashion via three prominent disulfide-linked insulin receptor structures of 360K, 300K, and 260K molecular weight.	Disulfides	77-86	insulin	Homo sapiens	94-101
6874691-0	1983	Isolation and characterization of a third proteoglycan (PG-Lt) from chick embryo cartilage which contains disulfide-bonded collagenous polypeptide.	Disulfides	106-115	versican	Gallus gallus	42-54
6871108-7	1983	From our results, we conclude that: (1) at least two distinct disulfide (S-S) bonds are required for maintenance of the Kell blood group antigen system; (2) Jsa and Jsb antigens are distinctly different from other Kell system antigens based upon sensitivity to treatment with DTT; these antigens may be located on a different antigenic domain; and (3) the Yta antigen requires at least one disulfide bond for its maintenance of antigen integrity.	Disulfides	62-71	Kell metallo-endopeptidase (Kell blood group)	Homo sapiens	120-144
6553501-1	1983	Human high molecular weight kininogen (HMWK), a single-chain protein with mol wt 120,000, is cleaved by human urinary kallikrein (HUK) to release kinin from within a disulfide loop and form a two-chain protein that retains all the procoagulant activity of the native molecule.	Disulfides	166-175	kininogen 1	Homo sapiens	6-37
6553501-1	1983	Human high molecular weight kininogen (HMWK), a single-chain protein with mol wt 120,000, is cleaved by human urinary kallikrein (HUK) to release kinin from within a disulfide loop and form a two-chain protein that retains all the procoagulant activity of the native molecule.	Disulfides	166-175	kininogen 1	Homo sapiens	39-43
6352535-7	1983	All three disulfide bonds of these insulin derivatives undergo reduction with tributylphosphine to give six sulfhydryls.	Disulfides	10-19	insulin	Homo sapiens	35-42
6222381-3	1983	C4bp is a high molecular weight plasma protein (Mr = 570,000) composed of apparently identical subunits (Mr = 70,000) linked by disulfide bonds.	Disulfides	128-137	complement component 4 binding protein alpha	Homo sapiens	0-4
6352535-11	1983	These studies strongly suggest that disulfide bonds formed during oxidation of reduced oxalyl-(Met)2-insulin and malonyl-(Met)2-insulin are identical to those found in insulin.	Disulfides	36-45	insulin	Homo sapiens	101-108
6352535-11	1983	These studies strongly suggest that disulfide bonds formed during oxidation of reduced oxalyl-(Met)2-insulin and malonyl-(Met)2-insulin are identical to those found in insulin.	Disulfides	36-45	insulin	Homo sapiens	128-135
6352535-11	1983	These studies strongly suggest that disulfide bonds formed during oxidation of reduced oxalyl-(Met)2-insulin and malonyl-(Met)2-insulin are identical to those found in insulin.	Disulfides	36-45	insulin	Homo sapiens	128-135
6310885-5	1983	Trypsinization of MCF-247 gp70 resulted in the production of a carboxy terminal fragment which resembled that of the ecotropic gp70 in that (1) it was disulfide linked to p15(E) but not to the amino terminal fragments, (2) reacted with monoclonal antibody 35/56, (3) contained cysteines but no methionines, and (4) carried only endo H-resistant oligosaccharide chains.	Disulfides	151-160	embigin	Homo sapiens	26-30
6310885-5	1983	Trypsinization of MCF-247 gp70 resulted in the production of a carboxy terminal fragment which resembled that of the ecotropic gp70 in that (1) it was disulfide linked to p15(E) but not to the amino terminal fragments, (2) reacted with monoclonal antibody 35/56, (3) contained cysteines but no methionines, and (4) carried only endo H-resistant oligosaccharide chains.	Disulfides	151-160	embigin	Homo sapiens	127-131
6310885-5	1983	Trypsinization of MCF-247 gp70 resulted in the production of a carboxy terminal fragment which resembled that of the ecotropic gp70 in that (1) it was disulfide linked to p15(E) but not to the amino terminal fragments, (2) reacted with monoclonal antibody 35/56, (3) contained cysteines but no methionines, and (4) carried only endo H-resistant oligosaccharide chains.	Disulfides	151-160	cyclin dependent kinase inhibitor 2B	Homo sapiens	171-174
6636042-1	1983	Lactoperoxidase catalyzed iodination has been used to probe for differences in surface orientation of tyrosine residues in the amino-terminal disulfide knot (N-DSK) domain of fibrinogen, in N-DSK and in Fb-N-DSK prepared from fibrin.	Disulfides	142-151	fibrinogen beta chain	Homo sapiens	175-185
6863272-4	1983	Photooxidation of the activated NH2-terminal disulfide knot, which is derived from fibrin and contains the NH2-terminal binding domain, reduced the ability of this fragment to bind to fibrinogen-Sepharose conjugate.	Disulfides	45-54	fibrinogen beta chain	Homo sapiens	184-194
6303761-0	1983	Role of disulfide bonds in human growth hormone binding and dissociation in isolated rat hepatocytes and liver plasma membranes.	Disulfides	8-17	growth hormone 1	Homo sapiens	33-47
6309861-4	1983	Binding in Pool II was irreversible and proceeded at a linear rate for 30 h. After 30 h of incubation, a significant proportion of fibronectin bound in Pool II was present as disulfide-bonded multimers.	Disulfides	175-184	fibronectin 1	Homo sapiens	131-142
6863267-1	1983	Native rat haptoglobin is an heterotetramer consisting of two alpha-subunits (Mr = approximately 9,500) and two glycosylated beta-subunits (Mr = approximately 38,000) joined by interchain disulfide bonds.	Disulfides	188-197	haptoglobin	Rattus norvegicus	11-22
6614484-1	1983	After precipitation of proteins; serum, hepatocytes, or glutathione-derivatized bovine serum albumin, by perchloric acid, dithiothreitol was used to reduce glutathione-protein mixed disulfides in the ether-washed, resuspended pellet.	Disulfides	182-192	albumin	Homo sapiens	87-100
6313454-1	1983	The receptors for insulin and the insulin-like growth factor (IGF) I are two structurally homologous disulfide-linked multisubunit complexes of apparent Mr = 350,000.	Disulfides	101-110	insulin	Homo sapiens	18-25
6313454-1	1983	The receptors for insulin and the insulin-like growth factor (IGF) I are two structurally homologous disulfide-linked multisubunit complexes of apparent Mr = 350,000.	Disulfides	101-110	insulin	Homo sapiens	34-41
6133865-0	1983	In vitro formation of disulfide-bonded fibronectin multimers.	Disulfides	22-31	fibronectin 1	Homo sapiens	39-50
6133865-4	1983	One- and two-dimensional gel electrophoresis indicated that a molecule of 40-60 kDa was disulfide-bonded to a minor portion of the fibronectin in whole human plasma and in preparations of purified fibronectin.	Disulfides	88-97	fibronectin 1	Homo sapiens	131-142
6133865-4	1983	One- and two-dimensional gel electrophoresis indicated that a molecule of 40-60 kDa was disulfide-bonded to a minor portion of the fibronectin in whole human plasma and in preparations of purified fibronectin.	Disulfides	88-97	fibronectin 1	Homo sapiens	197-208
6133865-5	1983	In addition, traces of disulfide-bonded multimers were present in preparations of purified fibronectin.	Disulfides	23-32	fibronectin 1	Homo sapiens	91-102
6133865-6	1983	The proportion of fibronectin in disulfide-bonded multimers increased in guanidine-containing solutions.	Disulfides	33-42	fibronectin 1	Homo sapiens	18-29
6133865-10	1983	The transition from dimeric to multimeric fibronectin can serve as a model for the formation of disulfide-bonded fibronectin multimers in the extracellular matrix.	Disulfides	96-105	fibronectin 1	Homo sapiens	42-53
6133865-10	1983	The transition from dimeric to multimeric fibronectin can serve as a model for the formation of disulfide-bonded fibronectin multimers in the extracellular matrix.	Disulfides	96-105	fibronectin 1	Homo sapiens	113-124
6860640-2	1983	Circular dichroism spectra of the partially folded trapped intermediates were measured in order to aid in the elucidation of the conformational forces which determine a nonrandom, nonsequential pathway of disulfide bond formation upon refolding of bovine pancreatic trypsin inhibitor.	Disulfides	205-214	trophoblast Kunitz domain protein 1	Bos taurus	266-283
6344921-0	1983	Insulin receptor: insulin-modulated interconversion between distinct molecular forms involving disulfide-sulfhydryl exchange.	Disulfides	95-104	insulin	Homo sapiens	18-25
6873882-11	1983	USA 80, 137-141] it may be concluded that the disulfide rich domains, made up by regions of internal homology of types I and II in the N-terminal portion of fibronectin, exhibit a remarkable conformational stability, whereas the disulfide free middle region which contains type III domains, is much less stable.	Disulfides	46-55	fibronectin 1	Homo sapiens	157-168
6852243-1	1983	A mild cathepsin D digest of fibronectin only contained single-chain peptides of 200, 140 and 70 kDa and double-chain fragments of about 300 and 140 kDa containing the C-terminal disulfide link.	Disulfides	179-188	fibronectin 1	Homo sapiens	29-40
6861897-4	1983	Using this chemically defined medium, we have compared the effects of dimeric and multimeric fibronectin (high molecular weight disulfide-bonded fibronectin produced by incubation of dimeric fibronectin with 3 M guanidine followed by dialysis against 0.05 M cyclohexylaminopropane sulfonic acid (CAPS) buffer, pH 11) on the adhesion and growth of the poorly differentiated primary glomerular cell type.	Disulfides	128-137	fibronectin 1	Homo sapiens	145-156
6861897-4	1983	Using this chemically defined medium, we have compared the effects of dimeric and multimeric fibronectin (high molecular weight disulfide-bonded fibronectin produced by incubation of dimeric fibronectin with 3 M guanidine followed by dialysis against 0.05 M cyclohexylaminopropane sulfonic acid (CAPS) buffer, pH 11) on the adhesion and growth of the poorly differentiated primary glomerular cell type.	Disulfides	128-137	fibronectin 1	Homo sapiens	145-156
6873882-11	1983	USA 80, 137-141] it may be concluded that the disulfide rich domains, made up by regions of internal homology of types I and II in the N-terminal portion of fibronectin, exhibit a remarkable conformational stability, whereas the disulfide free middle region which contains type III domains, is much less stable.	Disulfides	229-238	fibronectin 1	Homo sapiens	157-168
6219896-8	1983	Apo B and Lp(a)-protein seem to be linked by disulfide bonds in the native lipoprotein.	Disulfides	45-54	apolipoprotein B	Homo sapiens	0-5
6860649-0	1983	Dimeric half-molecules of human fibrinogen are joined through disulfide bonds in an antiparallel orientation.	Disulfides	62-71	fibrinogen beta chain	Homo sapiens	32-42
6572973-1	1983	Human insulin-like growth factor I (somatomedin C) with 70 amino acid residues and three disulfide bridges has been synthesized by the solid-phase method.	Disulfides	89-98	insulin like growth factor 1	Homo sapiens	6-34
6572973-1	1983	Human insulin-like growth factor I (somatomedin C) with 70 amino acid residues and three disulfide bridges has been synthesized by the solid-phase method.	Disulfides	89-98	insulin like growth factor 1	Homo sapiens	36-49
6862378-0	1983	The importance of the intramolecular disulfide bridges in porcine somatotropin for its biological activity.	Disulfides	37-46	growth hormone 1	Rattus norvegicus	66-78
6862378-1	1983	The dependance of the porcine somatotropin activity on the entireness of the intrachain disulfide bridges is investigated in three biological systems: bioassay in vivo, radioimmuno assay and receptor assay with rat liver membranes.	Disulfides	88-97	growth hormone 1	Rattus norvegicus	30-42
6297899-10	1983	The beta 1-anticollagenase--leukocyte-collagenase complex (latent enzyme) is activatable by disulfide-containing compounds such as cystine, oxidised glutathione, insulin, relaxin, trypsinogen and others, but not by 179,203-di(S-carboxymethyl)trypsinogen, or its trypsin derivative.	Disulfides	92-101	insulin	Homo sapiens	162-169
6185576-4	1983	In the present study, we show that B10.BR GT-TSF1 is composed of separate I-Jk and idiotype-bearing chains linked by disulfide bond(s).	Disulfides	117-126	granzyme C	Mus musculus	35-38
6830263-0	1983	Localization of the disulfide bond in human antithrombin III required for heparin-accelerated thrombin inactivation.	Disulfides	20-29	coagulation factor II, thrombin	Homo sapiens	48-56
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Disulfides	39-48	coagulation factor II, thrombin	Homo sapiens	61-69
6301526-3	1983	PDP-CaM was covalently coupled to free thiol-Sepharose 4B through formation of a stable mixed disulfide bond for use in affinity chromatography.	Disulfides	94-103	calmodulin 1	Homo sapiens	4-7
6301526-4	1983	The binding capacity of the disulfide-linked CaM-Sepharose for phosphodiesterase activity was proportional to substituent level up to 4 mg of CaM/mL of gel; the total capacity of the gel for binding phosphodiesterase was 4 times that of CNBr-coupled CaM-Sepharose.	Disulfides	28-37	calmodulin 1	Homo sapiens	45-48
6301526-4	1983	The binding capacity of the disulfide-linked CaM-Sepharose for phosphodiesterase activity was proportional to substituent level up to 4 mg of CaM/mL of gel; the total capacity of the gel for binding phosphodiesterase was 4 times that of CNBr-coupled CaM-Sepharose.	Disulfides	28-37	calmodulin 1	Homo sapiens	142-145
6301526-4	1983	The binding capacity of the disulfide-linked CaM-Sepharose for phosphodiesterase activity was proportional to substituent level up to 4 mg of CaM/mL of gel; the total capacity of the gel for binding phosphodiesterase was 4 times that of CNBr-coupled CaM-Sepharose.	Disulfides	28-37	calmodulin 1	Homo sapiens	142-145
6341987-0	1983	Partial disruption of naturally occurring groups of insulin receptors on adipocyte plasma membranes by dithiothreitol and N-ethylmaleimide: the role of disulfide bonds.	Disulfides	152-161	insulin	Homo sapiens	52-59
6341987-1	1983	In this ultrastructural study, monomeric ferritin-insulin was used to further elucidate the role of disulfide bonds in maintaining the natural groups of insulin receptors on adipocyte plasma membranes.	Disulfides	100-109	insulin	Homo sapiens	50-57
6341987-1	1983	In this ultrastructural study, monomeric ferritin-insulin was used to further elucidate the role of disulfide bonds in maintaining the natural groups of insulin receptors on adipocyte plasma membranes.	Disulfides	100-109	insulin	Homo sapiens	153-160
6341993-1	1983	Thrombospondin, a major glycoprotein released from alpha granules of thrombin-stimulated platelets, is a disulfide-bonded trimer of 160-kilodalton subunits.	Disulfides	105-114	coagulation factor II, thrombin	Homo sapiens	69-77
6885107-9	1983	We propose that Tb3+ (by inference Ca2+) binding takes place near the CRP subunit disulfide bond, where two histidine residues are present.	Disulfides	82-91	C-reactive protein	Homo sapiens	70-73
6688992-1	1983	Human haptoglobin (Hp) is a plasma glycoprotein composed of alpha and beta polypeptide chains that are covalently associated by disulfide bonds.	Disulfides	128-137	haptoglobin	Homo sapiens	6-17
6338918-0	1983	Generation of an acid-stable and protein-bound persulfide-like residue in alkali- or sulfhydryl-treated insulin by a mechanism consonant with the beta-elimination hypothesis of disulfide bond lysis.	Disulfides	177-186	insulin	Homo sapiens	104-111
6214556-1	1982	Modulation of phosphofructokinase activity by thiol/disulfide exchange.	Disulfides	52-61	ATP-dependent 6-phosphofructokinase, muscle type	Oryctolagus cuniculus	14-33
7159551-5	1982	Prolonged air oxidation of fully reduced thioredoxin created inactive, aggregated disulfide-containing molecules.	Disulfides	82-91	thioredoxin 1	Rattus norvegicus	41-52
6759610-4	1982	Control hamster sperm nuclei, which exhibited proteinase activity, decondensed when incubated in vitro with disulfide reducing agent.	Disulfides	108-117	endogenous retrovirus group K member 25	Homo sapiens	46-56
6759610-6	1982	When the proteinase associated with isolated sperm nuclei was removed with 0.5 M salt or inhibited with nitrophenyl-p-guanidinobenzoate, the nuclei were rendered incapable of decondensing in response to disulfide reducing agent in vitro.	Disulfides	203-212	endogenous retrovirus group K member 25	Homo sapiens	9-19
6815213-5	1982	With progressive reduction of disulfide bonds by dithiothreitol (DTT), the electron microscopic size of FVIII/vWF decreased in parallel with increased electrophoretic mobility on SDS-agarose gels; between 0.1 and 0.5 mM DTT its structure changed from predominantly fibrillar species to large nodular forms.	Disulfides	30-39	von Willebrand factor	Homo sapiens	110-113
7150571-2	1982	After initiation of disulfide bond formation associated with the folding process of reduced human lysozyme, molecules have been trapped in a stable form with iodoacetic acid (preserving disulfide bonds) at various times of reoxidation.	Disulfides	20-29	lysozyme	Homo sapiens	98-106
7150571-2	1982	After initiation of disulfide bond formation associated with the folding process of reduced human lysozyme, molecules have been trapped in a stable form with iodoacetic acid (preserving disulfide bonds) at various times of reoxidation.	Disulfides	186-195	lysozyme	Homo sapiens	98-106
6187626-5	1982	The landmark cysteine residues are found in the same positions in both polypeptide chains, presumably forming the same disulfide bridges in AFP as those found in the albumin.	Disulfides	119-128	alpha fetoprotein	Homo sapiens	140-143
6815213-6	1982	A 50% loss of vWF specific activity and FVIII procoagulant activity occurred at 0.4 mM DTT and 1 mM DTT, respectively, corresponding to the reduction of 4 and 12 disulfide bonds of the 62 disulfides per 200,000-dalton subunit.	Disulfides	162-171	von Willebrand factor	Homo sapiens	14-17
6815213-6	1982	A 50% loss of vWF specific activity and FVIII procoagulant activity occurred at 0.4 mM DTT and 1 mM DTT, respectively, corresponding to the reduction of 4 and 12 disulfide bonds of the 62 disulfides per 200,000-dalton subunit.	Disulfides	188-198	von Willebrand factor	Homo sapiens	14-17
6815213-7	1982	We conclude that reduction of a few critical disulfide bonds results in a major structural change by electron microscopy and a concomitant loss of approximately 50% of the vWF function.	Disulfides	45-54	von Willebrand factor	Homo sapiens	172-175
6214556-8	1982	These equilibrium constants for thiol/disulfide exchange are such that modulation of phosphofructokinase activity by thiol/disulfide exchange in vivo is feasible.	Disulfides	38-47	ATP-dependent 6-phosphofructokinase, muscle type	Oryctolagus cuniculus	85-104
6214556-8	1982	These equilibrium constants for thiol/disulfide exchange are such that modulation of phosphofructokinase activity by thiol/disulfide exchange in vivo is feasible.	Disulfides	123-132	ATP-dependent 6-phosphofructokinase, muscle type	Oryctolagus cuniculus	85-104
7174648-1	1982	Human C4 binding protein (C4bp), which is a macromolecular weight (Mr 450,000-590,000) cofactor of C3b/C4b inactivator (I), is composed of 6 or 8 disulfide-linked polypeptide chains of Mr 75,000.	Disulfides	146-155	complement component 4 binding protein alpha	Homo sapiens	6-24
6293818-9	1982	Based on the similarities between the data from these three systems and published data from other systems, we now propose that dithiol-disulfide interchange may play a general role in membrane-related processes such as transport, energy transduction and hormone-receptor interactions.	Disulfides	135-144	nuclear receptor subfamily 4 group A member 1	Homo sapiens	254-270
7174648-1	1982	Human C4 binding protein (C4bp), which is a macromolecular weight (Mr 450,000-590,000) cofactor of C3b/C4b inactivator (I), is composed of 6 or 8 disulfide-linked polypeptide chains of Mr 75,000.	Disulfides	146-155	complement component 4 binding protein alpha	Homo sapiens	26-30
7174648-2	1982	Chymotrypsin cleaved C4bp into two major fragments; a large fragment of Mr 160,000, which contained carbohydrate chains and was composed of disulfide-linked polypeptide chains of Mr 25,000, and a small fragment of Mr 48,000, which was a single polypeptide chain and had the cofactor activity of C4bp.	Disulfides	140-149	complement component 4 binding protein alpha	Homo sapiens	21-25
6754373-1	1982	Interchain disulfide crosslinks between the heavy-chain fragment in heavy meromyosin and myosin light chain 2, generated by 5,5"-dithiobis(2-nitrobenzoic acid (Nbs2), are formed under appropriate ionic conditions at neutral pH as revealed by liberation of the chromogenic 2-nitro-5-thiobenzoic acid.	Disulfides	11-20	myosin regulatory light chain 2, ventricular/cardiac muscle isoform	Oryctolagus cuniculus	89-109
6757503-0	1982	Potentiation of bradykinin-induced decrease of blood pressure in dogs by SO 14,551, the disulfide metabolite of captopril.	Disulfides	88-97	kininogen 1	Canis lupus familiaris	16-26
7138878-4	1982	The amino acid composition, the nature of the N-terminal residue and data obtained from the tryptic peptides and indicate that PSTI III lacks the N-terminal octapeptide of PSTI I; hence, it starts and ends with disulfide bridges.	Disulfides	211-220	serine peptidase inhibitor Kazal type 1	Homo sapiens	127-131
6292071-0	1982	Dependence of human somatotropin activity on interchain disulfide bridges.	Disulfides	56-65	growth hormone 1	Homo sapiens	20-32
6292071-1	1982	The importance of the disulfide bridges for human somatotropin activity is investigated.	Disulfides	22-31	growth hormone 1	Homo sapiens	50-62
7045258-10	1982	Large or small, complex peptides like insulin, oxytocin, or vasopressin that contain disulfide bridges are not hydrolyzed at the luminal brush border of the proximal tubule.	Disulfides	85-94	arginine vasopressin	Rattus norvegicus	60-71
6981613-0	1982	Studies on the disulfide region of alpha 1-protease inhibitor.	Disulfides	15-24	serpin family A member 1	Homo sapiens	35-61
6981613-1	1982	The single disulfide bond of purified human alpha 1-protease inhibitor was reduced with dithiothreitol in the absence of denaturant and the resultant sulfhydryl groups were alkylated with iodoacetamide-1-C14.	Disulfides	11-20	serpin family A member 1	Homo sapiens	44-70
6981613-8	1982	A variety of experiments involving gel filtration or dialysis of reduced or oxidized alpha 1-protease inhibitor indicate that this Cys-peptide is covalently bound to either free cysteine or to glutathione via a disulfide bridge.	Disulfides	211-220	serpin family A member 1	Homo sapiens	85-111
7106283-0	1982	Identification of the active site cysteine and of the disulfide bonds in the N-terminal part of the molecule of bovine spleen cathepsin B.	Disulfides	54-63	cathepsin B	Bos taurus	126-137
6954526-2	1982	Cultured skin fibroblasts from three individuals affected with the disease produce half-normal levels of type I procollagen, a disulfide-bonded trimer that contains two pro alpha 1(I) chains and one pro alpha 2(I) chain.	Disulfides	127-136	collagen type I alpha 2 chain	Homo sapiens	105-123
6276374-3	1982	Thus, to address this problem, disulfide bonds of ribonuclease-A and lysozyme were reductively cleaved under denaturing conditions, and the resulting 7-8 sulfhydryl groups were treated with a new sulfhydryl group reagent containing selenium, 6,6"-diselenobis(3-nitrobenzoic acid), to give proteins containing covalently attached selenium in the form of selenenyl sulfides.	Disulfides	31-40	lysozyme	Homo sapiens	69-77
6807576-3	1982	The antibody-bound form of labeled prolactin was separated from the unbound form by a method based on the thiol-disulfide interchange reaction.	Disulfides	112-121	prolactin	Homo sapiens	35-44
6176283-2	1982	Anti-FBP sera varied in the extent to which they cross-reacted with fibrinogen, the NH2-terminal disulfide knot of fibrinogen (N-DSK), B beta 1(Pyr)-118(Met), B beta 1(Pyr)-42(Arg), and desarginyl-FPB.	Disulfides	97-106	ECB2	Homo sapiens	5-8
7061516-6	1982	The phosphorylated region(s) of human fibronectin are apparently not located at the extreme COOH-terminal region containing the interchain disulfide bond, but seem to be within a 40,000-50,000 segment near one end of the molecule.	Disulfides	139-148	fibronectin 1	Homo sapiens	38-49
7076131-0	1982	Early and late cathepsin D-derived fragments of fibronectin containing the C-terminal interchain disulfide cross-link.	Disulfides	97-106	fibronectin 1	Homo sapiens	48-59
7076131-1	1982	Fibronectin consists of two very similar subunits connected by disulfide bonds close to their C-terminal ends.	Disulfides	63-72	fibronectin 1	Homo sapiens	0-11
7096442-1	1982	Thrombospondin, the major glycoprotein released from alpha-granules of thrombin-stimulated platelets, is a disulfide-bonded trimer of 160 kilodalton subunits and apparently functions as a platelet lectin.	Disulfides	107-116	coagulation factor II, thrombin	Homo sapiens	71-79
7044417-1	1982	The enthalpy changes for the reduction of three disulfide bonds of insulin by dithiothreitol (DTT) were calorimetrically measured at various temperatures ranging from 289 to 308 K. The reduction was performed in three different buffer solutions of pH 9.6, and the observed heat changes were corrected for the ionization heats of the buffer components to obtain the net heats of reduction of insulin with DTT.	Disulfides	48-57	insulin	Homo sapiens	67-74
7044417-4	1982	Using the heat of oxidation of the cysteine residue, we estimated the enthalpy change for the conformational transition of insulin induced by the cleavage of three disulfide bonds to be delta H conf = 91 kJ mol-1 at 298 K. The heat capacity change was 2.1 kJ mol-1 K-1.	Disulfides	164-173	insulin	Homo sapiens	123-130
6178839-2	1982	These monoclonal antibodies recognized a new type of viral antigenic determinant which appeared to be a conformational determinant associated with the env precursor polyprotein (pr80env) or its disulfide-linked gp70-p15(E) complex (gp80) but not with free gp70 or p15(E) or any other virion or virus-induced protein.	Disulfides	194-203	cyclin dependent kinase inhibitor 2B	Mus musculus	216-219
6178839-2	1982	These monoclonal antibodies recognized a new type of viral antigenic determinant which appeared to be a conformational determinant associated with the env precursor polyprotein (pr80env) or its disulfide-linked gp70-p15(E) complex (gp80) but not with free gp70 or p15(E) or any other virion or virus-induced protein.	Disulfides	194-203	cyclin dependent kinase inhibitor 2B	Mus musculus	264-267
6948605-1	1982	The toxic subunit of ricin has been conjugated by a disulfide bound to a monoclonal murine antibody (J-5) specific for the common acute lymphoblastic leukemia antigen (CALLA) expressed on human lymphoblastic cells.	Disulfides	52-61	membrane metalloendopeptidase	Homo sapiens	168-173
7118395-3	1982	Insoluble trypsin has been shown to attack preferentially some peptide bonds of ovine prolactin, within the large disulfide loop.	Disulfides	114-123	prolactin	Homo sapiens	86-95
6302119-9	1982	We conclude that the receptors for basic somatomedin and insulin are highly homologous structures with respect to their disulfide crosslinked composition, and with respect to the size of the major components detected by selective affinity-labeling procedures.	Disulfides	120-129	insulin	Homo sapiens	57-64
7295701-2	1981	As part of a conformational study of the pathway of unfolding and refolding of bovine pancreatic trypsin inhibitor that accompanies breakage and formation of its three disulfide bonds, circular dichroism spectra have been measured for several limiting conformational states: native and refolded, with the three correct disulfide bonds; the (30--51, 5--55) two-disulfide species trapped during unfolding and refolding, which have a stable nativelike conformation; the fully reduced protein, with no disulfide bonds.	Disulfides	168-177	trophoblast Kunitz domain protein 1	Bos taurus	97-114
7044895-4	1981	Controlled disulfide exchange in the S-sulfonate of the analog generated a molecule having high-pressure liquid chromatography (HPLC) and radioimmunoassay (RIA) behavior consistent with a proinsulin-like structure.	Disulfides	11-20	insulin	Homo sapiens	188-198
6269656-3	1981	A decrease of rotational mobility of rhodopsin in ROS induced by prolonged illumination is shown to result from irreversible protein aggregation caused by disulfide bond formation between "hydrophobic" SH-groups of rhodopsin.	Disulfides	155-164	rhodopsin	Homo sapiens	37-46
7305337-0	1981	Synthesis of type I procollagen: formation of interchain disulfide bonds before complete hydroxylation of the protein.	Disulfides	57-66	collagen type I alpha 2 chain	Homo sapiens	13-31
7017937-0	1981	Pineal N-acetyltransferase is inactivated by disulfide-containing peptides: insulin is the most potent.	Disulfides	45-54	insulin	Homo sapiens	76-83
7017937-2	1981	Some, but not all, disulfide-containing peptides can inactivate this enzyme; the most potent inactivator is insulin.	Disulfides	19-28	insulin	Homo sapiens	108-115
6269656-3	1981	A decrease of rotational mobility of rhodopsin in ROS induced by prolonged illumination is shown to result from irreversible protein aggregation caused by disulfide bond formation between "hydrophobic" SH-groups of rhodopsin.	Disulfides	155-164	rhodopsin	Homo sapiens	215-224
7024087-0	1981	Synthetic insulin by selective disulfide briding, II.	Disulfides	31-40	insulin	Homo sapiens	10-17
6114827-5	1981	Furthermore, disulfides [insulin, glutathione disulfide, L-cystine, and 5,5"-dithiobis (2-nitrobenzoic acid)] known to interact with thioredoxin-dependent enzyme systems inhibited sulindac reduction, as did sodium arsenite, a known inhibitor of thioredoxin reductase.	Disulfides	13-23	thioredoxin 1	Rattus norvegicus	133-144
6114827-5	1981	Furthermore, disulfides [insulin, glutathione disulfide, L-cystine, and 5,5"-dithiobis (2-nitrobenzoic acid)] known to interact with thioredoxin-dependent enzyme systems inhibited sulindac reduction, as did sodium arsenite, a known inhibitor of thioredoxin reductase.	Disulfides	13-23	peroxiredoxin 5	Rattus norvegicus	245-266
6457032-4	1981	Porcine plasma fibronectin consisted of two subunit chains of about 230,000-daltons linked by disulfide bonds(s).	Disulfides	94-103	fibronectin 1	Homo sapiens	15-26
6451630-6	1981	The D1 peptide does not interact with disulfide knot, fibrinogen, or Fragment D1, but it binds to thrombin-treated disulfide knot with a Kd of 1.45 X 10(-6) M at approximately two binding sites per molecule of disulfide knot.	Disulfides	115-124	coagulation factor II, thrombin	Homo sapiens	98-106
6166718-0	1981	Lyt-2 and lyt-3 antigens are on two different polypeptide subunits linked by disulfide bonds.	Disulfides	77-86	CD8b molecule	Homo sapiens	10-15
6166718-2	1981	Lyt-2 and Lyt-3 antigens are carried on separate disulfide-bonded subunits of the same cell surface macromolecules.	Disulfides	49-58	CD8b molecule	Homo sapiens	10-15
6166718-5	1981	Almost all of the Lyt-2 and Lyt-3 subunits on the cell are covalently linked by disulfide bonds.	Disulfides	80-89	CD8b molecule	Homo sapiens	28-33
6260790-8	1981	From these observations we conclude that native myeloperoxidase contains two heavy-light protomers, which are joined along their long axes by a single disulfide bond between the heavy subunits.	Disulfides	151-160	myeloperoxidase	Homo sapiens	48-63
6260790-9	1981	Selective reduction of this disulfide bond by the use of nondenaturing conditions results in the formation of hemi-myeloperoxidase, a catalytically active heavy-light protomer of native myeloperoxidase.	Disulfides	28-37	myeloperoxidase	Homo sapiens	115-130
6260790-9	1981	Selective reduction of this disulfide bond by the use of nondenaturing conditions results in the formation of hemi-myeloperoxidase, a catalytically active heavy-light protomer of native myeloperoxidase.	Disulfides	28-37	myeloperoxidase	Homo sapiens	186-201
6451630-6	1981	The D1 peptide does not interact with disulfide knot, fibrinogen, or Fragment D1, but it binds to thrombin-treated disulfide knot with a Kd of 1.45 X 10(-6) M at approximately two binding sites per molecule of disulfide knot.	Disulfides	115-124	coagulation factor II, thrombin	Homo sapiens	98-106
7225368-8	1981	No free cysteine sulfhydryl group could be detected, so that it was assumed that the two cysteine residues of ovine SS-28 formed an intramolecular disulfide bond.	Disulfides	147-156	somatostatin	Rattus norvegicus	116-121
6784722-0	1981	Gamma-crystallin, a major cytoplasmic polypeptide disulfide linked to membrane proteins in human cataract.	Disulfides	50-59	crystallin gamma A	Homo sapiens	0-19
6786355-3	1981	SDS-polyacrylamide gel electrophoresis showed that intersubunit bond and H-L bond were the most labile disulfide in polymeric and monomeric IgA, respectively.	Disulfides	103-112	CD79a molecule	Homo sapiens	140-143
7344476-2	1981	Because of a decrease in the intrahepatic free glutathione: mixed disulfide ratio, which is apparently mediated by c-AMP, the free glutathione pool contracts and turns over more rapidly in order to maintain glutathione synthesis.	Disulfides	66-75	cathelicidin antimicrobial peptide	Homo sapiens	115-120
6938960-1	1980	Plasma membrane insulin receptors, affinity labeled by covalent crosslinking to receptor-bound 125I-labeled insulin, are shown to appear as a heterogeneous population of three major disulfide-linked complexes (Mr 350,000, 320,000, and 290,000) upon electrophoresis in highly porous dodecyl sulfate/polyacrylamide gels in the absence of reductant.	Disulfides	182-191	insulin	Homo sapiens	16-23
6265168-7	1981	Furthermore, vasopressin and the vasoactive component of the extract were equally sensitive to several peptidases, and conditions which cleave disulfide bridges.	Disulfides	143-152	arginine vasopressin	Homo sapiens	13-24
7440724-0	1980	Disulfide reduction converts the insulin receptor of human placenta to a low affinity form.	Disulfides	0-9	insulin	Homo sapiens	33-40
7440724-6	1980	These results suggest that reduction of a critical disulfide bond in insulin receptors from human placenta converts the receptor to a low affinity form.	Disulfides	51-60	insulin	Homo sapiens	69-76
7026781-1	1981	In vitro incubation of human erythrocytes with disulfide reducing agents (dithiothreitol and 2-mercaptoethanol) produces a significant increase in specific binding of 125I insulin to the insulin receptor.	Disulfides	47-56	insulin	Homo sapiens	172-179
7026781-1	1981	In vitro incubation of human erythrocytes with disulfide reducing agents (dithiothreitol and 2-mercaptoethanol) produces a significant increase in specific binding of 125I insulin to the insulin receptor.	Disulfides	47-56	insulin	Homo sapiens	187-194
6938960-1	1980	Plasma membrane insulin receptors, affinity labeled by covalent crosslinking to receptor-bound 125I-labeled insulin, are shown to appear as a heterogeneous population of three major disulfide-linked complexes (Mr 350,000, 320,000, and 290,000) upon electrophoresis in highly porous dodecyl sulfate/polyacrylamide gels in the absence of reductant.	Disulfides	182-191	insulin	Homo sapiens	108-115
6776144-14	1980	By analogy to the apo(E--A-II) complex, which also occurs in human HDL, this mixed disulfide complex was designated as the apo(A-Icys--A-II) complex.	Disulfides	83-92	NLR family pyrin domain containing 3	Homo sapiens	25-29
6776144-14	1980	By analogy to the apo(E--A-II) complex, which also occurs in human HDL, this mixed disulfide complex was designated as the apo(A-Icys--A-II) complex.	Disulfides	83-92	NLR family pyrin domain containing 3	Homo sapiens	135-139
7189740-1	1980	Reduction of porcine pancreatic phospholipase A2 with 2-mercaptoethanol in the presence of 6M guanidinium hydrocholoride or 8M urea resulted in the complete disruption of all seven disulfide bridges and the concomitant loss of all enzymatic activity.	Disulfides	181-190	phospholipase A2 group IB	Homo sapiens	32-48
6774760-1	1980	Human plasma fibronectin migrated in electrophoresis after reduction of the disulfide bonds in SDS-polyacrylamide gels as two closely spaced polypeptide bands.	Disulfides	76-85	fibronectin 1	Homo sapiens	13-24
6997877-1	1980	The complete amino acid sequences and the disulfide arrangements of the two chains of human haptoglobin 1-1 were established.	Disulfides	42-51	haptoglobin	Homo sapiens	92-103
7440057-0	1980	Preparation of a two-disulfide bonded enzymically active derivative from hen egg lysozyme.	Disulfides	21-30	lysozyme	Homo sapiens	81-89
7440057-1	1980	A method has been developed for preparation of an enzymically active two-disulfide bonded derivative from hen egg lysozyme.	Disulfides	73-82	lysozyme	Homo sapiens	114-122
7440057-7	1980	Thus, the species containing two presumably native disulfide bonds and four free sulfhydryl groups at Cys 6, Cys 76, Cys 94 and Cys 127 appears to be only the intermediate accumulating during reduction of lysozyme with dithiothreitol.	Disulfides	51-60	lysozyme	Homo sapiens	205-213
7410374-8	1980	Thus, all five disulfide bonds in hCG-alpha were assigned and are located at positions 7 and 31, 10 and 32, 28 and 60, 59 and 87, and 82 and 84.	Disulfides	15-24	chromogranin A	Homo sapiens	34-43
6967100-4	1980	Radioiodinated vWF, a disulfide-linked polymer of 230,000 dalton subunits, attached to formalinized human platelets only in the presence of ristocetin.	Disulfides	22-31	von Willebrand factor	Homo sapiens	15-18
6769127-1	1980	Antibodies to the disulfide knot fragment of bovine fibrinogen have been used to locate the site of this fragment within the intact fibrinogen molecule.	Disulfides	18-27	fibrinogen beta chain	Homo sapiens	52-62
6769127-1	1980	Antibodies to the disulfide knot fragment of bovine fibrinogen have been used to locate the site of this fragment within the intact fibrinogen molecule.	Disulfides	18-27	fibrinogen beta chain	Homo sapiens	132-142
6769127-3	1980	Electron micrographs of reaction mixtures of bovine fibrinogen and antibodies against the disulfide knot fragment showed pairs of fibrinogen molecules crosslinked by antibody molecules as well as higher order antibody-fibrinogen complexes.	Disulfides	90-99	fibrinogen beta chain	Homo sapiens	52-62
6769127-3	1980	Electron micrographs of reaction mixtures of bovine fibrinogen and antibodies against the disulfide knot fragment showed pairs of fibrinogen molecules crosslinked by antibody molecules as well as higher order antibody-fibrinogen complexes.	Disulfides	90-99	fibrinogen beta chain	Homo sapiens	130-140
6769127-3	1980	Electron micrographs of reaction mixtures of bovine fibrinogen and antibodies against the disulfide knot fragment showed pairs of fibrinogen molecules crosslinked by antibody molecules as well as higher order antibody-fibrinogen complexes.	Disulfides	90-99	fibrinogen beta chain	Homo sapiens	130-140
6769127-4	1980	From an electron microscopic investigation of the crosslinked material, we conclude that the disulfide knot lies within the central nodule of the trinodular fibrinogen molecule.	Disulfides	93-102	fibrinogen beta chain	Homo sapiens	157-167
6993455-0	1980	Calorimetric study of the reduction of the disulfide bonds in insulin.	Disulfides	43-52	insulin	Homo sapiens	62-69
6993455-1	1980	Calorimetric measurement was made on the reduction of the three disulfide bonds of insulin by dithiothreitol (DTT).	Disulfides	64-73	insulin	Homo sapiens	83-90
114581-10	1979	The integrity of the hinge region appeared to be essential for full expression of cytophilic activity since reduction of the hinge-region disulfides in both human IgG1 and its Fc fragment markedly decreased their binding affinity.	Disulfides	138-148	immunoglobulin heavy constant gamma 1 (G1m marker)	Mus musculus	163-167
6995531-0	1980	Coupling of delta 5,3-ketosteroid isomerase to human placental lactogen with intermolecular disulfide bond formation.	Disulfides	92-101	chorionic somatomammotropin hormone 2	Homo sapiens	53-71
114208-2	1979	(1) Instead of the four labile interchain disulfide bridges ordinarily found in IgG1, the Dob protein has only a single interchain disulfide bridge, which connects its two light chains.	Disulfides	131-140	major histocompatibility complex, class II, DO beta	Homo sapiens	90-93
120192-5	1979	Active dimeric isozymes, generated apparently by the formation of intermolecular disulfide bridges, also occur but account for only a small proportion of the total protein and appear only when the concentration of CA III is particularly high.	Disulfides	81-90	carbonic anhydrase 3	Homo sapiens	214-220
572807-1	1979	The bis(S-methoxycarbonylthio)-B-chain of beef insulin was synthesized from B-chain bis(S-sulfonate) and methoxycarbonyl-sulfenylchloride and reacted with thioglycolic acid as well as with cysteine in acidic solution to the corresponding unsymmetrical disulfides in 80% yield.	Disulfides	252-262	insulin	Homo sapiens	47-54
314662-3	1979	Staining of disulfide-reduced factor VIII subunits, in polyacrylamide gels, with galactose-specific fluorescein-labelled Ricinus communis lectins, showed an increased binding affinity with increasing size and von Willebrand activity of the parent factor VIII.	Disulfides	12-21	coagulation factor VIII	Bos taurus	30-41
314662-3	1979	Staining of disulfide-reduced factor VIII subunits, in polyacrylamide gels, with galactose-specific fluorescein-labelled Ricinus communis lectins, showed an increased binding affinity with increasing size and von Willebrand activity of the parent factor VIII.	Disulfides	12-21	coagulation factor VIII	Bos taurus	247-258
115344-0	1979	Fully active insulin by selective formation of the disulfide bridges between a synthetic A-chain and natural B-chain.	Disulfides	51-60	insulin	Homo sapiens	13-20
88474-1	1979	Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and beta 1H globulin (beta 1H) cleaved the alpha-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact beta-chain (C3bi).	Disulfides	197-206	Fc gamma receptor and transporter	Homo sapiens	113-124
216702-1	1979	The apolipoprotein B polypeptide of human serum low density lipoprotein exists (after reduction of disulfide bonds) as a random coil with a molecular weight of 250,000 in concentrated solutions of guanidine hydrochloride.	Disulfides	99-108	apolipoprotein B	Homo sapiens	4-20
288074-5	1979	Sulfitolysis of highly purified material to break the inter- and intra-chain disulfide bridges and subsequent adsorption on a specific B-chain antibody covalently bound to Sepharose beads showed that the C-peptide was still connected to the B-chain.	Disulfides	77-86	insulin	Homo sapiens	204-213
429533-0	1979	Circulating big human prolactin: conversion to small human prolactin by reduction of disulfide bonds.	Disulfides	85-94	prolactin	Homo sapiens	22-31
429533-0	1979	Circulating big human prolactin: conversion to small human prolactin by reduction of disulfide bonds.	Disulfides	85-94	prolactin	Homo sapiens	59-68
429533-3	1979	These results suggest that the existence of circulating big hPRL is dependent upon the formation of interpolypeptide disulfide bonds and does not represent a classical biosynthetic precursor of hPRL.	Disulfides	117-126	prolactin	Homo sapiens	60-64
738701-0	1978	Disulfide bridges in the middle part of human fibrinogen.	Disulfides	0-9	fibrinogen beta chain	Homo sapiens	46-56
521210-0	1979	Synthesis of biological activity of human beta-endorphin analogs with disulfide bridges.	Disulfides	70-79	proopiomelanocortin	Homo sapiens	42-56
102363-4	1978	In the presence of diisopropylfluorophosphate, which in the experimental conditions used inhibited only partially the thrombin generated activity, products obtained upon activation of prothrombin by venom were F 1 and a two-chain, disulfide-bridged protein of 58 000 daltons called meizothrombin (des F 1).	Disulfides	231-240	coagulation factor II, thrombin	Homo sapiens	184-195
102363-5	1978	In the presence of hirudin, which fully inhibited thrombin generated activity, prothrombin activation by the venom did not liberate any fragment, but prothrombin was converted to a derivative composed of two disulfide-bridged polypeptide chains of 48 000 and 37 000 daltons, called meizothrombin.	Disulfides	208-217	coagulation factor II, thrombin	Homo sapiens	50-58
102363-5	1978	In the presence of hirudin, which fully inhibited thrombin generated activity, prothrombin activation by the venom did not liberate any fragment, but prothrombin was converted to a derivative composed of two disulfide-bridged polypeptide chains of 48 000 and 37 000 daltons, called meizothrombin.	Disulfides	208-217	coagulation factor II, thrombin	Homo sapiens	150-161
730118-1	1978	Preliminary note on a disulfide-containing internal peptide of the alpha-chain, obtained by plasmic digestion of fibrinogen.	Disulfides	22-31	Fc gamma receptor and transporter	Homo sapiens	67-78
720747-6	1978	By SDS-PAGE the molecular weight of labelled AMH was 123,000 and dissociation into a 72,000 subunit was demonstrated under conditions which reduce disulfide bonds.	Disulfides	147-156	anti-Mullerian hormone	Bos taurus	45-48
741445-0	1978	The arrangement of disulfide bonds in fragment D from human fibrinogen.	Disulfides	19-28	fibrinogen beta chain	Homo sapiens	60-70
517006-1	1979	A mercaptide chelated heme having the spectral characteristics of cytochrome P-450 has been prepared by coupling di-3-amino-propyl-disulfide to protoheme, followed by reduction and disulfide cleavage with sodium dithionithe.	Disulfides	131-140	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	66-82
711738-5	1978	Inactivation of free rhodanese by phenylglyoxal in the presence of cyanide was shown to be caused by a novel reaction in which disulfide bonds are formed between Cys-247 and either Cys-254 or Cys-263.	Disulfides	127-136	thiosulfate sulfurtransferase	Bos taurus	21-30
730118-1	1978	Preliminary note on a disulfide-containing internal peptide of the alpha-chain, obtained by plasmic digestion of fibrinogen.	Disulfides	22-31	fibrinogen beta chain	Homo sapiens	113-123
361081-3	1978	Soluble fibronectin is composed of two high molecular weight subunits held together by disulfide bonds.	Disulfides	87-96	fibronectin 1	Homo sapiens	8-19
738701-1	1978	Human fibrinogen contains 29 disulfide bridges per molecule.	Disulfides	29-38	fibrinogen beta chain	Homo sapiens	6-16
738701-3	1978	When fibrinogen is cleaved by cyanogen bromide five disulfide-containing fragments are formed.	Disulfides	52-61	fibrinogen beta chain	Homo sapiens	5-15
291368-4	1978	In the matrix, fibronectin is partially disulfide bonded into complexes.	Disulfides	40-49	fibronectin 1	Homo sapiens	15-26
629933-6	1978	Three disulfide bonds in GSP occur in similar positions in chymotrypsin, trypsin, and elastase.	Disulfides	6-15	mast cell protease 2	Rattus norvegicus	25-28
667030-1	1978	Reduction of disulfide linkages by dithiothreitol removes LETS (large, external, transformation-sensitive) protein from the cell surface.	Disulfides	13-22	fibronectin 1	Homo sapiens	58-62
684756-7	1978	Thioltransferase, known to catalyze thiol-disulfide exchange reactions, increased the regain of glyceraldehyde-3-phosphate dehydrogenase activity to nearly the original value.	Disulfides	42-51	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	96-136
632300-2	1978	IGF-I is a single chain polypeptide of 70 amino acid residues cross-linked by three disulfide bridges.	Disulfides	84-93	insulin like growth factor 1	Homo sapiens	0-5
629933-7	1978	However, GSP lacks a disulfide bond which is present in all known serine proteases (linking Cys-191 to Cys-220 in chymotrypsin).	Disulfides	21-30	mast cell protease 2	Rattus norvegicus	9-12
346077-3	1978	LETS glycoprotein is disulfide-bonded at the cell surface into dimers and higher aggregates.	Disulfides	21-30	fibronectin 1	Homo sapiens	0-4
346077-5	1978	Reduction of disulfide bonds leads to increased release of LETS protein from the cells, as does the addition of cytochalasin B. Purified LETS protein added to transformed cells binds to the cells in a fibrillar array similar to that seen on normal cells.	Disulfides	13-22	fibronectin 1	Homo sapiens	59-63
346077-5	1978	Reduction of disulfide bonds leads to increased release of LETS protein from the cells, as does the addition of cytochalasin B. Purified LETS protein added to transformed cells binds to the cells in a fibrillar array similar to that seen on normal cells.	Disulfides	13-22	fibronectin 1	Homo sapiens	137-141
24408196-11	1978	L-1 posesses a total of 9 cysteine molecules, 6 of which are present as disulfide bonds.	Disulfides	72-81	seed linoleate 13S-lipoxygenase-1	Glycine max	0-3
144599-0	1977	Stability of the disulfide bonds of fibrinogen and identification of specific subsets of surface-oriented histidine residue highly susceptible to alkylation.	Disulfides	17-26	fibrinogen beta chain	Homo sapiens	36-46
915274-3	1977	Reconstituted C1 was activatable as shown by cleavage of the 87,000 dalton polypeptide chain of C1s into disulfide linked subunits of 59,000 and 28,000 daltons, respectively, after incubation with aggregated IgG.	Disulfides	105-114	complement C1s	Homo sapiens	96-99
146273-1	1977	The molecular weights of derivatives obtained from chemical and enzymatic degradation of fibrinogen and fibrin support a model in which the two halves of the fibrinogen molecule are covalently linked by a set of disulfide bonds at the amino-terminal region.	Disulfides	212-221	fibrinogen beta chain	Homo sapiens	89-99
146273-1	1977	The molecular weights of derivatives obtained from chemical and enzymatic degradation of fibrinogen and fibrin support a model in which the two halves of the fibrinogen molecule are covalently linked by a set of disulfide bonds at the amino-terminal region.	Disulfides	212-221	fibrinogen beta chain	Homo sapiens	158-168
560871-1	1977	A bovine counterpart to human prealbumin was purified from bovine serum by thiol-disulfide exchange chromatography on thiol-Sepharose 4B and affinity chromatography on human retinol-binding protein linked to Sepharose 4B.	Disulfides	81-90	transthyretin	Bos taurus	30-40
911764-0	1977	Optical activity of disulfide bonds in proteins: studies on human choriomammotropin and bovine pituitary somatotropin.	Disulfides	20-29	chorionic somatomammotropin hormone 2	Homo sapiens	66-83
911764-1	1977	The contributions of the homologous carboxyl-terminal disulfide bonds in human choriomammotropin (human chorionic somatomammotropin, human placental lactogen) and bovine somatotropin (pituitary growth hormone), to the near ultraviolet circular dichroism spectra of these two proteins have been evaluated.	Disulfides	54-63	chorionic somatomammotropin hormone 2	Homo sapiens	79-96
911764-2	1977	The disulfide bond in the human placental protein displays a broad, negative band centered near 260 nm ([theta]M, 260nm = -2100 +/- 160 deg cm2 dmol-1) which is equivalent, within experimental error, to the band previously assigned to the identical disulfide in plasmin modified human somatotropin.	Disulfides	4-13	growth hormone 1	Homo sapiens	285-297
911768-0	1977	A Raman spectroscopic investigation of the disulfide conformation in oxytocin and lysine vasopressin.	Disulfides	43-52	arginine vasopressin	Homo sapiens	89-100
562134-0	1977	Identification of discrete disulfide-linked oligomers which distinguish 18 S from 14 S acetylcholinesterase.	Disulfides	27-36	acetylcholinesterase (Cartwright blood group)	Homo sapiens	87-107
887933-0	1977	Relaxin: a disulfide homolog of insulin.	Disulfides	11-20	insulin	Homo sapiens	32-39
70228-5	1977	In addition to the monomeric form of alpha-fetoprotein, we have identified human alpha-fetoprotein polymers, including dimeric and trimeric forms, which dissociate to the monomer only upon exposure to disulfide-reducing reagents, implying that their formation is dependent upon intermolecular disulfide bonds.	Disulfides	201-210	alpha fetoprotein	Homo sapiens	81-98
70228-5	1977	In addition to the monomeric form of alpha-fetoprotein, we have identified human alpha-fetoprotein polymers, including dimeric and trimeric forms, which dissociate to the monomer only upon exposure to disulfide-reducing reagents, implying that their formation is dependent upon intermolecular disulfide bonds.	Disulfides	293-302	alpha fetoprotein	Homo sapiens	81-98
142519-4	1977	These observations plus electrophoretic analyses of samples of plasmic digests of CIg indicate that the interchain disulfide bridging in the two chain molecule is located in a segment within approx.	Disulfides	115-124	fibronectin 1	Homo sapiens	82-85
891549-7	1977	Sterically unhindered thiol groups in the rat hemoglobin are thought to react with the usual adduct intermediate in GSH oxidation by diazene (formed from RCON = NCOR + GSH leads to RCON(SG)NHCOR) to produce mixed disulfides, from which GSH is not easily regenerated.	Disulfides	213-223	nuclear receptor co-repressor 1	Rattus norvegicus	161-165
1035218-3	1976	C1s(I) had a molecular weight of 106,000, consisting of H and L chains connected by disulfide bonds; the molecular weights of the chains were 70,000 and 36,000, respectively.	Disulfides	84-93	complement C1s subcomponent	Oryctolagus cuniculus	0-3
863899-0	1977	An interchain disulfide dimer of human growth hormone.	Disulfides	14-23	growth hormone 1	Homo sapiens	39-53
190236-3	1977	Utilizing methyl-5-bromovalerimidate, a disulfide cross-linked conjugate of human placental lactogen (hPL) and diphtheria toxin fragment A (toxin A) was synthesized.	Disulfides	40-49	chorionic somatomammotropin hormone 2	Homo sapiens	82-100
1009954-0	1976	Ca2+, K+-regulated intramolecular crosslinking of S-100 protein via disulfide bond formation.	Disulfides	68-77	S100 calcium binding protein B	Homo sapiens	50-55
1009954-1	1976	Reaction of the thiol reagent 5,5"-dithio-bis(2-nitrobenzoic acid) (Nbs2) with the brain-specific protein S-100 favours stabilization of the quaternary structure of the protein via disulfide bond formation.	Disulfides	181-190	S100 calcium binding protein B	Homo sapiens	106-111
1009954-3	1976	Ca2+ markedly favours the reaction of S-100 with Nbs2 but inhibits subsequent disulfide bond formation; K+, on the contrary, is much less effective in promoting interaction with Nbs2 but strongly stimulates disulfide bond formation.	Disulfides	207-216	S100 calcium binding protein B	Homo sapiens	38-43
1009954-4	1976	These findings are interpreted assuming that in presence of Ca2+ the three subunits forming the native S-100 protein have two cysteine residues exposed to the solvent but mismatched to form disulfides while in presence of K+ the sulphydryl groups are in a less accessible position to Nbs2 but suitable for S-S bond formation.	Disulfides	190-200	S100 calcium binding protein B	Homo sapiens	103-108
1009954-6	1976	This finding, and the demonstration that both the crosslinked and native S-100 proteins have identical profiles when analyzed by sucrose density centrifugation or gel chromatography indicate that disulfide bond formation occurs among subunits of the same molecule.	Disulfides	196-205	S100 calcium binding protein B	Homo sapiens	73-78
849256-8	1977	Since 2-mercaptoethanol can dissociate the Pa 1 protein into a probable monomeric form, and can dissociate SAPX 2 and SAPX 3 to give SAPX 1, it is probable that Pa 1 and Pa 2 monomers complex with SAPX 1 through disulfide bonds to give SAPX 2 or SAPX 3 types.	Disulfides	212-221	PAXIP1 associated glutamate rich protein 1	Homo sapiens	161-165
920499-0	1977	On the introduction of disulfide crosslinks into fibrous proteins and bovine serum albumin.	Disulfides	23-32	albumin	Homo sapiens	77-90
22044-2	1977	Behavior of sulfhydryl and disulfide groups in alkali-treated beta-lactoglobulin and alpha-lactalbumin].	Disulfides	27-36	lactalbumin alpha	Homo sapiens	85-102
1035218-4	1976	On the other hand, C1s(II), with a molecular weight of 72,000, consisted of two chains each with a molecular weight of about 37,000, which were also connected by disulfide bonds.	Disulfides	162-171	complement C1s subcomponent	Oryctolagus cuniculus	19-22
1002996-13	1976	Additional similarities between the C3a and C5a molecules include length of the polypeptide chain, number of disulfide bonds and an absence of tryptophan residues.	Disulfides	109-118	complement C5a receptor 1	Homo sapiens	44-47
999809-8	1976	Cyanogen bromide reaction of intact haptoglobin 1-1 resulted in the isolation of a beta-chain fragment, CNBr III, covalently attached to the intact alpha1 chain by a single disulfide bond.	Disulfides	173-182	haptoglobin	Homo sapiens	36-47
1276220-5	1976	Reagents capable of oxidizing SH groups to disulfides (tetrathionate, o-iodosobenzoate and hydroquinone) even render susceptible to pancreatic phospholipase A2 phosphatidylserine, a phospholipid supposed to be entirely located in the inner lipid layer of the membrane.	Disulfides	43-53	phospholipase A2 group IB	Homo sapiens	143-159
1085169-1	1976	alpha 1-Antitrypsin phenotypes Pi M and Z, purified by the thiol-disulfide exchange procedure, were desialylated by treatment with neuraminidase covalently coupled to Sepharose and used as acceptors of sialic acid in an assay system for serum sialic acid transferase (CMP-N-acetylneuraminate:D-galactosyl-glycoprotein N-acetylneuraminyltransferase, EC 2.4.99.1) activity.	Disulfides	65-74	serpin family A member 1	Homo sapiens	0-19
1085583-0	1976	alpha-1 Antitrypsin phenotypes determined by isoelectric focusing of the cysteine-antitrypsin mixed disulfide in serum.	Disulfides	100-109	serpin family A member 1	Homo sapiens	0-19
972143-1	1976	Human haptoglobin (Hp), a hemoglobin-binding glycoprotein containing two types of polypeptide chains, alpha and beta, in equimolar amounts linked by disulfide bonds, exists in three major phenotypes determined by the properties of the alpha chain: Hp 1-1 (alpha1), Hp 2-2 (alpha2), and Hp 2-1 (alpha1 and alpha2).	Disulfides	149-158	haptoglobin	Homo sapiens	6-17
955085-0	1976	Reactivity and biological importance of the disulfide bonds in human growth hormone.	Disulfides	44-53	growth hormone 1	Homo sapiens	69-83
776964-2	1976	Native tryptophanyl-tRNA synthetase purified from Escherichia coli B has on each identical subunit a single thiol group which rapidly forms a mixed disulfide with a thionitrobenzoate moiety of 5,5"-dithiobis(2-nitrobenzoic acid).	Disulfides	148-157	tryptophanyl-tRNA synthetase 1	Homo sapiens	7-35
1278162-7	1976	After reduction and carbamidomethylation of the disulfide bonds in thrombin modified ovine growth hormone, the two fragments (residues 1--133 and 134--191) were isolated.	Disulfides	48-57	growth hormone 1	Homo sapiens	91-105
815121-5	1976	These results indicate that the sequential degradative pathway is operative, both at low and high concentrations of insulin, in isolated liver cells, i.e., the insulin is first split at the disulfide bonds by glutathione-insulin transhydrogenase (GIT) into A and B chains, followed by proteolysis of the resultant polypeptides, and that this system might be used for well-defined studies of factors controlling insulin metabolism.	Disulfides	190-199	insulin	Homo sapiens	116-123
1254590-8	1976	Accessibility to tryptic hydrolysis and susceptibility of the disulfide bonds to reduction were increased in the derivative relative to lysozyme.	Disulfides	62-71	lysozyme	Homo sapiens	136-144
936108-0	1976	Disulfide bridges in nh2 -terminal part of human fibrinogen.	Disulfides	0-9	fibrinogen beta chain	Homo sapiens	49-59
943180-2	1976	These fragments were the three-chain, NH2-terminal disulfide knot (N-DSK) produced by CNBr cleavage of fibrinogen, the reduced, carboxymethyl Aalpha chain portion of the N-DSK, and fragment E produced by plasmin digestion of fibrinogen.	Disulfides	51-60	fibrinogen beta chain	Homo sapiens	103-113
943180-2	1976	These fragments were the three-chain, NH2-terminal disulfide knot (N-DSK) produced by CNBr cleavage of fibrinogen, the reduced, carboxymethyl Aalpha chain portion of the N-DSK, and fragment E produced by plasmin digestion of fibrinogen.	Disulfides	51-60	fibrinogen beta chain	Homo sapiens	225-235
815121-5	1976	These results indicate that the sequential degradative pathway is operative, both at low and high concentrations of insulin, in isolated liver cells, i.e., the insulin is first split at the disulfide bonds by glutathione-insulin transhydrogenase (GIT) into A and B chains, followed by proteolysis of the resultant polypeptides, and that this system might be used for well-defined studies of factors controlling insulin metabolism.	Disulfides	190-199	insulin	Homo sapiens	160-167
815121-5	1976	These results indicate that the sequential degradative pathway is operative, both at low and high concentrations of insulin, in isolated liver cells, i.e., the insulin is first split at the disulfide bonds by glutathione-insulin transhydrogenase (GIT) into A and B chains, followed by proteolysis of the resultant polypeptides, and that this system might be used for well-defined studies of factors controlling insulin metabolism.	Disulfides	190-199	insulin	Homo sapiens	160-167
1195561-0	1975	Role of the disulfide bridge and the C-terminal tripeptide in the antidiuretic action of vasopressin in man and the rat.	Disulfides	12-21	arginine vasopressin	Homo sapiens	89-100
1253791-2	1976	A complex between secretory component and an immunoglobulin A (IgA) myeloma dimer has been studied in vitro as a model to elucidate the mechanism of the formation of disulfide bonds during assembly in vivo of secretory immunoglobin A.	Disulfides	166-175	CD79a molecule	Homo sapiens	45-61
1253791-2	1976	A complex between secretory component and an immunoglobulin A (IgA) myeloma dimer has been studied in vitro as a model to elucidate the mechanism of the formation of disulfide bonds during assembly in vivo of secretory immunoglobin A.	Disulfides	166-175	CD79a molecule	Homo sapiens	63-66
1253791-4	1976	The SH-groups on IgA most likely exist as a result of incomplete oxidation of some intra-or interchain disulfide bonds of the molecule, analogous to what has been suggested for IgG.	Disulfides	103-112	CD79a molecule	Homo sapiens	17-20
1253791-5	1976	Several types of evidence indicated that the disulfide bonds between secretory component and IgA are formed after the noncovalent association of the two proteins by a sulfhydryl group-disulfide bond exchange reaction, in which the small amount of free sulfhydryl groups on the IgA dimer initiate the reaction by reducing a reactive disulfide bond on secretory component.	Disulfides	45-54	CD79a molecule	Homo sapiens	93-96
1253791-5	1976	Several types of evidence indicated that the disulfide bonds between secretory component and IgA are formed after the noncovalent association of the two proteins by a sulfhydryl group-disulfide bond exchange reaction, in which the small amount of free sulfhydryl groups on the IgA dimer initiate the reaction by reducing a reactive disulfide bond on secretory component.	Disulfides	45-54	CD79a molecule	Homo sapiens	277-280
1253791-5	1976	Several types of evidence indicated that the disulfide bonds between secretory component and IgA are formed after the noncovalent association of the two proteins by a sulfhydryl group-disulfide bond exchange reaction, in which the small amount of free sulfhydryl groups on the IgA dimer initiate the reaction by reducing a reactive disulfide bond on secretory component.	Disulfides	184-193	CD79a molecule	Homo sapiens	93-96
1253791-5	1976	Several types of evidence indicated that the disulfide bonds between secretory component and IgA are formed after the noncovalent association of the two proteins by a sulfhydryl group-disulfide bond exchange reaction, in which the small amount of free sulfhydryl groups on the IgA dimer initiate the reaction by reducing a reactive disulfide bond on secretory component.	Disulfides	184-193	CD79a molecule	Homo sapiens	277-280
1253791-5	1976	Several types of evidence indicated that the disulfide bonds between secretory component and IgA are formed after the noncovalent association of the two proteins by a sulfhydryl group-disulfide bond exchange reaction, in which the small amount of free sulfhydryl groups on the IgA dimer initiate the reaction by reducing a reactive disulfide bond on secretory component.	Disulfides	184-193	CD79a molecule	Homo sapiens	93-96
1253791-5	1976	Several types of evidence indicated that the disulfide bonds between secretory component and IgA are formed after the noncovalent association of the two proteins by a sulfhydryl group-disulfide bond exchange reaction, in which the small amount of free sulfhydryl groups on the IgA dimer initiate the reaction by reducing a reactive disulfide bond on secretory component.	Disulfides	184-193	CD79a molecule	Homo sapiens	277-280
1253791-6	1976	This exchange reaction, which thus proceeds by the mechanism of so-called disulfide interchange reactions, requires certain conformational features of one or both of the proteins and leads to the formation of presumably two new interchain disulfide bonds between secretory component and IgA.	Disulfides	74-83	CD79a molecule	Homo sapiens	287-290
1253791-6	1976	This exchange reaction, which thus proceeds by the mechanism of so-called disulfide interchange reactions, requires certain conformational features of one or both of the proteins and leads to the formation of presumably two new interchain disulfide bonds between secretory component and IgA.	Disulfides	239-248	CD79a molecule	Homo sapiens	287-290
1249422-2	1976	The acquisition of ability to activate C1s was associated with, and paralleled by, cleavage of each of the two noncovalently bonded 95,000 dalton chains of the molecule into disulfide linked subunits of 60,000 and 35,000 daltons, respectively.	Disulfides	174-183	complement C1s	Homo sapiens	39-42
974159-8	1976	Amino acid analysis and chemical determinations were performed: cathepsin D is a glycoprotein (2 or 3 osamine residues) including 344 amino acids and 4 disulfide bonds.	Disulfides	152-161	CTSD	Equus caballus	64-75
1180968-15	1975	The two disulfides 64-80 and 76-94 bring these two parts of the lysozyme molecule into a single reactive site.	Disulfides	8-18	lysozyme	Homo sapiens	64-72
54917-3	1976	Detergent solubilized H-2 antigens (molecular weight 116,000) consist of two disulfide-linked heavy chains (46,000 daltons) and two monocovalently associated light chains (12,000 daltons).	Disulfides	77-86	histocompatibility-2, MHC	Mus musculus	22-25
241414-2	1975	Reduction of lysozyme by diborane, followed by air oxidation of the reduced disulfides and chromatography on CM-cellulose, yielded a homogeneous derivative.	Disulfides	76-86	lysozyme	Homo sapiens	13-21
1156583-7	1975	The results are interpreted as indicating that immunoreactivity is lost after reduction of only one of the disulfide bonds of insulin whereas the two interchain disulfide linkages must be broken to produce the trichloroacetic acid-soluble A chain.	Disulfides	107-116	insulin	Homo sapiens	126-133
241414-4	1975	Correct re-forming of the disulfide bonds was demonstrated by peptide mapping of the tryptic hydrolysates of the derivative and lysozyme without breaking the disulfide bonds, followed by identification of the disulfide-containing peptides.	Disulfides	26-35	lysozyme	Homo sapiens	128-136
241414-6	1975	Preparations of the two-disulfide fragment from lysozyme and derivative had equal inhibitory activities (26 or 32%) of the reaction of lysozyme with two homologous antisera.	Disulfides	24-33	lysozyme	Homo sapiens	48-56
241414-6	1975	Preparations of the two-disulfide fragment from lysozyme and derivative had equal inhibitory activities (26 or 32%) of the reaction of lysozyme with two homologous antisera.	Disulfides	24-33	lysozyme	Homo sapiens	135-143
1158872-4	1975	CI globulin apparently consists of two polypeptide chains, each of molecular weight 2.0 x 10(5), held together by disulfide bonds.	Disulfides	114-123	fibronectin 1	Homo sapiens	0-11
1164516-8	1975	However, their disulfide bonds were slightly more accessible to reduction than lysozyme, with the increase being somewhat higher in derivatives I, II and III.	Disulfides	15-24	lysozyme	Homo sapiens	79-87
57886-0	1975	Isolation and immunological characterization of a disulfide loop region in human fibrinogen alpha chain.	Disulfides	50-59	fibrinogen alpha chain	Homo sapiens	81-103
1213676-3	1975	After cleavage of the disulfide bridges, reoxidation in very dilute solution reconstitutes about 60% of the original insulin activity.	Disulfides	22-31	insulin	Homo sapiens	117-124
126081-1	1975	Implications for the disulfide structure of fibrinogen.	Disulfides	21-30	fibrinogen beta chain	Homo sapiens	44-54
126081-8	1975	The data are compatible with a fibrinogen molecule in which the two halves are linked by a single locus of disulfide bonds at the amino terminus and with the asymmetric hypothesis of plasmic degradation to Fragments X, Y, D and E.	Disulfides	107-116	fibrinogen beta chain	Homo sapiens	31-41
1156583-8	1975	The results of the NADPH-coupled assay suggest that all three disulfide bonds of insulin are possible substrates for the enzyme.	Disulfides	62-71	insulin	Homo sapiens	81-88
1159056-3	1975	The results indicate that the existence of big GH is dependent upon the formation of inter-polypeptide chain disulfide bonds.	Disulfides	109-118	growth hormone 1	Homo sapiens	47-49
1137436-5	1975	Methyl ozonides catalyzed the formation of disulfide-linked interchain polymers between hemoglobin and ovalbumin.	Disulfides	43-52	serine (or cysteine) peptidase inhibitor, clade B, member 1, pseudogene	Mus musculus	103-112
125109-2	1975	Molecular model of the plasmin-resistant disulfide knot in monomeric fragment D. A mixture of fragments D, derived from fibrinogen by plasmic degradation, was S-reduced and carboxymethylated.	Disulfides	41-50	fibrinogen beta chain	Homo sapiens	120-130
1096943-9	1975	When bovine serum albumin was coupled to palmityl-aminoethylamino-agarose and digested with trypsin, two fragments were obtained: (a) peptide 115-184, containing the highly aromatic disulfide loop 3 of Brown"s model, and (b) a larger fragment, residues 377-581, containing disulfide loops 7-9.	Disulfides	182-191	albumin	Homo sapiens	12-25
237269-5	1975	The effect of calcium on Brdicka currents of bovine serum albumin in the absence of urea is attributed to an orientation of the protein on the surface of the electrode such that all disulfide groups are reduced and with other ligands can complex with Co(ii).	Disulfides	182-191	albumin	Homo sapiens	58-65
47881-0	1975	Biologic significance of disulfide bonds in human IgE molecules.	Disulfides	25-34	immunoglobulin heavy constant epsilon	Homo sapiens	50-53
47881-4	1975	The sensitizing activity of IgE did not change following reduction in 1 mM DTT, which split inter-heavy-light chain disulfide bond.	Disulfides	116-125	immunoglobulin heavy constant epsilon	Homo sapiens	28-31
47881-15	1975	Reduction of IgE with 10 mM DTT followed by alkylation resulted in cleavage of 5 disulfide bonds, which is accompanied by a loss of both sensitizing and blocking activities.	Disulfides	81-90	immunoglobulin heavy constant epsilon	Homo sapiens	13-16
125419-1	1975	Reduction and carbamidomethylation of the intrachain disulfide bridges of human growth hormone did not destroy its ability to stimulate weight gain or cartilage metabolism in hypophysectomized rats.	Disulfides	53-62	growth hormone 1	Homo sapiens	80-94
1126937-8	1975	These results suggest that J chain is disulfide-bonded to only two of the subunits of polymeric IgA and that the remaining subunits in the higher polymers are disulfide-bonded one to the other.	Disulfides	38-47	CD79a molecule	Homo sapiens	96-99
1170876-1	1975	Kinetic studies have been made with glutathione-insulin transhydrogenase, an enzyme which degrades insulin by promoting cleavage of its disulfide bonds via sulfhydryl-disulfide interchange.	Disulfides	136-145	insulin	Homo sapiens	48-55
49088-0	1975	Immunochemistry of the thrombin-altered NH2-terminal disulfide knot of human fibrinogen.	Disulfides	53-62	coagulation factor II, thrombin	Homo sapiens	23-31
1138882-7	1975	Such behavior suggested that cold-insoluble globulin is a multichain molecule whose subunit chains are linked by disulfide bridging.	Disulfides	113-122	fibronectin 1	Homo sapiens	29-52
1138882-8	1975	Strong support for this conclusion was obtained from electrophoretic analyses in gels containing dodecylsulfate, in that cold-insoluble globulin manifested an increased rate of migration after reduction of disulfide bridges.	Disulfides	206-215	fibronectin 1	Homo sapiens	121-144
49088-0	1975	Immunochemistry of the thrombin-altered NH2-terminal disulfide knot of human fibrinogen.	Disulfides	53-62	fibrinogen beta chain	Homo sapiens	77-87
1238375-0	1975	Selective reduction and alkylation of the COOH-terminal disulfide bridge in bovine growth hormone.	Disulfides	56-65	growth hormone 1	Homo sapiens	83-97
123195-1	1975	The biologically active component of plasmin digested human growth hormone consisted of residues 1-134 attached to residues 141-191 by the disulfide bond between residues 53 and 165.	Disulfides	139-148	growth hormone 1	Homo sapiens	60-74
234501-6	1975	From the light chain reactions obtained with isolated alpha1-AT and albumin it is concluded that alpha1-AT has a disulfide which efficiently interchanges with monomeric, light chain thiolate ions released from thionitrobenzoate derivates of light chains and that on interchange with the derivatized light chains albumin releases more free light chains into the solution than are bound to albumin.	Disulfides	113-122	serpin family A member 1	Homo sapiens	54-63
234501-6	1975	From the light chain reactions obtained with isolated alpha1-AT and albumin it is concluded that alpha1-AT has a disulfide which efficiently interchanges with monomeric, light chain thiolate ions released from thionitrobenzoate derivates of light chains and that on interchange with the derivatized light chains albumin releases more free light chains into the solution than are bound to albumin.	Disulfides	113-122	serpin family A member 1	Homo sapiens	97-106
234501-10	1975	The complexes are formed through thiol-disulfide interchange though neither the disulfide of native alpha1-AT nor the thiols of prealbumin is available for reaction with DTNB.	Disulfides	39-48	serpin family A member 1	Homo sapiens	100-109
1182213-2	1975	After purification, human transcortin trended to polymerize rapidly, with participation of both non covalent bonds and one disulfide bridge per dimer.	Disulfides	123-132	serpin family A member 6	Homo sapiens	26-37
1238375-1	1975	Conditions leading to the cleavage of both disulfide bridges in human growth hormone caused the reduction of only one disulfide bond in bovine growth hormone.	Disulfides	43-52	growth hormone 1	Homo sapiens	70-84
1238375-1	1975	Conditions leading to the cleavage of both disulfide bridges in human growth hormone caused the reduction of only one disulfide bond in bovine growth hormone.	Disulfides	43-52	growth hormone 1	Homo sapiens	143-157
1238375-1	1975	Conditions leading to the cleavage of both disulfide bridges in human growth hormone caused the reduction of only one disulfide bond in bovine growth hormone.	Disulfides	118-127	growth hormone 1	Homo sapiens	70-84
1238375-1	1975	Conditions leading to the cleavage of both disulfide bridges in human growth hormone caused the reduction of only one disulfide bond in bovine growth hormone.	Disulfides	118-127	growth hormone 1	Homo sapiens	143-157
4609936-0	1974	Facile assignment of disulfide bonds in ovine lactogenic hormone and human growth hormone.	Disulfides	21-30	growth hormone 1	Homo sapiens	75-89
4597069-0	1974	Simultaneous reduction and mercuration of disulfide bond A6-A11 of insulin by monovalent mercury.	Disulfides	42-51	insulin	Homo sapiens	67-74
4209784-0	1974	Evidence for the role of disulfide bonds in the masking of chromophore groups in bovine kappa-casein.	Disulfides	25-34	casein kappa	Bos taurus	88-100
4443293-0	1974	[Total synthesis of human insulin under directed formation of the disulfide bonds].	Disulfides	66-75	insulin	Homo sapiens	26-33
4741275-1	1973	Insulin fragments with intact disulfide bridges A20-B19].	Disulfides	30-39	insulin	Homo sapiens	0-7
4807800-0	1973	[Preparation and properties of mixed disulfides of insulin with glutathione and thioglycollic acid (author"s transl)].	Disulfides	37-47	insulin	Homo sapiens	51-58
4807801-0	1973	Dissociation of fibrinogen and fibrin peptide chains by partial cleavage of disulfide bonds.	Disulfides	76-85	fibrinogen beta chain	Homo sapiens	16-26
4700342-0	1973	The half-molecule of haptoglobin: studies on the product obtained by the selective cleavage of a haptoglobin disulfide.	Disulfides	109-118	haptoglobin	Homo sapiens	21-32
4700342-0	1973	The half-molecule of haptoglobin: studies on the product obtained by the selective cleavage of a haptoglobin disulfide.	Disulfides	109-118	haptoglobin	Homo sapiens	97-108
5315642-0	1971	Influence of the complex formation between trypsin and bovine basic trypsin inhibitor on the reactivity of certain disulfide bonds.	Disulfides	115-124	trophoblast Kunitz domain protein 1	Bos taurus	68-85
5564392-12	1971	Formation of fibrinogen degradation products was monitored by SDS-polyacrylamide gel electrophoresis of the corresponding fibrins after reduction of disulfide bonds (a method capable of distinguishing alpha-, beta- and gamma-chains).	Disulfides	149-158	fibrinogen beta chain	Homo sapiens	13-23
5546371-0	1971	[Synthesis of insulin fragments with disulfide bridges between intact chains A20-B19].	Disulfides	37-46	insulin	Homo sapiens	14-21
4097521-0	1970	Phosphorylation coupled to oxidation of thiol groups (GSH) by cytochrome c with disulfide (GSSG) as an essential catalyst.	Disulfides	80-89	cytochrome c, somatic	Homo sapiens	62-74
4319825-0	1970	Phosphorylation coupled to oxidation of thiol groups (GSH) by cytochrome c with disulfide (GSSG) as an essential catalyst.	Disulfides	80-89	cytochrome c, somatic	Homo sapiens	62-74
5415495-2	1970	Synthesis of the insulin sequence (B 17-30)-2 as a symmetrical disulfide and of the insulin B-chain as a disulfide polymer].	Disulfides	63-72	NADH:ubiquinone oxidoreductase subunit A12	Homo sapiens	17-45
5474790-0	1970	Phosphorylation coupled to oxidation of thiol groups (GSH) by cytochrome c with disulfide (GSSG) as an essential catalyst.	Disulfides	80-89	cytochrome c, somatic	Homo sapiens	62-74
5474791-0	1970	Phosphorylation coupled to oxidation of thiol groups (GSH) by cytochrome c with disulfide (GSSG) as an essential catalyst.	Disulfides	80-89	cytochrome c, somatic	Homo sapiens	62-74
5415499-2	1970	Synthesis of the insulin sequence (B1-26)-2 as a symmetrical disulfide].	Disulfides	61-70	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	17-43
4974308-22	1969	It is believed that the substitution of a strongly basic amino acid with a neutral hydroxy acid may result in considerable conformational changes in the N-terminal disulfide knot of fibrinogen which might affect the "active site" for polymerization.	Disulfides	164-173	fibrinogen beta chain	Homo sapiens	182-192
5387562-0	1969	Reduction and reoxidation of the disulfide bonds of bovine serum albumin.	Disulfides	33-42	albumin	Homo sapiens	59-72
5260926-3	1969	Both acetylcholinesterase and the macromolecular receptor of acetylcholine thus contain disulfide bonds.	Disulfides	88-97	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-25
19873643-5	1969	A disulfide bond breaking agent, dithiothreitol (DTT) alters in a parallel manner the reaction of AChE and the excitable membrane of the electroplax to TDF.	Disulfides	2-11	acetylcholinesterase (Cartwright blood group)	Homo sapiens	98-102
19873643-7	1969	Both AChE and the acetylcholine receptor thus contain disulfide bonds-they are closely related but not necessarily identical proteins.	Disulfides	54-63	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
14292170-2	1965	EFFECT OF HEAT DENATURATION OF BOVINE SERUM ALBUMIN (BSA) ON SULFHYDRYL AND REACTIVE DISULFIDE CONTENT.	Disulfides	85-94	albumin	Homo sapiens	38-51
5623710-0	1967	[Some properties of insulin with reduced and reoxidized disulfide bonds].	Disulfides	56-65	insulin	Homo sapiens	20-27
5844464-2	1965	Synthesis of a fragment of insulin containing the intrachain disulfide bridge.	Disulfides	61-70	insulin	Homo sapiens	27-34
5762967-0	1969	Photolysis of the disulfide linkages in insulin.	Disulfides	18-27	insulin	Homo sapiens	40-47
5971868-2	1966	The disulfide and sulfhydryl content of beef-liver catalase].	Disulfides	4-13	catalase	Homo sapiens	51-60
6006643-0	1966	The amino acid sequences around the disulfide bonds of soybean trypsin inhibitor.	Disulfides	36-45	kunitz trypsin protease inhibitor	Glycine max	63-80
14275603-0	1965	RUPTURE OF FIBRINOGEN DISULFIDE BONDS BY CYSTEINE.	Disulfides	22-31	fibrinogen beta chain	Homo sapiens	11-21
14284718-0	1965	AN UNUSUAL DISULFIDE BOND IN STREPTOCOCCAL PROTEINASE.	Disulfides	11-20	endogenous retrovirus group K member 25	Homo sapiens	43-53
5836519-0	1964	Necessity of the disulfide bond of vasopressin for antidiuretic activity.	Disulfides	17-26	arginine vasopressin	Homo sapiens	35-46
14189889-0	1964	INTERACTION OF PHOSPHOROTHIOATE WITH THE DISULFIDE BONDS OF RIBONUCLEASE AND LYSOZYME.	Disulfides	41-50	lysozyme	Homo sapiens	77-85
14173732-0	1964	[SPLITTING DISULFIDE FIBRINOGEN BONDS WITH CYSTEINE].	Disulfides	11-20	fibrinogen beta chain	Homo sapiens	21-31
14040204-0	1961	Reaction of reduced disulfide bonds in alpha-lactalbumin and beta-lactoglobulin with acrylonitrile.	Disulfides	20-29	lactalbumin alpha	Homo sapiens	39-56
14042998-5	1963	On the basis of the results it was postulated that hormone-receptor interaction can be considered a two-step process: (a) The binding or attachment of hormone to receptor site through ionic, hydrogen, and hydrophobic bonds and (b) a disulfide interchange reaction between hormonal disulfide and receptor sulfhydryl.	Disulfides	233-242	nuclear receptor subfamily 4 group A member 1	Homo sapiens	51-67
14042998-5	1963	On the basis of the results it was postulated that hormone-receptor interaction can be considered a two-step process: (a) The binding or attachment of hormone to receptor site through ionic, hydrogen, and hydrophobic bonds and (b) a disulfide interchange reaction between hormonal disulfide and receptor sulfhydryl.	Disulfides	281-290	nuclear receptor subfamily 4 group A member 1	Homo sapiens	51-67
14057350-1	1963	The tyrosyl groups of reduced and carboxymethylated human serum albumin, in which all disulfide bonds are broken, ionize at lower pH than those of native albumin, in spite of the greater negative charge on the protein produced by the S-carboxy-methyl groups.	Disulfides	86-95	albumin	Homo sapiens	58-71
13935833-0	1963	Effect of vasopressin and dehydration on protein-bound sulfhydryl and disulfide groups in renal cells.	Disulfides	70-79	arginine vasopressin	Homo sapiens	10-21
13876609-0	1962	The disulfide-sulfhydryl interchange as a mechanism of insulin action.	Disulfides	4-13	insulin	Homo sapiens	55-62
13628588-0	1958	[Accessibility of disulfide groups of bovine serum albumin].	Disulfides	18-27	albumin	Homo sapiens	51-58
13283114-0	1956	Concept of a common protein moiety, containing disulfide bonds, in prothrombin, prothrombin derivative (autoprothrombin) and thrombin.	Disulfides	47-56	coagulation factor II, thrombin	Homo sapiens	67-78
13283114-0	1956	Concept of a common protein moiety, containing disulfide bonds, in prothrombin, prothrombin derivative (autoprothrombin) and thrombin.	Disulfides	47-56	coagulation factor II, thrombin	Homo sapiens	80-91
13283114-0	1956	Concept of a common protein moiety, containing disulfide bonds, in prothrombin, prothrombin derivative (autoprothrombin) and thrombin.	Disulfides	47-56	coagulation factor II, thrombin	Homo sapiens	70-78
33652022-3	2021	It has been long recognized from in vitro evidence that Txnip forms a disulfide bridge through cysteine 247 (C247) with reduced thioredoxin to inhibit the anti-oxidative properties of thioredoxin.	Disulfides	70-79	thioredoxin interacting protein	Homo sapiens	56-61
33652022-13	2021	CONCLUSION: Txnip is a cysteine-containing redox protein that robustly regulates the thioredoxin system via a disulfide bond-switching mechanism in adult cardiomyocytes.	Disulfides	110-119	thioredoxin interacting protein	Mus musculus	12-17
20285166-0	1947	The relationship of sulfhydryl and disulfide groups to the antigenic power of bovine serum albumin.	Disulfides	35-44	albumin	Homo sapiens	85-98
33933962-6	2021	UPA further inhibited the formation of disulfide bonds of myosin head and increased gel firmness.	Disulfides	39-48	plasminogen activator, urokinase	Gallus gallus	0-3
33780570-13	2021	Bioinformatic and molecular modeling analysis suggests that these changes disrupt a key disulfide bond in the Dkk4 cysteine-rich domain 1 or Dkk4 signal peptide cleavage respectively.	Disulfides	88-97	dickkopf WNT signaling pathway inhibitor 4	Felis catus	110-114
33780570-13	2021	Bioinformatic and molecular modeling analysis suggests that these changes disrupt a key disulfide bond in the Dkk4 cysteine-rich domain 1 or Dkk4 signal peptide cleavage respectively.	Disulfides	88-97	dickkopf WNT signaling pathway inhibitor 4	Felis catus	141-145
34041901-5	2021	Hybrid albumin nanoparticles were assembled via the disulfide reprogramming method and encapsulated paclitaxel (PTX) to formulate PSN-HSA-PTX-IR780.	Disulfides	52-61	albumin	Homo sapiens	7-14
34048659-2	2021	In the present study, we report the neuroprotective effects of disulfide-rich, circular peptides from Clitoria ternatea (C. ternatea) (butterfly pea) on Abeta-induced toxicity in transgenic Caenorhabditis elegans.	Disulfides	63-72	amyloid beta precursor protein	Homo sapiens	153-158
33878389-2	2021	We used human growth hormone (hGH) as target protein that contains two internal disulfide bridges and an N-terminal phenylalanine.	Disulfides	80-89	growth hormone 1	Homo sapiens	14-28
33231477-7	2021	Insulin has disulfide bonds that produce Raman scattering near 513 cm-1, but no tryptophan.	Disulfides	12-21	insulin	Homo sapiens	0-7
34011552-5	2021	This defect is accompanied by reduced expression of two disulfide-linked gH/gL complexes that play crucial roles in viral entry: the heterotrimer of gH/gL with glycoprotein O (gO) and the pentameric complex of gH/gL with UL128, UL130, and UL131.	Disulfides	56-65	envelope glycoprotein UL130	Human betaherpesvirus 5	228-233
34020817-6	2021	The clade A trimer, which we named "BG505 DS-SOSIP.664", contained an engineered disulfide (201C-433C; DS) within gp120, which further stabilized this trimer in a prefusion-closed conformation resistant to CD4-induced triggering.	Disulfides	81-90	CD4 molecule	Homo sapiens	206-209
33974730-5	2021	Native mass spectrometry experiments show that the prochelators form stable disulfide conjugates with bovine serum albumin, thus affording novel bioconjugate prochelator systems.	Disulfides	76-85	albumin	Homo sapiens	109-122
34002274-3	2021	An MIP film for lysozyme was prepared by the copolymerization of {[2-(2-methacrylamido)ethyldithio]ethylcarbamoyl}methoxy acetic acid, a functional monomer possessing a modifiable disulfide bond, with acrylamide and N,N"-methylenebisacrylamide in the presence of lysozyme.	Disulfides	180-189	lysozyme	Homo sapiens	16-24
34002274-4	2021	After the removal of lysozyme, the disulfide bonds were cleaved by treatment with a reductant.	Disulfides	35-44	lysozyme	Homo sapiens	21-29
33231477-8	2021	For insulin-positive cells, we found that the application of multisource correlation analysis revealed a high correlation between insulin mRNA and Raman scattering in the disulfide region.	Disulfides	171-180	insulin	Homo sapiens	4-11
33231477-8	2021	For insulin-positive cells, we found that the application of multisource correlation analysis revealed a high correlation between insulin mRNA and Raman scattering in the disulfide region.	Disulfides	171-180	insulin	Homo sapiens	130-137
33231477-9	2021	In contrast, glucagon has no disulfide bonds but does contain tryptophan.	Disulfides	29-38	glucagon	Homo sapiens	13-21
33157095-1	2021	Whey acidic protein Four-Disulfide Core (WFDC) proteins, such as PI3 and SLPI, inhibit proteases in the epidermis and other tissues.	Disulfides	25-34	secretory leukocyte peptidase inhibitor	Homo sapiens	73-77
32311837-1	2021	In this work, we utilise the disulfide bond structure of insulin and a new benzothiazole Raman probe for the detection of human insulin by surface enhanced Raman spectroscopy (SERS).	Disulfides	29-38	insulin	Homo sapiens	57-64
32311837-1	2021	In this work, we utilise the disulfide bond structure of insulin and a new benzothiazole Raman probe for the detection of human insulin by surface enhanced Raman spectroscopy (SERS).	Disulfides	29-38	insulin	Homo sapiens	128-135
32311837-2	2021	The disulfide bond structure of the insulin was reduced to generate free sulfhydryl as a terminal group.	Disulfides	4-13	insulin	Homo sapiens	36-43
33601275-8	2021	MS with 18O-labeling has allowed identification of the residues involved in some cases (e.g. Cys25 from the Cys25-Cys80 disulfide in beta-2-microglobulin, with Cys149 or Cys244 of GAPDH).	Disulfides	120-129	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	180-185
33689304-3	2021	However, the chemical synthesis of insulin"s intricate 51-amino acid, two-chain, three-disulfide bond structure, together with the poor physicochemical properties of both the individual chains and the hormone itself, has long represented a major challenge to organic chemists.	Disulfides	87-96	insulin	Homo sapiens	35-42
33662873-5	2021	Early evidence in literature suggests that the thiol to disulfide balance of critical Cys residues of the COVID-19 spike protein and the ACE-2 receptor may influence the risk of infection and the severity of the disease, with a more oxidizing environment producing the worst prognosis.	Disulfides	56-65	covid-19 spike protein	None	106-128
33714740-0	2021	Crosslinking of human plasma C-reactive protein to human serum albumin via disulfide bond oxidation.	Disulfides	75-84	C-reactive protein	Homo sapiens	29-47
33714740-0	2021	Crosslinking of human plasma C-reactive protein to human serum albumin via disulfide bond oxidation.	Disulfides	75-84	albumin	Homo sapiens	63-70
33714740-6	2021	Here we demonstrate that photooxidation, or reaction with the biological oxidants HOCl and ONOOH, of the single disulfide present in the major human plasma inflammatory protein, C-reactive protein (CRP) can give rise to reversible disulfide bond formation with human serum albumin (HSA).	Disulfides	112-121	C-reactive protein	Homo sapiens	178-196
33714740-6	2021	Here we demonstrate that photooxidation, or reaction with the biological oxidants HOCl and ONOOH, of the single disulfide present in the major human plasma inflammatory protein, C-reactive protein (CRP) can give rise to reversible disulfide bond formation with human serum albumin (HSA).	Disulfides	112-121	C-reactive protein	Homo sapiens	198-201
33714740-6	2021	Here we demonstrate that photooxidation, or reaction with the biological oxidants HOCl and ONOOH, of the single disulfide present in the major human plasma inflammatory protein, C-reactive protein (CRP) can give rise to reversible disulfide bond formation with human serum albumin (HSA).	Disulfides	112-121	albumin	Homo sapiens	267-280
33714740-6	2021	Here we demonstrate that photooxidation, or reaction with the biological oxidants HOCl and ONOOH, of the single disulfide present in the major human plasma inflammatory protein, C-reactive protein (CRP) can give rise to reversible disulfide bond formation with human serum albumin (HSA).	Disulfides	231-240	C-reactive protein	Homo sapiens	178-196
33714740-6	2021	Here we demonstrate that photooxidation, or reaction with the biological oxidants HOCl and ONOOH, of the single disulfide present in the major human plasma inflammatory protein, C-reactive protein (CRP) can give rise to reversible disulfide bond formation with human serum albumin (HSA).	Disulfides	231-240	C-reactive protein	Homo sapiens	198-201
33714740-6	2021	Here we demonstrate that photooxidation, or reaction with the biological oxidants HOCl and ONOOH, of the single disulfide present in the major human plasma inflammatory protein, C-reactive protein (CRP) can give rise to reversible disulfide bond formation with human serum albumin (HSA).	Disulfides	231-240	albumin	Homo sapiens	267-280
33905803-2	2021	To address these issues, we reported in this study a one-pot preparation of dual-redox sensitive, stabilized supramolecular nanocontainers for potential programmable drug release by self-crosslinking of a multifunctional beta-CD unit that integrates a host cavity for oxidation-mediated reversible complexation with ferrocence (Fc) guest molecule and lipoic acids (LAs)-decorated primary and secondary faces for reversible in-situ crosslinking by the reducible disulfide links.	Disulfides	461-470	ACD shelterin complex subunit and telomerase recruitment factor	Homo sapiens	221-228
33785835-1	2021	The disulfide isomerase ERp57, originally found in the endoplasmic reticulum, is located in multiple cellular compartments, participates in diverse cell functions and interacts with a huge network of binding partners.	Disulfides	4-13	protein disulfide isomerase family A member 3	Homo sapiens	24-29
33923808-6	2021	Using culture media from motor neuron-like cells, NSC-34, extracellular misfolded wild-type, and four ALS-causing SOD1 mutants were characterized as a metal-free, disulfide oxidized form of SOD1 (apo-SOD1S-S).	Disulfides	163-172	superoxide dismutase 1	Homo sapiens	114-118
33923808-6	2021	Using culture media from motor neuron-like cells, NSC-34, extracellular misfolded wild-type, and four ALS-causing SOD1 mutants were characterized as a metal-free, disulfide oxidized form of SOD1 (apo-SOD1S-S).	Disulfides	163-172	superoxide dismutase 1	Homo sapiens	190-194
33854312-3	2021	In this system, sonosensitizers and catalase were encapsulated in disulfide-bridged mesoporous organosilicon nanoparticles with high loading, which protected the activity of catalase and ensure the stability of sonosensitizers and enzyme.	Disulfides	66-75	catalase	Homo sapiens	36-44
33854312-3	2021	In this system, sonosensitizers and catalase were encapsulated in disulfide-bridged mesoporous organosilicon nanoparticles with high loading, which protected the activity of catalase and ensure the stability of sonosensitizers and enzyme.	Disulfides	66-75	catalase	Homo sapiens	174-182
33629764-8	2021	Further analysis revealed that ASFV p15 forms disulfide-linked trimers between the Cys9 from one protomer and Cys30 from other protomer.	Disulfides	46-55	cyclin dependent kinase inhibitor 2B	Homo sapiens	36-39
33823404-0	2021	Synthesis and evaluation of disulfide-rich cyclic alpha-conotoxin [S9A]TxID analogues as novel alpha3beta4 nAChR antagonists.	Disulfides	28-37	cholinergic receptor nicotinic alpha 4 subunit	Homo sapiens	107-112
33731757-0	2021	Disulfide HMGB1 acts via TLR2/4 receptors to reduce the numbers of oligodendrocyte progenitor cells after traumatic injury in vitro.	Disulfides	0-9	toll like receptor 2	Homo sapiens	25-31
33692125-4	2021	We identify a pathological signaling cascade whereby reactive nitrogen species cause S-nitrosylation of TDP-43 (forming SNO-TDP-43) to facilitate disulfide linkage and consequent TDP-43 aggregation.	Disulfides	146-155	TAR DNA binding protein	Homo sapiens	104-110
33692125-4	2021	We identify a pathological signaling cascade whereby reactive nitrogen species cause S-nitrosylation of TDP-43 (forming SNO-TDP-43) to facilitate disulfide linkage and consequent TDP-43 aggregation.	Disulfides	146-155	TAR DNA binding protein	Homo sapiens	120-130
33692125-6	2021	Aggregated TDP-43 triggers additional nitrosative stress, representing positive feed forward leading to further SNO-TDP-43 formation and disulfide-linked oligomerization/aggregation.	Disulfides	137-146	TAR DNA binding protein	Homo sapiens	11-17
33855279-2	2021	Herein, we developed an in vitro system for directly monitoring PDI- or ERp46-catalyzed disulfide bond formation in ribosome-associated nascent chains of human serum albumin.	Disulfides	88-97	albumin	Homo sapiens	160-173
33727589-3	2021	Gal-9 also binds to protein disulfide isomerase (PDI), maintains PDI on surface of T cells, and increases free thiols in the disulfide/thiol cycles.	Disulfides	28-37	lectin, galactose binding, soluble 9	Mus musculus	0-5
33459316-5	2021	After Apt29@MNPs specifically purify and enrich thrombin from biological samples, they can form a nano "sandwich structure" when Apt15@ss@QDs are added, resulting in the release of the mass barcode for LC-MS/MS analysis via the cutting of the disulfide bond.	Disulfides	243-252	coagulation factor II, thrombin	Homo sapiens	48-56
33307764-3	2021	Methods: LC-MS/MS was used to identify S-sulfhydrated cysteines in endothelial cell proteins and beta3 integrin intra-protein disulfide bond rearrangement.	Disulfides	126-135	T cell immune regulator 1, ATPase H+ transporting V0 subunit a3	Homo sapiens	97-102
33190426-4	2021	In the present study, we evaluated an anti-HER2 scFv, which is specific for human epidermal growth receptor 2 (HER2) overexpressed in breast cancer, for functional expression in the cytoplasm of E. coli strains BL21(DE3) and SHuffle T7 Express, the latter of which is genetically engineered for cytoplasmic disulfide bond formation.	Disulfides	307-316	erb-b2 receptor tyrosine kinase 2	Homo sapiens	43-47
33190426-4	2021	In the present study, we evaluated an anti-HER2 scFv, which is specific for human epidermal growth receptor 2 (HER2) overexpressed in breast cancer, for functional expression in the cytoplasm of E. coli strains BL21(DE3) and SHuffle T7 Express, the latter of which is genetically engineered for cytoplasmic disulfide bond formation.	Disulfides	307-316	immunglobulin heavy chain variable region	Homo sapiens	48-52
33190426-4	2021	In the present study, we evaluated an anti-HER2 scFv, which is specific for human epidermal growth receptor 2 (HER2) overexpressed in breast cancer, for functional expression in the cytoplasm of E. coli strains BL21(DE3) and SHuffle T7 Express, the latter of which is genetically engineered for cytoplasmic disulfide bond formation.	Disulfides	307-316	erb-b2 receptor tyrosine kinase 2	Homo sapiens	111-115
33190426-6	2021	We also found that SHuffle T7 Express cells were capable of supporting high-level soluble production of anti-HER2 scFvs with intact disulfide bonds independent of variable domain orientation, providing further evidence that SHuffle T7 Express is a promising host for laboratory and preparative expression of functional scFv antibodies.	Disulfides	132-141	erb-b2 receptor tyrosine kinase 2	Homo sapiens	109-113
33190426-6	2021	We also found that SHuffle T7 Express cells were capable of supporting high-level soluble production of anti-HER2 scFvs with intact disulfide bonds independent of variable domain orientation, providing further evidence that SHuffle T7 Express is a promising host for laboratory and preparative expression of functional scFv antibodies.	Disulfides	132-141	immunglobulin heavy chain variable region	Homo sapiens	114-118
33515755-1	2021	Human serum albumin (HSA) contains 17 disulfides and only one reduced cysteine, Cys34, which can be oxidized to a relatively stable sulfenic acid (HSA-SOH).	Disulfides	38-48	albumin	Homo sapiens	6-19
33679289-0	2020	A Novel SOD1 Intermediate Oligomer, Role of Free Thiols and Disulfide Exchange.	Disulfides	60-69	superoxide dismutase 1	Homo sapiens	8-12
33619784-3	2021	Here, we showed that disulfide-bonded mutants, which prevented integrin alphav beta8 lower leg dissociation, bound ligands with similar level as the wild-type protein, suggesting that alphav beta8 ligand binding did not require lower leg disassociation.	Disulfides	21-30	immunoglobulin kappa variable 2D-23 (pseudogene)	Homo sapiens	79-84
33454336-4	2021	Limited reduction of disulfide bonds resulted in non-covalent aggregation of bovine serum albumin and cleavage of only inter-chain linkages of an antibody that had no effects on its overall structure.	Disulfides	21-30	albumin	Homo sapiens	84-97
32979223-9	2021	These findings led us to propose that ROS levels modulate RAGE and/or TLR4-mediated inflammatory allodynia by regulating the concentrations of disulfide HMGB1 or all-thiol HMGB1.	Disulfides	143-152	advanced glycosylation end product-specific receptor	Mus musculus	58-62
32979223-9	2021	These findings led us to propose that ROS levels modulate RAGE and/or TLR4-mediated inflammatory allodynia by regulating the concentrations of disulfide HMGB1 or all-thiol HMGB1.	Disulfides	143-152	toll-like receptor 4	Mus musculus	70-74
33679289-1	2020	Wild-type human SOD1 forms a highly conserved intra-molecular disulfide bond between C57-C146, and in its native state is greatly stabilized by binding one copper and one zinc atom per monomer rendering the protein dimeric.	Disulfides	62-71	superoxide dismutase 1	Homo sapiens	16-20
33679289-9	2020	Here we further investigate the role of reduction of the native C57-C146 disulfide bond in fibrillation of wild-type hSOD1, firstly through removal of free thiols by paired mutations C6A, C111S (AS-SOD1), and secondly in seeded fibrillation reactions modulated by reductant tris (2-carboxyethyl) phosphine (TCEP).	Disulfides	73-82	superoxide dismutase 1	Homo sapiens	117-122
33679289-10	2020	Fibrillation of AS-SOD1 was dependent upon disulfide reduction and showed classic lag and exponential growth phases compared with wild-type hSOD1 whose fibrillation trajectories were typically somewhat perturbed.	Disulfides	43-52	superoxide dismutase 1	Homo sapiens	19-23
33673243-4	2021	We present models based on small-angle X-ray scattering (SAXS) data that (1) confirm that the mode of binding of inhibitor to an active A3B C-terminal domain construct in the solution state is the same as the mode of binding substrate to inactive mutants of A3A and A3B revealed in X-ray crystal structures and (2) give insight into the disulfide-linked inactive dimer formed under the oxidizing conditions of purification.	Disulfides	337-346	apolipoprotein B mRNA editing enzyme catalytic subunit 3B	Homo sapiens	136-139
33588719-6	2021	TFF1 mainly exists as a monomer with an unusual free thiol group and only minor amounts form a disulfide linked homodimer as well as heterodimers with gastrokine-2 and IgG-Fc-binding protein (FCGBP).	Disulfides	95-104	trefoil factor 1	Homo sapiens	0-4
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	13-22	protein disulfide isomerase family A member 4	Homo sapiens	33-38
33578917-6	2021	Molecular interaction analyses in silico implied that dimeric IgA and albumin interacted not only via disulfide bond formation, but also via noncovalent bonds.	Disulfides	102-111	CD79a molecule	Homo sapiens	62-65
33578917-7	2021	Disulfide bonds were predicted between Cys34 of albumin and Cys311 of IgA, resulting in an oxidized form of albumin.	Disulfides	0-9	CD79a molecule	Homo sapiens	70-73
33541434-4	2021	The protein disulfide isomerase family member ERp57 is one of the main up-regulated proteins in tissue of ALS patients and mutant SOD1 mice, whereas point mutations in ERp57 were described as possible risk factors to develop the disease.	Disulfides	12-21	protein disulfide isomerase family A member 3	Homo sapiens	46-51
33541434-4	2021	The protein disulfide isomerase family member ERp57 is one of the main up-regulated proteins in tissue of ALS patients and mutant SOD1 mice, whereas point mutations in ERp57 were described as possible risk factors to develop the disease.	Disulfides	12-21	superoxide dismutase 1	Homo sapiens	130-134
33539422-12	2021	We also investigated changes in the redox state of HIF-1alpha using PEG-maleimide, which binds to thiols synthesized from disulfide bonds by reduction.	Disulfides	122-131	hypoxia inducible factor 1 subunit alpha	Homo sapiens	51-61
33539422-13	2021	An up-shift in the HIF-1alpha band by the overexpression of PDI was detected, suggesting that PDI formed disulfide bond in HIF-1alpha.	Disulfides	105-114	hypoxia inducible factor 1 subunit alpha	Homo sapiens	19-29
33539422-13	2021	An up-shift in the HIF-1alpha band by the overexpression of PDI was detected, suggesting that PDI formed disulfide bond in HIF-1alpha.	Disulfides	105-114	hypoxia inducible factor 1 subunit alpha	Homo sapiens	123-133
33539422-14	2021	HIF-1alpha oxidized by PDI was not degraded in HSC70-knockdown cells, indicating that the formation of disulfide bond in HIF-1alpha was important for decreases in HIF-1alpha expression.	Disulfides	103-112	hypoxia inducible factor 1 subunit alpha	Homo sapiens	0-10
33539422-14	2021	HIF-1alpha oxidized by PDI was not degraded in HSC70-knockdown cells, indicating that the formation of disulfide bond in HIF-1alpha was important for decreases in HIF-1alpha expression.	Disulfides	103-112	hypoxia inducible factor 1 subunit alpha	Homo sapiens	121-131
33539422-14	2021	HIF-1alpha oxidized by PDI was not degraded in HSC70-knockdown cells, indicating that the formation of disulfide bond in HIF-1alpha was important for decreases in HIF-1alpha expression.	Disulfides	103-112	hypoxia inducible factor 1 subunit alpha	Homo sapiens	121-131
33539422-16	2021	We also demonstrated that PDI formed disulfide bonds in HIF-1alpha 1-245 aa and decreased its expression.	Disulfides	37-46	hypoxia inducible factor 1 subunit alpha	Homo sapiens	56-66
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	13-22	serpin family A member 1	Homo sapiens	214-222
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	185-194	protein disulfide isomerase family A member 4	Homo sapiens	33-38
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	185-194	protein disulfide isomerase family A member 4	Homo sapiens	33-38
32773600-3	2021	Here, we examined whether the action of TLR4-activating, partially reduced disulfide HMGB1 on microglia induces nociceptive behaviors in a sex-dependent manner.	Disulfides	75-84	toll-like receptor 4	Mus musculus	40-44
33136395-11	2021	All four disulfide bonds of lysozyme were determined.	Disulfides	9-18	lysozyme	Homo sapiens	28-36
33446738-2	2021	Here we have found that some AMPs, such as TP4 from fish tilapia, and drugs, such as antipyretic ibuprofen, were bound by bovine serum albumin only in complex with alpha1-antitrypsin which is linked by disulfide bond.	Disulfides	202-211	albumin	Homo sapiens	129-142
33446738-2	2021	Here we have found that some AMPs, such as TP4 from fish tilapia, and drugs, such as antipyretic ibuprofen, were bound by bovine serum albumin only in complex with alpha1-antitrypsin which is linked by disulfide bond.	Disulfides	202-211	serpin family A member 1	Homo sapiens	164-182
33505395-2	2020	However, Pfs48/45 contains multiple disulfide bonds, that are critical for proper folding and induction of transmission-blocking (TB) antibodies.	Disulfides	36-45	pfs48/45	None	9-17
33530504-4	2021	The mechanism involves disulfide bond formation between KEAP1 cysteine residues, NRF2 stabilization and enhanced expression of the gamma-glutamil cysteine ligase regulatory subunit.	Disulfides	23-32	kelch like ECH associated protein 1	Homo sapiens	56-61
33530504-4	2021	The mechanism involves disulfide bond formation between KEAP1 cysteine residues, NRF2 stabilization and enhanced expression of the gamma-glutamil cysteine ligase regulatory subunit.	Disulfides	23-32	NFE2 like bZIP transcription factor 2	Homo sapiens	81-85
33326534-0	2021	Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-beta aggregation.	Disulfides	49-58	S100 calcium binding protein B	Homo sapiens	16-21
33326534-0	2021	Cu2+-binding to S100B triggers polymerization of disulfide cross-linked tetramers with enhanced chaperone activity against amyloid-beta aggregation.	Disulfides	49-58	amyloid beta precursor protein	Homo sapiens	123-135
32698065-1	2020	Reteplase is a deleted variant of human tissue plasminogen activator with a complex structure containing nine disulfide bonds.	Disulfides	110-119	plasminogen activator, tissue type	Homo sapiens	0-9
33161042-8	2021	This suggested that NO-stimulated GC1 contained more bound Cys, potentially disulfide bonds.	Disulfides	76-85	olfactomedin 4	Homo sapiens	34-37
33518643-3	2021	The reaction made it possible to independently construct a disulfide bridge without effecting the existing disulfide bonds, which resulted in a unique approach for the synthesis of human insulin by site-specific disulfide bond formation.	Disulfides	59-68	insulin	Homo sapiens	187-194
33518643-3	2021	The reaction made it possible to independently construct a disulfide bridge without effecting the existing disulfide bonds, which resulted in a unique approach for the synthesis of human insulin by site-specific disulfide bond formation.	Disulfides	107-116	insulin	Homo sapiens	187-194
33518643-3	2021	The reaction made it possible to independently construct a disulfide bridge without effecting the existing disulfide bonds, which resulted in a unique approach for the synthesis of human insulin by site-specific disulfide bond formation.	Disulfides	107-116	insulin	Homo sapiens	187-194
33458528-5	2021	The recombinant scFv fragments of about 30 kDa and a diameter of 5 nm were produced and purified from engineered Escherichia coli that can enhance cytosolic disulfide bond formation.	Disulfides	157-166	immunglobulin heavy chain variable region	Homo sapiens	16-20
33210532-6	2020	Subsequently, the modification of a HER2-targeting Fab with a fluorescein-conjugated variant of DiPODS (DiPODS-PEG4-FITC) reinforced the site-specificity of the reagent, illustrated its ability to rebridge disulfide linkages, and produced an immunoconjugate with in vitro properties superior to those of an analogous construct created using traditional stochastic bioconjugation techniques.	Disulfides	206-215	erb-b2 receptor tyrosine kinase 2	Homo sapiens	36-40
33291690-4	2020	The blood clotting protein, fibrinogen, and the protease inhibitor, alpha2-macroglobulin, exist in multiple disulfide-bonded or covalent states in the circulation.	Disulfides	108-117	fibrinogen beta chain	Homo sapiens	28-38
33030311-5	2020	Acromelic dysplasia subtypes that share symptoms with Marfan syndrome are associated with FBN1-TB5 disulfide disruptions, which are also commonly found in Marfan syndrome.	Disulfides	99-108	transforming growth factor beta regulator 1	Homo sapiens	95-98
33220304-0	2021	Fibrillation of Human Calcitonin and its Analogs: Effects of Phosphorylation and Disulfide Reduction.	Disulfides	81-90	calcitonin related polypeptide alpha	Homo sapiens	22-32
33161042-4	2021	We showed that GC1 activity is modulated via mixed-disulfide bond by protein disulfide isomerase and thioredoxin 1.	Disulfides	51-60	olfactomedin 4	Homo sapiens	15-18
33161042-5	2021	Herein we investigated the novel concept that NO-stimulated GC1 activity is mediated by thiol/disulfide switches and aimed to map the specific Cys that are involved.	Disulfides	94-103	olfactomedin 4	Homo sapiens	60-63
33396541-0	2020	PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly.	Disulfides	14-23	protein disulfide isomerase family A member 2	Homo sapiens	0-3
33396541-7	2020	Herein, the mechanism of PDI-regulated disulfide bond formation is important for understanding not only protein folding and associated diseases, but also the formation of functional biomolecular assembly.	Disulfides	39-48	protein disulfide isomerase family A member 2	Homo sapiens	25-28
33458549-0	2021	Disulfide Cross-Linked Poly(Methacrylic Acid) Iron Oxide Nanoparticles for Efficiently Selective Adsorption of Pb(II) from Aqueous Solutions.	Disulfides	0-9	submaxillary gland androgen regulated protein 3B	Homo sapiens	111-117
33458549-2	2021	In this study, the novel disulfide cross-linked poly(methacrylic acid) iron oxide (Fe3O4@S-S/PMAA) nanoparticles with selective adsorption, improved adsorption capability, and economic reusability were designed and prepared for selective adsorption of Pb(II) ions in aqueous solution.	Disulfides	25-34	submaxillary gland androgen regulated protein 3B	Homo sapiens	252-258
33154160-10	2020	The absence of genetic variation at B24 and other conserved sites near this disulfide bridge-excluded due to beta-cell dysfunction-suggests that insulin has evolved to the edge of foldability.	Disulfides	76-85	insulin	Homo sapiens	145-152
32916194-6	2020	Importantly, the proinsulin mutants formed abnormal intermolecular disulfide bonds that not only involved the mutant proinsulin, but also the co-expressed WT-proinsulin, forming misfolded disulfide-linked proinsulin complexes.	Disulfides	67-76	insulin	Homo sapiens	17-27
32916194-6	2020	Importantly, the proinsulin mutants formed abnormal intermolecular disulfide bonds that not only involved the mutant proinsulin, but also the co-expressed WT-proinsulin, forming misfolded disulfide-linked proinsulin complexes.	Disulfides	67-76	insulin	Homo sapiens	117-127
32916194-6	2020	Importantly, the proinsulin mutants formed abnormal intermolecular disulfide bonds that not only involved the mutant proinsulin, but also the co-expressed WT-proinsulin, forming misfolded disulfide-linked proinsulin complexes.	Disulfides	67-76	insulin	Homo sapiens	117-127
32916194-6	2020	Importantly, the proinsulin mutants formed abnormal intermolecular disulfide bonds that not only involved the mutant proinsulin, but also the co-expressed WT-proinsulin, forming misfolded disulfide-linked proinsulin complexes.	Disulfides	188-197	insulin	Homo sapiens	17-27
32916194-6	2020	Importantly, the proinsulin mutants formed abnormal intermolecular disulfide bonds that not only involved the mutant proinsulin, but also the co-expressed WT-proinsulin, forming misfolded disulfide-linked proinsulin complexes.	Disulfides	188-197	insulin	Homo sapiens	117-127
32916194-6	2020	Importantly, the proinsulin mutants formed abnormal intermolecular disulfide bonds that not only involved the mutant proinsulin, but also the co-expressed WT-proinsulin, forming misfolded disulfide-linked proinsulin complexes.	Disulfides	188-197	insulin	Homo sapiens	117-127
33159537-1	2020	SUMOylation has long been recognized to regulate multiple biological processes in pancreatic beta cells, but its impact on proinsulin disulfide maturation and endoplasmic reticulum (ER) stress remains elusive.	Disulfides	134-143	insulin	Homo sapiens	123-133
32413886-4	2020	Disulfide bonds linking Au and MSN nanoparticles were introduced to the MSN surface as the redox-sensitive and chemically removable components.	Disulfides	0-9	moesin	Homo sapiens	31-34
32413886-4	2020	Disulfide bonds linking Au and MSN nanoparticles were introduced to the MSN surface as the redox-sensitive and chemically removable components.	Disulfides	0-9	moesin	Homo sapiens	72-75
33173013-5	2020	ERp44 also patrols the secretion of correctly assembled disulfide-linked oligomeric proteins.	Disulfides	56-65	endoplasmic reticulum protein 44	Homo sapiens	0-5
33175491-7	2020	In the other, two dimers of ERF are assembled into a tetramer that is additionally locked by two Cys72-Cys72 disulfide bonds across the dimers.	Disulfides	109-118	ETS2 repressor factor	Homo sapiens	28-31
33030156-3	2020	Cytochrome c with the apoptosis inducing function was anchored on the surface of AuNR@MSN to prevent drug leakage through redox-responsive disulfide bonds.	Disulfides	139-148	cytochrome c, somatic	Homo sapiens	0-12
32392042-5	2020	Anti-human serum albumin pAbF antibody was modified with azide groups and conjugated to UCNP@PEG-alkyne via click reaction; alternatively, the antibody, after mild reduction of its disulfide bonds, was conjugated to UCNP@PEG-maleimide.	Disulfides	181-190	albumin	Homo sapiens	11-24
33030156-3	2020	Cytochrome c with the apoptosis inducing function was anchored on the surface of AuNR@MSN to prevent drug leakage through redox-responsive disulfide bonds.	Disulfides	139-148	moesin	Homo sapiens	86-89
32335140-5	2020	We recently identified two homologous disulfide-rich spider-venom peptides (Hm1a and Hm1b) that selectively potentiate NaV1.1, and showed that selective activation of NaV1.1 by Hm1a restores the function of inhibitory interneurons in a mouse model of DS.	Disulfides	38-47	sodium channel, voltage-gated, type I, alpha	Mus musculus	167-173
32997203-7	2020	In concert, these proteins mediate disulfide transfer from H2O2 to target proteins via PDI-Gpx7 fusions.	Disulfides	35-44	protein disulfide isomerase family A member 2	Homo sapiens	87-90
32524995-5	2020	The native 23-residue peptide, stabilised by two disulfide bonds, has been reported to inhibit rat NaV1.8 and mouse NaV1.9 with low micromolar activity, and may therefore represent a scaffold for development of novel modulators with activity at human tetrodotoxin-resistant NaV isoforms.	Disulfides	49-58	sodium voltage-gated channel alpha subunit 10	Rattus norvegicus	99-105
33879435-0	2020	Thiol-disulfide exchange reactions occurring at modified bovine serum albumin detected using ellman"s reagent (5, 5"-dithiobis (2-itrobenzoic acid).	Disulfides	6-15	albumin	Homo sapiens	64-77
33077910-6	2020	Cell surface Cnx-ERp57 complexes reduce these extracellular disulfide bonds and are essential for ECM degradation.	Disulfides	60-69	protein disulfide isomerase family A member 3	Homo sapiens	17-22
32913288-3	2020	Here, such difficulties are overcome through re-bridging of the inter-chain disulfides of cetuximab (CTX) with auristatin-bearing pyridazinediones, to yield a highly refined anti-epidermal growth factor receptor (EGFR) ADC.	Disulfides	76-86	epidermal growth factor receptor	Homo sapiens	179-211
32725381-10	2020	Interestingly, we found that the interaction of HSPA5 with negatively charged liposomes promotes an oligomerization process via intermolecular disulfide bonds in which the N-terminus end of the protein plays a critical role.	Disulfides	143-152	heat shock protein family A (Hsp70) member 5	Homo sapiens	48-53
32593758-0	2020	Reduction of a disulfide-constrained oligo-glutamate peptide triggers self-assembly of beta2-type amyloid fibrils with the chiroptical properties determined by supramolecular chirality.	Disulfides	15-24	ATPase H+ transporting V0 subunit a2	Homo sapiens	87-92
32768728-8	2020	Our results clearly suggest that, similar to the mutations located at metal sites/dimer interface/disulfide regions, the mutations at the far positioned site (Glu100) also induce significant conformational changes that could affect the metallation and structure of SOD1 molecule, resulting in formation of toxic intermediate species that cause ALS.	Disulfides	98-107	superoxide dismutase 1	Homo sapiens	265-269
32924471-4	2020	Compared with in-solution digestion of the same loadings, the sequence coverage of in-funnel digestion of ovalbumin (with one disulfide bond) and ovocystatin (with two disulfide bonds) increased from 36% to 65% and from 21% to 81%, respectively.	Disulfides	126-135	serine (or cysteine) peptidase inhibitor, clade B, member 1, pseudogene	Mus musculus	106-115
32988199-3	2020	Here, we focus on the highly amyloidogenic H-fragment of insulin comprising the disulfide-bonded N-terminal parts of both chains.	Disulfides	80-89	insulin	Homo sapiens	57-64
32988199-7	2020	Our study suggests that the N-terminal part of insulin"s A-chain containing the intact Cys6-Cys11 intrachain disulfide bond may constitute insulin"s major amyloid stretch which, through its bent conformation, enforces a parallel in-register alignment of beta-strands.	Disulfides	109-118	insulin	Homo sapiens	47-54
32988199-7	2020	Our study suggests that the N-terminal part of insulin"s A-chain containing the intact Cys6-Cys11 intrachain disulfide bond may constitute insulin"s major amyloid stretch which, through its bent conformation, enforces a parallel in-register alignment of beta-strands.	Disulfides	109-118	insulin	Homo sapiens	139-146
33335667-3	2020	However, since INSL5 has a complex structure of two chains and three disulfide bonds, its synthesis has proven to be extremely difficult via either chemical or recombinant approaches.	Disulfides	69-78	insulin like 5	Homo sapiens	15-20
33056994-5	2020	ERO1L was found to promote the secretion of IL6R by affecting the formation of disulfide bonds.	Disulfides	79-88	interleukin 6 receptor	Homo sapiens	44-48
33122656-2	2020	Here, we test this assumption by quantifying the redox state of disulfide bonds in the blood clotting protein fibrinogen.	Disulfides	64-73	fibrinogen beta chain	Homo sapiens	110-120
33122656-3	2020	The disulfide status of fibrinogen from healthy human donor plasma and cultured human hepatocytes are measured using differential cysteine alkylation and mass spectrometry.	Disulfides	4-13	fibrinogen beta chain	Homo sapiens	24-34
33122656-4	2020	This analysis identifies 13 disulfide bonds that are 10-50% reduced, indicating that fibrinogen is produced in multiple disulfide-bonded or covalent states.	Disulfides	28-37	fibrinogen beta chain	Homo sapiens	85-95
33122656-4	2020	This analysis identifies 13 disulfide bonds that are 10-50% reduced, indicating that fibrinogen is produced in multiple disulfide-bonded or covalent states.	Disulfides	120-129	fibrinogen beta chain	Homo sapiens	85-95
33163811-1	2020	Tissue transglutaminase (TG2) is a multifunctional protein that can act as a cross-linking enzyme, GTPase/ATPase, protein kinase, and protein disulfide isomerase.	Disulfides	142-151	transglutaminase 2	Homo sapiens	0-23
32841639-3	2020	Analysis from the perspective of structure-functionality elucidates that cathepsin L inhibitory proteins/peptides found in food share specific features: multiple disulfide crosslinks (buried in protein core), lack or low contents of (small) alpha-helices, and high surface hydrophobicity.	Disulfides	162-171	cathepsin L	Homo sapiens	73-84
33066432-7	2020	The reduction of NMDAR disulfide bonds by either 1 mM DTT or 1 mM HCY decreased GluN1/2A currents activated by HCY.	Disulfides	23-32	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	80-85
33066432-9	2020	In fact, cleaving NMDAR disulfide bonds in neurons reversed the HCY-induced Ca2+ accumulation, making it dependent on GluN2B- rather than GluN2A-containing NMDARs.	Disulfides	24-33	glutamate ionotropic receptor NMDA type subunit 2A	Homo sapiens	138-144
32924471-4	2020	Compared with in-solution digestion of the same loadings, the sequence coverage of in-funnel digestion of ovalbumin (with one disulfide bond) and ovocystatin (with two disulfide bonds) increased from 36% to 65% and from 21% to 81%, respectively.	Disulfides	168-177	serine (or cysteine) peptidase inhibitor, clade B, member 1, pseudogene	Mus musculus	106-115
32980662-2	2020	We have previously shown that oxidative stress activates RyR2 in rabbit cardiomyocytes by promoting the formation of disulfide bonds between neighboring RyR2 subunits.	Disulfides	117-126	ryanodine receptor 2	Homo sapiens	57-61
33054088-0	2020	Murine tissue factor disulfide mutation causes a bleeding phenotype with sex specific organ pathology and lethality.	Disulfides	21-30	coagulation factor III	Mus musculus	7-20
33054088-3	2020	To investigate the role of this allosteric disulfide bond in vivo, we generated a C213G mutant tissue factor mouse by replacing Cys213 of the corresponding disulfide Cys190-Cys213 in murine tissue factor.	Disulfides	156-165	coagulation factor III	Mus musculus	95-108
33054088-11	2020	These experiments show that the tissue factor allosteric disulfide bond is of crucial importance for normal in vivo expression, post-translational processing and activity of murine tissue factor.	Disulfides	57-66	coagulation factor III	Mus musculus	32-45
33054088-11	2020	These experiments show that the tissue factor allosteric disulfide bond is of crucial importance for normal in vivo expression, post-translational processing and activity of murine tissue factor.	Disulfides	57-66	coagulation factor III	Mus musculus	181-194
32531564-5	2020	Chicken AvBD5 is composed of a signal, pro, and mature peptides containing one alpha-helix, four beta-sheet, and three disulfide bonds.	Disulfides	119-128	avian beta-defensin 5	Gallus gallus	8-13
32980662-2	2020	We have previously shown that oxidative stress activates RyR2 in rabbit cardiomyocytes by promoting the formation of disulfide bonds between neighboring RyR2 subunits.	Disulfides	117-126	ryanodine receptor 2	Homo sapiens	153-157
32971812-4	2020	The data from the molten globule-like structures of ribonuclease, lysozyme, bovine serum albumin and chymotrypsinogen identified new speeding agents, i.e., hydrophobic/electrostatic interactions and productive complex formations involving the protein and thiol reagent, which were able to confer exceptional reactivity to structural cysteines which were only intended to form disulfides.	Disulfides	376-386	lysozyme	Homo sapiens	66-74
32971812-4	2020	The data from the molten globule-like structures of ribonuclease, lysozyme, bovine serum albumin and chymotrypsinogen identified new speeding agents, i.e., hydrophobic/electrostatic interactions and productive complex formations involving the protein and thiol reagent, which were able to confer exceptional reactivity to structural cysteines which were only intended to form disulfides.	Disulfides	376-386	albumin	Homo sapiens	83-96
32678573-3	2020	The modified heptad sequences, termed as CCK and CCE, respectively, can specifically recognize each other and induce the formation of a disulfide bond between cysteine residues.	Disulfides	136-145	cholecystokinin	Homo sapiens	41-44
32686399-0	2020	Tagging Transferrin Receptor with a Disulfide FRET Probe to Gauge the Redox State in Endosomal Compartments.	Disulfides	36-45	transferrin	Homo sapiens	8-19
32779697-2	2020	Previous studies have revealed discrepancies between the oligomerization state of certain DAN family members, with SOST (a poor antagonist of BMP signaling) forming a monomer while Grem1, Grem2, and NBL1 (more potent BMP antagonists) form non-disulfide linked dimers.	Disulfides	243-252	NBL1, DAN family BMP antagonist	Homo sapiens	90-93
32780615-2	2020	CXCL8 harbors 2 disulfide bonds for its stability.	Disulfides	16-25	C-X-C motif chemokine ligand 8	Homo sapiens	0-5
33159202-10	2020	Insulin consists of two chains, the A- and B-chain, which are connected by two disulfide-bridges.	Disulfides	79-88	insulin	Homo sapiens	0-7
32788339-3	2020	The ECM protein fibronectin circulates in the blood as a globular protein that dimerizes through disulfide bridges generated by cysteine oxidation.	Disulfides	97-106	fibronectin 1	Homo sapiens	16-27
32661419-5	2020	Here, we find that disulfide bonding between a native cysteine pair at the groove (C55) and C-terminal alpha9 helix (C175) of BFL-1 operates as a redox switch to control the accessibility of the anti-apoptotic pocket.	Disulfides	19-28	BCL2 related protein A1	Homo sapiens	126-131
32661419-6	2020	Reducing the C55-C175 disulfide triggers alpha9 release, which promotes mitochondrial translocation, groove exposure for BH3 interaction and inhibition of mitochondrial permeabilization by pro-apoptotic BAX.	Disulfides	22-31	BCL2 associated X, apoptosis regulator	Homo sapiens	203-206
32661419-7	2020	C55-C175 disulfide formation in an oxidative cellular environment abrogates the ability of BFL-1 to bind BH3 domains.	Disulfides	9-18	BCL2 related protein A1	Homo sapiens	91-96
32305461-0	2020	Protein Disulfide Exchange by the Intramembrane Enzymes DsbB, DsbD, and CcdA.	Disulfides	8-17	plasmid maintenance protein CcdA	Escherichia coli	72-76
33133530-5	2020	SPI with a higher pH produced more disulfide-mediated aggregates at the expense of sulfhydryl groups and experienced greater losses of protein tertiary structure and a faster reduction in solubility.	Disulfides	35-44	chromogranin A	Homo sapiens	0-3
32788339-4	2020	We found that cellular (fibrillar) fibronectin on the surface of transforming growth factor-beta1 (TGF-beta1)-activated human myofibroblasts underwent multimerization by o,o"-dityrosine cross-linking under reducing conditions that disrupt disulfide bridges, but soluble fibronectin did not.	Disulfides	239-248	fibronectin 1	Homo sapiens	35-46
32788339-4	2020	We found that cellular (fibrillar) fibronectin on the surface of transforming growth factor-beta1 (TGF-beta1)-activated human myofibroblasts underwent multimerization by o,o"-dityrosine cross-linking under reducing conditions that disrupt disulfide bridges, but soluble fibronectin did not.	Disulfides	239-248	transforming growth factor beta 1	Homo sapiens	65-97
32788339-4	2020	We found that cellular (fibrillar) fibronectin on the surface of transforming growth factor-beta1 (TGF-beta1)-activated human myofibroblasts underwent multimerization by o,o"-dityrosine cross-linking under reducing conditions that disrupt disulfide bridges, but soluble fibronectin did not.	Disulfides	239-248	transforming growth factor beta 1	Homo sapiens	99-108
32196765-3	2020	Despite consisting of just 51 amino acids, insulin contains 17 of the proteinogenic amino acids, A- and B-chains, three disulfide bridges, and it folds with 3 a-helices and a short b-sheet segment.	Disulfides	120-129	insulin	Homo sapiens	43-50
32749217-4	2020	In the complex, the luminal surface of CLC-7 is entirely covered by a dimer of the heavily glycosylated and disulfide-bonded OSTM1, which serves to protect CLC-7 from the degradative environment of the lysosomal lumen.	Disulfides	108-117	osteoclastogenesis associated transmembrane protein 1	Homo sapiens	125-130
32453609-3	2020	Lp(a) is a low-density lipoprotein with an added apolipoprotein(a) attached to the apolipoprotein B component via a disulfide bond.	Disulfides	116-125	apolipoprotein B	Homo sapiens	83-99
32376199-5	2020	Their mixture contains a mixed disulfide between insulin B-chain and thioredoxin-Cys73, which limits their activities.	Disulfides	31-40	insulin	Homo sapiens	49-56
32939274-4	2020	A careful analysis of the chemical environment of disulfide bonds in the structures of elastase, lysozyme, acetylcholinesterase and other proteins suggests that S-S bonds which engage in a close contact with a carbonyl O atom along the extension of the S-S bond vector are more susceptible to reduction than the others.	Disulfides	50-59	lysozyme	Homo sapiens	97-105
32939274-4	2020	A careful analysis of the chemical environment of disulfide bonds in the structures of elastase, lysozyme, acetylcholinesterase and other proteins suggests that S-S bonds which engage in a close contact with a carbonyl O atom along the extension of the S-S bond vector are more susceptible to reduction than the others.	Disulfides	50-59	acetylcholinesterase (Cartwright blood group)	Homo sapiens	107-127
31910038-2	2020	This review addresses emerging evidence that exported thiol oxidoreductases(TOR) such as thioredoxin, protein disulfide isomerases, QSOX1 and peroxiredoxins, composing a peri/epicellular (pec)TOR pool, mediates relevant signaling.	Disulfides	110-119	RAR related orphan receptor C	Homo sapiens	76-79
31910038-2	2020	This review addresses emerging evidence that exported thiol oxidoreductases(TOR) such as thioredoxin, protein disulfide isomerases, QSOX1 and peroxiredoxins, composing a peri/epicellular (pec)TOR pool, mediates relevant signaling.	Disulfides	110-119	RAR related orphan receptor C	Homo sapiens	192-195
32436653-5	2020	METHODS AND RESULTS: Non-conserved amino acids within the beta1 ECII loop (compared with the amino acids constituting the ECII loop of the beta2 -adrenoceptor) were one by one replaced with alanine; potential intra-loop disulfide bridges were probed by cysteine-serine exchanges.	Disulfides	220-229	BCL2 related protein A1	Homo sapiens	58-63
32593213-4	2020	A disulfide isomerase, anterior gradient 2 (AGR2), has been shown to increase hypoxia-inducible factor 1, alpha subunit (HIF-1alpha) stability in breast cancer.	Disulfides	2-11	hypoxia inducible factor 1 subunit alpha	Homo sapiens	78-119
32593213-4	2020	A disulfide isomerase, anterior gradient 2 (AGR2), has been shown to increase hypoxia-inducible factor 1, alpha subunit (HIF-1alpha) stability in breast cancer.	Disulfides	2-11	hypoxia inducible factor 1 subunit alpha	Homo sapiens	121-131
32636308-5	2020	Mutational analysis and solution studies confirmed that the strained disulfides function as redox "switches" to reversibly regulate the activity and dimerization of FN3K.	Disulfides	69-79	fructosamine 3 kinase	Homo sapiens	165-169
32400108-5	2020	The peptide was subsequently modified via PEGylation and biotinylation, and cyclized through disulfide bridge formation, mimicking the native loop conformation in CFTR protein.	Disulfides	93-102	CF transmembrane conductance regulator	Homo sapiens	163-167
32428440-3	2020	In conjunction with the secondary structural changes of proteins, the S-S stretching vibrational mode of a disulfide bond (~514 cm-1) and the ratio of the tyrosine doublet I850/I826 were also found to be markers distinguishing polymorphisms of insulin amyloid fibrils by principal component analysis.	Disulfides	107-116	insulin	Homo sapiens	244-251
32459964-0	2020	Effects of Disulfide Bonds on Bindings of Inhibitors to BACE1 Decoded by Multiple Replica Accelerated Molecular Dynamics Simulations.	Disulfides	11-20	beta-secretase 1	Homo sapiens	56-61
32459964-3	2020	In this work, multiple replica accelerated molecular dynamics (MR-aMD) simulations, principal component (PC) analysis and free energy landscapes were integrated to decode effect of disulfide bonds (SSBs) in BACE1 on bindings of three inhibitors 3KO, 3KT and 779 to BACE1.	Disulfides	181-190	beta-secretase 1	Homo sapiens	207-212
32630599-6	2020	Within recent years, the formation of disulfide-linked heterodimers was documented for TFF1 and TFF3, e.g., with gastrokine-2 and IgG Fc binding protein (FCGBP).	Disulfides	38-47	trefoil factor 3, intestinal	Mus musculus	96-100
32630599-6	2020	Within recent years, the formation of disulfide-linked heterodimers was documented for TFF1 and TFF3, e.g., with gastrokine-2 and IgG Fc binding protein (FCGBP).	Disulfides	38-47	Fc fragment of IgG binding protein	Mus musculus	130-152
32630599-6	2020	Within recent years, the formation of disulfide-linked heterodimers was documented for TFF1 and TFF3, e.g., with gastrokine-2 and IgG Fc binding protein (FCGBP).	Disulfides	38-47	Fc fragment of IgG binding protein	Mus musculus	154-159
32413285-0	2020	Identification of a Covalent Molecular Inhibitor of Anti-apoptotic BFL-1 by Disulfide Tethering.	Disulfides	76-85	BCL2 related protein A1	Homo sapiens	67-72
32413285-6	2020	We found that a disulfide-bearing N-acetyltryptophan analog (304 Da adduct) effectively targeted BFL-1 C55 and reversed BFL-1-mediated suppression of mitochondrial apoptosis.	Disulfides	16-25	BCL2 related protein A1	Homo sapiens	97-102
32061786-4	2020	METHODS: Human recombinant GAPDH with the mutation C156S (hGAPDH_C156S) was obtained to prevent the formation of the disulfide bridge.	Disulfides	117-126	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	27-32
32545905-6	2020	CD10 C143Y, however, forms a disulfide bond-mediated oligomer that does not appear by the wild-type CD10.	Disulfides	29-38	membrane metalloendopeptidase	Homo sapiens	0-4
32369051-8	2020	The disulfide LMWG loaded with a thiol-containing protein (bovine serum albumin) features sustained release in vitro, whereas a dextran of the same molecular weight, lacking a thiol biomolecule, shows quick release.	Disulfides	4-13	albumin	Homo sapiens	66-79
32061786-4	2020	METHODS: Human recombinant GAPDH with the mutation C156S (hGAPDH_C156S) was obtained to prevent the formation of the disulfide bridge.	Disulfides	117-126	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	58-64
32061786-8	2020	In the case of hGAPDH, the mixed disulfide breaks down yielding Cys152-Cys156 disulfide bridge in the active site.	Disulfides	33-42	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	15-21
32061786-9	2020	In hGAPDH_C156S, the mixed disulfide is stable.	Disulfides	27-36	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	3-9
32469364-0	2020	Synthesis of unsymmetrical disulfides via PPh3-mediated reductive coupling of thiophenols with sulfonyl chlorides.	Disulfides	27-37	caveolin 1	Homo sapiens	42-46
32269095-2	2020	In peripheral APCs, gamma-IFN-inducible lysosomal thiol reductase (GILT) is critical for MHC class II-restricted presentation of disulfide bond-containing proteins, including the self-antigen and melanoma Ag tyrosinase-related protein 1 (TRP1).	Disulfides	129-138	amyloid P component, serum	Mus musculus	14-18
32514176-6	2020	By comparison with the structure of PrPC, we propose that two alpha-helices in the C-terminal domain of PrPC are converted into beta-strands stabilized by a disulfide bond in the PrP fibril.	Disulfides	157-166	prion protein	Homo sapiens	36-40
32514176-6	2020	By comparison with the structure of PrPC, we propose that two alpha-helices in the C-terminal domain of PrPC are converted into beta-strands stabilized by a disulfide bond in the PrP fibril.	Disulfides	157-166	prion protein	Homo sapiens	104-108
32514176-6	2020	By comparison with the structure of PrPC, we propose that two alpha-helices in the C-terminal domain of PrPC are converted into beta-strands stabilized by a disulfide bond in the PrP fibril.	Disulfides	157-166	prion protein	Homo sapiens	36-39
32297376-5	2020	Despite sharing this conserved ligand-binding module, IR and EGFR family members are considered mechanistically distinct-in part because IR is a disulfide-linked (alphabeta)2 dimer regardless of ligand binding, whereas EGFR is a monomer that undergoes ligand-induced dimerization.	Disulfides	145-154	epidermal growth factor receptor	Homo sapiens	61-65
31913846-2	2020	We recently found that formation of disulfide-linked complexes of apolipoprotein (apo) E3 prevented apoE3 from irreversible oxidation.	Disulfides	36-45	apolipoprotein E	Homo sapiens	100-105
31891446-3	2020	The HLA-B*38:55Q allele was detected as an HLA-B blank specificity; DNA sequencing identified a single polymorphism at position 373 in exon 3 (TGC > CGC), which results in the replacement of cysteine 101 with an arginine in the HLA-B heavy chain, thus, impairing disulfide bridge formation in the alpha-2 domain, essential for the normal expression of the HLA molecules.	Disulfides	263-272	glycoprotein hormone subunit alpha 2	Homo sapiens	297-304
32070740-1	2020	The so-called "H-fragment" of insulin is an extremely amyloidogenic double chain peptide consisting of the N-terminal parts of A-chain and B-chain linked by a disulfide bond between Cys-7A and Cys7B.	Disulfides	159-168	insulin	Homo sapiens	30-37
32032465-2	2020	Here we report the chemical synthesis of interleukin-2 (IL-2) variants on a multimiligram scale and the formation of non-natural disulfide mimetics that improve stability against reduction.	Disulfides	129-138	interleukin 2	Homo sapiens	41-54
32032465-2	2020	Here we report the chemical synthesis of interleukin-2 (IL-2) variants on a multimiligram scale and the formation of non-natural disulfide mimetics that improve stability against reduction.	Disulfides	129-138	interleukin 2	Homo sapiens	56-60
31913846-10	2020	Redox-mediated modification of Cys thiols of apoE2 or apoE3, especially disulfide bond formation with apoAII, affects lipid metabolism and consequently may be responsible for the diverse isoform specificity of apoE.	Disulfides	72-81	apolipoprotein E	Homo sapiens	45-50
31913846-10	2020	Redox-mediated modification of Cys thiols of apoE2 or apoE3, especially disulfide bond formation with apoAII, affects lipid metabolism and consequently may be responsible for the diverse isoform specificity of apoE.	Disulfides	72-81	apolipoprotein E	Homo sapiens	54-59
31913846-10	2020	Redox-mediated modification of Cys thiols of apoE2 or apoE3, especially disulfide bond formation with apoAII, affects lipid metabolism and consequently may be responsible for the diverse isoform specificity of apoE.	Disulfides	72-81	apolipoprotein E	Homo sapiens	45-49
32316996-8	2020	RESULTS: The percentage of the disulfide-bonded HA trimers increased significantly in the PDIs-overexpressed 293 T cells, and ERp57 was more valid to the stability of HA than PDI.	Disulfides	31-40	protein disulfide isomerase family A member 2	Homo sapiens	90-93
32191862-0	2020	Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1.	Disulfides	28-37	superoxide dismutase 1	Homo sapiens	56-60
32191862-7	2020	We speculate that the molecular mechanisms giving rise to the internal friction of disulfide-reduced mSOD1 might play a role in the amyotrophic lateral sclerosis-linked aggregation of SOD1.	Disulfides	83-92	superoxide dismutase 1, soluble	Mus musculus	101-106
32191862-7	2020	We speculate that the molecular mechanisms giving rise to the internal friction of disulfide-reduced mSOD1 might play a role in the amyotrophic lateral sclerosis-linked aggregation of SOD1.	Disulfides	83-92	superoxide dismutase 1	Homo sapiens	102-106
32316996-9	2020	The knockdown of ERp57 by small interfering RNA significantly decreased the percentage of the disulfide-bonded HA trimers.	Disulfides	94-103	protein disulfide isomerase family A member 3	Homo sapiens	17-22
32249844-3	2020	The present clinical and experimental studies investigated the role of the disulfide bond-forming oxidoreductase A-like protein (DsbA-L) gene, which has antioxidant and adiponectin multimeric (i.e. activation) properties, on the respiratory function of the elderly.	Disulfides	75-84	adiponectin, C1Q and collagen domain containing	Homo sapiens	169-180
32309706-0	2020	Direct Ultraviolet Laser-Induced Reduction of Disulfide Bonds in Insulin and Vasopressin.	Disulfides	46-55	insulin	Homo sapiens	65-72
32260401-0	2020	Molecular Dynamics Simulation and Kinetic Study of Fluoride Binding to V21C/V66C Myoglobin with a Cytoglobin-like Disulfide Bond.	Disulfides	114-123	cytoglobin	Homo sapiens	98-108
32309706-0	2020	Direct Ultraviolet Laser-Induced Reduction of Disulfide Bonds in Insulin and Vasopressin.	Disulfides	46-55	arginine vasopressin	Homo sapiens	77-88
32260401-2	2020	In the absence of structural evidence for cytoglobin (Cgb) with an intramolecular disulfide bond, we recently designed a de novo disulfide bond in myoglobin (Mb) based on structural alignment (i.e., V21C/V66C Mb double mutant).	Disulfides	82-91	cytoglobin	Homo sapiens	54-57
32197489-0	2020	PDI-Mediated Reduction of Disulfide Bond on PSD95 Increases Spontaneous Seizure Activity by Regulating NR2A-PSD95 Interaction in Epileptic Rats Independent of S-Nitrosylation.	Disulfides	26-35	DLG associated protein 2	Rattus norvegicus	44-49
31760526-0	2020	Intra-subunit Disulfide Determines the Conversion and Structural Stability of CRP Isoforms.	Disulfides	14-23	C-reactive protein	Homo sapiens	78-81
31760526-2	2020	CRP dissociates into subunits at inflammatory loci forming monomeric CRP (mCRP) with substantially enhanced activities, which can be further activated by reducing the intra-subunit disulfide bond.	Disulfides	181-190	C-reactive protein	Homo sapiens	0-3
31760526-2	2020	CRP dissociates into subunits at inflammatory loci forming monomeric CRP (mCRP) with substantially enhanced activities, which can be further activated by reducing the intra-subunit disulfide bond.	Disulfides	181-190	C-reactive protein	Homo sapiens	69-72
32197489-0	2020	PDI-Mediated Reduction of Disulfide Bond on PSD95 Increases Spontaneous Seizure Activity by Regulating NR2A-PSD95 Interaction in Epileptic Rats Independent of S-Nitrosylation.	Disulfides	26-35	glutamate ionotropic receptor NMDA type subunit 2A	Rattus norvegicus	103-107
32197489-4	2020	However, the involvement of PDI in disulfide bond formation/S-nitrosylation of PSD95 and its role in epilepsy are still unknown.	Disulfides	35-44	DLG associated protein 2	Rattus norvegicus	79-84
32197489-0	2020	PDI-Mediated Reduction of Disulfide Bond on PSD95 Increases Spontaneous Seizure Activity by Regulating NR2A-PSD95 Interaction in Epileptic Rats Independent of S-Nitrosylation.	Disulfides	26-35	DLG associated protein 2	Rattus norvegicus	108-113
32197489-9	2020	These findings indicate that PDI-mediated reduction of disulfide-bond formations may facilitate the NR2A-PSD95 binding and contribute to spontaneous seizure generation in epileptic animals.	Disulfides	55-64	glutamate ionotropic receptor NMDA type subunit 2A	Rattus norvegicus	100-104
32197489-2	2020	A couple of cysteine residues in the N-terminus of PSD95 are potential sites for disulfide bonding, S-nitrosylation and/or palmitoylation.	Disulfides	81-90	DLG associated protein 2	Rattus norvegicus	51-56
32197489-9	2020	These findings indicate that PDI-mediated reduction of disulfide-bond formations may facilitate the NR2A-PSD95 binding and contribute to spontaneous seizure generation in epileptic animals.	Disulfides	55-64	DLG associated protein 2	Rattus norvegicus	105-110
32161259-5	2020	sERr is relieved upon protein synthesis attenuation and is accompanied by the generation of large mixed disulfide bonded complexes, including ERp44.	Disulfides	104-113	endoplasmic reticulum protein 44	Homo sapiens	142-147
32161266-3	2020	Here, we characterize a disulfide-stabilized version of the human class I molecule HLA-A*02:01 that is stable in the absence of peptide and can readily exchange cognate peptides.	Disulfides	24-33	major histocompatibility complex, class I, A	Homo sapiens	83-88
31814373-7	2020	Conclusion: The results showed that thiol/disulfide homeostasis in patients with autoimmune gastritis caused an increase in ischemia modified albumin and disulfide whereas a decrease in thiols.	Disulfides	42-51	albumin	Homo sapiens	142-149
31931014-5	2020	A disulfide-stabilized, trimeric Env ectodomain -- the "SOSIP" construct -- has many of the relevant properties; it is also particularly suitable for structure determination.	Disulfides	2-11	endogenous retrovirus group W member 1, envelope	Homo sapiens	33-36
32152335-3	2020	We investigated the hypothesis that MSE supplementation increases the adiponectin (APN) multimerization via the up-regulation of disulfide bond A oxidoreductase-like protein (DsbA-L) under either or both physiological and obese conditions.	Disulfides	129-138	adiponectin, C1Q and collagen domain containing	Homo sapiens	83-86
32056106-5	2020	The predominant subsets of the total SOD1 expression set which comprised the nucleation phase were both soluble and insoluble inactive monomers, trimers, and hexamers with reduced intra-disulfide bonds.	Disulfides	186-195	superoxide dismutase 1	Homo sapiens	37-41
31959898-4	2020	Here, we demonstrate that Nur77 could inhibit HCC development via transcriptional activation of the lncRNA WAP four-disulfide core domain 21 pseudogene (WFDC21P).	Disulfides	116-125	nuclear receptor subfamily 4 group A member 1	Homo sapiens	26-31
31809037-0	2020	Apolipoprotein E Peptide-Guided Disulfide-Cross-Linked Micelles for Targeted Delivery of Sorafenib to Hepatocellular Carcinoma.	Disulfides	32-41	apolipoprotein E	Homo sapiens	0-16
31809037-3	2020	Here, we report on apolipoprotein E peptide-decorated disulfide-cross-linked micellar SF (ApoE-Ms-SF) as a targeted and intelligent formulation for HCC therapy.	Disulfides	54-63	apolipoprotein E	Homo sapiens	19-35
31809037-3	2020	Here, we report on apolipoprotein E peptide-decorated disulfide-cross-linked micellar SF (ApoE-Ms-SF) as a targeted and intelligent formulation for HCC therapy.	Disulfides	54-63	apolipoprotein E	Homo sapiens	90-94
31863908-6	2020	Such an abnormal SOD1 with the non-canonical disulfide bond was conformationally extended with significant cytotoxicity as well as high propensity to aggregate.	Disulfides	45-54	superoxide dismutase 1	Homo sapiens	17-21
31952808-7	2020	[R273C]p53 aggregation is disulfide mediated, leading to cross-beta, thioflavin-T-positive aggregates, whereas hydrophobic interactions dominate self-assembly in [R273L]p53, leading to a mixture of amyloid and amorphous aggregates.	Disulfides	26-35	tumor protein p53	Homo sapiens	7-10
31952808-7	2020	[R273C]p53 aggregation is disulfide mediated, leading to cross-beta, thioflavin-T-positive aggregates, whereas hydrophobic interactions dominate self-assembly in [R273L]p53, leading to a mixture of amyloid and amorphous aggregates.	Disulfides	26-35	tumor protein p53	Homo sapiens	169-172
32038043-0	2020	The thrombospondin module 1 domain of the matricellular protein CCN3 shows an atypical disulfide pattern and incomplete CWR layers.	Disulfides	87-96	thrombospondin 1	Homo sapiens	4-27
32038043-3	2020	Here, the crystal structure of the thrombospondin module 1 (TSP1) domain of CCN3 (previously known as Nov) is presented, which shares a similar three-stranded fold with the thrombospondin type 1 repeats of thrombospondin-1 and spondin-1, but with variations in the disulfide connectivity.	Disulfides	265-274	thrombospondin 1	Homo sapiens	35-58
32038043-3	2020	Here, the crystal structure of the thrombospondin module 1 (TSP1) domain of CCN3 (previously known as Nov) is presented, which shares a similar three-stranded fold with the thrombospondin type 1 repeats of thrombospondin-1 and spondin-1, but with variations in the disulfide connectivity.	Disulfides	265-274	thrombospondin 1	Homo sapiens	60-64
31877449-2	2020	While secondary structural propensity of both proteins is larger in glycerol, results for tertiary structure and translational diffusion coefficient with increasing glycerol provide two contrasting depictions - lysozyme becomes increasingly compact, plausibly due to disulfide bridge constraints, but cytochrome c expands and loses the tertiary structure.	Disulfides	267-276	lysozyme	Homo sapiens	211-219
31863908-7	2020	Taken together, we propose a new model of SOD1 misfolding under oxidizing environment, in which formation of the non-canonical intramolecular disulfide bond plays a pivotal role.	Disulfides	142-151	superoxide dismutase 1	Homo sapiens	42-46
31931282-6	2020	We show that MG reacts preferentially with the disulfide-reduced, demetallated form of SOD1, gradually causing its unfolding, and to a lesser extent, with the intermediate state of maturation - the reduced, zinc-bound homodimer - causing its gradual monomerization.	Disulfides	47-56	superoxide dismutase 1	Homo sapiens	87-91
31794946-1	2020	Disulfide bond formation is catalyzed by the protein disulfide Isomerases (PDI) family.	Disulfides	0-9	protein disulfide isomerase family A member 2	Homo sapiens	45-73
31794946-1	2020	Disulfide bond formation is catalyzed by the protein disulfide Isomerases (PDI) family.	Disulfides	0-9	protein disulfide isomerase family A member 2	Homo sapiens	75-78
31691197-5	2020	Due to the presence of two disulfide bond, scFv expression in reducing bacterial cytoplasm may cause formation of inclusion bodies.	Disulfides	27-36	immunglobulin heavy chain variable region	Homo sapiens	43-47
31963721-11	2020	Furthermore, a minor subset of Tff1 forms a disulfide-linked heterodimer with IgG Fc binding protein (Fcgbp).	Disulfides	44-53	Fc fragment of IgG binding protein	Mus musculus	78-100
31963721-11	2020	Furthermore, a minor subset of Tff1 forms a disulfide-linked heterodimer with IgG Fc binding protein (Fcgbp).	Disulfides	44-53	Fc fragment of IgG binding protein	Mus musculus	102-107
32010829-3	2020	Herein, we describe the synthesis of HER2-targeting ADCs with three disulfide rebridging heads, allowing homogeneous and site-specific bioconjugation: dibromomaleimide (DBM), dithiomaleimide (DTM), and hybrid thio-bromomaleimide (TBM) chemical bricks to combine the properties of both previously used heads.	Disulfides	68-77	erb-b2 receptor tyrosine kinase 2	Homo sapiens	37-41
31782617-5	2020	GPx8 binds covalently to caspase-4/11 via disulfide bonding between cysteine 79 of GPx8 and cysteine 118 of caspase-4 and thus restrains caspase-4/11 activation, while GPx8 deficiency leads to caspase-4/11-induced inflammation during colitis and septic shock.	Disulfides	42-51	caspase 4, apoptosis-related cysteine peptidase	Mus musculus	25-34
31782617-5	2020	GPx8 binds covalently to caspase-4/11 via disulfide bonding between cysteine 79 of GPx8 and cysteine 118 of caspase-4 and thus restrains caspase-4/11 activation, while GPx8 deficiency leads to caspase-4/11-induced inflammation during colitis and septic shock.	Disulfides	42-51	caspase 4, apoptosis-related cysteine peptidase	Mus musculus	108-117
31782617-5	2020	GPx8 binds covalently to caspase-4/11 via disulfide bonding between cysteine 79 of GPx8 and cysteine 118 of caspase-4 and thus restrains caspase-4/11 activation, while GPx8 deficiency leads to caspase-4/11-induced inflammation during colitis and septic shock.	Disulfides	42-51	caspase 4, apoptosis-related cysteine peptidase	Mus musculus	108-117
31782617-5	2020	GPx8 binds covalently to caspase-4/11 via disulfide bonding between cysteine 79 of GPx8 and cysteine 118 of caspase-4 and thus restrains caspase-4/11 activation, while GPx8 deficiency leads to caspase-4/11-induced inflammation during colitis and septic shock.	Disulfides	42-51	caspase 4, apoptosis-related cysteine peptidase	Mus musculus	108-117
31871151-3	2020	Gga-AvBD11 is an atypical double-sized defensin, predicted to possess 2 motifs related to beta-defensins and 6 disulfide bridges.	Disulfides	111-120	avian beta-defensin 11	Gallus gallus	4-10
29848267-5	2020	The cysteine sulfenic acid reacts with reduced glutathione (GSH) to form a mixed disulfide (S-glutathionylated GAPDH) that further reacts with Cys154 yielding the disulfide bond in the active site of the enzyme.	Disulfides	81-90	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	111-116
29848267-5	2020	The cysteine sulfenic acid reacts with reduced glutathione (GSH) to form a mixed disulfide (S-glutathionylated GAPDH) that further reacts with Cys154 yielding the disulfide bond in the active site of the enzyme.	Disulfides	163-172	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	111-116
32962582-6	2020	In addition, serum disulfide level was positively correlated with CRP (r=0.736, p<0.001) and disulfide/native thiol ratio (r=0.779, p<0.001).	Disulfides	19-28	C-reactive protein	Homo sapiens	66-69
32962582-7	2020	Furthermore, in multiple regression analyses, the disulfide level was independently associated with CRP (beta=0.226, p=0.005).	Disulfides	50-59	C-reactive protein	Homo sapiens	100-103
31995732-4	2020	The CLCA1 VWA contains a disulfide bond between alpha3 and alpha4 in close proximity to the MIDAS that is invariant in the CLCA family and unique in VWA structures.	Disulfides	25-34	T cell immune regulator 1, ATPase H+ transporting V0 subunit a3	Homo sapiens	48-65
31963646-0	2020	Disulfide-Linked Peptides for Blocking BTLA/HVEM Binding.	Disulfides	0-9	TNF receptor superfamily member 14	Homo sapiens	44-48
31945064-4	2020	Locking the bundle via a disulfide bond leads to loss of apoA1 lipidation.	Disulfides	25-34	apolipoprotein A1	Homo sapiens	57-62
31956274-2	2020	Protein disulfide isomerases (PDIs) can activate beta3 integrin in various cells to promote cell migration, adhesion and fusion.	Disulfides	8-17	cholinergic receptor, nicotinic, alpha polypeptide 3	Mus musculus	49-54
31479573-1	2020	BACKGROUND: A molecular basis for VWF self-inhibition has been proposed by which the N- and C-terminal flanking sequences of the globular A1 domain disulfide loop bind to and suppress the conformational dynamics of A1.	Disulfides	148-157	von Willebrand factor	Homo sapiens	34-37
31754972-2	2020	Native MPO is a homodimer, consisting of two identical protomers (monomeric MPO) connected by a single disulfide bond but in inflammatory foci as a result of disulfide cleavage monomeric MPO (hemi-MPO) can also be produced.	Disulfides	103-112	myeloperoxidase	Homo sapiens	7-10
31754972-2	2020	Native MPO is a homodimer, consisting of two identical protomers (monomeric MPO) connected by a single disulfide bond but in inflammatory foci as a result of disulfide cleavage monomeric MPO (hemi-MPO) can also be produced.	Disulfides	158-167	myeloperoxidase	Homo sapiens	7-10
31691197-12	2020	Our findings indicated that correct disulfide bond formation in SHuffle  strain can result in enhanced solubility and higher biological activity level of anti-HER2 scFv.	Disulfides	36-45	erb-b2 receptor tyrosine kinase 2	Homo sapiens	159-163
31691197-12	2020	Our findings indicated that correct disulfide bond formation in SHuffle  strain can result in enhanced solubility and higher biological activity level of anti-HER2 scFv.	Disulfides	36-45	immunglobulin heavy chain variable region	Homo sapiens	164-168
32286937-6	2020	RESULT: The native conformation of PS-2 peptide is a cyclic loop, which is supposed to be constrained by adding a disulfide bond across the spatially vicinal residue pair Arg87-Phe96 or Met86- Phe95 at the peptide"s two ends, consequently resulting in two intramolecular cyclized counterparts of linear PS-2 peptide, namely PS-2(cyc87,96) and PS-2(cyc86,95).	Disulfides	114-123	taste 2 receptor member 64 pseudogene	Homo sapiens	35-39
32286937-6	2020	RESULT: The native conformation of PS-2 peptide is a cyclic loop, which is supposed to be constrained by adding a disulfide bond across the spatially vicinal residue pair Arg87-Phe96 or Met86- Phe95 at the peptide"s two ends, consequently resulting in two intramolecular cyclized counterparts of linear PS-2 peptide, namely PS-2(cyc87,96) and PS-2(cyc86,95).	Disulfides	114-123	taste 2 receptor member 64 pseudogene	Homo sapiens	303-307
31629169-7	2020	In both organisms, H2O2 induces transient disulfide-linked conjugates between the MAP3K and a typical 2-Cys peroxiredoxin.	Disulfides	42-51	peroxiredoxin 2	Homo sapiens	108-121
32286937-6	2020	RESULT: The native conformation of PS-2 peptide is a cyclic loop, which is supposed to be constrained by adding a disulfide bond across the spatially vicinal residue pair Arg87-Phe96 or Met86- Phe95 at the peptide"s two ends, consequently resulting in two intramolecular cyclized counterparts of linear PS-2 peptide, namely PS-2(cyc87,96) and PS-2(cyc86,95).	Disulfides	114-123	taste 2 receptor member 64 pseudogene	Homo sapiens	303-307
32286937-6	2020	RESULT: The native conformation of PS-2 peptide is a cyclic loop, which is supposed to be constrained by adding a disulfide bond across the spatially vicinal residue pair Arg87-Phe96 or Met86- Phe95 at the peptide"s two ends, consequently resulting in two intramolecular cyclized counterparts of linear PS-2 peptide, namely PS-2(cyc87,96) and PS-2(cyc86,95).	Disulfides	114-123	taste 2 receptor member 64 pseudogene	Homo sapiens	303-307
31539802-4	2020	Here we report that oxidation of the single cysteine in p16INK4A in human cells occurs under relatively mild oxidizing conditions and leads to disulfide-dependent dimerization.	Disulfides	143-152	cyclin dependent kinase inhibitor 2A	Homo sapiens	56-64
31760358-7	2020	Functional in vitro assays demonstrated that 6-OHDA inactivates protein disulfide isomerase (PDI), which is a central player in protein folding and redox homeostasis.	Disulfides	72-81	protein disulfide isomerase family A member 2	Homo sapiens	93-96
31796585-6	2019	Consistently, restriction of MHC-I groove plasticity through the introduction of a disulfide bond between the alpha1/alpha2 helices abrogates TAPBPR binding, both in solution and on a cellular membrane, while intracellular binding is tolerant of many destabilizing MHC-I substitutions.	Disulfides	83-92	BCL2 related protein A1	Homo sapiens	110-123
31941852-8	2020	To characterize p.C133Y, which may disrupt one of the three disulfide bonds of the N-terminal ASM saposin domain, we performed immunoblotting analysis to explore the expression of a mutant ASM protein in the patient"s fibroblasts, showing that the protein was detected as a 70-kDa protein, similar to the wild-type ASM protein.	Disulfides	60-69	sphingomyelin phosphodiesterase 1	Homo sapiens	189-192
31941852-8	2020	To characterize p.C133Y, which may disrupt one of the three disulfide bonds of the N-terminal ASM saposin domain, we performed immunoblotting analysis to explore the expression of a mutant ASM protein in the patient"s fibroblasts, showing that the protein was detected as a 70-kDa protein, similar to the wild-type ASM protein.	Disulfides	60-69	sphingomyelin phosphodiesterase 1	Homo sapiens	189-192
31851937-4	2019	Accordingly, we demonstrate that COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding.	Disulfides	73-83	cytochrome c oxidase assembly factor 6	Homo sapiens	33-37
31726009-0	2019	Development of a cysteine-conjugatable disulfide FRET probe: Influence of Charge on Linker Cleavage and Payload Trafficking for an anti-HER2 antibody conjugate.	Disulfides	39-48	erb-b2 receptor tyrosine kinase 2	Homo sapiens	136-140
31726009-4	2019	We demonstrate the utility of this probe to study disulfide reduction during HER2 receptor-mediated uptake of a Cys-engineered anti-HER2 THIOMAB  antibody.	Disulfides	50-59	erb-b2 receptor tyrosine kinase 2	Homo sapiens	77-81
31726009-4	2019	We demonstrate the utility of this probe to study disulfide reduction during HER2 receptor-mediated uptake of a Cys-engineered anti-HER2 THIOMAB  antibody.	Disulfides	50-59	erb-b2 receptor tyrosine kinase 2	Homo sapiens	132-136
31851937-4	2019	Accordingly, we demonstrate that COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding.	Disulfides	73-83	synthesis of cytochrome C oxidase 1	Homo sapiens	108-112
31851937-4	2019	Accordingly, we demonstrate that COA6 can reduce the copper-coordinating disulfides of its client proteins, SCO1 and COX2, allowing for copper binding.	Disulfides	73-83	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	117-121
31851937-5	2019	Finally, our determination of the interaction surfaces and reduction potentials of COA6 and its client proteins provides a mechanism of how metallochaperone and disulfide reductase activities are coordinated to deliver copper to CcO.	Disulfides	161-170	cytochrome c oxidase assembly factor 6	Homo sapiens	83-87
31580947-6	2019	In contrast, hPrxII was present predominantly as the disulfide in unstressed cells and readily converted to its hyperoxidized, peroxidase-inactive form even with mild oxidative stress.	Disulfides	53-62	peroxiredoxin 2	Homo sapiens	13-19
31847122-7	2019	A fusion of the nascent Golgi membranes after BFA washout is forced by giantin re-dimerization via disulfide bond in its luminal domain and assisted by Rab6a GTPase.	Disulfides	99-108	golgin B1	Homo sapiens	71-78
31836799-4	2019	The cnidarian proline-rich protein 1 (CPP-1) characterized by a "rigid" polyproline motif and the elastic Cnidoin possessing a silk-like domain were shown to be part of the capsule structure via short cysteine-rich domains that spontaneously crosslink the proteins via disulfide bonds.	Disulfides	269-278	opiorphin prepropeptide	Homo sapiens	14-36
31780677-2	2019	However, INSL5 with two chains and three disulfide bridges is an extremely difficult peptide to assemble by chemical or recombinant means.	Disulfides	41-50	insulin like 5	Homo sapiens	9-14
31419547-8	2019	Furthermore, tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) fusion with the third disulfide loop of TGF-alpha (TGF3L-TRAIL) fused with the NCTR25-tag retained the stability and superactivity of His-TGF3L-TRAIL.	Disulfides	105-114	TNF superfamily member 10	Homo sapiens	134-145
31781343-0	2019	4-Phenylbutyric Acid Reduces Endoplasmic Reticulum Stress in Chondrocytes That Is Caused by Loss of the Protein Disulfide Isomerase ERp57.	Disulfides	112-121	protein disulfide isomerase family A member 3	Homo sapiens	132-137
32110371-0	2020	Novel four-disulfide insulin analog with high aggregation stability and potency.	Disulfides	11-20	insulin	Homo sapiens	21-28
32110371-3	2020	Here, in an effort to mitigate this problem, we introduced a 4th disulfide bond between a C-terminal extended insulin A chain and residues near the C-terminus of the B chain.	Disulfides	65-74	insulin	Homo sapiens	110-117
32110371-4	2020	Insulin activity was retained by an analog with an additional disulfide bond between residues A22 and B22, while other linkages tested resulted in much reduced potency.	Disulfides	62-71	insulin	Homo sapiens	0-7
32110371-6	2020	We further demonstrate that this four-disulfide analog has similar in vivo potency in mice compared to native insulin and demonstrates higher aggregation stability.	Disulfides	38-47	insulin	Homo sapiens	110-117
32110371-7	2020	In conclusion, we have discovered a novel four-disulfide insulin analog with high aggregation stability and potency.	Disulfides	47-56	insulin	Homo sapiens	57-64
31530638-3	2019	Rca is inhibited by ADP, and the extent of ADP sensitivity of the Rca complex can be modulated by the CTE of the alpha isoform, particularly in relation to a disulfide bond structure that is specifically reduced by the redox-regulatory enzyme thioredoxin-f.	Disulfides	158-167	thioredoxin H4-2	Triticum aestivum	243-254
31623608-0	2019	pH and redox dual-responsive nanoparticles based on disulfide-containing poly(beta-amino ester) for combining chemotherapy and COX-2 inhibitor to overcome drug resistance in breast cancer.	Disulfides	52-61	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	127-132
31472963-3	2019	In the present study, we focused on the oxidative alteration of Prxs and demonstrated that, in human red blood cells (RBCs), peroxiredoxin 2 (Prx2) is readily reactive with H2O2, forming disulfide dimers, but was not easily hyperoxidized.	Disulfides	187-196	peroxiredoxin 2	Homo sapiens	125-140
31472963-3	2019	In the present study, we focused on the oxidative alteration of Prxs and demonstrated that, in human red blood cells (RBCs), peroxiredoxin 2 (Prx2) is readily reactive with H2O2, forming disulfide dimers, but was not easily hyperoxidized.	Disulfides	187-196	peroxiredoxin 2	Homo sapiens	142-146
31472961-2	2019	Since the homo-dimerization of MC1R by four inter-subunit disulfide bonds is known to be functionally important for melanogenesis, we investigated the importance of MC1R dimerization for cell migration.	Disulfides	58-67	melanocortin 1 receptor	Mus musculus	31-35
31501427-2	2019	Here, we reveal that L-plastin (LPL), an established tumor marker, is reversibly regulated by ROS-induced thiol oxidation on Cys101, which forms a disulfide bridge with Cys42.	Disulfides	147-156	lymphocyte cytosolic protein 1	Homo sapiens	21-30
31513391-3	2019	Here, we report on trastuzumab-decorated disulfide-cross-linked polymersomes (Tra-Ps) for specific delivery of epirubicin hydrochloride (EPI HCl) to HER2-positive SKOV-3 ovarian tumor.	Disulfides	41-50	erb-b2 receptor tyrosine kinase 2	Homo sapiens	149-153
31478604-2	2019	Treatment of fac-[Ir(aet)3 ] with aqueous HBF4 under aerobic conditions gave dinuclear [Ir2 (aet)4 (cysta)]2+ ([1]2+ ; cysta=cystamine) with a single S-S disulfide bond, while dimeric [Ir2 (aet)3 (Haet)3 ](BF4 )3 ([2](BF4 )3 ) with a triple S-H   S hydrogen bond was formed by similar treatment under anaerobic conditions.	Disulfides	154-163	FA complementation group C	Homo sapiens	13-16
33417782-5	2019	In this study, bovine serum albumin (BSA) was self-assembled into sub-100 nm nanoparticles via an intermolecular disulfide network as the inner core.	Disulfides	113-122	albumin	Homo sapiens	22-35
31515291-5	2019	These structures show that Coa6 has a 3-helical bundle structure, with the first 2 helices tethered by disulfide bonds, one of which likely provides the copper-binding site.	Disulfides	103-112	cytochrome c oxidase assembly factor 6	Homo sapiens	27-31
31501427-2	2019	Here, we reveal that L-plastin (LPL), an established tumor marker, is reversibly regulated by ROS-induced thiol oxidation on Cys101, which forms a disulfide bridge with Cys42.	Disulfides	147-156	lymphocyte cytosolic protein 1	Homo sapiens	32-35
31230748-3	2019	In the present study, we analyzed the role of two SOD1 mutants V14G and E100G which are located far away from the metal sites, dimer interface and disulfide region.	Disulfides	147-156	superoxide dismutase 1	Homo sapiens	50-54
30820867-7	2019	The total thiol, native thiol, and disulfide level was lower in TSC and NF1 group than the healthy control group.	Disulfides	35-44	TSC complex subunit 1	Homo sapiens	64-67
30820867-7	2019	The total thiol, native thiol, and disulfide level was lower in TSC and NF1 group than the healthy control group.	Disulfides	35-44	neurofibromin 1	Homo sapiens	72-75
30820867-9	2019	We detected that the total thiol, native thiol, and disulfide levels were lower in TSC and NF1 group than the healthy control group.	Disulfides	52-61	TSC complex subunit 1	Homo sapiens	83-86
30820867-9	2019	We detected that the total thiol, native thiol, and disulfide levels were lower in TSC and NF1 group than the healthy control group.	Disulfides	52-61	neurofibromin 1	Homo sapiens	91-94
31355389-4	2019	Protein tyrosine kinase 7 (PTK7) antibody mediated active targetability can facilitate the cellular uptake of triphenylphosphine-docetaxel (TD) and microRNA-31(miR-31) and the breakage of the disulfide bond can also enhance intracellular drug release.	Disulfides	192-201	protein tyrosine kinase 7 (inactive)	Homo sapiens	0-25
31355389-4	2019	Protein tyrosine kinase 7 (PTK7) antibody mediated active targetability can facilitate the cellular uptake of triphenylphosphine-docetaxel (TD) and microRNA-31(miR-31) and the breakage of the disulfide bond can also enhance intracellular drug release.	Disulfides	192-201	protein tyrosine kinase 7 (inactive)	Homo sapiens	27-31
30977272-8	2019	Despite its in vitro ADPRT activity, the reduction of C230S CARDS toxin-mediated ADPRT activity-associated IL-1beta production in U937 cells and the recovery of vacuolating activity in the protease-released carboxy region of C230S indicated that the disulfide bond was essential not only to maintain the conformational stability of CARDS toxin but also to properly execute its cytopathic effects.	Disulfides	250-259	poly(ADP-ribose) polymerase 1	Homo sapiens	81-86
31343157-0	2019	A Disulfide Scan of Insulin by [3 + 1] Methodology Exhibits Site-Specific Influence on Bioactivity.	Disulfides	2-11	insulin	Homo sapiens	20-27
31343157-2	2019	Building upon advances in insulin synthetic methodology, we have developed a straightforward route to novel insulins containing a fourth disulfide bond in a [3 + 1] fashion establishing the first disulfide scan of the hormone.	Disulfides	137-146	insulin	Homo sapiens	26-33
31343157-2	2019	Building upon advances in insulin synthetic methodology, we have developed a straightforward route to novel insulins containing a fourth disulfide bond in a [3 + 1] fashion establishing the first disulfide scan of the hormone.	Disulfides	196-205	insulin	Homo sapiens	26-33
31331172-3	2019	The theranostic nanoparticle, DHP, consisting of a disulfide-bond-linked hydroxyethyl starch paclitaxel conjugate (HES-SS-PTX) and a near-infrared (NIR) cyanine fluorophore DiR, is prepared with a simple one-step dialysis method.	Disulfides	51-60	dihydropyrimidinase	Homo sapiens	30-33
31331172-5	2019	Nonetheless, once DHP is internalized by cancer cells, the disulfide bond of HES-SS-PTX can be cleaved by intracellular GSH, leading to the synchronized release of conjugated PTX and loaded DiR.	Disulfides	59-68	dihydropyrimidinase	Homo sapiens	18-21
31331172-5	2019	Nonetheless, once DHP is internalized by cancer cells, the disulfide bond of HES-SS-PTX can be cleaved by intracellular GSH, leading to the synchronized release of conjugated PTX and loaded DiR.	Disulfides	59-68	arginine vasopressin receptor 2	Homo sapiens	190-193
31168947-8	2019	The released GQDs-miRNA are taken up by the macrophages in atherosclerotic plaques, and the disulfide linkages between the GQDs and the miRNA are cleaved through gamma-interferon-inducible lysosomal thiol reductase (GILT) in the lysosome.	Disulfides	92-101	IFI30 lysosomal thiol reductase	Homo sapiens	162-214
31168947-8	2019	The released GQDs-miRNA are taken up by the macrophages in atherosclerotic plaques, and the disulfide linkages between the GQDs and the miRNA are cleaved through gamma-interferon-inducible lysosomal thiol reductase (GILT) in the lysosome.	Disulfides	92-101	IFI30 lysosomal thiol reductase	Homo sapiens	216-220
31087045-4	2019	The proximity of GSTO2 to the condensed sperm nucleus led us to hypothesize that this enzyme may facilitate nuclear decondensation by reducing disulfide bonds before the recruitment of GSTO enzymes from within the ooplasm.	Disulfides	143-152	glutathione S-transferase omega 2	Mus musculus	17-22
31292775-8	2019	Only complete Sod1 activation (i.e. active site copper delivery and intra-subunit disulfide bond formation) breaks the Sod1 Ccs Ctr1c complex.	Disulfides	82-91	superoxide dismutase 1	Homo sapiens	14-18
31292775-8	2019	Only complete Sod1 activation (i.e. active site copper delivery and intra-subunit disulfide bond formation) breaks the Sod1 Ccs Ctr1c complex.	Disulfides	82-91	superoxide dismutase 1	Homo sapiens	119-123
31292775-8	2019	Only complete Sod1 activation (i.e. active site copper delivery and intra-subunit disulfide bond formation) breaks the Sod1 Ccs Ctr1c complex.	Disulfides	82-91	calcitonin receptor	Homo sapiens	128-133
31085461-3	2019	The secondary hydroxyl groups of beta-CD were modified by dodecyl to form a hydrophobic core and the primary hydroxyl groups of beta-CD were decorated with PEG through disulfide bond to form a hydrophilic shell.	Disulfides	168-177	ACD shelterin complex subunit and telomerase recruitment factor	Homo sapiens	128-135
31181988-7	2019	The Tm of the disulfide-stabilized scFv was largely unperturbed, yet it remained monodispersed at high protein concentration.	Disulfides	14-23	immunglobulin heavy chain variable region	Homo sapiens	35-39
30980592-0	2019	Beyond amino acid sequence: disulfide bonds and the origins of the extreme amyloidogenic properties of insulin"s H-fragment.	Disulfides	28-37	insulin	Homo sapiens	103-110
30980592-2	2019	Insulin"s three disulfide bridges stabilize the native state and prevent aggregation.	Disulfides	16-25	insulin	Homo sapiens	0-7
30980592-3	2019	Partial proteolysis of insulin releases highly amyloidogenic and inherently disordered two-chain "H-fragment" retaining insulin"s Cys7A-Cys7B and Cys6A-Cys11A disulfide bonds.	Disulfides	159-168	insulin	Homo sapiens	23-30
30980592-10	2019	The fact that the intact Cys6A-Cys11A bond promotes fibrillization of the H-fragment is remarkable in light of the previously established role of the same disulfide bond in preventing formation of insulin fibrils.	Disulfides	155-164	insulin	Homo sapiens	197-204
30880408-3	2019	For the de novo formation of disulfide bonds, reduced PDI must be reoxidized by an ER-located oxidase (ERO1).	Disulfides	29-38	ER oxidoreductin	Saccharomyces cerevisiae S288C	103-107
31316622-5	2019	Gene sequencing analysis revealed a novel heterozygous mutation, c.268A&gt;T (p.Lys90Ter), in exon 2 of the AVP-NPII gene, in the patient and the patient"s mother, which led to the loss of 6 cysteine residues and aberrant disulfide bonds, which is predicted to alter the mature protein structure.	Disulfides	222-231	arginine vasopressin	Homo sapiens	108-116
31158417-5	2019	Misfolded proinsulin formed aberrant disulfide-linked dimers and high molecular weight proinsulin complexes, and induced ER stress.	Disulfides	37-46	insulin	Homo sapiens	10-20
31138621-1	2019	Disulfide bonds are essential for the folding of the eukaryotic secretory and membrane proteins in the endoplasmic reticulum (ER), and ER oxidoreductin-1 (Ero1) and its homologs are the major disulfide donors that supply oxidizing equivalents in the ER.	Disulfides	0-9	ER oxidoreductin	Saccharomyces cerevisiae S288C	135-153
31138621-1	2019	Disulfide bonds are essential for the folding of the eukaryotic secretory and membrane proteins in the endoplasmic reticulum (ER), and ER oxidoreductin-1 (Ero1) and its homologs are the major disulfide donors that supply oxidizing equivalents in the ER.	Disulfides	0-9	ER oxidoreductin	Saccharomyces cerevisiae S288C	155-159
31138621-1	2019	Disulfide bonds are essential for the folding of the eukaryotic secretory and membrane proteins in the endoplasmic reticulum (ER), and ER oxidoreductin-1 (Ero1) and its homologs are the major disulfide donors that supply oxidizing equivalents in the ER.	Disulfides	192-201	ER oxidoreductin	Saccharomyces cerevisiae S288C	135-153
31138621-1	2019	Disulfide bonds are essential for the folding of the eukaryotic secretory and membrane proteins in the endoplasmic reticulum (ER), and ER oxidoreductin-1 (Ero1) and its homologs are the major disulfide donors that supply oxidizing equivalents in the ER.	Disulfides	192-201	ER oxidoreductin	Saccharomyces cerevisiae S288C	155-159
31125568-6	2019	Using a combination of electron paramagnetic resonance, on spin-labeled protein, and disulfide crosslinking, we show that TRIM63 follows the structural conservation of the TRIM dimerization domain, observed in other proteins.	Disulfides	85-94	tripartite motif containing 63	Homo sapiens	122-128
31324690-3	2019	Peptide-loaded disulfide-stabilized HLA-A*02:01 shows complete structural overlap with wild-type HLA-A*02:01.	Disulfides	15-24	major histocompatibility complex, class I, A	Homo sapiens	36-41
31324690-3	2019	Peptide-loaded disulfide-stabilized HLA-A*02:01 shows complete structural overlap with wild-type HLA-A*02:01.	Disulfides	15-24	major histocompatibility complex, class I, A	Homo sapiens	97-102
31324690-4	2019	Peptide-MHC multimers prepared using disulfide-stabilized HLA-A*02:01, HLA-A*24:02, and H-2Kb can be used to identify antigen-specific T cells, and they provide a better staining index for antigen-specific T cell detection compared with multimers prepared with wild-type MHC class I molecules.	Disulfides	37-46	major histocompatibility complex, class I, A	Homo sapiens	58-63
31324690-4	2019	Peptide-MHC multimers prepared using disulfide-stabilized HLA-A*02:01, HLA-A*24:02, and H-2Kb can be used to identify antigen-specific T cells, and they provide a better staining index for antigen-specific T cell detection compared with multimers prepared with wild-type MHC class I molecules.	Disulfides	37-46	major histocompatibility complex, class I, A	Homo sapiens	71-76
31183991-3	2019	Consequently, the disulfide in AG1 is not required for activation of G6PD, and a number of analogues were prepared without this reactive moiety.	Disulfides	18-27	NBPF member 10	Homo sapiens	31-34
31460422-4	2019	This approach was validated by conjugation of an anionic derivative of the tubulin-binding cytotoxin colchinol methyl ether to lysine residues of the HER2-targeting antibody trastuzumab (Herceptin) via a disulfide.	Disulfides	204-213	erb-b2 receptor tyrosine kinase 2	Homo sapiens	150-154
31417599-12	2019	The activity of oxidized AtAMY3 was completely restored by simultaneous reduction by both glutaredoxin (specific for the removal of glutathione-mixed disulfide) and thioredoxin (specific for the reduction of protein disulfide), supporting a possible liaison between both redox modifications.	Disulfides	150-159	alpha-amylase-like 3	Arabidopsis thaliana	25-31
31417599-12	2019	The activity of oxidized AtAMY3 was completely restored by simultaneous reduction by both glutaredoxin (specific for the removal of glutathione-mixed disulfide) and thioredoxin (specific for the reduction of protein disulfide), supporting a possible liaison between both redox modifications.	Disulfides	216-225	alpha-amylase-like 3	Arabidopsis thaliana	25-31
31324691-4	2019	We have developed a disulfide-stabilized HLA-A*02:01 molecule that is stable without peptide but can form peptide-MHC complexes (pMHCs) with ligands of choice in a one-step loading procedure.	Disulfides	20-29	major histocompatibility complex, class I, A	Homo sapiens	41-46
31324691-6	2019	In addition, we demonstrate a high-throughput binding kinetics measurement platform to analyze the binding characteristics of bispecific TCR (bsTCR) molecules against diverse pMHC libraries produced with the disulfide-stabilized HLA-A*02:01 molecule.	Disulfides	208-217	major histocompatibility complex, class I, A	Homo sapiens	229-234
31277465-2	2019	A disulfide cyclic peptide ligand [CTVRTSADC] 1 has been previously found to target extra domain B of fibronectin (EDB-FN) in the extracellular matrix that can differentiate aggressive PCa from benign prostatic hyperplasia.	Disulfides	2-11	fibronectin 1	Homo sapiens	102-113
31277465-2	2019	A disulfide cyclic peptide ligand [CTVRTSADC] 1 has been previously found to target extra domain B of fibronectin (EDB-FN) in the extracellular matrix that can differentiate aggressive PCa from benign prostatic hyperplasia.	Disulfides	2-11	fibronectin 1	Homo sapiens	115-118
31333616-6	2019	There are two cysteine residues in the structure of wild type vasopressin, which form a disulfide bridge in the mature peptide.	Disulfides	88-97	arginine vasopressin	Homo sapiens	62-73
31333465-3	2019	Since interaction with nAChRs was earlier shown for synthetic fragments of the alpha-neurotoxin central loop II, we synthesized a 15-membered fragment of human Lynx1, its form with two Cys residues added at the N- and C-termini and forming a disulfide, as well as similar forms of human SLURP1, SLURP2, and of Drosophila sleepless protein (SSS).	Disulfides	242-251	Ly6/neurotoxin 1	Homo sapiens	160-165
31333616-7	2019	Here, we show it is possible to direct the biosynthesis of vasopressin variants in such a way that the disulfide bridge is replaced by a thioether bridge using the nisin modification machinery NisBTC, albeit at low efficiency.	Disulfides	103-112	arginine vasopressin	Homo sapiens	59-70
31059082-3	2019	D-alpha-tocopheryl polyethylene glycol 1000 succinate (TPGS) conjugated to doxorubicin (DOX) through disulfide (S-S) bonds to constitute TPGS-S-S-DOX was synthesized; furthermore, hyaluronic acid (HA) was conjugated to TPGS to obtain HA-TPGS.	Disulfides	101-110	dark	Mus musculus	0-7
30863976-4	2019	Mainly located to the reducing cytosol, mature SOD1 contains an oxidized disulfide bond that is important for its stability.	Disulfides	73-82	superoxide dismutase 1	Homo sapiens	47-51
30863976-6	2019	By combining biochemical approaches in an extensive range of genetically distinct patient-derived cell lines, we show that the disulfide bond is an Achilles heel of the SOD1 protein.	Disulfides	127-136	superoxide dismutase 1	Homo sapiens	169-173
31209055-8	2019	Outside the membrane this symmetry is broken by the disulfide-bridged dimerization of the extracellular Ig domains of Igalpha and Igbeta.	Disulfides	52-61	CD79a molecule	Homo sapiens	118-125
31244485-0	2019	Penaeus monodon GILT enzyme restricts WSSV infectivity by reducing disulfide bonds in WSSV proteins.	Disulfides	67-76	IFI30 lysosomal thiol reductase	Homo sapiens	16-20
31209258-1	2019	Transforming growth factor beta is a disulfide-linked dimeric cytokine that occurs in three highly related isoforms (TGFbeta1-TGFbeta3) engaged in signaling functions through binding of cognate TGFbeta receptors.	Disulfides	37-46	tumor necrosis factor	Homo sapiens	0-31
30924212-5	2019	This strategy was applied to the synthesis of complex disulfide-rich peptides such as Rho-conotoxin rho-TIA and native human insulin.	Disulfides	54-63	insulin	Homo sapiens	125-132
31012517-0	2019	Substitution of an Internal Disulfide Bridge with a Diselenide Enhances both Foldability and Stability of Human Insulin.	Disulfides	28-37	insulin	Homo sapiens	112-119
31012517-2	2019	Whereas chemical syntheses of the individual A and B chains were accomplished in the early 1960s, their combination to form native insulin remains inefficient because of competing disulfide pairing and aggregation.	Disulfides	180-189	insulin	Homo sapiens	131-138
31184302-3	2019	In human (or rodent) islets with a perturbed endoplasmic reticulum folding environment, non-native proinsulin enters intermolecular disulfide-linked complexes.	Disulfides	132-141	insulin	Homo sapiens	99-109
31015146-6	2019	The myeloperoxidase-derived oxidants hypochlorous acid, taurine chloramine, hypobromous acid, and hypothiocyanous acid, all at 10 muM, cross-linked calprotectin (5 muM) via reversible disulfide bonds.	Disulfides	184-193	myeloperoxidase	Homo sapiens	4-19
30915639-7	2019	As L35 residue contributes to its hydrophobic core of the protein, the L35Q substitution is predicated to affect B19-A20 disulfide bond and therefore disrupt the folding of the proinsulin, which ultimately results in beta cell apoptosis by inducing ER stress.	Disulfides	121-130	insulin	Homo sapiens	177-187
30947639-4	2019	In this article, BSA was treated with urea and glutathione to prepare bovine serum albumin hydrogel controlled by two dynamic equilibrium bonds (disulfide and hydrogen bonds).	Disulfides	145-154	albumin	Homo sapiens	77-90
31010851-5	2019	Despite possessing an intact N terminus and preserved disulfide bonds, SpyCEP-cleaved CXCL8 had impaired binding to both CXCR1 and CXCR2, pointing to a requirement for the C-terminal alpha-helix.	Disulfides	54-63	C-X-C motif chemokine ligand 8	Homo sapiens	86-91
31177989-7	2019	Both the all-thiol and disulfide types of HMGB1 induced CitH3 via their specific receptors, CXCR4 and TLR4, respectively.	Disulfides	23-32	toll-like receptor 4	Rattus norvegicus	102-106
30991141-7	2019	In addition, PDT promoted intramolecular disulfide formation and inactivation of tumor suppressor PTEN, thereby favoring Akt and p300 activation leading to iNOS upregulation.	Disulfides	41-50	AKT serine/threonine kinase 1	Homo sapiens	121-124
30991141-7	2019	In addition, PDT promoted intramolecular disulfide formation and inactivation of tumor suppressor PTEN, thereby favoring Akt and p300 activation leading to iNOS upregulation.	Disulfides	41-50	nitric oxide synthase 2	Homo sapiens	156-160
30895794-4	2019	Here, we report a general and reliable strategy for the design and synthesis of a range of structurally diverse cross-link-dense peptide (CDP) scaffolds with two orthogonal disulfide bonds and a bisthioether bridge that are not subject to disulfide isomerizations.	Disulfides	173-182	natriuretic peptide A	Homo sapiens	112-136
30944182-2	2019	Here we examine two previously reported Env mutants designed to be stabilized in this conformation by the introduction of artificial disulfide bonds: A501C/T605C (called SOS) and I201C/A433C (called DS).	Disulfides	133-142	xylosyltransferase 2	Homo sapiens	170-173
30895794-4	2019	Here, we report a general and reliable strategy for the design and synthesis of a range of structurally diverse cross-link-dense peptide (CDP) scaffolds with two orthogonal disulfide bonds and a bisthioether bridge that are not subject to disulfide isomerizations.	Disulfides	173-182	natriuretic peptide A	Homo sapiens	138-141
30895794-4	2019	Here, we report a general and reliable strategy for the design and synthesis of a range of structurally diverse cross-link-dense peptide (CDP) scaffolds with two orthogonal disulfide bonds and a bisthioether bridge that are not subject to disulfide isomerizations.	Disulfides	239-248	natriuretic peptide A	Homo sapiens	138-141
30718919-3	2019	We previously showed that disruption of disulfide bond formation by Disulfide Disrupting Agents (DDAs) kills HER2/EGFR overexpressing cells through multiple mechanisms.	Disulfides	40-49	epidermal growth factor receptor	Homo sapiens	114-118
30862546-8	2019	In contrast, Prx1 and Prx2 were present in neutrophils from human blood as disulfides, and PMA or S. aureus caused no further oxidation.	Disulfides	75-85	peroxiredoxin 2	Homo sapiens	22-26
30718919-3	2019	We previously showed that disruption of disulfide bond formation by Disulfide Disrupting Agents (DDAs) kills HER2/EGFR overexpressing cells through multiple mechanisms.	Disulfides	40-49	erb-b2 receptor tyrosine kinase 2	Homo sapiens	109-113
30718919-3	2019	We previously showed that disruption of disulfide bond formation by Disulfide Disrupting Agents (DDAs) kills HER2/EGFR overexpressing cells through multiple mechanisms.	Disulfides	68-77	erb-b2 receptor tyrosine kinase 2	Homo sapiens	109-113
30718919-3	2019	We previously showed that disruption of disulfide bond formation by Disulfide Disrupting Agents (DDAs) kills HER2/EGFR overexpressing cells through multiple mechanisms.	Disulfides	68-77	epidermal growth factor receptor	Homo sapiens	114-118
31114584-12	2019	During evolution, changes in the intrachain disulfide and interchain disulfide bonds and changes in the glycosylation status of CRP may be responsible for different structure-function relationships of CRP in various species.	Disulfides	44-53	C-reactive protein	Homo sapiens	201-204
30948502-0	2019	Redox equilibrium of serum apolipoprotein E3: a buffering effect of disulfide-linked complexes against oxidative stress on apolipoprotein E3-containing lipoproteins.	Disulfides	68-77	apolipoprotein E	Homo sapiens	27-44
30948502-0	2019	Redox equilibrium of serum apolipoprotein E3: a buffering effect of disulfide-linked complexes against oxidative stress on apolipoprotein E3-containing lipoproteins.	Disulfides	68-77	apolipoprotein E	Homo sapiens	123-140
30948502-3	2019	Here, we hypothesized that the disulfide-linked complexes of apoE3 corresponding to the representative reversible-modified apoE3 play a protective role against oxidative stress.	Disulfides	31-40	apolipoprotein E	Homo sapiens	61-66
30948502-3	2019	Here, we hypothesized that the disulfide-linked complexes of apoE3 corresponding to the representative reversible-modified apoE3 play a protective role against oxidative stress.	Disulfides	31-40	apolipoprotein E	Homo sapiens	123-128
30948502-4	2019	The effects of disulfide bond formation on oxidative stress on apoE3 were evaluated with a band-shift assay.	Disulfides	15-24	apolipoprotein E	Homo sapiens	63-68
31223112-1	2019	Objective To investigate the expression and clinical significance of whey acidic protein (WAP) 4-disulfide core domain 2/human epididymis protein 4 (WFDC2/HE4) in lung adenocarcinoma.	Disulfides	97-106	secretory leukocyte peptidase inhibitor	Homo sapiens	69-96
31114584-12	2019	During evolution, changes in the intrachain disulfide and interchain disulfide bonds and changes in the glycosylation status of CRP may be responsible for different structure-function relationships of CRP in various species.	Disulfides	69-78	C-reactive protein	Homo sapiens	201-204
30642920-2	2019	D1 and D2 in the prodomain and D"D3 in mature VWF at Golgi pH form helical VWF tubules in Weibel Palade bodies and template dimerization of D3 through disulfides to form ultralong VWF concatemers.	Disulfides	151-161	von Willebrand factor	Homo sapiens	75-78
30936056-5	2019	In support of this, A2-domain mutations that prevent domain unfolding due to disulfide bridging of N- and C-terminal residues ("Lock-VWF") reduce self-association and platelet activation under various experimental conditions.	Disulfides	77-86	von Willebrand factor	Homo sapiens	133-136
30913878-0	2019	Role of Disulfide Bonds and Topological Frustration in the Kinetic Partitioning of Lysozyme Folding Pathways.	Disulfides	8-17	lysozyme	Homo sapiens	83-91
30913878-2	2019	Lysozyme has four disulfide bonds and is widely studied for its antibacterial properties.	Disulfides	18-27	lysozyme	Homo sapiens	0-8
30913878-5	2019	Using a coarse-grained protein model and simulations, we show that two out of the four disulfide bonds, which are present in the alpha-domain of lysozyme, are responsible for the slow folding pathway.	Disulfides	87-96	lysozyme	Homo sapiens	145-153
30913878-14	2019	These results show that lysozyme also serves as a very good model system to probe the role of disulfide bonds and topological frustration in protein folding.	Disulfides	94-103	lysozyme	Homo sapiens	24-32
30642920-2	2019	D1 and D2 in the prodomain and D"D3 in mature VWF at Golgi pH form helical VWF tubules in Weibel Palade bodies and template dimerization of D3 through disulfides to form ultralong VWF concatemers.	Disulfides	151-161	von Willebrand factor	Homo sapiens	75-78
30642920-11	2019	The organizing principle for the D3 assembly has implications for other D assemblies and the construction of higher-order, disulfide-linked assemblies in the Golgi in both VWF and mucins.	Disulfides	123-132	von Willebrand factor	Homo sapiens	172-175
30807169-5	2019	Besides a three-protein mixture, a mixture of disulfide bond reduced insulin was also studied by this MCE-restrained modeling method.	Disulfides	46-55	insulin	Homo sapiens	69-76
30604098-2	2019	All insulin superfamily members contain three absolutely conserved disulfide linkages and a nonchiral Gly residue immediately following the first B-chain cysteine.	Disulfides	67-76	insulin	Homo sapiens	4-11
30735910-1	2019	Protein disulfide isomerases (PDI) are a family of redox chaperones that catalyze formation or isomerization of disulfide bonds in proteins.	Disulfides	8-17	protein disulfide isomerase family A member 2	Homo sapiens	30-33
30700553-5	2019	Substitution within the Kunitz inhibitor domain of the amyloid precursor protein (APPI) that incorporated a new disulfide bond between residues 17 and 34 reduced proteolysis by mesotrypsin 74-fold.	Disulfides	112-121	amyloid beta precursor protein	Homo sapiens	55-80
30700553-5	2019	Substitution within the Kunitz inhibitor domain of the amyloid precursor protein (APPI) that incorporated a new disulfide bond between residues 17 and 34 reduced proteolysis by mesotrypsin 74-fold.	Disulfides	112-121	amyloid beta precursor protein	Homo sapiens	82-86
30700553-7	2019	Crystal structures of disulfide-engineered APPI and KD1TFPI1 variants in a complex with mesotrypsin at 1.5 and 2.0 A resolution, respectively, confirmed the formation of well-ordered disulfide bonds positioned to stabilize the binding loop.	Disulfides	22-31	amyloid beta precursor protein	Homo sapiens	43-47
30700553-7	2019	Crystal structures of disulfide-engineered APPI and KD1TFPI1 variants in a complex with mesotrypsin at 1.5 and 2.0 A resolution, respectively, confirmed the formation of well-ordered disulfide bonds positioned to stabilize the binding loop.	Disulfides	183-192	amyloid beta precursor protein	Homo sapiens	43-47
30830762-5	2019	Mixtures of holo- and apo-myoglobin (Mb) and disulfide isomers of lysozyme (Lyz) were characterized in a conformer-specific fashion using this strategy, followed by conformation interrogation for the sequentially eluted 2H-labeled species in real-time using top-down MS.	Disulfides	45-54	lysozyme	Homo sapiens	66-74
30830762-6	2019	Under mildly denaturing conditions that minimize the charge difference, disulfide isomers of Lyz were differentially labeled with 2H during separation based on their disulfide-dependent sizes.	Disulfides	72-81	lysozyme	Homo sapiens	93-96
30830762-6	2019	Under mildly denaturing conditions that minimize the charge difference, disulfide isomers of Lyz were differentially labeled with 2H during separation based on their disulfide-dependent sizes.	Disulfides	166-175	lysozyme	Homo sapiens	93-96
30941117-4	2019	The C-terminal domain of YAP1 contains cysteine residues that, under oxidizing conditions, form an intramolecular disulfide bridge locking the molecule in a conformation where the nuclear export sequence is masked.	Disulfides	114-123	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	25-29
30599297-6	2019	All individuals shared a substitution of a cysteine residue, disrupting disulfide bonds in the FN type-I assembly domains located in the N-terminal assembly region.	Disulfides	72-81	fibronectin 1	Homo sapiens	95-97
30735910-5	2019	Treatment with a PDI inhibitor, LOC14 inhibited PDIA3 activity in lung epithelial cells, decreased intramolecular disulfide bonds and subsequent oligomerization (maturation) of HA in both H1N1 (A/PR8/34) and H3N2 (X31, A/Aichi/68) infected lung epithelial cells.	Disulfides	114-123	protein disulfide isomerase family A member 2	Homo sapiens	17-20
30670593-5	2019	ERp57 attenuated ficolin-3 ligand recognition and complement activation by cleaving intermolecular disulfide bonds in large ficolin-3 multimers, thereby reducing multimer size and ligand-binding affinity.	Disulfides	99-108	protein disulfide isomerase family A member 3	Homo sapiens	0-5
30670593-8	2019	We conclude that extensive multimerization in large ficolin-3 multimers leads to a high affinity for ligands and strong complement-activating potential and that ERp57 suppresses complement activation by cleaving disulfide bonds in ficolin-3 and reducing its multimer size.	Disulfides	212-221	protein disulfide isomerase family A member 3	Homo sapiens	161-166
30841526-2	2019	Building on this scaffold, a disulfide-linked conjugate with the purported EGFR-binding (EGFR, epidermal growth factor receptor) peptide GE11 was then prepared.	Disulfides	29-38	epidermal growth factor receptor	Homo sapiens	75-79
30635404-7	2019	EVs from brains and spinal cords of the SOD1G93A ALS mouse model, as well as from human SOD1 familial ALS patient spinal cord, contained abundant misfolded and nonnative disulfide-cross-linked aggregated SOD1.	Disulfides	170-179	superoxide dismutase 1	Homo sapiens	88-92
30635404-7	2019	EVs from brains and spinal cords of the SOD1G93A ALS mouse model, as well as from human SOD1 familial ALS patient spinal cord, contained abundant misfolded and nonnative disulfide-cross-linked aggregated SOD1.	Disulfides	170-179	superoxide dismutase 1	Homo sapiens	88-92
30841526-2	2019	Building on this scaffold, a disulfide-linked conjugate with the purported EGFR-binding (EGFR, epidermal growth factor receptor) peptide GE11 was then prepared.	Disulfides	29-38	epidermal growth factor receptor	Homo sapiens	89-93
30841526-2	2019	Building on this scaffold, a disulfide-linked conjugate with the purported EGFR-binding (EGFR, epidermal growth factor receptor) peptide GE11 was then prepared.	Disulfides	29-38	epidermal growth factor receptor	Homo sapiens	95-127
30317562-4	2019	In this study, we first demonstrated that an intramolecular disulfide bond was formed between cysteine-102 and cysteine-121 in FGF21, implying that the oxidation of the cysteine to cysteic acid, which may interfere with the active conformation of FGF21, did not occur during the iodination procedures, and thus ruled out the possibility of the two conserved cysteine residues mediating the loss of FGF21 binding affinity to FGFR1-KLB upon iodination.	Disulfides	60-69	fibroblast growth factor 21	Homo sapiens	127-132
30714345-3	2019	The target gene of PS-ATNF-alpha, with a poly(dA) tail through a disulfide bond (-SS-), interacts with s-LNT to form a rod-like nanocomposite of s-LNT/poly(dA)-SS-PS-ATNF-alpha, which significantly inhibits lipopolysaccharide (LPS)-induced TNF-alpha at the protein level by 38.2% and mRNA level by 48.9% in RAW264.7 macrophages.	Disulfides	65-74	tumor necrosis factor	Homo sapiens	23-32
30554018-4	2019	PEG modified glycolipid-like polymer (P-CSSO) was electrostatic interacted with p53 to form P-CSSO/p53 complexes, which exhibited an enhanced redox sensitivity in that the disulfide bond was degraded and the rate the plasmid released from P-CSSO was 2.29-fold that of nonresponsive platform (P-CSO-SA) in 10 mM levels of glutathione (GSH).	Disulfides	172-181	tumor protein p53	Homo sapiens	80-83
30554018-4	2019	PEG modified glycolipid-like polymer (P-CSSO) was electrostatic interacted with p53 to form P-CSSO/p53 complexes, which exhibited an enhanced redox sensitivity in that the disulfide bond was degraded and the rate the plasmid released from P-CSSO was 2.29-fold that of nonresponsive platform (P-CSO-SA) in 10 mM levels of glutathione (GSH).	Disulfides	172-181	tumor protein p53	Homo sapiens	99-102
30839289-2	2019	OSM1 genetically interacts with ERO1, which encodes an essential ER oxidoreductase for disulfide-bond formation under anaerobic conditions.	Disulfides	87-96	fumarate reductase	Saccharomyces cerevisiae S288C	0-4
30317562-4	2019	In this study, we first demonstrated that an intramolecular disulfide bond was formed between cysteine-102 and cysteine-121 in FGF21, implying that the oxidation of the cysteine to cysteic acid, which may interfere with the active conformation of FGF21, did not occur during the iodination procedures, and thus ruled out the possibility of the two conserved cysteine residues mediating the loss of FGF21 binding affinity to FGFR1-KLB upon iodination.	Disulfides	60-69	fibroblast growth factor 21	Homo sapiens	247-252
30317562-4	2019	In this study, we first demonstrated that an intramolecular disulfide bond was formed between cysteine-102 and cysteine-121 in FGF21, implying that the oxidation of the cysteine to cysteic acid, which may interfere with the active conformation of FGF21, did not occur during the iodination procedures, and thus ruled out the possibility of the two conserved cysteine residues mediating the loss of FGF21 binding affinity to FGFR1-KLB upon iodination.	Disulfides	60-69	fibroblast growth factor 21	Homo sapiens	247-252
30317562-4	2019	In this study, we first demonstrated that an intramolecular disulfide bond was formed between cysteine-102 and cysteine-121 in FGF21, implying that the oxidation of the cysteine to cysteic acid, which may interfere with the active conformation of FGF21, did not occur during the iodination procedures, and thus ruled out the possibility of the two conserved cysteine residues mediating the loss of FGF21 binding affinity to FGFR1-KLB upon iodination.	Disulfides	60-69	fibroblast growth factor receptor 1	Homo sapiens	424-429
30867929-5	2019	They are connected by an exposed linker with a rigid, disulfide-linked "CPDCP-trunk", and are followed by a C-terminal region (CTR) with little regular secondary structure.	Disulfides	54-63	calcitonin receptor	Homo sapiens	108-125
29947407-7	2019	Incorporation of this linker, or "helping hand", on the N-terminus greatly improved the solubility of chicken insulin A-chain, which is analogous to human insulin, and allowed for coupling of the insulin A- and B-chain via directed disulfide bond formation.	Disulfides	232-241	insulin	Homo sapiens	110-117
31011701-1	2019	Abstract: Fibrinogen, involved in coagulation, is a soluble protein composed of two sets of disulfide-bridged Aalpha, Bbeta, and gamma-chains.	Disulfides	92-101	fibrinogen beta chain	Homo sapiens	10-20
30754725-4	2019	We have also proposed that at least two FKBPs, namely FKBP36, encoded by the Fkbp6 gene and FKBP51, encoded by the Fkbp5 gene, can form dimers bound via a disulfide bridge in the nucleus.	Disulfides	155-164	FKBP prolyl isomerase 5	Homo sapiens	115-120
30502392-5	2019	Accordingly, Arabidopsis GRXS16 reacted efficiently with oxidized forms of glutathione, leading to the formation of an intramolecular disulfide between Cys158 and the semi-conserved Cys215, which has a midpoint redox potential of - 298 mV at pH 7.0 and is reduced by plastidial thioredoxins (TRXs) but not GSH.	Disulfides	134-143	CAX-interacting protein 2	Arabidopsis thaliana	25-31
30600179-3	2019	Human PrP contains two cysteines at positions 179 (C179) and 214 (C214) enabling disulfide bonding.	Disulfides	81-90	prion protein	Homo sapiens	6-9
30600179-4	2019	Here, we report that our recombinant human PrP (r-hPrP) preparations contain 0.2-0.8% dimer, which is linked by either one or two disulfide bonds, connected by C179-C179, C214-C214, or C179-C214.	Disulfides	130-139	prion protein	Homo sapiens	43-46
30502392-6	2019	By promoting the formation of this disulfide, Cys215 modulates GRXS16 oxidoreductase activity.	Disulfides	35-44	CAX-interacting protein 2	Arabidopsis thaliana	63-69
30502392-8	2019	Hence, disulfide formation may constitute a redox switch mechanism controlling GRXS16 function in response to day/night transition or oxidizing conditions.	Disulfides	7-16	CAX-interacting protein 2	Arabidopsis thaliana	79-85
32254726-3	2019	In particular, the anti-epithelial cell adhesion molecule (anti-EpCAM) antibody was introduced with a disulfide bond-containing linker for further bio-friendly recovery of the CTCs.	Disulfides	102-111	epithelial cell adhesion molecule	Homo sapiens	24-57
30570212-5	2019	Arabidopsis SerRS displays structural features typical of canonical SerRSs, except for a unique intrasubunit disulfide bridge.	Disulfides	109-118	Seryl-tRNA synthetase	Arabidopsis thaliana	12-17
30520161-0	2019	Disulfide bridge formation influences ligand recognition by the ATAD2 bromodomain.	Disulfides	0-9	ATPase family AAA domain containing 2	Homo sapiens	64-69
30520161-3	2019	We solved the crystal structure of the ATAD2 bromodomain and found that it contains a disulfide bridge near the base of the acetyllysine binding pocket (Cys1057-Cys1079).	Disulfides	86-95	ATPase family AAA domain containing 2	Homo sapiens	39-44
30520161-5	2019	Isothermal titration calorimetry experiments in combination with the Ellman"s assay demonstrated that formation of an intramolecular disulfide bridge negatively impacts the ligand binding affinities and alters the thermodynamic parameters of the ATAD2 bromodomain interaction with a histone H4K5ac peptide as well as a small molecule bromodomain ligand.	Disulfides	133-142	ATPase family AAA domain containing 2	Homo sapiens	246-251
30520161-6	2019	Molecular dynamics simulations indicate that the formation of the disulfide bridge in the ATAD2 bromodomain does not alter the structure of the folded state or flexibility of the acetyllysine binding pocket.	Disulfides	66-75	ATPase family AAA domain containing 2	Homo sapiens	90-95
30394319-2	2019	Studies using in vivo and in vitro model systems demonstrated that diverse post-translational modifications, including phosphorylation, glycosylation, serotonylation, and disulfide bond formation, all favorably influences SERT conformation and allows the transporter to function most efficiently.	Disulfides	171-180	solute carrier family 6 member 4	Homo sapiens	222-226
32254726-3	2019	In particular, the anti-epithelial cell adhesion molecule (anti-EpCAM) antibody was introduced with a disulfide bond-containing linker for further bio-friendly recovery of the CTCs.	Disulfides	102-111	epithelial cell adhesion molecule	Homo sapiens	64-69
30395443-5	2019	Disulfide exchange between the mutated cysteines and the activated disulfides yielded 20 foldamer-IL4 and 20 foldamer-CypA adducts.	Disulfides	0-9	interleukin 4	Homo sapiens	98-101
30429345-1	2019	Binding to the receptor CD4 triggers entry-related conformational changes in the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer, (gp120/gp41)3 Soluble versions of HIV-1 Env trimers (sgp140 SOSIP.664) stabilized by a gp120-gp41 disulfide bond and a change (I559P) in gp41 have been structurally characterized.	Disulfides	259-268	CD4 molecule	Homo sapiens	24-27
30395443-5	2019	Disulfide exchange between the mutated cysteines and the activated disulfides yielded 20 foldamer-IL4 and 20 foldamer-CypA adducts.	Disulfides	67-77	interleukin 4	Homo sapiens	98-101
30252537-10	2019	Complexation with TBA polymers appeared to result in disulfide bridge formation between the polymers and insulin.	Disulfides	53-62	insulin	Homo sapiens	105-112
30248376-4	2019	RESULTS: By forcing the formation of a disulfide bridge between Cys residues at positions 57 and 87 we obtained a destabilized p17 capable of promoting B cell proliferation.	Disulfides	39-48	family with sequence similarity 72 member B	Homo sapiens	127-130
30172908-1	2019	The reduction of disulfide bonds of exogenous antigens is crucial to the MHC-II class antigen processing and presenting pathway and is catalysed by interferon-gamma-inducible lysosomal thiol reductase (GILT).	Disulfides	17-26	gamma-interferon-inducible lysosomal thiol reductase	Pelodiscus sinensis	148-200
30172908-1	2019	The reduction of disulfide bonds of exogenous antigens is crucial to the MHC-II class antigen processing and presenting pathway and is catalysed by interferon-gamma-inducible lysosomal thiol reductase (GILT).	Disulfides	17-26	gamma-interferon-inducible lysosomal thiol reductase	Pelodiscus sinensis	202-206
30687084-3	2018	These disulfide-rich peptides provide a large number of evolutionarily refined templates that can be used to develop conopeptides that are highly selective for the various nAChR subtypes.	Disulfides	6-15	cholinergic receptor nicotinic alpha 4 subunit	Homo sapiens	172-177
29725115-7	2019	We show that MICU3 forms a disulfide bond-mediated dimer with MICU1, but not with MICU2, and it acts as enhancer of MCU-dependent mitochondrial Ca2+ uptake.	Disulfides	27-36	mitochondrial calcium uniporter	Homo sapiens	116-119
30284335-6	2019	As previously observed, a crucial difference between PRDX1 and PRDX2 is on the resolution step of the catalytic cycle, the rate of disulfide formation (11 s-1 for PRDX1, 0.2 s-1 for PRDX2, independent of the oxidant) which correlates with their different sensitivity to hyperoxidation.	Disulfides	131-140	peroxiredoxin 2	Homo sapiens	63-68
30284335-6	2019	As previously observed, a crucial difference between PRDX1 and PRDX2 is on the resolution step of the catalytic cycle, the rate of disulfide formation (11 s-1 for PRDX1, 0.2 s-1 for PRDX2, independent of the oxidant) which correlates with their different sensitivity to hyperoxidation.	Disulfides	131-140	peroxiredoxin 2	Homo sapiens	182-187
30284335-8	2019	The longer lifetime of PRDX2 sulfenic acid allows it to react with other protein thiols to translate the signal via an intermediate mixed disulfide (involving its peroxidatic cysteine), whereas PRDX1 continues the cycle forming disulfide involving its resolving cysteine to function as a redox relay.	Disulfides	138-147	peroxiredoxin 2	Homo sapiens	23-28
30284335-8	2019	The longer lifetime of PRDX2 sulfenic acid allows it to react with other protein thiols to translate the signal via an intermediate mixed disulfide (involving its peroxidatic cysteine), whereas PRDX1 continues the cycle forming disulfide involving its resolving cysteine to function as a redox relay.	Disulfides	228-237	peroxiredoxin 2	Homo sapiens	23-28
30367523-4	2019	Accordingly, the co-crystallization of Tom20 and a presequence peptide required a disulfide-bond cross-linking.	Disulfides	82-91	translocase of outer mitochondrial membrane 20	Homo sapiens	39-44
30367523-7	2019	Here, we have performed replica-exchange molecular dynamics (REMD) simulations to study the effect of disulfide-bond linker and single amino acid difference in the spacer region of the linker on the conformational dynamics of Tom20-presequence complex.	Disulfides	102-111	translocase of outer mitochondrial membrane 20	Homo sapiens	226-231
30429329-4	2018	The resulting disulfide bonds unfold the globular domain of DksA, signaling high-affinity interaction of the C-terminal alpha-helix to DnaJ.	Disulfides	14-23	DnaJ heat shock protein family (Hsp40) member A2	Homo sapiens	135-139
30514088-5	2018	Herein, a new self-assembly method based on a robust dye SQSS of which two squaraine molecules were conjugated through disulfide bond was developed for highly selective and sensitive detection of serum albumin (SA) in aqueous solution and live cells.	Disulfides	119-128	albumin	Homo sapiens	196-209
30429329-5	2018	Oxidoreductase and chaperone activities of DnaJ reduce the disulfide bonds of its client and promote productive interactions between DksA and RNA polymerase.	Disulfides	59-68	DnaJ heat shock protein family (Hsp40) member A2	Homo sapiens	43-47
30531830-0	2018	The reduced activity of PP-1alpha under redox stress condition is a consequence of GSH-mediated transient disulfide formation.	Disulfides	106-115	protein phosphatase 1 catalytic subunit alpha	Homo sapiens	24-33
30342934-4	2018	A proposed second disulfide bridge in the endothelin-B receptor tethering the N-terminal domain with the third extracellular loop was not essential for ET-1 recognition and binding, but increased the receptor thermostability.	Disulfides	18-27	endothelin receptor type B	Homo sapiens	42-63
30531830-3	2018	We propose here that formation of transient disulfide bridges in PP-1alpha might play a leading role in oxidative stress response.	Disulfides	44-53	protein phosphatase 1 catalytic subunit alpha	Homo sapiens	65-74
30531830-5	2018	By applying this method, we demonstrate the formation of unexpected transient disulfides in PP-1alpha to shelter against over-oxidation.	Disulfides	78-88	protein phosphatase 1 catalytic subunit alpha	Homo sapiens	92-101
30453601-1	2018	The redox regulation of proteins via reversible dithiol/disulfide exchange reactions involves the thioredoxin system, which is composed of a reductant, a thioredoxin reductase (TR), and thioredoxin (Trx).	Disulfides	56-65	thioredoxin family protein	Methanosarcina mazei Go1	98-109
30574097-8	2018	Out of ninety cysteine residues per RyR2 subunit, twenty one were reported to be in reduced state that could be potential targets for redox modifications that include S-nitrosylation, S-glutathionylation, and disulfide cross-linking.	Disulfides	209-218	ryanodine receptor 2	Homo sapiens	36-40
30351116-3	2018	Different preparations of FH can also reduce the disulfide bonds linking large Von Willebrand factor (VWF) multimers into smaller, less adhesive forms.	Disulfides	49-58	von Willebrand factor	Homo sapiens	79-100
30351116-3	2018	Different preparations of FH can also reduce the disulfide bonds linking large Von Willebrand factor (VWF) multimers into smaller, less adhesive forms.	Disulfides	49-58	von Willebrand factor	Homo sapiens	102-105
30451826-5	2018	Moreover, ER-resident Osm1 can transfer electrons from the Ero1 FAD cofactor to fumarate either by free FAD or by a direct interaction, allowing de novo disulfide bond formation in the absence of oxygen.	Disulfides	153-162	fumarate reductase	Saccharomyces cerevisiae S288C	22-26
30451826-5	2018	Moreover, ER-resident Osm1 can transfer electrons from the Ero1 FAD cofactor to fumarate either by free FAD or by a direct interaction, allowing de novo disulfide bond formation in the absence of oxygen.	Disulfides	153-162	ER oxidoreductin	Saccharomyces cerevisiae S288C	59-63
30361244-2	2018	There are currently alternative hypotheses that attempt to describe the abnormally viscous and elastic mucus that is a hallmark of CF airways disease, including: 1) loss of CF transmembrane regulator (CFTR)-dependent airway surface volume (water) secretion, producing mucus hyperconcentration-dependent increased viscosity, and 2) impaired bicarbonate secretion by CFTR, producing acidification of airway surfaces and increased mucus viscosity.A series of experiments was conducted to determine the contributions of mucus concentration versus pH to the rheological properties of airway mucus across length scales from the nanoscopic to macroscopic.For length scales greater than the nanoscopic, i.e. those relevant to mucociliary clearance, the effect of mucus concentration dominated over the effect of airway acidification.Mucus hydration and chemical reduction of disulfide bonds that connect mucin monomers are more promising therapeutic approaches than alkalisation.	Disulfides	867-876	CF transmembrane conductance regulator	Homo sapiens	201-205
30250978-2	2018	Because mSA contains a structurally important disulfide bond, the molecule does not fold correctly when expressed inside the cell.	Disulfides	46-55	exonuclease 1	Mus musculus	8-11
30412834-0	2018	A novel fibrinogen gamma-chain mutation, p.Cys165Arg, causes disruption of the gamma165Cys-Bbeta227Cys disulfide bond and ultimately leads to hypofibrinogenemia.	Disulfides	103-112	fibrinogen gamma chain	Homo sapiens	8-30
30412834-10	2018	CONCLUSIONS: Fibrinogen gammaCys165Arg mutations cause damage to the interchain disulfide bonds of fibrinogen and hinder fibrinogen secretion, possibly explaining the pathological mechanism associated with congenital hypofibrinogenemia.	Disulfides	80-89	fibrinogen beta chain	Homo sapiens	13-23
30412834-10	2018	CONCLUSIONS: Fibrinogen gammaCys165Arg mutations cause damage to the interchain disulfide bonds of fibrinogen and hinder fibrinogen secretion, possibly explaining the pathological mechanism associated with congenital hypofibrinogenemia.	Disulfides	80-89	fibrinogen beta chain	Homo sapiens	99-109
30315102-6	2018	MS analysis of these complexes helped identify the disulfide-linked PDIp targets in vivo, revealing that PDIp interacts directly with a number of pancreatic digestive enzymes.	Disulfides	51-60	protein disulfide isomerase family A member 2	Homo sapiens	68-72
30315102-6	2018	MS analysis of these complexes helped identify the disulfide-linked PDIp targets in vivo, revealing that PDIp interacts directly with a number of pancreatic digestive enzymes.	Disulfides	51-60	protein disulfide isomerase family A member 2	Homo sapiens	105-109
30453601-1	2018	The redox regulation of proteins via reversible dithiol/disulfide exchange reactions involves the thioredoxin system, which is composed of a reductant, a thioredoxin reductase (TR), and thioredoxin (Trx).	Disulfides	56-65	thioredoxin family protein	Methanosarcina mazei Go1	154-165
30453601-1	2018	The redox regulation of proteins via reversible dithiol/disulfide exchange reactions involves the thioredoxin system, which is composed of a reductant, a thioredoxin reductase (TR), and thioredoxin (Trx).	Disulfides	56-65	thioredoxin family protein	Methanosarcina mazei Go1	154-165
30453601-1	2018	The redox regulation of proteins via reversible dithiol/disulfide exchange reactions involves the thioredoxin system, which is composed of a reductant, a thioredoxin reductase (TR), and thioredoxin (Trx).	Disulfides	56-65	thioredoxin family protein	Methanosarcina mazei Go1	199-202
30346746-7	2018	Parallel enzymatic studies on the CDO variant C93G were carried out with the abt substrate and show that reaction with O2 leads to disulfide formation, as opposed to S-oxygenation.	Disulfides	131-140	cell adhesion associated, oncogene regulated	Homo sapiens	34-37
29064322-7	2018	Due to the linkage between chain of insulin and chain of disulfide bonds, opposite directional movements of N terminal part of chain A (toward nanoparticle surface) and N termini of chain B (toward solution) make insulin unfolding.	Disulfides	57-66	insulin	Homo sapiens	213-220
30464464-10	2018	Intracellular trafficking and in vitro expression study indicated that the DHP nanocomplex escaped from lysosomes and the disulfide bonds between PAMAM and PEG cleaved due to the high concentration of GSH in the cytoplasm, pDNA consequently became exclusively located in the nucleus under the guidance of HMGB1, thereby promoting the red fluorescence protein (RFP) expression.	Disulfides	122-131	dihydropyrimidinase	Homo sapiens	75-78
30388869-8	2018	The activated HGFAC cleaves proHGF at Arg494-Val495, resulting in the formation of the active disulfide-linked heterodimer HGF.	Disulfides	94-103	HGF activator	Homo sapiens	14-19
30350608-7	2018	Coupling different degrees of partial disulfide reduction with ESI-MS/MS allows disulfide mapping as demonstrated for characterizing the three disulfide bonds in insulin.	Disulfides	38-47	insulin	Homo sapiens	162-169
30350608-7	2018	Coupling different degrees of partial disulfide reduction with ESI-MS/MS allows disulfide mapping as demonstrated for characterizing the three disulfide bonds in insulin.	Disulfides	80-89	insulin	Homo sapiens	162-169
30350608-7	2018	Coupling different degrees of partial disulfide reduction with ESI-MS/MS allows disulfide mapping as demonstrated for characterizing the three disulfide bonds in insulin.	Disulfides	80-89	insulin	Homo sapiens	162-169
30560017-1	2018	Gamma-interferon-inducible lysosomal thiol reductase (GILT), expressed in antigen-presenting cells (APCs), facilitates the reduction of disulfide bonds of endocytosed proteins in the endocytic pathway and they are further processed for presentation of immunogenic peptides loaded on major histocompatibility complex (MHC) class II.	Disulfides	136-145	IFI30 lysosomal thiol reductase	Homo sapiens	0-52
30560017-1	2018	Gamma-interferon-inducible lysosomal thiol reductase (GILT), expressed in antigen-presenting cells (APCs), facilitates the reduction of disulfide bonds of endocytosed proteins in the endocytic pathway and they are further processed for presentation of immunogenic peptides loaded on major histocompatibility complex (MHC) class II.	Disulfides	136-145	IFI30 lysosomal thiol reductase	Homo sapiens	54-58
30339677-3	2018	Insulin is composed of A- and B-chain containing three disulfide bonds (one intarchain and two interchains).	Disulfides	55-64	insulin	Homo sapiens	0-7
30351115-2	2018	Using serum albumin as a model, this study aims to expand our understanding of this relationship for a larger (66 kDa), multidomain protein that contains 17 internal disulfide bonds.	Disulfides	166-175	albumin	Homo sapiens	6-19
31458105-8	2018	We further show that GdmCl denatures lysozyme with the disulfide bonds intact in the protein, whereas urea denatures the protein only when the disulfide bonds are broken using reducing agents.	Disulfides	55-64	lysozyme	Homo sapiens	37-45
30130449-3	2018	To improve biochemical stability, cysteine residues are often engineered on the heavy- and light-chain regions of the scFv to form an intrachain disulfide bond.	Disulfides	145-154	immunglobulin heavy chain variable region	Homo sapiens	118-122
30130449-6	2018	Structural characterization studies showed that the size variants resulted from the engineered disulfide bond on the scFv, whereby the engineered disulfide was found to be either open or unable to form an intrachain disulfide bond due to cysteinylation or glutathionylation of the cysteines.	Disulfides	95-104	immunglobulin heavy chain variable region	Homo sapiens	117-121
30130449-6	2018	Structural characterization studies showed that the size variants resulted from the engineered disulfide bond on the scFv, whereby the engineered disulfide was found to be either open or unable to form an intrachain disulfide bond due to cysteinylation or glutathionylation of the cysteines.	Disulfides	146-155	immunglobulin heavy chain variable region	Homo sapiens	117-121
30130449-6	2018	Structural characterization studies showed that the size variants resulted from the engineered disulfide bond on the scFv, whereby the engineered disulfide was found to be either open or unable to form an intrachain disulfide bond due to cysteinylation or glutathionylation of the cysteines.	Disulfides	146-155	immunglobulin heavy chain variable region	Homo sapiens	117-121
30130449-7	2018	Furthermore, the scFv engineered cysteines also formed intermolecular disulfide bonds, leading to the formation of highly stable dimers and aggregates.	Disulfides	70-79	immunglobulin heavy chain variable region	Homo sapiens	17-21
30375487-2	2018	Here we show that egg lysozyme displays a clever strategy to prevent this deleterious aggregation during the nascent phase when disulfides are still absent.	Disulfides	128-138	lysozyme	Homo sapiens	22-30
30190325-5	2018	H2O2 treatment of JNK2 resulted in detectable levels of peptides containing intramolecular disulfides between Cys-222 and either Cys-213 or Cys-177, without evidence of dimer formation.	Disulfides	91-101	mitogen-activated protein kinase 9	Homo sapiens	18-22
30284837-1	2018	A direct C(sp2)-H thiolation of aromatic amides with disulfides was developed.	Disulfides	53-63	Sp2 transcription factor	Homo sapiens	9-14
30429951-4	2018	Oxa/cis-platin is able to interact with hSOD1 in the disulfide oxidized apo form by binding cysteine 111 (Cys111).	Disulfides	53-62	superoxide dismutase 1	Homo sapiens	40-45
29866275-7	2018	Monothiol- and disulfide-containing compounds differentially regulated TGase2 transamidase and kinase activities.	Disulfides	15-24	transglutaminase 2	Homo sapiens	71-77
29961824-4	2018	Non-covalent Prph2/Rom1 homo- and hetero-tetramers assemble into higher-order covalently linked complexes held together by an intermolecular disulfide bond at Prph2-C150/Rom1-C153.	Disulfides	141-150	peripherin 2	Mus musculus	13-18
29961824-4	2018	Non-covalent Prph2/Rom1 homo- and hetero-tetramers assemble into higher-order covalently linked complexes held together by an intermolecular disulfide bond at Prph2-C150/Rom1-C153.	Disulfides	141-150	rod outer segment membrane protein 1	Mus musculus	19-23
29961824-4	2018	Non-covalent Prph2/Rom1 homo- and hetero-tetramers assemble into higher-order covalently linked complexes held together by an intermolecular disulfide bond at Prph2-C150/Rom1-C153.	Disulfides	141-150	peripherin 2	Mus musculus	159-164
29961824-4	2018	Non-covalent Prph2/Rom1 homo- and hetero-tetramers assemble into higher-order covalently linked complexes held together by an intermolecular disulfide bond at Prph2-C150/Rom1-C153.	Disulfides	141-150	rod outer segment membrane protein 1	Mus musculus	170-174
29585927-2	2018	Mature active MPO isolated from normal human neutrophils is a 145 kDa homodimer, which consists of 2 identical protomers, connected by a single disulfide bond.	Disulfides	144-153	myeloperoxidase	Homo sapiens	14-17
30138815-6	2018	These results revealed the potential for peptide degradation via the cleavage of disulfide cyclization bonds to form free thiols when using one of these C18 cartridges.	Disulfides	81-90	Bardet-Biedl syndrome 9	Homo sapiens	153-156
30111624-5	2018	It was observed that a majority of the UGT1A10 protein expressed in HEK293 cells existed in covalently crosslinked higher-order oligomers via formation of intermolecular disulfide bonds, whereas formation of the intermolecular disulfide bonds was not observed in the UGT1A10 protein expressed in CHO cells.	Disulfides	170-179	UDP glucuronosyltransferase family 1 member A10	Homo sapiens	39-46
30472958-4	2018	HBD-EPO contained two disulfide bonds, as shown by MALDI-TOF mass spectrometry.	Disulfides	22-31	erythropoietin	Homo sapiens	4-7
30111624-5	2018	It was observed that a majority of the UGT1A10 protein expressed in HEK293 cells existed in covalently crosslinked higher-order oligomers via formation of intermolecular disulfide bonds, whereas formation of the intermolecular disulfide bonds was not observed in the UGT1A10 protein expressed in CHO cells.	Disulfides	227-236	UDP glucuronosyltransferase family 1 member A10	Homo sapiens	39-46
30068531-5	2018	Cells lacking LMF1 were hypersensitive to depletion of glutathione, but not DTT treatment, suggesting that LMF1 helps reduce the ER Accordingly, we found that loss of LMF1 results in a more oxidized ER Our data show that LMF1 has a broader role than simply folding lipases, and we identified fibronectin and the low-density lipoprotein receptor (LDLR) as novel LMF1 clients that contain multiple, non-sequential disulfide bonds.	Disulfides	412-421	fibronectin 1	Homo sapiens	292-303
29931617-6	2018	This pattern of coagulation kinetic response was interpreted as copper mediated fibrinogen dysfunction, perhaps via oxidation of key fibrinogen disulfide bridges.	Disulfides	144-153	fibrinogen beta chain	Homo sapiens	80-90
29931617-6	2018	This pattern of coagulation kinetic response was interpreted as copper mediated fibrinogen dysfunction, perhaps via oxidation of key fibrinogen disulfide bridges.	Disulfides	144-153	fibrinogen beta chain	Homo sapiens	133-143
30081385-9	2018	Furthermore, the two surface-exposed cysteine residues of CYGB were oxidized upon treatment, leading to the formation of intermolecular disulfide bridges, and potentially also intramolecular disulfide bridges.	Disulfides	136-145	cytoglobin	Homo sapiens	58-62
30128635-5	2018	These studies showed that the number and position of native disulfide linkages contained within the ScTx-Bax structure significantly influences the ability for these constructs to target anti-apoptotic BCL2 proteins in vitro.	Disulfides	60-69	BCL2 associated X, apoptosis regulator	Homo sapiens	105-108
30128635-5	2018	These studies showed that the number and position of native disulfide linkages contained within the ScTx-Bax structure significantly influences the ability for these constructs to target anti-apoptotic BCL2 proteins in vitro.	Disulfides	60-69	BCL2 apoptosis regulator	Homo sapiens	202-206
30128635-6	2018	The goal of the present study is to investigate the contribution of two disulfide linkages in the folding and biological activity of ScTx-Bax proteins.	Disulfides	72-81	BCL2 associated X, apoptosis regulator	Homo sapiens	138-141
30128635-7	2018	Here, we report the full chemical synthesis of three ScTx-Bax sequence variants, each presenting two native disulfide linkages at different positions within the folded structure.	Disulfides	108-117	BCL2 associated X, apoptosis regulator	Homo sapiens	58-61
30128635-8	2018	It was observed that two disulfide linkages were sufficient to fold ScTx-Bax proteins into native-like architectures reminiscent of wild-type ScTx.	Disulfides	25-34	BCL2 associated X, apoptosis regulator	Homo sapiens	73-76
30128635-9	2018	Furthermore, we show that select (bis)disulfide ScTx-Bax variants can target Bcl-2 (proper) in vitro and that the position of the disulfide bonds significantly influences binding affinity.	Disulfides	38-47	BCL2 associated X, apoptosis regulator	Homo sapiens	53-56
30128635-9	2018	Furthermore, we show that select (bis)disulfide ScTx-Bax variants can target Bcl-2 (proper) in vitro and that the position of the disulfide bonds significantly influences binding affinity.	Disulfides	38-47	BCL2 apoptosis regulator	Homo sapiens	77-82
30081385-9	2018	Furthermore, the two surface-exposed cysteine residues of CYGB were oxidized upon treatment, leading to the formation of intermolecular disulfide bridges, and potentially also intramolecular disulfide bridges.	Disulfides	191-200	cytoglobin	Homo sapiens	58-62
30128635-10	2018	Despite exhibiting only modest binding to Bcl-2, the successful synthesis of ScTx-Bax proteins containing two disulfide linkages represents a viable route to ScTx-based BH3 domain mimetics that preserve native-like conformations.	Disulfides	110-119	BCL2 associated X, apoptosis regulator	Homo sapiens	82-85
30081385-10	2018	In addition, molecular dynamics and docking simulations confirmed, and further show, that the formation of an intramolecular disulfide bond, due to oxidative conditions, affects the CYGB 3D structure, thereby opening the access to the heme group, through gate functioning of His117.	Disulfides	125-134	cytoglobin	Homo sapiens	182-186
30028086-1	2018	Human serum albumin (HSA) is characterized by 17 disulfides and by only one unpaired cysteine (Cys34 ), which can be free in the reduced albumin or linked as a mixed disulfide with cysteine, or in minor amount with other natural thiols, in the oxidized albumin.	Disulfides	49-59	albumin	Homo sapiens	6-19
30542587-1	2018	The chemical synthesis of insulin is an enduring challenge due to the hydrophobic peptide chains and construction of the correct intermolecular disulfide pattern.	Disulfides	144-153	insulin	Homo sapiens	26-33
30542587-2	2018	We report a new approach to the chemical synthesis of insulin using a short, traceless, prosthetic C-peptide that facilitates the formation of the correct disulfide pattern during folding and its removal by basic treatment.	Disulfides	155-164	insulin	Homo sapiens	54-61
30040421-7	2018	One HER2-targeting conjugate that contained a thiophenol-derived disulfide prodrug was an exception to this stability trend.	Disulfides	65-74	erb-b2 receptor tyrosine kinase 2	Homo sapiens	4-8
30059675-2	2018	The third disulfide loop of TGF-alpha (TGF3L peptide) with a very low affinity for EGFR has been reported to enhance the activity of fused antigens or cytokines.	Disulfides	10-19	epidermal growth factor receptor	Homo sapiens	83-87
29534931-2	2018	Peptides that mimic the beta-turn in the Keap1 active site and are constrained by a disulfide bridge have high affinity for Keap1 but no intracellular activity.	Disulfides	84-93	kelch like ECH associated protein 1	Homo sapiens	124-129
30028086-1	2018	Human serum albumin (HSA) is characterized by 17 disulfides and by only one unpaired cysteine (Cys34 ), which can be free in the reduced albumin or linked as a mixed disulfide with cysteine, or in minor amount with other natural thiols, in the oxidized albumin.	Disulfides	49-58	albumin	Homo sapiens	6-19
30038021-3	2018	We analyzed aberrant human SOD1WT species over the lifetime of transgenic mice and found the accumulation of disulfide-cross-linked high-molecular-weight SOD1WT aggregates during aging.	Disulfides	109-118	superoxide dismutase 1	Homo sapiens	27-33
30005164-2	2018	In this study, human serum albumin was hybridized with hemoglobin by intermolecular disulfide bonds to develop a hybrid protein oxygen nanocarrier with chlorine e6 encapsulated (C@HPOC) for oxygen self-sufficient photodynamic therapy (PDT).	Disulfides	84-93	albumin	Homo sapiens	21-34
30104382-0	2018	Interleukin 4 is inactivated via selective disulfide-bond reduction by extracellular thioredoxin.	Disulfides	43-52	interleukin 4	Homo sapiens	0-13
30104382-2	2018	Recently, we showed that TRX activates extracellular transglutaminase 2 via reduction of an allosteric disulfide bond.	Disulfides	103-112	transglutaminase 2	Homo sapiens	53-71
30104382-5	2018	To test this hypothesis, the C35S mutant of human TRX was shown to form a mixed disulfide bond with recombinant IL-4 but not IL-13.	Disulfides	80-89	interleukin 4	Homo sapiens	112-116
30104382-7	2018	Mass spectrometry identified the C46-C99 bond of IL-4 as the target of TRX, consistent with the essential role of this disulfide bond in IL-4 activity.	Disulfides	119-128	interleukin 4	Homo sapiens	49-53
30104382-9	2018	By establishing that IL-4 is posttranslationally regulated by TRX-promoted reduction of a disulfide bond, our findings highlight a novel regulatory mechanism of the type 2 immune response that is specific to IL-4 over IL-13.	Disulfides	90-99	interleukin 4	Homo sapiens	21-25
30104382-9	2018	By establishing that IL-4 is posttranslationally regulated by TRX-promoted reduction of a disulfide bond, our findings highlight a novel regulatory mechanism of the type 2 immune response that is specific to IL-4 over IL-13.	Disulfides	90-99	interleukin 4	Homo sapiens	208-212
30104382-9	2018	By establishing that IL-4 is posttranslationally regulated by TRX-promoted reduction of a disulfide bond, our findings highlight a novel regulatory mechanism of the type 2 immune response that is specific to IL-4 over IL-13.	Disulfides	90-99	interleukin 13	Homo sapiens	218-223
30089863-4	2018	Using single-molecule force-clamp spectroscopy, here we show that mechanical force promotes the thermodynamically disfavored SN2 cleavage of an individual protein disulfide bond by poor nucleophilic organic thiols.	Disulfides	163-172	solute carrier family 38 member 5	Homo sapiens	125-128
30024150-2	2018	Reactions of cobalt(II) salts with disulfide ligand L1SSL1 (L1SSL1 = di-2-(bis(2-pyridylmethyl)amino)-ethyl disulfide) result in the formation of either the high-spin cobalt(II) disulfide compound [CoII2(L1SSL1)Cl4] or a low-spin, octahedral cobalt(III) thiolate compound, such as [CoIII(L1S)(MeCN)2](BF4)2.	Disulfides	35-44	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	249-252
30038021-3	2018	We analyzed aberrant human SOD1WT species over the lifetime of transgenic mice and found the accumulation of disulfide-cross-linked high-molecular-weight SOD1WT aggregates during aging.	Disulfides	109-118	superoxide dismutase 1, soluble	Mus musculus	27-31
30038021-4	2018	Subcellular fractionation of spinal cord tissue and protein overexpression in NSC-34 motoneuron-like cells revealed that endoplasmic reticulum (ER) localization favors oxidation and disulfide-dependent aggregation of SOD1WT We established a pharmacological paradigm of chronic ER stress in vivo, which recapitulated SOD1WTaggregation in young transgenic mice.	Disulfides	182-191	superoxide dismutase 1, soluble	Mus musculus	217-221
30123389-6	2018	When Grx6 was incubated with FeSO4 7H2O and (NH4)2Fe(SO4)2 6H2O, a disulfide bond was formed between the cysteine 136 and glutathione, and the concentration of dimer and tetramer was increased.	Disulfides	67-76	glutathione-disulfide reductase GRX6	Saccharomyces cerevisiae S288C	5-9
30038021-7	2018	Finally, the disulfide-cross-linked SOD1WT species were also found augmented in spinal cord tissue of sALS patients, correlating with the presence of ER stress markers.	Disulfides	13-22	superoxide dismutase 1	Homo sapiens	36-40
29845893-10	2018	RESULTS: Mutations of two cysteine residues (C118 and C1165), involved in the formation of the intramolecular disulfide bridge between the N-terminal ectodomain and one of the extracellular loops, mildly altered the function and the targeting of DUOX1, while this bridge is crucial for DUOX2 function.	Disulfides	110-119	dual oxidase 2	Homo sapiens	286-291
29441426-4	2018	State-dependent formation of both disulfide bonds and Cd2+ bridges occurred for pairs of cysteine side-chains introduced into the extreme extracellular ends of transmembrane helices (TMs) 1, 6, and 12.	Disulfides	34-43	PYD and CARD domain containing	Homo sapiens	160-189
29927574-3	2018	The nanovaccine structure was stabilized by free cysteines within each antigen (ovalbumin, OVA), which were tempospatially exposed and heat-driven to form an extensive intermolecular disulfide network.	Disulfides	183-192	serine (or cysteine) peptidase inhibitor, clade B, member 1, pseudogene	Mus musculus	80-89
29884768-5	2018	A comparison of a new, 2.15-A-resolution crystal structure of Prx2 in the oxidized, disulfide-bonded state with the hyperoxidized structure of Prx2 and Prx1 in complex with sulfiredoxin revealed three structural regions that rearrange during catalysis.	Disulfides	84-93	paired related homeobox 2	Homo sapiens	62-66
29845893-6	2018	Recently, intra- and intermolecular disulfide bridges were identified that are essential for the structure and the function of the DUOX2-DUOXA2 complex.	Disulfides	36-45	dual oxidase 2	Homo sapiens	131-136
30008086-11	2018	In terms of the structural shifts, there are three potential disulfide bridges between the M1 and M3 helices of the gamma2 and 2 alpha1 subunits in the model.	Disulfides	61-70	tryptophanyl-tRNA synthetase 1	Homo sapiens	116-135
30009290-3	2018	In particular, we demonstrate that the native tertiary structure of lysozyme is preserved if, and only if, its four intramolecular disulfide bridges are intact.	Disulfides	131-140	lysozyme	Homo sapiens	68-76
29714059-5	2018	Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322.	Disulfides	116-125	selenoprotein W	Homo sapiens	54-69
29714059-5	2018	Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322.	Disulfides	116-125	selenoprotein W	Homo sapiens	142-146
29858230-4	2018	We further show that ER oxidoreductin 1alpha (Ero1alpha), the pivotal sulfhydryl oxidase that catalyzes disulfide formation in the ER, is phosphorylated by Fam20C in the Golgi apparatus and retrograde-transported to the ER mediated by ERp44.	Disulfides	104-113	endoplasmic reticulum protein 44	Homo sapiens	235-240
29902373-3	2018	Analysis of insulin showcased the ability of UVPD to cleave multiple disulfide bonds and provide sequence coverage of the peptide chains in the same MS/MS event.	Disulfides	69-78	insulin	Homo sapiens	12-19
29902373-5	2018	The 4 disulfide bonds of lysozyme and the 19 disulfide bonds of serotransferrin were characterized through LC/UVPD-MS analysis of nonreduced and partially reduced protein digests.	Disulfides	45-54	transferrin	Homo sapiens	64-79
29789425-3	2018	The aim of the present work was to characterize their circulating forms to better understand how their activities are regulated in vivo First, by cotransfecting BMP9 and BMP10, we found that both can form a disulfide-bonded heterodimer in vitro and that this heterodimer is functional on endothelial cells via ALK1.	Disulfides	207-216	activin A receptor, type II-like 1	Mus musculus	310-314
30050648-2	2018	Peroxiredoxin 4 (Prdx4) catalyzes disulfide bond formation in proteins via the action of hydrogen peroxide and hence decreases oxidative stress and supports oxidative protein folding for the secretion of lipoproteins.	Disulfides	34-43	peroxiredoxin 4	Mus musculus	0-15
29992955-6	2018	F-protein folding depends on ER-resident glycoprotein-specific thiol-oxidoreductase ERp57 for correct disulfide-bond architecture.	Disulfides	102-111	protein disulfide isomerase family A member 3	Homo sapiens	84-89
29878755-9	2018	Applying this workflow, we successfully mapped the complex disulfide bonds of tertiapin and the epidermal growth factor (EGF) family members transforming growth factor alpha (TGFalpha) and EGF.	Disulfides	59-68	tumor necrosis factor	Homo sapiens	141-173
29969106-4	2018	While ERp18 has a canonical active-site motif and is involved in native disulfide-bond formation, AGR2 and AGR3 lack elements of the active-site motif found in other family members and may both interact with mucins.	Disulfides	72-81	thioredoxin domain containing 12	Homo sapiens	6-11
29698786-7	2018	It contained fibrillar structures only, and their organization reflected the initial native structure of fibrinogen: typically, six polypeptide chains connected by multiple disulfide bonds were seen.	Disulfides	173-182	fibrinogen beta chain	Homo sapiens	105-115
30050648-2	2018	Peroxiredoxin 4 (Prdx4) catalyzes disulfide bond formation in proteins via the action of hydrogen peroxide and hence decreases oxidative stress and supports oxidative protein folding for the secretion of lipoproteins.	Disulfides	34-43	peroxiredoxin 4	Mus musculus	17-22
29746862-8	2018	Further analysis using a human recombinant active TGF-beta1 revealed that H2S cleaved the disulfide bond in the dimeric active TGF-beta1 and promoted the formation of inactive TGF-beta1 monomer.	Disulfides	90-99	transforming growth factor beta 1	Homo sapiens	50-59
30456358-5	2018	First, both human Ero1 isoforms exist in a dynamic mixed disulfide complex with protein disulfide isomerase, which involves cysteines (Cys166 in Ero1alpha and Cys165 in Ero1beta) that have previously been regarded as being nonfunctional.	Disulfides	57-66	endoplasmic reticulum oxidoreductase 1 beta	Homo sapiens	169-177
29932420-6	2018	Cell adhesion assays and molecular dynamics simulations demonstrate that cleavage of the disulfide induces long-range allosteric effects within the betaI-domain, mainly affecting the metal-binding sites, that results in release of fibrinogen.	Disulfides	89-98	fibrinogen beta chain	Homo sapiens	231-241
29746862-8	2018	Further analysis using a human recombinant active TGF-beta1 revealed that H2S cleaved the disulfide bond in the dimeric active TGF-beta1 and promoted the formation of inactive TGF-beta1 monomer.	Disulfides	90-99	transforming growth factor beta 1	Homo sapiens	127-136
29746862-8	2018	Further analysis using a human recombinant active TGF-beta1 revealed that H2S cleaved the disulfide bond in the dimeric active TGF-beta1 and promoted the formation of inactive TGF-beta1 monomer.	Disulfides	90-99	transforming growth factor beta 1	Homo sapiens	127-136
29869502-15	2018	Intracellular wild-type SOD1 spontaneously binds zinc, while it needs the copper chaperone for superoxide dismutase (CCS) for copper delivery and disulfide bond formation.	Disulfides	146-155	superoxide dismutase 1	Homo sapiens	24-28
29570977-3	2018	Cystamine, a symmetric disulfide compound, is one of the earliest reported TG2 inhibitors.	Disulfides	23-32	transglutaminase 2	Homo sapiens	75-78
29570977-6	2018	Through mass spectrometric disulfide mapping and site-directed mutagenesis, we show that cystamine promotes the formation of a physiologically relevant disulfide bond between Cys370 and Cys371 that allosterically abrogates the catalytic activity of human TG2.	Disulfides	152-161	transglutaminase 2	Homo sapiens	255-258
29900929-0	2018	Whey Acidic Protein/Four-Disulfide Core Domain 21 Regulate Sepsis Pathogenesis in a Mouse Model and a Macrophage Cell Line via the Stat3/Toll-Like Receptor 4 (TLR4) Signaling Pathway.	Disulfides	25-34	toll-like receptor 4	Mus musculus	131-157
29874090-1	2018	A simplified route to synthesis of INSL5 is reported, where the elimination of intermediate purification steps and nonconventional disulfide pairing results in final yields that are an order of magnitude higher than in previously reported stepwise syntheses.	Disulfides	131-140	insulin like 5	Homo sapiens	35-40
29900929-0	2018	Whey Acidic Protein/Four-Disulfide Core Domain 21 Regulate Sepsis Pathogenesis in a Mouse Model and a Macrophage Cell Line via the Stat3/Toll-Like Receptor 4 (TLR4) Signaling Pathway.	Disulfides	25-34	toll-like receptor 4	Mus musculus	159-163
29257879-0	2018	1,2,3-Triazole Rings as a Disulfide Bond Mimetic in Chimeric AGRP-Melanocortin Peptides: Design, Synthesis, and Functional Characterization.	Disulfides	26-35	agouti related neuropeptide	Mus musculus	61-65
28988628-5	2018	This review will discuss the challenges of developing peptidomimetics of therapeutically important insulin superfamily peptides, particularly those which have two chains (A and B) and three disulfide bonds and whose receptors are known, namely insulin, H2 relaxin, H3 relaxin, INSL3 and INSL5.	Disulfides	190-199	insulin	Homo sapiens	99-106
29659026-4	2018	An intramolecular disulfide bond of beta1 was identified to be essential for stabilisation of inactivation, but not activation, against mechanical stress using molecular dynamics simulations, homology modelling and site-directed mutagenesis.	Disulfides	18-27	BCL2 related protein A1	Homo sapiens	36-41
29659026-13	2018	Using molecular dynamics simulation, homology modelling and site-directed mutagenesis, we identify an intramolecular disulfide bond of beta1 (Cys21-Cys43) which is partially involved in this process: the beta1-C43A mutant prevents mechanical modulation of voltage dependence of activation, but not of fast inactivation.	Disulfides	117-126	BCL2 related protein A1	Homo sapiens	135-140
30362439-1	2018	Lipoprotein(a) [Lp(a)] consists of an LDL-like particle in which the apolipoprotein B100 is covalently bound to apolipoprotein(a) by a single disulfide bond.	Disulfides	142-151	apolipoprotein B	Homo sapiens	69-88
29643237-7	2018	Mutations of all five cysteines in GP41 individually had minor effects on GP41 oligomer formation, albeit certain mutations impaired infectious BV production, suggesting flexibility in the intermolecular disulfide bonding.	Disulfides	204-213	occlusion-derived virus glycoprotein	Autographa californica nucleopolyhedrovirus	35-39
29643237-14	2018	In this study, we identified trimers as the functional structure of GP41 in baculovirus virion morphogenesis and showed that both disulfide bridging and protein-protein interactions via the two leucine zipper-like domains are involved in the formation of different oligomeric states.	Disulfides	130-139	occlusion-derived virus glycoprotein	Autographa californica nucleopolyhedrovirus	68-72
29574146-0	2018	A mathematical analysis of Prx2-STAT3 disulfide exchange rate constants for a bimolecular reaction mechanism.	Disulfides	38-47	peroxiredoxin 2	Homo sapiens	27-31
29574146-0	2018	A mathematical analysis of Prx2-STAT3 disulfide exchange rate constants for a bimolecular reaction mechanism.	Disulfides	38-47	signal transducer and activator of transcription 3	Homo sapiens	32-37
29574146-2	2018	In addition to their status as the primary reducers of H2O2 to water, the oxidized peroxiredoxin byproduct of this reaction has recently been shown capable of participation in H2O2-mediated signaling pathways through disulfide exchange reactions with the transcription factor STAT3.	Disulfides	217-226	peroxiredoxin 2	Homo sapiens	83-96
29574146-2	2018	In addition to their status as the primary reducers of H2O2 to water, the oxidized peroxiredoxin byproduct of this reaction has recently been shown capable of participation in H2O2-mediated signaling pathways through disulfide exchange reactions with the transcription factor STAT3.	Disulfides	217-226	signal transducer and activator of transcription 3	Homo sapiens	276-281
29574146-8	2018	This analysis suggests the existence of more complex mechanisms, potentially involving currently unknown protein-protein recognition partners, which facilitate disulfide exchange reactions between peroxiredoxin-2 and STAT3.	Disulfides	160-169	peroxiredoxin 2	Homo sapiens	197-212
29574146-8	2018	This analysis suggests the existence of more complex mechanisms, potentially involving currently unknown protein-protein recognition partners, which facilitate disulfide exchange reactions between peroxiredoxin-2 and STAT3.	Disulfides	160-169	signal transducer and activator of transcription 3	Homo sapiens	217-222
29686043-5	2018	Fibrillation was achieved more easily in disulfide-reduced monomeric SOD1 when compared with wild-type and mutant monomeric SOD1.	Disulfides	41-50	superoxide dismutase 1	Homo sapiens	69-73
29196860-1	2018	High mobility group box 1 (HMGB1), a nuclear protein, once released into the extracellular space under pathological conditions, plays a pronociceptive role in redox-dependent distinct active forms, all-thiol HMGB1 (at-HMGB1) and disulfide HMGB1 (ds-HMGB1), that accelerate nociception through the receptor for advanced glycation endproducts (RAGE) and Toll-like receptor 4 (TLR4), respectively.	Disulfides	229-238	advanced glycosylation end product-specific receptor	Mus musculus	342-346
29196860-1	2018	High mobility group box 1 (HMGB1), a nuclear protein, once released into the extracellular space under pathological conditions, plays a pronociceptive role in redox-dependent distinct active forms, all-thiol HMGB1 (at-HMGB1) and disulfide HMGB1 (ds-HMGB1), that accelerate nociception through the receptor for advanced glycation endproducts (RAGE) and Toll-like receptor 4 (TLR4), respectively.	Disulfides	229-238	toll-like receptor 4	Mus musculus	352-372
29196860-1	2018	High mobility group box 1 (HMGB1), a nuclear protein, once released into the extracellular space under pathological conditions, plays a pronociceptive role in redox-dependent distinct active forms, all-thiol HMGB1 (at-HMGB1) and disulfide HMGB1 (ds-HMGB1), that accelerate nociception through the receptor for advanced glycation endproducts (RAGE) and Toll-like receptor 4 (TLR4), respectively.	Disulfides	229-238	toll-like receptor 4	Mus musculus	374-378
29500669-3	2018	In control ventricular myocytes, oxidative stress induced formation of disulfide bonds between RyR2 subunits: intersubunit cross-linking (XL).	Disulfides	71-80	ryanodine receptor 2	Oryctolagus cuniculus	95-99
29257879-3	2018	The aim of this study was to explore the potential of replacing the disulfide bridge in chimeric AGRP-melanocortin peptide Tyr-c[Cys-His-d-Phe-Arg-Trp-Asn-Ala-Phe-Cys]-Tyr-NH2 (1) with 1,2,3-triazole moieties.	Disulfides	68-77	agouti related neuropeptide	Mus musculus	97-101
29415129-1	2018	Heavily glycosylated secreted mucin MUC5AC, by the virtue of its cysteine-rich repeats, can form inter- and intramolecular disulfide linkages resulting in complex polymers, which in turn craft the framework of the polymeric mucus gel on epithelial cell surfaces.	Disulfides	123-132	mucin 5, subtypes A and C, tracheobronchial/gastric	Mus musculus	36-42
29382723-7	2018	Here, we show that sortilin forms homodimers with an intermolecular disulfide bond at the cysteine 783 (Cys783) residue, and because Cys783 can be palmitoylated, it could be shared via palmitoylation and an intermolecular disulfide bond.	Disulfides	68-77	sortilin 1	Homo sapiens	19-27
29220697-3	2018	Here we examined RSS metabolism by Cu/Zn superoxide dismutase (SOD) using amperometric electrodes for dissolved H2S, a polysulfide-specific fluorescent probe (SSP4), and mass spectrometry to identify specific polysulfides (H2S2-H2S5).	Disulfides	223-227	superoxide dismutase 1	Homo sapiens	63-66
29220697-4	2018	H2S was concentration- and oxygen-dependently oxidized by 1muM SOD to polysulfides (mainly H2S2, and to a lesser extent H2S3 and H2S5) with an EC50 of approximately 380muM H2S.	Disulfides	91-95	superoxide dismutase 1	Homo sapiens	63-66
29377149-3	2018	Ordinarily, nascent proinsulin entering the ER rapidly folds via the formation of three evolutionarily conserved disulfide bonds (B7-A7, B19-A20, and A6-A11).	Disulfides	113-122	insulin	Homo sapiens	20-30
29377149-4	2018	A modest amount of proinsulin misfolding, including both intramolecular disulfide mispairing and intermolecular disulfide-linked protein complexes, is a natural by-product of proinsulin biosynthesis, as is the case for many proteins.	Disulfides	72-81	insulin	Homo sapiens	19-29
29377149-4	2018	A modest amount of proinsulin misfolding, including both intramolecular disulfide mispairing and intermolecular disulfide-linked protein complexes, is a natural by-product of proinsulin biosynthesis, as is the case for many proteins.	Disulfides	112-121	insulin	Homo sapiens	19-29
29377149-4	2018	A modest amount of proinsulin misfolding, including both intramolecular disulfide mispairing and intermolecular disulfide-linked protein complexes, is a natural by-product of proinsulin biosynthesis, as is the case for many proteins.	Disulfides	112-121	insulin	Homo sapiens	175-185
29556960-8	2018	RESULTS: Non-reducing and reducing Lys-C peptide mapping showed a highly similar peak profile, confirming that LBDE and NESP  have the same primary structure and disulfide bonds.	Disulfides	162-171	GNAS complex locus	Homo sapiens	120-124
29505764-9	2018	The N-terminal loop is connected to alpha helix 2 via a disulfide bond previously observed in Na-ASP-2.	Disulfides	56-65	beta-secretase 1	Homo sapiens	97-102
29596046-5	2018	Furthermore, our insulin-bound IDE structures explain how IDE processively degrades insulin by stochastically cutting either chain without breaking disulfide bonds.	Disulfides	148-157	insulin	Homo sapiens	17-24
29596046-5	2018	Furthermore, our insulin-bound IDE structures explain how IDE processively degrades insulin by stochastically cutting either chain without breaking disulfide bonds.	Disulfides	148-157	insulin	Homo sapiens	84-91
29501381-3	2018	The chloroplast protein CP12 is a model of such proteins and acts as a redox switch by formation/disruption of its two disulfide bridges.	Disulfides	119-128	uncharacterized protein	Chlamydomonas reinhardtii	24-28
29649293-4	2018	Cytochrome c and transferrin were cross-linked with a redox sensitive disulfide bond for the intra-cellular release of the protein upon endocytosis by the transferrin receptor.	Disulfides	70-79	cytochrome c, somatic	Homo sapiens	0-12
29649293-4	2018	Cytochrome c and transferrin were cross-linked with a redox sensitive disulfide bond for the intra-cellular release of the protein upon endocytosis by the transferrin receptor.	Disulfides	70-79	transferrin	Homo sapiens	17-28
29649293-4	2018	Cytochrome c and transferrin were cross-linked with a redox sensitive disulfide bond for the intra-cellular release of the protein upon endocytosis by the transferrin receptor.	Disulfides	70-79	transferrin	Homo sapiens	155-166
29393338-1	2018	Normal prion protein (PrP) contains two cysteines at amino acids 179 and 214, which may form intra- and interpeptide disulfide bonds.	Disulfides	117-126	prion protein	Homo sapiens	22-25
29393338-7	2018	These data indicated that formation of a disulfide bond induces marked alterations in the secondary structure and biochemical characteristics of PrP.	Disulfides	41-50	prion protein	Homo sapiens	145-148
29881431-5	2018	The TNF-alpha recombinant protein was expressed in genetically engineered Escherichia coli SHuffle  T7 Express, for the first time, which is able to express disulfide-bonded recombinant proteins into their correctly folded states.	Disulfides	157-166	tumor necrosis factor	Homo sapiens	4-13
29429693-5	2018	Furthermore, swirling cavitation treatment significantly enhanced the surface hydrophobicity, altered the disulfide bond and exposed sulfhydryl group contents of the SPI.	Disulfides	106-115	chromogranin A	Homo sapiens	166-169
29382723-7	2018	Here, we show that sortilin forms homodimers with an intermolecular disulfide bond at the cysteine 783 (Cys783) residue, and because Cys783 can be palmitoylated, it could be shared via palmitoylation and an intermolecular disulfide bond.	Disulfides	222-231	sortilin 1	Homo sapiens	19-27
29382723-8	2018	Formation of this intermolecular disulfide bond leads to trafficking of sortilin to EVs by preventing palmitoylation, which further promotes sortilin trafficking to the Golgi apparatus.	Disulfides	33-42	sortilin 1	Homo sapiens	72-80
29382723-8	2018	Formation of this intermolecular disulfide bond leads to trafficking of sortilin to EVs by preventing palmitoylation, which further promotes sortilin trafficking to the Golgi apparatus.	Disulfides	33-42	sortilin 1	Homo sapiens	141-149
29382723-10	2018	In conclusion, sortilin is transported to EVs via the formation of homodimers with an intermolecular disulfide bond, which is endogenously regulated by its own propeptide.	Disulfides	101-110	sortilin 1	Homo sapiens	15-23
29545539-7	2018	To address them, here, we first identified four disulfide bonds in hbeta4-loop by mass spectroscopy and NMR techniques.	Disulfides	48-57	potassium calcium-activated channel subfamily M regulatory beta subunit 4	Homo sapiens	67-73
29554910-8	2018	The binding between KTN and porcine gastric mucin (PGM) is dominated by electrostatic attractions and hydrogen bondings at pH 4.5, and disulfide bonds also plays a key role in the interaction at pH 7.4.	Disulfides	135-144	keratocan	Homo sapiens	20-23
29031766-0	2018	Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage.	Disulfides	0-9	transferase	Arabidopsis thaliana	67-78
29470989-0	2018	Redox exchange of the disulfides of human two-domain CD4 regulates the conformational dynamics of each domain, providing insight into its mechanisms of control.	Disulfides	22-32	CD4 molecule	Homo sapiens	53-56
29470989-4	2018	While we have shown previously that elimination of the pre-stressed D2 disulfide results in a favorable structural collapse that increases the stability of a CD4 variant comprising only D1 and D2 (2dCD4), we sought to further localize and determine the nature of the biophysical modifications that take place upon redox exchange of the D1 and D2 disulfides by using amide hydrogen-deuterium exchange mass spectrometry (HDX-MS) to measure induced changes in conformational dynamics.	Disulfides	71-80	CD4 molecule	Homo sapiens	158-161
29470989-7	2018	Increases in the dynamics of regions important for HIV gp120 and MHCII binding in D1 also result allosterically after reducing the D2 disulfide, which are likely a consequence of the structural changes that take place in D2, findings that advance our understanding of the mechanisms by which redox exchange of the CD4 disulfides regulates its function.	Disulfides	318-328	CD4 molecule	Homo sapiens	314-317
29304403-5	2018	A highly biocompatible nano system for codelivery of the TRAIL DNA and the death receptor sensitizer monensin was developed, in which low-molecular-weight PEI (LMW-PEI) was crosslinked by the sulfhydryl cyclodextrin via disulfide bonds, and then bound with DNA, thus forming the bioreducible polyplex cores.	Disulfides	220-229	TNF superfamily member 10	Homo sapiens	57-62
29376647-3	2018	Group 5 and 4 disulfides (VS2, NbS2, TaS2, TiS2, ZrS2, and HfS2) in particular show anchoring capabilities superior to those of group 6 disulfides (CrS2, MoS2, and WS2).	Disulfides	14-24	msh homeobox 2	Homo sapiens	148-152
29440498-2	2018	Here, we report the near-atomic resolution cryo-EM structure of nucleotide-free ABCB1 trapped by an engineered disulfide cross-link between the nucleotide-binding domains (NBDs) and bound to the antigen-binding fragment of the human-specific inhibitory antibody UIC2 and to the third-generation ABCB1 inhibitor zosuquidar.	Disulfides	111-120	ATP binding cassette subfamily B member 1	Homo sapiens	80-85
29440498-2	2018	Here, we report the near-atomic resolution cryo-EM structure of nucleotide-free ABCB1 trapped by an engineered disulfide cross-link between the nucleotide-binding domains (NBDs) and bound to the antigen-binding fragment of the human-specific inhibitory antibody UIC2 and to the third-generation ABCB1 inhibitor zosuquidar.	Disulfides	111-120	ATP binding cassette subfamily B member 1	Homo sapiens	295-300
29305423-1	2018	Transglutaminase 2 (TG2) is a ubiquitously expressed, intracellular as well as extracellular protein with multiple modes of post-translational regulation, including an allosteric disulfide bond between Cys-370-Cys-371 that renders the enzyme inactive in the extracellular matrix.	Disulfides	179-188	transglutaminase 2	Homo sapiens	0-18
29305423-1	2018	Transglutaminase 2 (TG2) is a ubiquitously expressed, intracellular as well as extracellular protein with multiple modes of post-translational regulation, including an allosteric disulfide bond between Cys-370-Cys-371 that renders the enzyme inactive in the extracellular matrix.	Disulfides	179-188	transglutaminase 2	Homo sapiens	20-23
29305423-9	2018	We conclude that, to the best of our knowledge, the disulfide bond switch in human TG2 represents the first example of a post-translational redox regulatory mechanism that is reversibly and allosterically modulated by two distinct proteins (ERp57 and TRX).	Disulfides	52-61	transglutaminase 2	Homo sapiens	83-86
29305423-9	2018	We conclude that, to the best of our knowledge, the disulfide bond switch in human TG2 represents the first example of a post-translational redox regulatory mechanism that is reversibly and allosterically modulated by two distinct proteins (ERp57 and TRX).	Disulfides	52-61	protein disulfide isomerase family A member 3	Homo sapiens	241-246
28372502-5	2018	Recent Advances: Physicochemical data argue against a rapid, nonenzymatic reaction of MSH with oxidants, disulfides, or electrophiles.	Disulfides	105-115	msh homeobox 2	Homo sapiens	86-89
28372502-11	2018	A novel tool for in vivo imaging of the MSH/mycothiol disulfide (MSSM) status allows following changes in the mycothiol redox state during macrophage infection and its relationship with antibiotic sensitivity.	Disulfides	54-63	msh homeobox 2	Homo sapiens	40-43
29723147-3	2018	Hemi-MPO obtained from dimeric MPO by reductive cleavage of a disulfide bond between protomeric subunits was used as the monomeric form.	Disulfides	62-71	myeloperoxidase	Homo sapiens	5-8
29723147-3	2018	Hemi-MPO obtained from dimeric MPO by reductive cleavage of a disulfide bond between protomeric subunits was used as the monomeric form.	Disulfides	62-71	myeloperoxidase	Homo sapiens	31-34
29723147-11	2018	By using Western-blotting with antibodies to MPO, we showed, for the first time, that the dimeric molecule of MPO could be cleaved into two monomeric subunits by HOCl, most probably due to oxidation of the disulfide bond between these subunits.	Disulfides	206-215	myeloperoxidase	Homo sapiens	45-48
29723147-11	2018	By using Western-blotting with antibodies to MPO, we showed, for the first time, that the dimeric molecule of MPO could be cleaved into two monomeric subunits by HOCl, most probably due to oxidation of the disulfide bond between these subunits.	Disulfides	206-215	myeloperoxidase	Homo sapiens	110-113
29348271-3	2018	We demonstrated that intratumor payload exposures correlated well with the corresponding efficacies of several disulfide-linked ADCs, bearing an DNA alkylating agent, pyrrolo[2,1-c][1,4]benzodiazepine-dimer (PBD), in HER2-expressing xenograft models.	Disulfides	111-120	erb-b2 receptor tyrosine kinase 2	Homo sapiens	217-221
29507883-0	2018	Autoregulation of von Willebrand factor function by a disulfide bond switch.	Disulfides	54-63	von Willebrand factor	Homo sapiens	18-39
29507883-7	2018	Significantly, the A2 disulfide bond is cleaved in ~75% of VWF subunits in healthy human donor plasma but in just ~25% of plasma VWF subunits from heart failure patients who have received extracorporeal membrane oxygenation support.	Disulfides	22-31	von Willebrand factor	Homo sapiens	59-62
29507883-7	2018	Significantly, the A2 disulfide bond is cleaved in ~75% of VWF subunits in healthy human donor plasma but in just ~25% of plasma VWF subunits from heart failure patients who have received extracorporeal membrane oxygenation support.	Disulfides	22-31	von Willebrand factor	Homo sapiens	129-132
29507883-9	2018	These findings demonstrate that a disulfide bond switch regulates mechanopresentation of VWF.	Disulfides	34-43	von Willebrand factor	Homo sapiens	89-92
29475957-1	2018	The activity of human transglutaminase 2 (TG2), which forms protein cross-links between glutamine and lysine residues, is controlled by an allosteric disulfide bond.	Disulfides	150-159	transglutaminase 2	Homo sapiens	22-40
29475957-1	2018	The activity of human transglutaminase 2 (TG2), which forms protein cross-links between glutamine and lysine residues, is controlled by an allosteric disulfide bond.	Disulfides	150-159	transglutaminase 2	Homo sapiens	42-45
29440720-4	2018	Using X-ray crystallography and single-molecule FRET, we characterize a prothrombin construct locked in the closed conformation through an engineered disulfide bond.	Disulfides	150-159	coagulation factor II, thrombin	Homo sapiens	72-83
29298893-0	2018	Allosteric control of human cystathionine beta-synthase activity by a redox active disulfide bond.	Disulfides	83-92	cystathionine beta-synthase	Homo sapiens	28-55
29298893-6	2018	The Cys272-Cys275 disulfide bond in CBS has a midpoint potential of -314 mV at pH 7.4.	Disulfides	18-27	cystathionine beta-synthase	Homo sapiens	36-39
29298893-9	2018	These findings indicate that CBS is post-translationally regulated by a redox-active disulfide bond in the CXXC motif.	Disulfides	85-94	cystathionine beta-synthase	Homo sapiens	29-32
32254267-1	2018	This article describes a novel reduction degradable supramolecular nanoparticle gene delivery system via host-guest interaction based on cyclodextrin-conjugated polyaspartamide with disulfide linkage (Pasp-SS-CD) and adamantyl-terminated polyethylenimine (Ad4-PEI).	Disulfides	182-191	presenilin 2	Homo sapiens	256-259
29080907-5	2018	In this study, we demonstrate that the m-type thioredoxins TRX-m1, TRX-m2, and TRX-m4 (TRX-ms) interact with the xanthophyll cycle enzyme zeaxanthin epoxidase (ZE) and are required for maintaining the redox-dependent stabilization of ZE by regulating its intermolecular disulfide bridges.	Disulfides	270-279	zeaxanthin epoxidase (ZEP) (ABA1)	Arabidopsis thaliana	138-158
28786096-4	2018	The MS3 CTD/CID reaction effectively broke the disulfide linkages, separated the two chains, and yielded more structurally informative fragment ions within the inter-chain cyclic region.	Disulfides	47-56	MS3	Homo sapiens	4-7
29277598-8	2018	CONCLUSIONS: The capacity of thioredoxin 1 and glutaredoxin 1 to reduce intra-protein disulfide bridges is weakened in Rap1 deficient mice, resulting in hyper-activation of NADPH oxidase and greater reactive oxygen species generation.	Disulfides	86-95	glutaredoxin	Mus musculus	47-61
29277598-8	2018	CONCLUSIONS: The capacity of thioredoxin 1 and glutaredoxin 1 to reduce intra-protein disulfide bridges is weakened in Rap1 deficient mice, resulting in hyper-activation of NADPH oxidase and greater reactive oxygen species generation.	Disulfides	86-95	telomeric repeat binding factor 2, interacting protein	Mus musculus	119-123
29156095-6	2018	Then, reduced thioredoxin (Trx) with a reducing system (Trx reductase and NADPH) reduces the sulfenate to restore activity; meanwhile, Cys154 and Cys263 form an intermolecular disulfide bond, which serves as another redox-sensing switch.	Disulfides	176-185	thioredoxin 1	Rattus norvegicus	14-25
29156095-6	2018	Then, reduced thioredoxin (Trx) with a reducing system (Trx reductase and NADPH) reduces the sulfenate to restore activity; meanwhile, Cys154 and Cys263 form an intermolecular disulfide bond, which serves as another redox-sensing switch.	Disulfides	176-185	thioredoxin 1	Rattus norvegicus	27-30
29156095-6	2018	Then, reduced thioredoxin (Trx) with a reducing system (Trx reductase and NADPH) reduces the sulfenate to restore activity; meanwhile, Cys154 and Cys263 form an intermolecular disulfide bond, which serves as another redox-sensing switch.	Disulfides	176-185	thioredoxin 1	Rattus norvegicus	56-59
29156095-7	2018	Consequently, Trx specifically cleaves the intermolecular disulfide bond by converting it from the inactive form (dimer) to the active form (monomer).	Disulfides	58-67	thioredoxin 1	Rattus norvegicus	14-17
29240412-7	2018	The new method is used to measure fucosylation levels of a plasma protein haptoglobin at the whole protein level following online reduction of disulfide-linked tetrameric species to monomeric units.	Disulfides	143-152	haptoglobin	Homo sapiens	74-85
29158275-2	2018	Human defensin 5 (HD5) is an endogenous peptide with a complex architecture and antibacterial activity against MDRAb In the present study, we attempted to simplify the structure of HD5 by removing disulfide bonds.	Disulfides	197-206	defensin alpha 5	Homo sapiens	6-16
29158275-2	2018	Human defensin 5 (HD5) is an endogenous peptide with a complex architecture and antibacterial activity against MDRAb In the present study, we attempted to simplify the structure of HD5 by removing disulfide bonds.	Disulfides	197-206	defensin alpha 5	Homo sapiens	18-21
29158275-2	2018	Human defensin 5 (HD5) is an endogenous peptide with a complex architecture and antibacterial activity against MDRAb In the present study, we attempted to simplify the structure of HD5 by removing disulfide bonds.	Disulfides	197-206	defensin alpha 5	Homo sapiens	181-184
29342139-7	2018	Multiple levels of MCP-MCP interaction-including six sets of stacked hairpins lining the hexon channel, disulfide bonds across channel and buttress domains in neighbouring MCPs, and an interaction network forged by the N-lasso domain and secured by the dimerization domain-define a robust capsid that is resistant to the pressure exerted by the enclosed genome.	Disulfides	104-113	CD46 molecule	Homo sapiens	19-22
29342139-7	2018	Multiple levels of MCP-MCP interaction-including six sets of stacked hairpins lining the hexon channel, disulfide bonds across channel and buttress domains in neighbouring MCPs, and an interaction network forged by the N-lasso domain and secured by the dimerization domain-define a robust capsid that is resistant to the pressure exerted by the enclosed genome.	Disulfides	104-113	CD46 molecule	Homo sapiens	23-26
29231709-3	2018	The dual functionalization of interleukin 2 and EYFP proceeded with no loss of bioactivity in a stepwise fashion applying maleimide and disulfide rebridging allyl-sulfone groups.	Disulfides	136-145	interleukin 2	Homo sapiens	30-43
29203246-5	2018	This paper provides evidences that binding to integrin ligands initiate changes in free thiol pattern on cell surface and that thiol-disulfide exchange mediated by PDI leads to activation of integrin subunit alpha11.	Disulfides	133-142	integrin subunit alpha 11	Homo sapiens	191-215
29211467-4	2018	With this unique approach of directly delivering H2S2, our findings reaffirmed that S-persulfidation leads to decreased activity of glyceraldehyde 3-phosphate dehydrogenase.	Disulfides	49-53	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	132-172
29343861-3	2018	Upon changing from a non-reducing to a reducing condition, ion-current blockage events from the monomeric state dominate, consistent with the expected reduction of the two inter-chain VEGF disulfide bonds.	Disulfides	189-198	vascular endothelial growth factor A	Homo sapiens	184-188
28398822-4	2018	Heightened oxidative stress evokes formation of disulfide-bound heterotrimers linking dimeric PRDX1 to monomeric FOXO3.	Disulfides	48-57	forkhead box O3	Homo sapiens	113-118
29296021-7	2018	Molecular dynamics and site-directed mutagenesis experiments suggest that homocysteine regulates the conformation of the AT1 receptor both orthosterically and allosterically by forming a salt bridge and a disulfide bond with its Arg167 and Cys289 residues, respectively.	Disulfides	205-214	angiotensin II receptor, type 1a	Mus musculus	121-124
29298351-2	2018	Prolonged exposure to oxidative stress may cause, inter alia, the formation of intermolecular disulfide bonds leading to accumulation of GAPDH aggregates and ultimately to cell death.	Disulfides	94-103	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	137-142
29146186-5	2018	TMalpha and TM"s D123, but not D1, promoted the thrombin-dependent degradation of all-thiol (at-HMGB1) and disulfide HMGB1 (ds-HMGB1), an effect mimicked by TM"s D2, though to a lesser extent.	Disulfides	107-116	coagulation factor II	Mus musculus	48-56
29113799-5	2018	This effect is significantly prevented by decreasing oxidized glutathione as well as glutathione depletion, indicating that S-glutathionylation and the formation of protein-glutathione mixed disulfides is related to HIF-1alpha protein levels.	Disulfides	191-201	hypoxia inducible factor 1 subunit alpha	Homo sapiens	216-226
29950795-2	2018	Ccs1 delivers a single copper ion and catalyzes oxidation of an intra-subunit disulfide bond within each Sod1 monomer through a mechanistically ambiguous process.	Disulfides	78-87	superoxide dismutase 1	Homo sapiens	105-109
29175210-2	2018	SDS-PAGE analysis under non-reducing conditions showed that the C11A and C30A mutants produced a disulfide (SS) isomer in addition to a protein with a native SS bond (Cys73-Cys120).	Disulfides	97-106	endogenous retrovirus group K member 25	Homo sapiens	64-68
29299985-1	2018	The vascular endothelial growth factor (VEGF) is a homodimeric disulfide bound glycoprotein that promotes endothelial growth, accompanied by higher vascular permeability, and therefore represents an important factor for angiogenesis and vascularization.	Disulfides	63-72	vascular endothelial growth factor A	Homo sapiens	4-38
29299985-1	2018	The vascular endothelial growth factor (VEGF) is a homodimeric disulfide bound glycoprotein that promotes endothelial growth, accompanied by higher vascular permeability, and therefore represents an important factor for angiogenesis and vascularization.	Disulfides	63-72	vascular endothelial growth factor A	Homo sapiens	40-44
29151266-4	2018	Crystallization and X-ray diffraction studies of the full-length DHRS4_CAEEL protein in complex with diacetyl revealed its tetrameric structure and showed that two subunits are connected via an intermolecular disulfide bridge that is formed by N-terminal cysteine residues (Cys5) of each protein chain, which increases the enzymatic activity.	Disulfides	209-218	Dehydrogenase/reductase SDR family member 4	Caenorhabditis elegans	65-70
29950795-4	2018	Ccs1 preferentially binds a completely immature form of Sod1 that is metal deficient and disulfide reduced (E, E-Sod1SH).	Disulfides	89-98	superoxide dismutase 1	Homo sapiens	56-60
29956268-2	2018	Here I describe a protocol for obtaining well-folded human granulins A, C, and F by expressing them as thioredoxin fusion proteins in Origami (DE3) Escherichia coli cells promoting disulfide bond formation in the cytoplasm environment.	Disulfides	181-190	granulin precursor	Homo sapiens	59-68
29317059-5	2018	Fibrinogen modification involves intra-to intermolecular disulfide rearrangement induced by the reductive power of hydroxyl radicals that result in the exposition of buried hydrophobic epitopes.	Disulfides	57-66	fibrinogen beta chain	Homo sapiens	0-10
29956269-1	2018	Granulin (GRN) structural motif represents a ladderlike stack of beta-hairpins reinforced with six parallel disulfide bridges.	Disulfides	108-117	granulin precursor	Homo sapiens	0-8
29956269-1	2018	Granulin (GRN) structural motif represents a ladderlike stack of beta-hairpins reinforced with six parallel disulfide bridges.	Disulfides	108-117	granulin precursor	Homo sapiens	10-13
29956269-6	2018	At first, GRN disulfide species are crudely separated by reversed-phase HPLC chromatography.	Disulfides	14-23	granulin precursor	Homo sapiens	10-13
29956269-9	2018	Additionally, NMR characterization of model peptides derived from the GRN amino acid sequences can help resolve ambiguities in disulfide bond assignment.	Disulfides	127-136	granulin precursor	Homo sapiens	70-73
31080944-1	2018	von Willebrand factor (VWF) is a multimeric protein composed of monomeric subunits (~280 kD) linked by disulfide bonds.	Disulfides	103-112	von Willebrand factor	Homo sapiens	23-26
29126850-3	2017	Interchain disulfide bridging of an alphaCD3 Fab enabled installation of either the PSMA-targeting small molecule DUPA (SynFab) or the attachment of an alphaPSMA Fab (BisFab) by covalent linkage.	Disulfides	11-20	folate hydrolase 1	Homo sapiens	84-88
29172484-3	2017	Here, we report a new method for the total chemical synthesis of IGF-1 analogs, which entails the solid-phase synthesis of two IGF-1 precursor chains that is followed by the CuI-catalyzed azide-alkyne cycloaddition ligation and by biomimetic formation of a native pattern of disulfides.	Disulfides	275-285	insulin like growth factor 1	Homo sapiens	65-70
29172484-3	2017	Here, we report a new method for the total chemical synthesis of IGF-1 analogs, which entails the solid-phase synthesis of two IGF-1 precursor chains that is followed by the CuI-catalyzed azide-alkyne cycloaddition ligation and by biomimetic formation of a native pattern of disulfides.	Disulfides	275-285	insulin like growth factor 1	Homo sapiens	127-132
29172484-5	2017	These new synthetic IGF-1 analogs are unique examples of disulfide bonds" rich proteins with intra main-chain triazole links.	Disulfides	57-66	insulin like growth factor 1	Homo sapiens	20-25
29202233-1	2017	Novel hybrid molecule containing 2-mercaptoethylamine was synthesized starting from O-propyloxime-N-propoxy bacteriopurpurinimide (dipropoxy-BPI), which was readily oxidized in oxygen atmosphere yielding the corresponding disulfide analogue (disulfide-BPI).	Disulfides	222-231	bactericidal permeablility increasing protein	Mus musculus	141-144
29202233-1	2017	Novel hybrid molecule containing 2-mercaptoethylamine was synthesized starting from O-propyloxime-N-propoxy bacteriopurpurinimide (dipropoxy-BPI), which was readily oxidized in oxygen atmosphere yielding the corresponding disulfide analogue (disulfide-BPI).	Disulfides	222-231	bactericidal permeablility increasing protein	Mus musculus	252-255
29435172-4	2018	Then, the promiximab was conjugated with a potent DNA alkylating agent duocarmycin via reduced interchain disulfides to yield the promiximab-Duocarmycin (promiximab-DUBA) conjugates.	Disulfides	106-116	OTU deubiquitinase 5	Homo sapiens	165-169
29241459-0	2017	To Mia or not to Mia: stepwise evolution of the mitochondrial intermembrane space disulfide relay.	Disulfides	82-91	MIA SH3 domain containing	Homo sapiens	3-6
29241459-0	2017	To Mia or not to Mia: stepwise evolution of the mitochondrial intermembrane space disulfide relay.	Disulfides	82-91	MIA SH3 domain containing	Homo sapiens	17-20
29234142-3	2017	The Copper Chaperone for SOD1 (CCS) transiently interacts with SOD1 and promotes its correct maturation by transferring copper and catalyzing disulfide bond formation.	Disulfides	142-151	superoxide dismutase 1	Homo sapiens	25-29
29234142-3	2017	The Copper Chaperone for SOD1 (CCS) transiently interacts with SOD1 and promotes its correct maturation by transferring copper and catalyzing disulfide bond formation.	Disulfides	142-151	superoxide dismutase 1	Homo sapiens	63-67
29030430-0	2017	Direct binding to integrins and loss of disulfide linkage in interleukin-1beta (IL-1beta) are involved in the agonistic action of IL-1beta.	Disulfides	40-49	interleukin 1 beta	Homo sapiens	61-78
29030430-10	2017	We studied whether the disulfide linkage plays a role in agonistic action of IL-1beta.	Disulfides	23-32	interleukin 1 beta	Homo sapiens	77-85
29030430-0	2017	Direct binding to integrins and loss of disulfide linkage in interleukin-1beta (IL-1beta) are involved in the agonistic action of IL-1beta.	Disulfides	40-49	interleukin 1 beta	Homo sapiens	80-88
29030430-0	2017	Direct binding to integrins and loss of disulfide linkage in interleukin-1beta (IL-1beta) are involved in the agonistic action of IL-1beta.	Disulfides	40-49	interleukin 1 beta	Homo sapiens	130-138
29059501-4	2017	We based our designs on two known disulfide-containing, peptide-based inhibitors of the vWF-collagen interaction.	Disulfides	34-43	von Willebrand factor	Homo sapiens	88-91
27766889-6	2017	During the theoretical analysis of homology models, unexpected role of number of disulfide bonds and secondary structure elements has been witnessed in case of Wnt3 and Wnt3a proteins.	Disulfides	81-90	Wnt family member 3	Homo sapiens	160-164
28551866-6	2017	Two predicted disulfide bonds in Lm-AlpI were composed of four cysteines (C152-C214 and C499-C506), which were homologous to those of mammals.	Disulfides	14-23	alkaline phosphatase, intestinal	Homo sapiens	36-40
29096436-8	2017	Cross-linking was associated with formation of sulfenic acids (RS-OH species), oxidation of methionine residues, cleavage of disulfide bonds in alpha-lactalbumin, altered conformation of disulfide bonds in beta-lactoglobulin, alterations in the fluorescence intensity and maximum emission wavelength of endogenous tryptophan residues, and binding of the hydrophobic probe 8-anilinonaphthalenesulfonate.	Disulfides	125-134	lactalbumin alpha	Homo sapiens	144-161
29192194-7	2017	Interaction of BIR1 with copper(II) results in the oxidation of cysteine 12, with the formation of either an intermolecular disulfide bond between two BIR1 molecules or a mixed disulfide bond with glutathione, whereas the zinc binding site is not affected by the interaction.	Disulfides	124-133	potassium inwardly rectifying channel subfamily J member 6	Homo sapiens	15-19
29192194-7	2017	Interaction of BIR1 with copper(II) results in the oxidation of cysteine 12, with the formation of either an intermolecular disulfide bond between two BIR1 molecules or a mixed disulfide bond with glutathione, whereas the zinc binding site is not affected by the interaction.	Disulfides	124-133	potassium inwardly rectifying channel subfamily J member 6	Homo sapiens	151-155
29192194-7	2017	Interaction of BIR1 with copper(II) results in the oxidation of cysteine 12, with the formation of either an intermolecular disulfide bond between two BIR1 molecules or a mixed disulfide bond with glutathione, whereas the zinc binding site is not affected by the interaction.	Disulfides	177-186	potassium inwardly rectifying channel subfamily J member 6	Homo sapiens	15-19
28924868-0	2017	Photodegradation Pathways of Protein Disulfides: Human Growth Hormone.	Disulfides	37-47	growth hormone 1	Homo sapiens	55-69
28672263-7	2017	The SPI nanoaggregates were used to prepare oil-in-water nanoemulsions with canola oil, which exhibited good stability over 21days at 4 C. In addition, the pH 12-MTS samples had resulted in the highest protein solubility, lowest turbidity, free sulfhydryl and disulfide bonds, surface hydrophobicity, antioxidant activity, and rheological and emulsifying properties than the other samples.	Disulfides	260-269	chromogranin A	Homo sapiens	4-7
28924868-1	2017	PURPOSE: Comprehensive product characterization was performed for the photodegradation of protein disulfides, representatively of human growth hormone (somatotropin; hGH), in order to provide a product database, which will be useful for the general analysis of protein stability.	Disulfides	98-108	growth hormone 1	Homo sapiens	136-150
28924868-1	2017	PURPOSE: Comprehensive product characterization was performed for the photodegradation of protein disulfides, representatively of human growth hormone (somatotropin; hGH), in order to provide a product database, which will be useful for the general analysis of protein stability.	Disulfides	98-108	growth hormone 1	Homo sapiens	152-164
28899696-0	2017	Serotonin 2A receptor disulfide bridge integrity is crucial for ligand binding to different signalling states but not for its homodimerization.	Disulfides	22-31	5-hydroxytryptamine receptor 2A	Homo sapiens	0-21
28899696-1	2017	The serotonin 2A (5-HT2A) receptor is a G-protein coupled receptor (GPCR) with a conserved disulfide bridge formed by Cys148 (transmembrane helix 3, TM3) and Cys227 (extracellular loop 2, ECL-2).	Disulfides	91-100	5-hydroxytryptamine receptor 2A	Homo sapiens	4-34
28899696-2	2017	We hypothesized that disulfide bridges may determine serotonin 5-HT2A receptor functions such as receptor activation, functional selectivity and ligand recognition.	Disulfides	21-30	5-hydroxytryptamine receptor 2A	Homo sapiens	53-78
28939765-7	2017	In response to H2O2 treatment in cardiomyocytes, mTOR exhibited a high molecular weight shift in non-reducing SDS-PAGE in a 2-mercaptoethanol-sensitive manner, suggesting that mTOR is oxidized and forms disulfide bonds with itself or other proteins.	Disulfides	203-212	mechanistic target of rapamycin kinase	Homo sapiens	49-53
28939765-7	2017	In response to H2O2 treatment in cardiomyocytes, mTOR exhibited a high molecular weight shift in non-reducing SDS-PAGE in a 2-mercaptoethanol-sensitive manner, suggesting that mTOR is oxidized and forms disulfide bonds with itself or other proteins.	Disulfides	203-212	mechanistic target of rapamycin kinase	Homo sapiens	176-180
28629863-1	2017	Mechanical unfolding of mutated apo, disulfide-reduced, monomeric superoxide dismutase 1 protein (SOD1) has been simulated via force spectroscopy techniques, using both an all-atom (AA), explicit solvent model and a coarse-grained heavy-atom Go (HA-Go) model.	Disulfides	37-46	superoxide dismutase 1	Homo sapiens	98-102
29223155-5	2017	Results of MALDI-TOF mass spectrometry showed that after refolding 6His-s-tag-EPO formed a structure similar to that of one of native EPO with two disulfide bonds.	Disulfides	147-156	erythropoietin	Homo sapiens	78-81
28949004-6	2017	Here, we show that the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD against PDI-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 inhibition.	Disulfides	113-122	heat shock protein family A (Hsp70) member 5	Homo sapiens	67-72
28949004-6	2017	Here, we show that the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD against PDI-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 inhibition.	Disulfides	113-122	protein disulfide isomerase family A member 2	Homo sapiens	99-102
29079747-0	2017	Disulfide cross-linked multimers of TDP-43 and spinal motoneuron loss in a TDP-43A315T ALS/FTD mouse model.	Disulfides	0-9	TAR DNA binding protein	Mus musculus	36-42
29055186-7	2017	The steered molecular dynamics studies have revealed that the Inhibitor-1 with disulfide linker unit is more stable at the active site due to greater noncovalent interactions compared to the SCH28080.	Disulfides	79-88	protein phosphatase 1 regulatory inhibitor subunit 1A	Homo sapiens	62-73
28976190-0	2017	Biochemical and Functional Evaluation of the Intramolecular Disulfide Bonds in the Zinc-Chelating Antimicrobial Protein Human S100A7 (Psoriasin).	Disulfides	60-69	S100 calcium binding protein A7	Homo sapiens	126-132
28976190-22	2017	Metal substitution experiments suggest that the disulfide bonds in S100A7 may enhance metal sequestration by the His3Asp sites and thereby confer growth inhibitory properties to S100A7ox.	Disulfides	48-57	S100 calcium binding protein A7	Homo sapiens	67-73
29085013-3	2017	Here, we used peptide design to perform targeted chemical modifications to Ang II to generate conformationally restricted (disulfide-crosslinked) peptide derivatives with suppressed vasoconstrictor activity and increased stability.	Disulfides	123-132	angiotensinogen	Homo sapiens	75-81
29079747-8	2017	Unexpectedly, we identified the presence of different species of disulfide-dependent TDP-43 aggregates in cortex and spinal cord tissue.	Disulfides	65-74	TAR DNA binding protein	Mus musculus	85-91
29204107-2	2017	The CD13-targeting moiety NGR was synthesized and cyclized by native chemical ligation (NCL) instead of disulfide bridging, leading to a cyclic peptide backbone: cyclo(Cys-Asn-Gly-Arg-Gly) (coNGR).	Disulfides	104-113	reticulon 4 receptor	Mus musculus	26-29
28814504-6	2017	In reconstitution studies with reduced Tim13, Mia40, and Erv1, the addition of Osm1 and fumarate completes the disulfide exchange pathway that results in Tim13 oxidation.	Disulfides	111-120	translocase of inner mitochondrial membrane 13	Homo sapiens	154-159
28981461-4	2017	Excess reducing equivalents may regulate cellular signaling pathways, modify transcriptional activity, induce alterations in the formation of disulfide bonds in proteins, reduce mitochondrial function, decrease cellular metabolism, and thus, contribute to the development of some diseases in which NF-kappaB, a redox-sensitive transcription factor, participates.	Disulfides	142-151	nuclear factor kappa B subunit 1	Homo sapiens	298-307
29030641-3	2017	Disulfide bound complexes of lubricin and cartilage oligomeric matrix protein (COMP) have recently been identified in arthritic synovial fluid suggesting they may be lost from the cartilage surface in osteoarthritis and inflammatory arthritis.	Disulfides	0-9	proteoglycan 4	Homo sapiens	29-37
28918898-1	2017	In the endoplasmic reticulum (ER), Ero1 catalyzes disulfide bond formation and promotes glutathione (GSH) oxidation to GSSG.	Disulfides	50-59	ER oxidoreductin	Saccharomyces cerevisiae S288C	35-39
28849192-1	2017	High molecular weight (HMW) adiponectin (APN) is closely correlated with the development of fatty liver and is modulated by the Akt/forkhead box protein O1 (FOXO1) pathway through disulfide-bond A oxidoreductase-like protein (DsbA-L).	Disulfides	180-189	AKT serine/threonine kinase 1	Rattus norvegicus	128-131
27576262-10	2017	Two out of five predicted models caught the experimental verified disulfide bonds in vasopressin V2 receptor.	Disulfides	66-75	arginine vasopressin receptor 2	Homo sapiens	85-108
28585802-0	2017	Cu/Zn Superoxide Dismutase Forms Amyloid Fibrils under Near-Physiological Quiescent Conditions: The Roles of Disulfide Bonds and Effects of Denaturant.	Disulfides	109-118	superoxide dismutase 1	Homo sapiens	0-26
28585802-4	2017	Here we show that monomeric apo-SOD1 in the disulfide-reduced state forms fibrillar aggregates under near-physiological quiescent conditions.	Disulfides	44-53	superoxide dismutase 1	Homo sapiens	32-36
28585802-5	2017	Monomeric apo-SOD1 with an intact intramolecular disulfide bond is highly resistant to aggregation under the same conditions.	Disulfides	49-58	superoxide dismutase 1	Homo sapiens	14-18
28585802-6	2017	A cysteine-free variant of SOD1 exhibits fibrillization behavior and fibril morphology identical to those of disulfide-reduced SOD1, firmly establishing that intermolecular disulfide bonds or intramolecular disulfide shuffling are not required for aggregation and fibril formation.	Disulfides	109-118	superoxide dismutase 1	Homo sapiens	27-31
28585802-6	2017	A cysteine-free variant of SOD1 exhibits fibrillization behavior and fibril morphology identical to those of disulfide-reduced SOD1, firmly establishing that intermolecular disulfide bonds or intramolecular disulfide shuffling are not required for aggregation and fibril formation.	Disulfides	109-118	superoxide dismutase 1	Homo sapiens	127-131
28585802-6	2017	A cysteine-free variant of SOD1 exhibits fibrillization behavior and fibril morphology identical to those of disulfide-reduced SOD1, firmly establishing that intermolecular disulfide bonds or intramolecular disulfide shuffling are not required for aggregation and fibril formation.	Disulfides	173-182	superoxide dismutase 1	Homo sapiens	27-31
28585802-6	2017	A cysteine-free variant of SOD1 exhibits fibrillization behavior and fibril morphology identical to those of disulfide-reduced SOD1, firmly establishing that intermolecular disulfide bonds or intramolecular disulfide shuffling are not required for aggregation and fibril formation.	Disulfides	173-182	superoxide dismutase 1	Homo sapiens	27-31
28829564-0	2017	Novel Methods for the Chemical Synthesis of Insulin Superfamily Peptides and of Analogues Containing Disulfide Isosteres.	Disulfides	101-110	insulin	Homo sapiens	44-51
28829564-1	2017	The insulin superfamily of peptides is ubiquitous within vertebrates and invertebrates and is characterized by the presence of a set of three disulfide bonds in a unique disposition.	Disulfides	142-151	insulin	Homo sapiens	4-11
28829564-12	2017	Together, these synthesis improvements and the novel chemical developments of cysteine/cystine analogues have greatly aided in the development of novel insulin-like peptide (INSL) analogues, principally with intra-A-chain disulfide isosteres, possessing not only improved functional properties such as increased receptor selectivity but also, with one important and unexpected exception, greater in vivo half-lives due to stability against disulfide reductases.	Disulfides	222-231	insulin	Homo sapiens	152-159
28894122-0	2017	Onset of disorder and protein aggregation due to oxidation-induced intermolecular disulfide bonds: case study of RRM2 domain from TDP-43.	Disulfides	82-91	TAR DNA binding protein	Homo sapiens	130-136
28810662-5	2017	While endogenous galectin-9 is not required for basal cell surface PDI expression, exogenous galectin-9 mediated retention of cell surface PDI shifted the disulfide/thiol equilibrium on the T cell surface.	Disulfides	155-164	galectin 9	Homo sapiens	93-103
28373131-9	2017	The close proximity of the non-covalent and disulfide binding domains on lubricin suggest a two-step mechanism to strongly bind lubricin to COMP.	Disulfides	44-53	proteoglycan 4	Homo sapiens	73-81
28373131-9	2017	The close proximity of the non-covalent and disulfide binding domains on lubricin suggest a two-step mechanism to strongly bind lubricin to COMP.	Disulfides	44-53	proteoglycan 4	Homo sapiens	128-136
28692093-4	2017	Using the disulfide moiety in a 3,3"-dithiodipropionic acid dihydrazide (DTP)-linked beta-d-NAG probe, Au nanoparticles (AuNPs) are employed for enriching DTP-linked beta-d-NAG after enzymatic reaction, and the ligand-bound AuNPs are subsequently deposited on a MALDI plate for analysis.	Disulfides	10-19	N-acetyl-alpha-glucosaminidase	Homo sapiens	92-95
28912774-2	2017	KIR3DL2, also known as CD158k, is expressed as a disulfide-linked homodimer.	Disulfides	49-58	killer cell immunoglobulin like receptor, three Ig domains and long cytoplasmic tail 2	Homo sapiens	0-7
28912774-2	2017	KIR3DL2, also known as CD158k, is expressed as a disulfide-linked homodimer.	Disulfides	49-58	killer cell immunoglobulin like receptor, three Ig domains and long cytoplasmic tail 2	Homo sapiens	23-29
28653773-4	2017	Thiol-functionalized transferrin (Tf-SH) is anchored onto the surface of MoS2 nanosheets by the formation of disulfide bonds, which could further enhance the cellular uptake of DOX and MoS2 to HepG2 cells for high-efficiency synergetic therapy.	Disulfides	109-118	transferrin	Homo sapiens	21-32
28686251-5	2017	The mechanism of Ccs1-mediated Sod1 activation involves both insertion of the catalytic copper ion and mediating disulfide bond formation.	Disulfides	113-122	superoxide dismutase 1	Homo sapiens	31-35
28686251-6	2017	Since Sod1 is a highly abundant enzyme residing within the highly reducing cytoplasm, the question of disulfide bond formation is significant yet unresolved.	Disulfides	102-111	superoxide dismutase 1	Homo sapiens	6-10
28686251-7	2017	The processes involved in Sod1 activation are reviewed with a focus on copper ion insertion and disulfide bond formation.	Disulfides	96-105	superoxide dismutase 1	Homo sapiens	26-30
28771323-10	2017	The discovery and application of biomimetic connecting peptides simplifies proper disulfide formation and the subsequent traceless removal by chemical methods dramatically simplifies the total synthesis of virtually any two-chain insulin-like peptide.	Disulfides	82-91	insulin	Homo sapiens	230-237
28739909-2	2017	Crystal structures of MAL revealed a nontypical Toll/interleukin-1 receptor (TIR)-domain fold stabilized by two disulfide bridges.	Disulfides	112-121	mal, T cell differentiation protein	Homo sapiens	22-25
28739909-5	2017	The solution structure of the reduced form of the MAL TIR domain, determined by NMR spectroscopy, reveals a remarkable structural rearrangement compared with the disulfide-bonded structure, which includes the relocation of a beta-strand and repositioning of the functionally important "BB-loop" region to a location more typical for TIR domains.	Disulfides	162-171	mal, T cell differentiation protein	Homo sapiens	50-53
28648616-7	2017	Notably, introducing disulfide bonds between subdomains SD2 and SD3 modulated IFN binding and activity in accordance with the relative attenuation of cooperative movements with varying distance from the hinge center, whereas locking the SD3-SD4 interface flexibility in favor of an extended conformer increased activity.	Disulfides	21-30	interferon alpha 1	Homo sapiens	78-81
28363599-1	2017	A distinctive and personalized nanocarrier is described here for controlled and targeted antitumor drug delivery and real-time bioimaging by combining a redox/enzyme dual-responsive disulfide-conjugated carbon dot with mesoporous silica nanoparticles (MSN-SS-CDHA).	Disulfides	182-191	moesin	Homo sapiens	252-255
28501743-6	2017	Furthermore, while it has been extensively reported that human cytoglobin is essentially monomeric and can form an intramolecular disulfide bridge that can influence the ligand binding kinetics, 3D modeling of the Antarctic fish cytoglobins indicates that the cysteine residues are too far apart to form such an intramolecular bridge.	Disulfides	130-139	cytoglobin	Homo sapiens	63-73
28827692-3	2017	Here we show that in-frame fusion of human C-propeptide of alpha1(I) collagen (Trimer-Tag) to the C-terminus of mature human TRAIL leads to a disulfide bond-linked homotrimer which can be expressed at high levels as a secreted protein from CHO cells.	Disulfides	142-151	TNF superfamily member 10	Homo sapiens	125-130
28771323-2	2017	Insulin resides within in a superfamily of structurally related peptides that are distinguished by three invariant disulfide bonds that anchor the three-dimensional conformation of the hormone.	Disulfides	115-124	insulin	Homo sapiens	0-7
28771323-6	2017	This Account presents a historical context for the advances in the chemical synthesis of insulin and the related peptides, with division into two general categories where disulfide bond formation is facilitated by native conformational folding or alternatively orthogonal chemical reactivity.	Disulfides	171-180	insulin	Homo sapiens	89-96
28655765-4	2017	Here, using crystallographic and biochemical analyses, we show that the beta4 extracellular domains directly interact with each other in a parallel manner that involves an intermolecular disulfide bond between the unpaired Cys residues (Cys58) in the loop connecting strands B and C and intermolecular hydrophobic and hydrogen-bonding interactions of the N-terminal segments (Ser30-Val35).	Disulfides	187-196	adaptor related protein complex 4 subunit beta 1	Homo sapiens	72-77
28628095-3	2017	Upon reacting with H2O2, Orp1 catalytic cysteine oxidizes to a sulfenic acid, which then engages into either an intermolecular disulfide with Yap1, leading to Yap1 activation, or an intramolecular disulfide that commits the enzyme into its peroxidatic cycle.	Disulfides	127-136	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	142-146
28628095-3	2017	Upon reacting with H2O2, Orp1 catalytic cysteine oxidizes to a sulfenic acid, which then engages into either an intermolecular disulfide with Yap1, leading to Yap1 activation, or an intramolecular disulfide that commits the enzyme into its peroxidatic cycle.	Disulfides	127-136	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	159-163
28628095-5	2017	We show that the Yap1-binding protein Ybp1 brings together Orp1 and Yap1 into a ternary complex that selectively activates condensation of the Orp1 sulfenylated cysteine with one of the six Yap1 cysteines while inhibiting Orp1 intramolecular disulfide formation.	Disulfides	242-251	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	17-21
28628095-5	2017	We show that the Yap1-binding protein Ybp1 brings together Orp1 and Yap1 into a ternary complex that selectively activates condensation of the Orp1 sulfenylated cysteine with one of the six Yap1 cysteines while inhibiting Orp1 intramolecular disulfide formation.	Disulfides	242-251	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	68-72
28628095-5	2017	We show that the Yap1-binding protein Ybp1 brings together Orp1 and Yap1 into a ternary complex that selectively activates condensation of the Orp1 sulfenylated cysteine with one of the six Yap1 cysteines while inhibiting Orp1 intramolecular disulfide formation.	Disulfides	242-251	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	68-72
28533431-2	2017	The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering copper and facilitating the oxidation of the Sod1 intramolecular disulfide bond.	Disulfides	191-200	superoxide dismutase 1	Homo sapiens	106-110
28533431-2	2017	The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering copper and facilitating the oxidation of the Sod1 intramolecular disulfide bond.	Disulfides	191-200	superoxide dismutase 1	Homo sapiens	171-175
28533431-5	2017	Copper-mediated sulfenylation leads to a sulfenic acid intermediate that eventually resolves to form the Sod1 disulfide bond with concomitant release of copper into the Sod1 active site.	Disulfides	110-119	superoxide dismutase 1	Homo sapiens	105-109
28533431-5	2017	Copper-mediated sulfenylation leads to a sulfenic acid intermediate that eventually resolves to form the Sod1 disulfide bond with concomitant release of copper into the Sod1 active site.	Disulfides	110-119	superoxide dismutase 1	Homo sapiens	169-173
28533431-6	2017	Sod1 is the predominant disulfide bond-requiring enzyme in the cytoplasm, and this copper-induced mechanism of disulfide bond formation obviates the need for a thiol/disulfide oxidoreductase in that compartment.	Disulfides	24-33	superoxide dismutase 1	Homo sapiens	0-4
28533431-6	2017	Sod1 is the predominant disulfide bond-requiring enzyme in the cytoplasm, and this copper-induced mechanism of disulfide bond formation obviates the need for a thiol/disulfide oxidoreductase in that compartment.	Disulfides	111-120	superoxide dismutase 1	Homo sapiens	0-4
28733604-5	2017	We found that TDP-43 NTD forms a homodimer in solution in a concentration-dependent manner, and formation of intermolecular disulfide results in further tetramerization.	Disulfides	124-133	TAR DNA binding protein	Homo sapiens	14-20
28692093-4	2017	Using the disulfide moiety in a 3,3"-dithiodipropionic acid dihydrazide (DTP)-linked beta-d-NAG probe, Au nanoparticles (AuNPs) are employed for enriching DTP-linked beta-d-NAG after enzymatic reaction, and the ligand-bound AuNPs are subsequently deposited on a MALDI plate for analysis.	Disulfides	10-19	N-acetyl-alpha-glucosaminidase	Homo sapiens	173-176
28300559-3	2017	SAP-2 has a conserved tertiary structure containing three disulfide bonds and conformational epitopes.	Disulfides	58-67	ETS transcription factor ELK3	Homo sapiens	0-5
28533135-1	2017	Mutation of the cysteines forming the disulfide loop of the platelet GPIbalpha adhesive A1 domain of von Willebrand factor (VWF) causes quantitative VWF deficiencies in the blood and von Willebrand disease.	Disulfides	38-47	von Willebrand factor	Homo sapiens	101-122
28533135-1	2017	Mutation of the cysteines forming the disulfide loop of the platelet GPIbalpha adhesive A1 domain of von Willebrand factor (VWF) causes quantitative VWF deficiencies in the blood and von Willebrand disease.	Disulfides	38-47	von Willebrand factor	Homo sapiens	124-127
28533135-5	2017	Constrained by the disulfide, conformational selection between weak and tight binding states of A1 takes precedence and drives normal platelet adhesion to VWF.	Disulfides	19-28	von Willebrand factor	Homo sapiens	155-158
28300559-4	2017	Therefore, antigenicity of SAP-2 is greatly depends on disulfide bond formation and proper folding.	Disulfides	55-64	ETS transcription factor ELK3	Homo sapiens	27-32
28461071-1	2017	Alphaviruses require conserved cysteine residues for proper folding and assembly of the E1 and E2 envelope glycoproteins, and likely depend on host protein disulfide isomerase-family enzymes (PDI) to aid in facilitating disulfide bond formation and isomerization in these proteins.	Disulfides	156-165	protein disulfide isomerase family A member 2	Homo sapiens	192-195
27363428-4	2017	Thiols of flagellar proteins, such as outer dense fibre protein 1 (ODF1), are oxidised to form disulfides during epididymal transit and the spermatozoa become motile.	Disulfides	95-105	outer dense fiber of sperm tails 1	Homo sapiens	67-71
28508285-7	2017	Results from analyses of AAs and insulin indicated that HNO3 could not only react with basic amino acid residues, but also with disulfide bonds to form [M-3H+(HNO3)n]3- complex ions.	Disulfides	128-137	insulin	Homo sapiens	33-40
27215901-8	2017	Homocysteinylation of GAPDH may stabilize aggregates of the enzyme by additional disulfide bonding.	Disulfides	81-90	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	22-27
28456374-2	2017	Their association with ERp57, a member of PDI family proteins (PDIs) which promote disulfide bond formation of unfolded proteins, has been well documented.	Disulfides	83-92	protein disulfide isomerase family A member 3	Homo sapiens	23-28
28620198-6	2017	Molecular hydrogen (H2) was found to be more effectively protected H2O2-induced IP3R1 dysfunction by reducing disulfide bonds, rather than quenching ROS.	Disulfides	110-119	inositol 1,4,5-trisphosphate receptor type 1	Homo sapiens	80-85
28357481-0	2017	Disulfide-modified antigen for detection of celiac disease-associated anti-tissue transglutaminase autoantibodies.	Disulfides	0-9	transglutaminase 2	Homo sapiens	75-98
28357481-2	2017	The antigenic protein tissue transglutaminase was chemically modified, introducing disulfide groups through different moieties of the molecule (amine, carboxylic, and hydroxyl groups), self-assembled on gold surfaces, and used for the detection of IgA and IgG autoantibodies.	Disulfides	83-92	transglutaminase 2	Homo sapiens	22-45
28357481-3	2017	The modified proteins were evaluated using enzyme-linked immunosorbent assay and surface plasmon resonance, which showed that only introduction of the disulfide groups through amine moieties in the tissue transglutaminase preserved its antigenic properties.	Disulfides	151-160	transglutaminase 2	Homo sapiens	198-221
28351690-6	2017	The apo form of alpha-lactalbumin (aLA) forms liprotides at room temperature, however, Ovalbumin (Ova) and Bovine Serum Albumin (BSA) require elevated temperatures (&gt;=60 C) to form liprotides, and in addition, they need to be returned to lower temperatures to remain stable; repeated cycles of heating and cooling gradually dissociate the liprotides in parallel with the formation of disulfide-bonded aggregates.	Disulfides	387-396	lactalbumin alpha	Homo sapiens	16-33
27966089-6	2017	Raman shifts and the alteration of spectral features observed in the ClO2-treated lysozyme samples are associated with loss of the alpha-helix secondary structure, tertiary structure, and disulfide bond.	Disulfides	188-197	lysozyme	Homo sapiens	82-90
28152568-9	2017	In addition, apo(a) covalently links to the apolipoprotein B component of a low-density lipoprotein through a disulfide bridge to form lipoprotein(a).	Disulfides	110-119	apolipoprotein B	Homo sapiens	44-60
28389559-9	2017	Furthermore, we also show that whereas STEP and PTPRR stabilize their reversibly oxidized state by forming an intramolecular disulfide bond, HePTP uses an unexpected mechanism, namely, formation of a reversible intermolecular disulfide bond.	Disulfides	226-235	protein tyrosine phosphatase non-receptor type 7	Homo sapiens	141-146
28348082-6	2017	Kinetic and simulation data suggest that the oxidation of Prx2 by urate hydroperoxide occurs by a three-step mechanism, where the peroxide reversibly associates with the enzyme; then it oxidizes the peroxidatic cysteine, and finally, the rate-limiting disulfide bond is formed.	Disulfides	252-261	peroxiredoxin 2	Homo sapiens	58-62
28348082-7	2017	Of relevance, the disulfide bond formation was much slower in Prx2 (k3 = 0.31 s-1) than Prx1 (k3 = 14.9 s-1).	Disulfides	18-27	peroxiredoxin 2	Homo sapiens	62-66
28340507-0	2017	Understanding the contribution of disulfide bridges to the folding and misfolding of an anti-Abeta scFv.	Disulfides	34-43	immunglobulin heavy chain variable region	Homo sapiens	99-103
28340507-2	2017	Production of scFv molecules is not a straightforward procedure because of the occurrence of disulfide scrambled conformations generated in the refolding process.	Disulfides	93-102	immunglobulin heavy chain variable region	Homo sapiens	14-18
28394477-2	2017	The replacement of the interchain disulfide with a diselenide bridge, which is more resistant to reduction and internal bond rotation, can enhance the lifetime of insulin in the presence of the insulin-degrading enzyme (IDE) without impairing the hormonal function.	Disulfides	34-43	insulin	Homo sapiens	163-170
28545586-0	2017	Disulfide high mobility group box-1 causes bladder pain through bladder Toll-like receptor 4.	Disulfides	0-9	toll-like receptor 4	Mus musculus	72-92
28545586-13	2017	CONCLUSIONS: The disulfide form of HMGB1 mediates bladder pain directly (not secondary to inflammation or injury) through activation of TLR4 receptors in the bladder.	Disulfides	17-26	toll-like receptor 4	Mus musculus	136-140
28593139-3	2017	The two cysteine sulfhydryls of Cygb were modified to form either an intramolecular disulfide bond (Cygb_SS), thioether bonds to N-ethylmaleimide (NEM; Cygb_SC), or were maintained as free SH groups (Cygb_SH).	Disulfides	84-93	cytoglobin	Homo sapiens	32-36
28235456-4	2017	With disulfide bonds reduced, HRG and Fgn alpha-chain reactions were demonstrated.	Disulfides	5-14	histidine-rich glycoprotein	Oryctolagus cuniculus	30-33
28425707-5	2017	Peptides that contained only two native disulfide bonds lack the characteristic granulin beta-hairpin structure.	Disulfides	40-49	granulin precursor	Homo sapiens	80-88
28363871-0	2017	Impact of antibody subclass and disulfide isoform differences on the biological activity of CD200R and betaklotho agonist antibodies.	Disulfides	32-41	CD200 receptor 1	Homo sapiens	92-98
28267577-10	2017	The reduction of disulfide bonds leads to a rearrangement and redirects assembly of Abeta amyloid fibrils.	Disulfides	17-26	amyloid beta precursor protein	Homo sapiens	84-89
28392212-4	2017	Peroxiredoxin-2 was also affected during storage, with a progressive accumulation of disulfide-linked dimers and hetero-protein complexes in the cytosol and also in the membrane of stored RBC.	Disulfides	85-94	peroxiredoxin 2	Homo sapiens	0-15
28267577-12	2017	This pathway involves the formation of oligomers resulting from the arrangement of Abeta dimers linked by covalent di-sulfide link, being these oligomers harmful for the membranes.	Disulfides	115-125	amyloid beta precursor protein	Homo sapiens	83-88
28423644-0	2017	Disulfide bond disrupting agents activate the unfolded protein response in EGFR- and HER2-positive breast tumor cells.	Disulfides	0-9	epidermal growth factor receptor	Homo sapiens	75-79
28326661-3	2017	In this communication, the contribution of single disulfides in the folding and function of ScTx-Bax peptides was investigated.	Disulfides	50-60	BCL2 associated X, apoptosis regulator	Homo sapiens	97-100
28326661-5	2017	It was determined that the position of the disulfide linkage had significant implications on the structure and function of ScTx-Bax peptides.	Disulfides	43-52	BCL2 associated X, apoptosis regulator	Homo sapiens	128-131
27243554-1	2017	BACKGROUND AND PURPOSE: Insulin-like peptide 5 (INSL5) is a two-chain, three-disulfide-bonded peptide of the insulin/relaxin superfamily, uniquely expressed in enteroendocrine L-cells of the colon.	Disulfides	77-86	insulin like 5	Homo sapiens	24-46
27243554-1	2017	BACKGROUND AND PURPOSE: Insulin-like peptide 5 (INSL5) is a two-chain, three-disulfide-bonded peptide of the insulin/relaxin superfamily, uniquely expressed in enteroendocrine L-cells of the colon.	Disulfides	77-86	insulin like 5	Homo sapiens	48-53
28413192-1	2017	The secondary structural changes of human serum albumin with the intact 17 disulfide bridges (HSA) and the disulfide bridges-cleaved human serum albumin (RCM-HSA) in thermal denaturation were examined.	Disulfides	75-84	albumin	Homo sapiens	42-55
28413192-1	2017	The secondary structural changes of human serum albumin with the intact 17 disulfide bridges (HSA) and the disulfide bridges-cleaved human serum albumin (RCM-HSA) in thermal denaturation were examined.	Disulfides	107-116	albumin	Homo sapiens	139-152
28423644-0	2017	Disulfide bond disrupting agents activate the unfolded protein response in EGFR- and HER2-positive breast tumor cells.	Disulfides	0-9	erb-b2 receptor tyrosine kinase 2	Homo sapiens	85-89
28423644-6	2017	We previously identified a class of compounds we termed Disulfide bond Disrupting Agents (DDAs) that selectively kill EGFR+ and HER2+ breast cancer cells in vitro and blocked the growth of HER2+ breast tumors in an animal model.	Disulfides	56-65	epidermal growth factor receptor	Homo sapiens	118-122
28423644-6	2017	We previously identified a class of compounds we termed Disulfide bond Disrupting Agents (DDAs) that selectively kill EGFR+ and HER2+ breast cancer cells in vitro and blocked the growth of HER2+ breast tumors in an animal model.	Disulfides	56-65	erb-b2 receptor tyrosine kinase 2	Homo sapiens	128-132
28423644-6	2017	We previously identified a class of compounds we termed Disulfide bond Disrupting Agents (DDAs) that selectively kill EGFR+ and HER2+ breast cancer cells in vitro and blocked the growth of HER2+ breast tumors in an animal model.	Disulfides	56-65	erb-b2 receptor tyrosine kinase 2	Homo sapiens	189-193
28373561-10	2017	Mutational analyses showed that ERp44 forms mixed disulfides with specific cysteines residing on negatively charged loop regions of Ero1alpha.	Disulfides	50-60	endoplasmic reticulum protein 44	Homo sapiens	32-37
28432788-0	2017	Structure of Fam20A reveals a pseudokinase featuring a unique disulfide pattern and inverted ATP-binding.	Disulfides	62-71	FAM20A golgi associated secretory pathway pseudokinase	Homo sapiens	13-19
28432788-4	2017	Fam20A exhibits a distinct disulfide bond pattern mediated by a unique insertion region.	Disulfides	27-36	FAM20A golgi associated secretory pathway pseudokinase	Homo sapiens	0-6
28232486-5	2017	The disulfide bond cross-link caused a &gt;=95% loss of cytochrome c reductase activity that was reversible with DTT treatment, whereas graded cross-link lengthening gradually increased activity, thus defining the conformational constraints in the catalytic process.	Disulfides	4-13	cytochrome c, somatic	Homo sapiens	56-68
28230989-0	2017	Development of the First Generation of Disulfide-Based Subtype-Selective and Potent Covalent Pyruvate Dehydrogenase Kinase 1 (PDK1) Inhibitors.	Disulfides	39-48	pyruvate dehydrogenase kinase, isoenzyme 1	Mus musculus	126-130
28245108-7	2017	Since the ten Cys residues are highly conserved in Meteorin and Cometin, it is likely that the disulfide linkages are also conserved.	Disulfides	95-104	meteorin, glial cell differentiation regulator-like	Mus musculus	64-71
28088015-2	2017	In this system, transferrin (Tf), a naturally existing protein, is grafted on the surfaces of MSNs via redox-cleavable disulfide bonds, serving as both a capping agent and a targeting ligand simultaneously.	Disulfides	119-128	transferrin	Homo sapiens	16-27
28088015-2	2017	In this system, transferrin (Tf), a naturally existing protein, is grafted on the surfaces of MSNs via redox-cleavable disulfide bonds, serving as both a capping agent and a targeting ligand simultaneously.	Disulfides	119-128	transferrin	Homo sapiens	29-31
28106297-2	2017	Both human alpha defensin type 5 (HD5) and human beta defensin type 3 (hBD-3) have 6 cysteine residues which form 3 pairs of disulfide bonds in oxidizing condition.	Disulfides	125-134	defensin alpha 5	Homo sapiens	34-37
28106297-4	2017	In this project, microsecond long molecular dynamics simulations were performed to study the structure and dynamics of HD5 and hBD-3 wildtype and analogs which have all 3 disulfide bonds released in reducing condition.	Disulfides	171-180	defensin alpha 5	Homo sapiens	119-122
28106297-6	2017	The disulfide bridge breaking order of HD5 and hBD-3 in reducing condition was predicted by two kinds of methods, which gave consistent results.	Disulfides	4-13	defensin alpha 5	Homo sapiens	39-42
28106297-7	2017	It was found that the disulfide bonds breaking pathways for HD5 and hBD-3 are very different.	Disulfides	22-31	defensin alpha 5	Homo sapiens	60-63
28214511-4	2017	Yme1p degrades Tim10 more rapidly than Tim9 despite high sequence and structural similarity, and loss of Tim10 is accelerated by the disruption of conserved disulfide bonds within the substrate.	Disulfides	157-166	protein transporter TIM10	Saccharomyces cerevisiae S288C	105-110
28319665-0	2017	Synthesis of Four-Disulfide Insulin Analogs via Sequential Disulfide Bond Formation.	Disulfides	18-27	insulin	Homo sapiens	28-35
28319665-0	2017	Synthesis of Four-Disulfide Insulin Analogs via Sequential Disulfide Bond Formation.	Disulfides	59-68	insulin	Homo sapiens	28-35
28319665-3	2017	We report here a straightforward and effective approach based on stepwise, sequentially directed disulfide bond formation, exemplified by the synthesis of four-disulfide bond-containing insulin analogs.	Disulfides	97-106	insulin	Homo sapiens	186-193
28319665-3	2017	We report here a straightforward and effective approach based on stepwise, sequentially directed disulfide bond formation, exemplified by the synthesis of four-disulfide bond-containing insulin analogs.	Disulfides	160-169	insulin	Homo sapiens	186-193
28319665-5	2017	This report describes chemistry that is broadly applicable to cysteine-rich peptides and the influence of a fourth disulfide bond on insulin bioactivity.	Disulfides	115-124	insulin	Homo sapiens	133-140
28230989-0	2017	Development of the First Generation of Disulfide-Based Subtype-Selective and Potent Covalent Pyruvate Dehydrogenase Kinase 1 (PDK1) Inhibitors.	Disulfides	39-48	pyruvate dehydrogenase kinase, isoenzyme 1	Mus musculus	93-124
28230989-3	2017	Here, on the basis of the scaffold of 16, we identify two novel types of disulfide-based PDK1 inhibitors.	Disulfides	73-82	pyruvate dehydrogenase kinase, isoenzyme 1	Mus musculus	89-93
28273916-5	2017	Herein, we demonstrate that covalently binding, through a disulfide bridge, a peptide mimicking the S4-S5 linker (S4-S5L) to the channel S6 C-terminus (S6T) completely inhibits hERG.	Disulfides	58-67	ETS transcription factor ERG	Homo sapiens	177-181
28423625-0	2017	Inhibition activity of a disulfide-stabilized diabody against basic fibroblast growth factor in lung cancer.	Disulfides	25-34	fibroblast growth factor 2	Homo sapiens	62-92
28423625-3	2017	In this study, a Disulfide-stabilized diabody (ds-Diabody) against bFGF was constructed by site-directed mutation and overlap extension PCR (SOE-PCR) at the position of VH44 and VL100 in the scFv.	Disulfides	17-26	fibroblast growth factor 2	Homo sapiens	67-71
28423625-3	2017	In this study, a Disulfide-stabilized diabody (ds-Diabody) against bFGF was constructed by site-directed mutation and overlap extension PCR (SOE-PCR) at the position of VH44 and VL100 in the scFv.	Disulfides	17-26	immunglobulin heavy chain variable region	Homo sapiens	191-195
28150932-5	2017	Here, PTX was incorporated in nontoxic and endogenous material, human serum albumin (HSA), via an innovative disulfide reduction method to construct HSA-based PTX nanoparticle (HSA-PTX NP) to not only realize redox-responsive drug release but also improve in vivo stability.	Disulfides	109-118	albumin	Homo sapiens	70-83
30792886-2	2017	Doxorubicin (DOX) was loaded into HMSNs and blocked with cytochrome C conjugated lactobionic acid (CytC-LA) via redox-cleavable disulfide bonds and pH-disassociation boronate ester bonds as intermediate linkers.	Disulfides	128-137	cytochrome c, somatic	Homo sapiens	57-69
27982442-13	2017	Renal clearance of small fragments may be faster, whereas clearance of larger fragments appears to depend on their neonatal Fc receptor (FcRn) functionality, which in turn may be impeded by disulfide bond cleavage.	Disulfides	190-199	Fc gamma receptor and transporter	Homo sapiens	137-141
27876599-6	2017	RESULTS: Generated thiolated Eudragit  S100 displaying 235+-14mumol of free thiol groups and 878+-101mumol of disulfide bonds per gram polymer showed a great improvement in both: dynamic viscosity with mucus and adhesion time on mucosal tissue compared to the unmodified polymer.	Disulfides	110-119	S100 calcium binding protein A1	Homo sapiens	39-43
27977888-5	2017	Also, such an abnormal SOD1 dimer with significant structural disorder was prone to irreversibly forming the oligomers crosslinked via disulfide bonds.	Disulfides	135-144	superoxide dismutase 1, soluble	Mus musculus	23-27
27977888-6	2017	The disulfide-crosslinked oligomers of SOD1 were detected in the spinal cords of the diseased mice expressing mutant SOD1.	Disulfides	4-13	superoxide dismutase 1, soluble	Mus musculus	39-43
27977888-6	2017	The disulfide-crosslinked oligomers of SOD1 were detected in the spinal cords of the diseased mice expressing mutant SOD1.	Disulfides	4-13	superoxide dismutase 1, soluble	Mus musculus	117-121
28203238-4	2017	Although most cathelicidins possessed DNA complexing activity, only the alpha-helical BMAP cathelicidins and the cysteine-rich disulfide-bridged Bac1 were able to enhance the sensing of nucleic acids by primary epithelial cells.	Disulfides	127-136	cathelicidin-1	Bos taurus	145-149
28231771-0	2017	Novel synthetic analogues of avian beta-defensin-12: the role of charge, hydrophobicity, and disulfide bridges in biological functions.	Disulfides	93-102	defensin beta 112	Homo sapiens	35-51
28154140-5	2017	The CA10-neurexin complex is stable and stoichiometric, and results in formation of intermolecular disulfide bonds between conserved cysteine residues in neurexins and CA10.	Disulfides	99-108	carbonic anhydrase 10	Mus musculus	4-8
28154140-5	2017	The CA10-neurexin complex is stable and stoichiometric, and results in formation of intermolecular disulfide bonds between conserved cysteine residues in neurexins and CA10.	Disulfides	99-108	carbonic anhydrase 10	Mus musculus	168-172
28241453-1	2017	Some peptide-based drugs, including oxytocin, vasopressin, ziconotide, pramlintide, nesiritide, and octreotide, contain one intramolecular disulfide bond.	Disulfides	139-148	arginine vasopressin	Homo sapiens	46-57
28120612-8	2017	Catalase was immobilized on the SeNPs by the formation of disulfide bonds.	Disulfides	58-67	catalase	Homo sapiens	0-8
28120612-9	2017	Intracellular reduction of disulfide bonds induced the subsequent release of catalase, which catalyzed the decomposition of H2O2.	Disulfides	27-36	catalase	Homo sapiens	77-85
27864139-5	2017	Morning levels of overoxidized PRDX2 correlated with polysomnographic (PSG)-arousal index and metabolic parameters whereas the evening level of disulfide-linked dimer (associated with peroxidase activity of PRDX2) correlated with PSG parameters.	Disulfides	144-153	peroxiredoxin 2	Homo sapiens	207-212
28139814-6	2017	Of special importance is the sequential formation of disulfide bonds with different functions in structural support of VWF multimers, which are packaged, stored and further processed after secretion.	Disulfides	53-62	von Willebrand factor	Homo sapiens	119-122
27997792-2	2017	A sequon was tethered to an archaeal OST enzyme via a disulfide bond.	Disulfides	54-63	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	37-40
28005346-10	2017	C(10)A and C(260)A mutations suggest that these residues form a second disulfide bridge in the extracellular domain of GPR55, occluding ligand extracellular entry in the TMH1-TMH7 region of GPR55.	Disulfides	71-80	G protein-coupled receptor 55	Homo sapiens	119-124
28005346-10	2017	C(10)A and C(260)A mutations suggest that these residues form a second disulfide bridge in the extracellular domain of GPR55, occluding ligand extracellular entry in the TMH1-TMH7 region of GPR55.	Disulfides	71-80	G protein-coupled receptor 55	Homo sapiens	190-195
27064983-1	2017	The study aimed to compare the dynamic thiol/disulfide homeostasis between patients with premature ovarian failure (POF) and healthy women.	Disulfides	45-54	POF1B actin binding protein	Homo sapiens	116-119
27770625-1	2017	Previously, we have shown that flies under-expressing the two mitochondrial peroxiredoxins (Prxs), dPrx3 and dPrx5, display increases in tissue-specific apoptosis and dramatically shortened life span, associated with a redox crisis, manifested as changes in GSH:GSSG and accumulation of protein mixed disulfides.	Disulfides	301-311	Peroxiredoxin 3	Drosophila melanogaster	99-104
28188021-2	2017	Lipoprotein (a) [Lp(a)] is a lipoprotein defined by presenting a specific apolipoprotein, ApoA, linked to the ApoB-100 by different types of chemical bonds, including a disulfide bridge.	Disulfides	169-178	apolipoprotein B	Homo sapiens	110-118
28057013-2	2017	Oligomerization of SOD1 via abnormal disulfide crosslinks has been proposed as one of the misfolding pathways occurring in mutant SOD1; however, the pathological relevance of such oligomerization in the SOD1-ALS cases still remains obscure.	Disulfides	37-46	superoxide dismutase 1	Homo sapiens	19-23
28057013-2	2017	Oligomerization of SOD1 via abnormal disulfide crosslinks has been proposed as one of the misfolding pathways occurring in mutant SOD1; however, the pathological relevance of such oligomerization in the SOD1-ALS cases still remains obscure.	Disulfides	37-46	superoxide dismutase 1	Homo sapiens	130-134
28057013-2	2017	Oligomerization of SOD1 via abnormal disulfide crosslinks has been proposed as one of the misfolding pathways occurring in mutant SOD1; however, the pathological relevance of such oligomerization in the SOD1-ALS cases still remains obscure.	Disulfides	37-46	superoxide dismutase 1	Homo sapiens	130-134
28057013-3	2017	METHODS: We prepared antibodies exclusively recognizing the SOD1 oligomers cross-linked via disulfide bonds in vitro.	Disulfides	92-101	superoxide dismutase 1	Homo sapiens	60-64
28057013-5	2017	RESULTS: We showed the recognition specificity of our antibodies exclusively toward the disulfide-crosslinked SOD1 oligomers by ELISA using various forms of purified SOD1 proteins in conformationally distinct states in vitro.	Disulfides	88-97	superoxide dismutase 1	Homo sapiens	110-114
28057013-5	2017	RESULTS: We showed the recognition specificity of our antibodies exclusively toward the disulfide-crosslinked SOD1 oligomers by ELISA using various forms of purified SOD1 proteins in conformationally distinct states in vitro.	Disulfides	88-97	superoxide dismutase 1	Homo sapiens	166-170
28057013-8	2017	CONCLUSIONS: Our findings here suggest that the SOD1 oligomerization through the disulfide-crosslinking associates with exposure of the SOD1 structural interior and is a pathological process occurring in the SOD1-ALS cases.	Disulfides	81-90	superoxide dismutase 1, soluble	Mus musculus	48-52
28057013-8	2017	CONCLUSIONS: Our findings here suggest that the SOD1 oligomerization through the disulfide-crosslinking associates with exposure of the SOD1 structural interior and is a pathological process occurring in the SOD1-ALS cases.	Disulfides	81-90	superoxide dismutase 1, soluble	Mus musculus	136-140
28057013-8	2017	CONCLUSIONS: Our findings here suggest that the SOD1 oligomerization through the disulfide-crosslinking associates with exposure of the SOD1 structural interior and is a pathological process occurring in the SOD1-ALS cases.	Disulfides	81-90	superoxide dismutase 1, soluble	Mus musculus	136-140
28429674-4	2017	Lipoprotein (a), or Lp(a), is a type of low-density lipoprotein containing an integral apolipoprotein B100 (apoB100) component with an attached apolipoprotein A-1 (ApoA-1) isoform via a disulfide linkage.	Disulfides	186-195	apolipoprotein A1	Homo sapiens	164-170
27064983-7	2017	This is the first study demonstrating the thiol/disulfide homeostasis in women with POF and may help us understanding the pathophysiology.	Disulfides	48-57	POF1B actin binding protein	Homo sapiens	84-87
27719550-5	2017	The release of insulin from the nanoparticles slowed down because of the presence of disulfide bonds and increased with increasing glucose level in the medium.	Disulfides	85-94	insulin	Homo sapiens	15-22
29036827-2	2017	We have developed a non-invasive diagnosis tool based on magnetic resonance molecular imaging (MRMI) of amyloid-beta peptide using ultra-small particles of iron oxide (USPIO) functionalized with a disulfide constrained cyclic heptapeptide (PHO) identified by phage display (USPIO-PHO).	Disulfides	197-206	amyloid beta precursor protein	Homo sapiens	104-116
27511456-3	2016	The iAGT conformation exists as oxidized AGT (oxi-AGT) and reduced AGT (red-AGT) in a disulfide bond, and oxi-AGT has a higher affinity for renin, which may exacerbate RAS-associated diseases.	Disulfides	86-95	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	5-8
26629743-0	2016	Distinct structural changes in wild-type and amyloidogenic chicken cystatin caused by disruption of C95-C115 disulfide bond.	Disulfides	109-118	cystatin C	Gallus gallus	67-75
27470143-5	2016	Particularly, a C-terminal engineering to confer an interchain disulfide bond appeared to be able to enhance its heterodimeric integrity and EGFR-binding activity.	Disulfides	63-72	epidermal growth factor receptor	Homo sapiens	141-145
26629743-4	2016	In this study, we used molecular dynamics simulations to assess the importance of disulfide bridge formation upon the stability of chicken cystatin and how this may influence the propensity for amyloid formation.	Disulfides	82-91	cystatin C	Gallus gallus	139-147
26629743-5	2016	We found that disulfide bridge formation between Cys95 and Cys115 in human cystatin played a critical role in overall protein stability.	Disulfides	14-23	cystatin C	Gallus gallus	75-83
26629743-7	2016	We hypothesized that correct disulfide bridge formation is a critical step in stabilizing cystatin toward its native conformation.	Disulfides	29-38	cystatin C	Gallus gallus	90-98
26629743-8	2016	Disrupting Cys95-Cys115 disulfide bridge formation within cystatin appears to significantly enhance the amyloidogenic properties of this protein.	Disulfides	24-33	cystatin C	Gallus gallus	58-66
27748778-3	2016	Recently, we developed a cationic dextran nanogel in which a model antigen (ovalbumin, OVA) is reversibly conjugated via disulfide bonds to the nanogel network to enable redox-sensitive intracellular release.	Disulfides	121-130	serine (or cysteine) peptidase inhibitor, clade B, member 1, pseudogene	Mus musculus	76-85
27742562-0	2016	Soluble expression of disulfide-bonded C-type lectin like domain of human CD93 in the cytoplasm of Escherichia coli.	Disulfides	22-31	CD93 molecule	Homo sapiens	74-78
27742562-4	2016	In order to address further functional and structural analyses, we expressed human CD93 CTLD with several disulfide bonds in an E. coli expression system.	Disulfides	106-115	CD93 molecule	Homo sapiens	83-87
27062681-4	2016	From high-performance liquid chromatography spectra, we observed that one uremic solute binds to HD-ALB via the formation of disulfide bonds between HD-ALB and the uremic solute.	Disulfides	125-134	albumin	Homo sapiens	100-103
27867347-9	2016	We next utilized mass spectrometry to interrogate the structural consequences of metal loss and disulfide reduction on fALS-associated SOD1 variant structure.	Disulfides	96-105	superoxide dismutase 1	Homo sapiens	135-139
27574188-7	2016	Moreover, disulfide HMGB1 facilitates formation of prothrombotic neutrophil extracellular traps (NETs) mediated by RAGE, exposing additional HMGB1 on their extracellular DNA strands.	Disulfides	10-19	advanced glycosylation end product-specific receptor	Mus musculus	115-119
27685835-0	2016	The extreme hyper-reactivity of selected cysteines drives hierarchical disulfide bond formation in serum albumin.	Disulfides	71-80	albumin	Homo sapiens	99-112
27900366-4	2016	Exome sequencing revealed a germline heterozygous EGFR mutation that breaks a disulfide bond in the receptor"s extracellular domain, resulting in constitutive activation.	Disulfides	78-87	epidermal growth factor receptor	Homo sapiens	50-54
27685835-1	2016	After mild reduction of serum albumin, seven among the 34 cysteines forming the disulfide network displayed a surprising hyper-reactivity.	Disulfides	80-89	albumin	Homo sapiens	24-37
27642162-4	2016	Our data reveal that ERp44 binds the oxidized form of peroxiredoxin 4 via thiol-disulfide interchange reactions.	Disulfides	80-89	endoplasmic reticulum protein 44	Homo sapiens	21-26
27575053-19	2016	The Cys362-Cys482 disulfide bond is involved in enhancing FXI activation following its reduction, possibly by increasing thrombin accessibility to FXI.	Disulfides	18-27	coagulation factor II, thrombin	Homo sapiens	121-129
27569046-5	2016	The p24beta1 and p24delta1 GOLD domains share a common beta-sandwich fold with a characteristic intrasheet disulfide bond.	Disulfides	107-116	transmembrane p24 trafficking protein 2	Homo sapiens	4-12
27810970-5	2016	The cleavage of Mst77F is very similar to the processing of protamine P2 during human spermiogenesis and notably leaves the cysteine residues in the mature protein intact, suggesting that they participate in the formation of disulfide cross-links.	Disulfides	225-234	Male-specific transcript 77F	Drosophila melanogaster	16-22
27459325-4	2016	The ROSE system condensing tumor suppressor microRNA-34a (miR-34a) therapeutics becomes ROSE/miR-34a nanoparticles that could facilitate gene transfection in HCC cells with satisfied stability and efficiency, possibly due to proton sponge effect by polycations, PEGlyation protection, and controlled release by breakdown of disulfide bonds.	Disulfides	324-333	microRNA 34a	Mus musculus	44-56
27459325-4	2016	The ROSE system condensing tumor suppressor microRNA-34a (miR-34a) therapeutics becomes ROSE/miR-34a nanoparticles that could facilitate gene transfection in HCC cells with satisfied stability and efficiency, possibly due to proton sponge effect by polycations, PEGlyation protection, and controlled release by breakdown of disulfide bonds.	Disulfides	324-333	microRNA 34a	Mus musculus	58-65
27486258-0	2016	Intermolecular disulfide bond influences unphosphorylated STAT3 dimerization and function.	Disulfides	15-24	signal transducer and activator of transcription 3	Homo sapiens	58-63
27459325-4	2016	The ROSE system condensing tumor suppressor microRNA-34a (miR-34a) therapeutics becomes ROSE/miR-34a nanoparticles that could facilitate gene transfection in HCC cells with satisfied stability and efficiency, possibly due to proton sponge effect by polycations, PEGlyation protection, and controlled release by breakdown of disulfide bonds.	Disulfides	324-333	microRNA 34a	Mus musculus	93-100
27486258-4	2016	Although many reports describe the active role of U-STAT3 in oncogenesis in addition to phosphorylated STAT3, the U-STAT3 functional pathway remains elusive.In this report, we describe the molecular mechanism of U-STAT3 dimerization, and we identify the presence of two intermolecular disulfide bridges between Cys367 and Cys542 and Cys418 and Cys426, respectively.	Disulfides	285-294	signal transducer and activator of transcription 3	Homo sapiens	52-57
27480846-4	2016	Proteomics analysis showed that UNG1 bound to eight proteins in the mitochondria, including PAPSS2, CD70 antigen, and AGR2 under normal growth conditions, whereas UNG1 mainly bound to Peroxiredoxin 3 (PRDX3) via a disulfide linkage under oxidative stress.	Disulfides	214-223	uracil DNA glycosylase	Homo sapiens	32-36
27486258-5	2016	Recently, we reported that the same cysteines contribute to the redox regulation of STAT3 signaling pathway both in vitro and in vivo The presence of these disulfides is here demonstrated to largely contribute to the structure and the stability of U-STAT3 dimer as the dimeric form rapidly dissociates upon reduction in the S-S bonds.	Disulfides	156-166	signal transducer and activator of transcription 3	Homo sapiens	84-89
27486258-5	2016	Recently, we reported that the same cysteines contribute to the redox regulation of STAT3 signaling pathway both in vitro and in vivo The presence of these disulfides is here demonstrated to largely contribute to the structure and the stability of U-STAT3 dimer as the dimeric form rapidly dissociates upon reduction in the S-S bonds.	Disulfides	156-166	signal transducer and activator of transcription 3	Homo sapiens	250-255
27486258-6	2016	In particular, the Cys367-Cys542 disulfide bridge is shown to be critical for U-STAT3 DNA-binding activity.	Disulfides	33-42	signal transducer and activator of transcription 3	Homo sapiens	80-85
27486258-9	2016	Finally, we propose a reaction scheme of U-STAT3 dimerization with a first common step followed by stabilization through the formation of interchain disulfide bonds.	Disulfides	149-158	signal transducer and activator of transcription 3	Homo sapiens	43-48
27629822-8	2016	Remarkably, yeast naturally contains Thr-Ser variants (Tsa1 and Tsa2, respectively) with distinct oligomeric stabilities in their disulfide states.	Disulfides	130-139	thioredoxin peroxidase TSA2	Saccharomyces cerevisiae S288C	64-68
27766215-1	2016	Human serum albumin (HSA) is a non-glycosylated, negatively charged protein (Mw: about 65-kDa) that has one free cystein residue (Cys 34), and 17 disulfide bridges that these bridges have main role in its stability and longer biological life-time (15 to 19 days).	Disulfides	146-155	albumin	Homo sapiens	6-19
27343352-6	2016	After the loose of its partner in Bbeta-chain, the gammaCys135 was probably disulfide-bridged to its corresponding Cys residue of another abnormal fibrinogen molecule, forming dimmer with an abnormal electrophoretic profile.	Disulfides	76-85	fibrinogen beta chain	Homo sapiens	147-157
27233453-9	2016	CONCLUSIONS: Changes in the extracellular redox environment, potentially mediated by allosteric consequences of functional disulfide bond oxidoreduction, may represent a signal for translocation of CD4 into DRM clusters, and this sequestration, another potential mechanism by which the anti-HIV effects of cell surface oxidoreductase inhibition are exerted.	Disulfides	123-132	CD4 molecule	Homo sapiens	198-201
27378311-7	2016	We obtained atomic-resolution evidence that the nascent WT SOD1 without metalation and disulfide bridge is also highly disordered as L126Z.	Disulfides	87-96	superoxide dismutase 1	Homo sapiens	59-63
27583304-9	2016	The mutated cysteine 143 forms a disulfide bridge, which is 100% conserved in NEP and in similar enzymes.	Disulfides	33-42	membrane metalloendopeptidase	Homo sapiens	78-81
27566173-3	2016	We explored the disulfide conformational isomerization of the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor (BPTI), by performing an NMR line-shape analysis of its Cys carbon peaks.	Disulfides	16-25	trophoblast Kunitz domain protein 1	Bos taurus	110-127
27566173-3	2016	We explored the disulfide conformational isomerization of the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor (BPTI), by performing an NMR line-shape analysis of its Cys carbon peaks.	Disulfides	74-83	trophoblast Kunitz domain protein 1	Bos taurus	110-127
32263467-4	2016	Inorganic pyrophosphatase (PPase) was conjugated through a one-step thiol-disulfide exchange reaction with a series of well-defined and molecular weight-controlled glycopolymers, poly(2-methacrylamido glucopyranose) (PMAG), prepared via reversible addition-fragmentation chain transfer (RAFT) polymerization.	Disulfides	74-83	inorganic pyrophosphatase 1	Homo sapiens	0-25
32263467-4	2016	Inorganic pyrophosphatase (PPase) was conjugated through a one-step thiol-disulfide exchange reaction with a series of well-defined and molecular weight-controlled glycopolymers, poly(2-methacrylamido glucopyranose) (PMAG), prepared via reversible addition-fragmentation chain transfer (RAFT) polymerization.	Disulfides	74-83	inorganic pyrophosphatase 1	Homo sapiens	27-32
27210512-4	2016	The Clit-Def mature peptide has the features to be involved in the antimicrobial function: a predicted cationic isoelectric point of 8.94, six cysteine residues that form three disulfide bonds, and the typical cysteine-stabilized alpha-helix beta-sheet (CSalphabeta) structural fold.	Disulfides	177-186	peptide deformylase	Escherichia coli	9-12
27495374-10	2016	Importantly, we have discovered that a class of compounds termed Disulfide bond Disrupting Agents (DDAs) blocks CDCP1/EGFR/Src ternary complex formation and downstream signaling.	Disulfides	65-74	epidermal growth factor receptor	Homo sapiens	118-122
27556028-4	2016	Recently, we have reproduced the formation of SOD1 oligomers abnormally cross-linked via disulfide bonds in a test tube.	Disulfides	89-98	superoxide dismutase 1	Homo sapiens	46-50
27261461-2	2016	Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols.	Disulfides	146-155	superoxide dismutase 1	Homo sapiens	6-10
27261461-2	2016	Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols.	Disulfides	146-155	superoxide dismutase 1	Homo sapiens	12-17
27495374-10	2016	Importantly, we have discovered that a class of compounds termed Disulfide bond Disrupting Agents (DDAs) blocks CDCP1/EGFR/Src ternary complex formation and downstream signaling.	Disulfides	65-74	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	123-126
27223606-5	2016	Nanobioconjugates made of low molecular weight polyethylenimine (LMW-PEI) and transferrin (Tf) were synthesized to contain a bioreducible disulfide bond.	Disulfides	138-147	transferrin	Homo sapiens	78-89
27432987-4	2016	AtSAL1 phosphatase activity is suppressed by dimerization, intramolecular disulfide formation, and glutathionylation, allowing accumulation of its substrate, PAP, a chloroplast stress retrograde signal that regulates expression of plastid redox associated nuclear genes (PRANGs).	Disulfides	74-83	SAL1 phosphatase-like protein	Arabidopsis thaliana	0-6
27251178-0	2016	Construction of a disulfide-stabilized diabody against fibroblast growth factor-2 and the inhibition activity in targeting breast cancer.	Disulfides	18-27	fibroblast growth factor 2	Homo sapiens	55-81
27251178-3	2016	In this study, a disulfide-stabilized diabody (ds-Diabody) that specifically targets FGF-2 was designed.	Disulfides	17-26	fibroblast growth factor 2	Homo sapiens	85-90
27374339-4	2016	Here we report the crystal structure of Izumo1, which reveals a membrane distal region composed of a four-helix bundle connected to a carboxy-terminal immunoglobulin (Ig)-like domain through a beta-hairpin stabilized by disulfide bonds.	Disulfides	220-229	izumo sperm-egg fusion 1	Homo sapiens	40-46
27226537-0	2016	Role of Conserved Disulfide Bridges and Aromatic Residues in Extracellular Loop 2 of Chemokine Receptor CCR8 for Chemokine and Small Molecule Binding.	Disulfides	18-27	C-C motif chemokine receptor 8	Homo sapiens	104-108
27226537-3	2016	Here we investigate the importance of conserved extracellular disulfide bridges and aromatic residues in extracellular loop 2 (ECL-2) for ligand binding and activation in the chemokine receptor CCR8.	Disulfides	62-71	C-C motif chemokine receptor 8	Homo sapiens	194-198
27467220-0	2016	Disulfide-Trapping Identifies a New, Effective Chemical Probe for Activating the Nuclear Receptor Human LRH-1 (NR5A2).	Disulfides	0-9	nuclear receptor subfamily 5 group A member 2	Homo sapiens	104-109
27467220-0	2016	Disulfide-Trapping Identifies a New, Effective Chemical Probe for Activating the Nuclear Receptor Human LRH-1 (NR5A2).	Disulfides	0-9	nuclear receptor subfamily 5 group A member 2	Homo sapiens	111-116
27467220-2	2016	Here, we investigated whether disulfide-trapping, an approach new to nuclear receptors, would provide effective lead compounds targeting human liver receptor homolog 1 (hLRH-1, NR5A2).	Disulfides	30-39	nuclear receptor subfamily 5 group A member 2	Homo sapiens	169-175
27467220-2	2016	Here, we investigated whether disulfide-trapping, an approach new to nuclear receptors, would provide effective lead compounds targeting human liver receptor homolog 1 (hLRH-1, NR5A2).	Disulfides	30-39	nuclear receptor subfamily 5 group A member 2	Homo sapiens	177-182
27467220-4	2016	Using disulfide-trapping, we identified a lead compound that conjugates with remarkably high-efficiency to a native cysteine residue (Cys346) lining the hydrophobic cavity in the ligand binding domain of hLRH-1.	Disulfides	6-15	nuclear receptor subfamily 5 group A member 2	Homo sapiens	204-210
27393305-5	2016	Here, we directly imaged GroEL-GroES interaction in the presence of disulfide-reduced alpha-lactalbumin as a substrate protein using high-speed atomic force microscopy.	Disulfides	68-77	lactalbumin alpha	Homo sapiens	86-103
27251465-1	2016	Cooperative cascade catalysis by bovine serum albumin (BSA)-iodine allows for the first time the performance of C(sp(2))-H sulfenylation of indole from readily available thiophenol (-SH bond) via in situ generation/cleavage of disulfide (S-S bond) in air under aqueous conditions, whereas BSA or I2 individually do not permit this two step sequence to occur in the same pot towards C-S bond formation.	Disulfides	227-236	albumin	Homo sapiens	40-53
27463727-7	2016	The most active of these, SS1-Fab-DS3-PE24, shows a longer serum half-life than an RIT without the disulfide bond and has the same anti-tumor activity, despite being less cytotoxic in vitro.	Disulfides	99-108	major histocompatibility complex, class II, DR beta 1	Homo sapiens	26-29
26860867-5	2016	Our results suggest that some of these sulfur containing pyrimidines interact with redoxactive -SH groups required for successful HIV entry, including a redox active disulfide in the CD4 molecule as well as -SH groups in HIV viral envelope gp120.	Disulfides	166-175	CD4 molecule	Homo sapiens	183-186
27414797-3	2016	A fully active recombinant FGF2 retaining a unique exposed cysteine (Cys) residue was chemically conjugated with an engineered NanoLuc carrying a unique exposed Cys residue at the C-terminus via formation of an intermolecular disulfide linkage.	Disulfides	226-235	fibroblast growth factor 2	Homo sapiens	27-31
27259101-1	2016	Human insulin-like peptide-6 (INSL-6) belongs to the insulin superfamily and shares the distinctive disulfide bond configuration of human insulin.	Disulfides	100-109	insulin	Homo sapiens	6-13
27259101-1	2016	Human insulin-like peptide-6 (INSL-6) belongs to the insulin superfamily and shares the distinctive disulfide bond configuration of human insulin.	Disulfides	100-109	insulin	Homo sapiens	53-60
27091403-4	2016	A population of Cox26 was observed to exist in a disulfide bond partnership with the Cox2 subunit of complex IV.	Disulfides	49-58	cytochrome c oxidase subunit 2	Saccharomyces cerevisiae S288C	16-20
27578123-8	2016	The substitution of a cysteine residue in the Ly6 domain of GPIHBP1 is predicted to abolish one of the disulfide bridges required to maintain the structure of GPIHBP1.	Disulfides	103-112	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	60-67
27578123-8	2016	The substitution of a cysteine residue in the Ly6 domain of GPIHBP1 is predicted to abolish one of the disulfide bridges required to maintain the structure of GPIHBP1.	Disulfides	103-112	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	159-166
27309808-5	2016	IZUMO1 exhibits an elongated rod-shaped structure comprised of a helical bundle IZUMO domain and an immunoglobulin-like domain that are each firmly anchored to an intervening beta-hairpin region through conserved disulfide bonds.	Disulfides	213-222	izumo sperm-egg fusion 1	Homo sapiens	0-6
26928883-4	2016	The aim of this study was to investigate thiol levels and thiol/disulfide homeostasis in CSX patients.	Disulfides	64-73	NK2 homeobox 5	Homo sapiens	89-92
27031930-9	2016	Due to the cleavage of disulfide bonds triggered by the high-content GSH in cytoplasm, the complexes would be degraded and released p53 for co-therapy to improve antitumor efficacy.	Disulfides	23-32	tumor protein p53	Homo sapiens	132-135
27129265-5	2016	Increased sensitivity of anionic trypsinogen to CTRC-mediated degradation was due to an additional cleavage site at Leu-148 in the autolysis loop and the lack of the conserved Cys-139-Cys-206 disulfide bond.	Disulfides	192-201	serine protease 2	Homo sapiens	25-44
27129265-6	2016	Significant stabilization of anionic trypsinogen against degradation was achieved by simultaneous mutations of CTRC cleavage sites Leu-81 and Leu-148, autolytic cleavage site Arg-122, and restoration of the missing disulfide bridge.	Disulfides	215-224	serine protease 2	Homo sapiens	29-48
26928883-8	2016	Serum total thiol, native thiol, and disulfide levels decreased significantly in the CSX group compared with the control group (P&lt;0.001).	Disulfides	37-46	NK2 homeobox 5	Homo sapiens	85-88
26887678-0	2016	Thiol-Disulfide Exchange in Human Growth Hormone.	Disulfides	6-15	growth hormone 1	Homo sapiens	34-48
26928883-10	2016	Although disulfide/native thiol levels increased in the CSX group, this reduction did not reach statistical significance (5.8 vs. 5.5, P&gt;0.05).	Disulfides	9-18	NK2 homeobox 5	Homo sapiens	56-59
27107845-8	2016	IFN-gamma treatment resulted in striking increases in the expression of disulfide-linked HLA-B27 heavy chains, even in cells with normal ERAP1 expression.	Disulfides	72-81	interferon gamma	Homo sapiens	0-9
26887678-1	2016	PURPOSE: Thiol-disulfide exchange was monitored in recombinant human growth hormone (hGH) and in model tryptic peptides derived from hGH to investigate the effects of higher-order structure on the reaction.	Disulfides	15-24	growth hormone 1	Homo sapiens	69-83
27041594-3	2016	Through structure-based design, we developed ID2, which consists of the ID expressed independently of the outer domain and stabilized in the CD4-bound conformation by an inter-layer disulfide bond.	Disulfides	182-191	CD4 molecule	Homo sapiens	141-144
26826314-2	2016	Here, two by-products of disulfide-linked oligomers and disulfide-isomerized monomers were clearly identified during proinsulin aspart"s refolding through multiple analytic methods.	Disulfides	25-34	insulin	Homo sapiens	117-127
26826314-2	2016	Here, two by-products of disulfide-linked oligomers and disulfide-isomerized monomers were clearly identified during proinsulin aspart"s refolding through multiple analytic methods.	Disulfides	56-65	insulin	Homo sapiens	117-127
27194337-0	2016	Death Domain Signaling by Disulfide-Linked Dimers of the p75 Neurotrophin Receptor Mediates Neuronal Death in the CNS.	Disulfides	26-35	nerve growth factor receptor (TNFR superfamily, member 16)	Mus musculus	57-82
27194337-9	2016	We conclude that, both in vitro and in vivo, neuronal death induced by p75(NTR) requires the DD and TM Cys(259), supporting the physiological relevance of DD signaling by disulfide-linked dimers of p75(NTR) in the CNS.	Disulfides	171-180	nerve growth factor receptor (TNFR superfamily, member 16)	Mus musculus	71-74
27194337-9	2016	We conclude that, both in vitro and in vivo, neuronal death induced by p75(NTR) requires the DD and TM Cys(259), supporting the physiological relevance of DD signaling by disulfide-linked dimers of p75(NTR) in the CNS.	Disulfides	171-180	nerve growth factor receptor (TNFR superfamily, member 16)	Mus musculus	75-78
27194337-9	2016	We conclude that, both in vitro and in vivo, neuronal death induced by p75(NTR) requires the DD and TM Cys(259), supporting the physiological relevance of DD signaling by disulfide-linked dimers of p75(NTR) in the CNS.	Disulfides	171-180	nerve growth factor receptor (TNFR superfamily, member 16)	Mus musculus	198-201
27194337-13	2016	Our results indicate a requirement for DD signaling by disulfide-linked dimers of p75(NTR) for neuronal death induced by proneurotrophins and epileptic seizures.	Disulfides	55-64	nerve growth factor receptor (TNFR superfamily, member 16)	Mus musculus	82-90
26945066-0	2016	Oxidant-induced Interprotein Disulfide Formation in Cardiac Protein DJ-1 Occurs via an Interaction with Peroxiredoxin 2.	Disulfides	29-38	peroxiredoxin 2	Homo sapiens	104-119
26826314-7	2016	Moreover, it was demonstrated that not redox pairs but only oxidant was necessary to facilitate the native disulfide bonds formation for the reduced denatured proinsulin.	Disulfides	107-116	insulin	Homo sapiens	159-169
27086995-1	2016	Disulfide bond shuffling in the presence of the reducing agents dithiothreitol (DTT) or beta-mercaptoethanol (BME) strongly affects the surface properties of lysozyme solutions.	Disulfides	0-9	lysozyme	Homo sapiens	158-166
27137918-0	2016	The Human Sodium-Glucose Cotransporter (hSGLT1) Is a Disulfide-Bridged Homodimer with a Re-Entrant C-Terminal Loop.	Disulfides	53-62	solute carrier family 5 member 1	Homo sapiens	40-46
27137918-9	2016	A systematic mutational study of endogenous cysteine residues in hSGLT1 showed that a disulfide bridge is formed between the C355 residues of two neighbouring hSGLT1 molecules.	Disulfides	86-95	solute carrier family 5 member 1	Homo sapiens	65-71
27137918-9	2016	A systematic mutational study of endogenous cysteine residues in hSGLT1 showed that a disulfide bridge is formed between the C355 residues of two neighbouring hSGLT1 molecules.	Disulfides	86-95	solute carrier family 5 member 1	Homo sapiens	159-165
27137918-10	2016	It is concluded that, 1) hSGLT1 is expressed as a disulfide bridged homodimer via C355 and that 2) a portion of the intracellular 12-13 loop is re-entrant and readily accessible from the extracellular milieu.	Disulfides	50-59	solute carrier family 5 member 1	Homo sapiens	25-31
26910514-2	2016	This review highlights milestones in the chemical synthesis of insulin that can be divided into two separate approaches: (i) disulfide bond formation driven by protein folding and (ii) chemical reactivity-directed sequential disulfide bond formation.	Disulfides	125-134	insulin	Homo sapiens	63-70
26910514-2	2016	This review highlights milestones in the chemical synthesis of insulin that can be divided into two separate approaches: (i) disulfide bond formation driven by protein folding and (ii) chemical reactivity-directed sequential disulfide bond formation.	Disulfides	225-234	insulin	Homo sapiens	63-70
27114880-2	2016	Bovine odorant-binding protein (bOBP) differs from other lipocalins by lacking the conserved disulfide bond and for being able to form the domain-swapped dimers.	Disulfides	93-102	odorant-binding protein	Bos taurus	7-30
26725377-11	2016	Conclusion PDI-sAb is a sensitive and real-time reporter of platelet- and vascular-derived disulfide reduction that targets clots as they form under flow to reveal spatial gradients.	Disulfides	91-100	protein disulfide isomerase family A member 2	Homo sapiens	11-14
26725377-11	2016	Conclusion PDI-sAb is a sensitive and real-time reporter of platelet- and vascular-derived disulfide reduction that targets clots as they form under flow to reveal spatial gradients.	Disulfides	91-100	SH3 domain binding protein 5	Homo sapiens	15-18
26957645-2	2016	All seven Grns (A-G) contain 12 conserved cysteines that form 6 intramolecular disulfide bonds, rendering this family of proteins unique.	Disulfides	79-88	granulin precursor	Homo sapiens	10-14
26957645-10	2016	Collectively, the presented data establish that the intrinsic disorder of rGrnB governs conformational dynamics within the reduced form of the protein, and suggest that the overall structure of Grns could be entirely dictated by disulfide bonds.	Disulfides	229-238	granulin precursor	Homo sapiens	194-198
32263341-0	2016	Disulfide-crosslinked albumin hydrogels.	Disulfides	0-9	albumin	Homo sapiens	22-29
32263341-2	2016	In this study, we obtained disulfide-crosslinked albumin hydrogels using the protein"s own thiol groups.	Disulfides	27-36	albumin	Homo sapiens	49-56
32263341-3	2016	In the water solutions with denaturants such as urea and guanidinium, the disulfide-crosslinked albumin hydrogels showed a normal swelling profile.	Disulfides	74-83	albumin	Homo sapiens	96-103
26808719-5	2016	The ligands 1 and 2 are based on the pharmacophore of the nonpeptidic NTS1 antagonist SR142948A, allowing the formation of a disulfide bond to an engineered cysteine residue of NTS1.	Disulfides	125-134	neurotensin	Homo sapiens	70-74
26808719-5	2016	The ligands 1 and 2 are based on the pharmacophore of the nonpeptidic NTS1 antagonist SR142948A, allowing the formation of a disulfide bond to an engineered cysteine residue of NTS1.	Disulfides	125-134	neurotensin	Homo sapiens	177-181
27009680-0	2016	Human CD4 Metastability Is a Function of the Allosteric Disulfide Bond in Domain 2.	Disulfides	56-65	CD4 molecule	Homo sapiens	6-9
27009680-2	2016	CD4 has four ecto-domains (D1-D4) of which D1, D2, and D4 contain disulfide bonds.	Disulfides	66-75	CD4 molecule	Homo sapiens	0-3
27009680-4	2016	D2 of CD4 possesses one such "allosteric" disulfide.	Disulfides	42-51	CD4 molecule	Homo sapiens	6-9
27009680-5	2016	While it is becoming accepted that redox exchange of the D2 allosteric disulfide plays an essential role in regulating CD4 activity, the biophysical consequences of its reduction remain incompletely understood.	Disulfides	71-80	CD4 molecule	Homo sapiens	119-122
27009680-7	2016	Conversely, ablating the structural disulfide of D1 results in destabilizing structural rearrangements in CD4.	Disulfides	36-45	CD4 molecule	Homo sapiens	106-109
27009680-8	2016	These findings expand our understanding of the mechanisms by which oxidoreduction of the D2 allosteric disulfide regulates CD4 function; they reveal the intrinsic disulfide-dependent metastability of D2 and illustrate that redox shuffling of the allosteric disulfide results in previously undescribed conformational changes in CD4 that are likely important for its interaction with its protein partners.	Disulfides	103-112	CD4 molecule	Homo sapiens	123-126
27009680-8	2016	These findings expand our understanding of the mechanisms by which oxidoreduction of the D2 allosteric disulfide regulates CD4 function; they reveal the intrinsic disulfide-dependent metastability of D2 and illustrate that redox shuffling of the allosteric disulfide results in previously undescribed conformational changes in CD4 that are likely important for its interaction with its protein partners.	Disulfides	103-112	CD4 molecule	Homo sapiens	327-330
27009680-8	2016	These findings expand our understanding of the mechanisms by which oxidoreduction of the D2 allosteric disulfide regulates CD4 function; they reveal the intrinsic disulfide-dependent metastability of D2 and illustrate that redox shuffling of the allosteric disulfide results in previously undescribed conformational changes in CD4 that are likely important for its interaction with its protein partners.	Disulfides	163-172	CD4 molecule	Homo sapiens	123-126
27009680-8	2016	These findings expand our understanding of the mechanisms by which oxidoreduction of the D2 allosteric disulfide regulates CD4 function; they reveal the intrinsic disulfide-dependent metastability of D2 and illustrate that redox shuffling of the allosteric disulfide results in previously undescribed conformational changes in CD4 that are likely important for its interaction with its protein partners.	Disulfides	163-172	CD4 molecule	Homo sapiens	123-126
26661035-5	2016	Three variants of human INSL5 were prepared using solid phase peptide synthesis and subsequent sequential regioselective disulfide bond formation.	Disulfides	121-130	insulin like 5	Homo sapiens	24-29
27068954-6	2016	This involves the direct reduction of disulfides within ER Ca(2+)handling proteins themselves, but also the regulated interaction of ER chaperones and oxidoreductases such as calnexin or ERp57 with them.	Disulfides	38-48	protein disulfide isomerase family A member 3	Homo sapiens	187-192
26846856-1	2016	The formation of disulfide bonds in the endoplasmic reticulum (ER) of eukaryotic cells is catalyzed by the sulfhydryl oxidase, ER oxidoreductin 1 (Ero1), and protein-disulfide isomerase (PDI).	Disulfides	17-26	ER oxidoreductin	Saccharomyces cerevisiae S288C	147-151
26846856-2	2016	PDI is oxidized by Ero1 to continuously introduce disulfides into substrates, and feedback regulates Ero1 activity by manipulating the regulatory disulfides of Ero1.	Disulfides	50-60	ER oxidoreductin	Saccharomyces cerevisiae S288C	19-23
26846856-2	2016	PDI is oxidized by Ero1 to continuously introduce disulfides into substrates, and feedback regulates Ero1 activity by manipulating the regulatory disulfides of Ero1.	Disulfides	146-156	ER oxidoreductin	Saccharomyces cerevisiae S288C	101-105
26846856-2	2016	PDI is oxidized by Ero1 to continuously introduce disulfides into substrates, and feedback regulates Ero1 activity by manipulating the regulatory disulfides of Ero1.	Disulfides	146-156	ER oxidoreductin	Saccharomyces cerevisiae S288C	101-105
26846856-3	2016	In this study we find that yeast Ero1p is enzymatically active even with its regulatory disulfides intact, and further activation of Ero1p by reduction of the regulatory disulfides requires the reduction of non-catalytic Cys(90)-Cys(97)disulfide in Pdi1p.	Disulfides	88-98	ER oxidoreductin	Saccharomyces cerevisiae S288C	33-38
26846856-3	2016	In this study we find that yeast Ero1p is enzymatically active even with its regulatory disulfides intact, and further activation of Ero1p by reduction of the regulatory disulfides requires the reduction of non-catalytic Cys(90)-Cys(97)disulfide in Pdi1p.	Disulfides	170-180	ER oxidoreductin	Saccharomyces cerevisiae S288C	33-38
26846856-3	2016	In this study we find that yeast Ero1p is enzymatically active even with its regulatory disulfides intact, and further activation of Ero1p by reduction of the regulatory disulfides requires the reduction of non-catalytic Cys(90)-Cys(97)disulfide in Pdi1p.	Disulfides	170-180	ER oxidoreductin	Saccharomyces cerevisiae S288C	133-138
26846856-3	2016	In this study we find that yeast Ero1p is enzymatically active even with its regulatory disulfides intact, and further activation of Ero1p by reduction of the regulatory disulfides requires the reduction of non-catalytic Cys(90)-Cys(97)disulfide in Pdi1p.	Disulfides	88-97	ER oxidoreductin	Saccharomyces cerevisiae S288C	33-38
26846856-4	2016	The principal client-binding site in the Pdi1pb" domain is necessary not only for the functional Ero1p-Pdi1p disulfide relay but also for the activation of Ero1p.	Disulfides	109-118	ER oxidoreductin	Saccharomyces cerevisiae S288C	97-102
26846856-4	2016	The principal client-binding site in the Pdi1pb" domain is necessary not only for the functional Ero1p-Pdi1p disulfide relay but also for the activation of Ero1p.	Disulfides	109-118	ER oxidoreductin	Saccharomyces cerevisiae S288C	156-161
26846856-5	2016	We also demonstrate by complementary activation assays that the regulatory disulfides in Ero1p are much more stable than those in human Ero1alpha.	Disulfides	75-85	ER oxidoreductin	Saccharomyces cerevisiae S288C	89-94
27054568-5	2016	Prerequisites postulated for physiological GARP function include membrane anchorage of GARP, disulfide bridges between the propeptide of TGFbeta and GARP and connection of this propeptide to alphavbeta6 or alphavbeta8 integrins of target cells during mechanical TGFbeta release.	Disulfides	93-102	transforming growth factor beta 1	Homo sapiens	137-144
27054568-8	2016	Surprisingly, soluble GARP and TGFbeta formed stable non-covalent complexes in addition to disulfide-coupled complexes, depending on the redox conditions of the microenvironment.	Disulfides	91-100	transforming growth factor beta 1	Homo sapiens	31-38
26407855-9	2016	In this study, we show that TNF-alpha impairs adiponectin multimerization and consequently decreases adiponectin secretion by altering disulfide bond modification in the endoplasmic reticulum.	Disulfides	135-144	tumor necrosis factor	Homo sapiens	28-37
26780347-6	2016	Moreover, we have reported that three kinds of oxidative stress, ultraviolet light-induced stress, osmotic stress and arsenic-induced stress, modulate kinase activity of RET-PTC1 without an extracellular domain as well as c-RET by conformational change of RET protein (dimerization) via disulfide bond formation.	Disulfides	287-296	patched 1	Homo sapiens	174-178
26780347-6	2016	Moreover, we have reported that three kinds of oxidative stress, ultraviolet light-induced stress, osmotic stress and arsenic-induced stress, modulate kinase activity of RET-PTC1 without an extracellular domain as well as c-RET by conformational change of RET protein (dimerization) via disulfide bond formation.	Disulfides	287-296	PYD and CARD domain containing	Homo sapiens	219-223
26822090-0	2016	Disulfide Mispairing During Proinsulin Folding in the Endoplasmic Reticulum.	Disulfides	0-9	insulin	Homo sapiens	28-38
26822090-1	2016	Proinsulin folding within the endoplasmic reticulum (ER) remains incompletely understood, but it is clear that in mutant INS gene-induced diabetes of youth (MIDY), progression of the (three) native disulfide bonds of proinsulin becomes derailed, causing insulin deficiency, beta-cell ER stress, and onset of diabetes.	Disulfides	198-207	insulin	Homo sapiens	217-227
26822090-2	2016	Herein, we have undertaken a molecular dissection of proinsulin disulfide bond formation, using bioengineered proinsulins that can form only two (or even only one) of the native proinsulin disulfide bonds.	Disulfides	64-73	insulin	Homo sapiens	53-63
26822090-2	2016	Herein, we have undertaken a molecular dissection of proinsulin disulfide bond formation, using bioengineered proinsulins that can form only two (or even only one) of the native proinsulin disulfide bonds.	Disulfides	64-73	insulin	Homo sapiens	110-120
26822090-2	2016	Herein, we have undertaken a molecular dissection of proinsulin disulfide bond formation, using bioengineered proinsulins that can form only two (or even only one) of the native proinsulin disulfide bonds.	Disulfides	189-198	insulin	Homo sapiens	110-120
26822090-4	2016	Interestingly, formation of these two "interchain" disulfide bonds demonstrates cooperativity, and together, they are sufficient to confer intracellular transport competence to proinsulin.	Disulfides	51-60	insulin	Homo sapiens	177-187
26822090-6	2016	MIDY mutations inhibit Cys(B19)-Cys(A20) formation, but treatment to force oxidation of this disulfide bond improves folding and results in a small but detectable increase of proinsulin export.	Disulfides	93-102	insulin	Homo sapiens	175-185
26656632-4	2016	Our in vitro studies in Panc-1 human pancreatic ductal adenocarcinoma cells confirm that gemcitabine encapsulated in EGFR-targeted gelatin nanoparticles, released through disulfide bond cleavage, had a significantly improved cytotoxic profile.	Disulfides	171-180	epidermal growth factor receptor	Homo sapiens	117-121
26670633-3	2016	VWF is dimerized in the endoplasmic reticulum by formation of disulfide bonds between the C-terminal cysteine knot (CK) domains of 2 monomers.	Disulfides	62-71	von Willebrand factor	Homo sapiens	0-3
26670633-9	2016	On the basis of protein-protein docking and molecular dynamics simulations, combined with fluorescence microscopy studies of VWF CK-domain mutants, we suggest the following mechanism of VWF dimerization: PDI initiates VWF dimerization by forming the first 2 disulfide bonds Cys2771-2773" and Cys2771"-2773.	Disulfides	258-267	von Willebrand factor	Homo sapiens	186-189
26670633-9	2016	On the basis of protein-protein docking and molecular dynamics simulations, combined with fluorescence microscopy studies of VWF CK-domain mutants, we suggest the following mechanism of VWF dimerization: PDI initiates VWF dimerization by forming the first 2 disulfide bonds Cys2771-2773" and Cys2771"-2773.	Disulfides	258-267	von Willebrand factor	Homo sapiens	186-189
26684250-5	2016	The reducing agent DTT elicited a large potentiation of the macroscopic conductance of D110C/K892C-CFTR, likely due to breakage of a spontaneous disulfide bond between C110 and C892.	Disulfides	145-154	CF transmembrane conductance regulator	Homo sapiens	99-103
26769413-0	2016	Binding to and Inhibition of Insulin-Regulated Aminopeptidase by Macrocyclic Disulfides Enhances Spine Density.	Disulfides	77-87	leucyl and cystinyl aminopeptidase	Homo sapiens	29-61
26964514-0	2016	Secreted APE1/Ref-1 inhibits TNF-alpha-stimulated endothelial inflammation via thiol-disulfide exchange in TNF receptor.	Disulfides	85-94	tumor necrosis factor	Homo sapiens	29-38
26960718-1	2016	Oxidized human defensin 5 (HD5OX), a Paneth cell-secreted antibacterial peptide with three characteristic disulfide bonds, protects the host from invasion by morbigenous microbes in the small intestine.	Disulfides	106-115	defensin alpha 5	Homo sapiens	15-25
26407855-9	2016	In this study, we show that TNF-alpha impairs adiponectin multimerization and consequently decreases adiponectin secretion by altering disulfide bond modification in the endoplasmic reticulum.	Disulfides	135-144	adiponectin, C1Q and collagen domain containing	Homo sapiens	46-57
26407855-9	2016	In this study, we show that TNF-alpha impairs adiponectin multimerization and consequently decreases adiponectin secretion by altering disulfide bond modification in the endoplasmic reticulum.	Disulfides	135-144	adiponectin, C1Q and collagen domain containing	Homo sapiens	101-112
26435004-9	2016	Furthermore, we observed that disulfide bridges in eotaxin, epidermal growth factor, and periostin were also decreased in the lungs of house dust mite-challenged ERp57-deleted mice.	Disulfides	30-39	periostin, osteoblast specific factor	Mus musculus	89-98
26783088-3	2016	A dimetal site, glycosylation pattern and a disulfide bond network are likely to be conserved also in human aSMase.	Disulfides	44-53	sphingomyelin phosphodiesterase 1	Homo sapiens	108-114
26725192-2	2016	Our previous reports suggest that nitric oxide-induced intramolecular disulfide-bonding GAPDH aggregation, which occurs through oxidation of the active site cysteine (Cys-152), participates in a mechanism to account for nitric oxide-induced death signaling in some neurodegenerative/neuropsychiatric disorders.	Disulfides	70-79	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	88-93
26435004-9	2016	Furthermore, we observed that disulfide bridges in eotaxin, epidermal growth factor, and periostin were also decreased in the lungs of house dust mite-challenged ERp57-deleted mice.	Disulfides	30-39	chemokine (C-C motif) ligand 11	Mus musculus	51-58
26928300-0	2016	Ligand-dependent responses of the silkworm prothoracicotropic hormone receptor, Torso, are maintained by unusual intermolecular disulfide bridges in the transmembrane region.	Disulfides	128-137	tyrosine-protein kinase receptor torso	Bombyx mori	80-85
26928300-3	2016	In this study, using heterologous expression in cultured Drosophila S2 cells, we detected ligand-independent dimerization of silkworm Torso, and found that the receptor molecules in the dimer were linked by intermolecular disulfide bridges.	Disulfides	222-231	tyrosine-protein kinase receptor torso	Bombyx mori	134-139
26928300-7	2016	The unique Torso structure with the intermolecular disulfide bridges in the transmembrane region is necessary to maintain the ligand-dependent receptor functions of autophosphorylation and downstream activation.	Disulfides	51-60	tyrosine-protein kinase receptor torso	Bombyx mori	11-16
26702061-4	2016	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a beta-sandwich topology formed by 2 sheets of antiparallel beta strands stabilized by the hallmark disulfide bond between the B and F strands.	Disulfides	193-202	immunoglobulin heavy chain diversity region-2	Homo sapiens	50-54
26694608-2	2016	SOD1 is an enzyme that matures through the binding of copper and zinc ions and the formation of an intramolecular disulfide bond.	Disulfides	114-123	superoxide dismutase 1	Homo sapiens	0-4
26809098-0	2016	A soluble form of the interleukin-6 family signal transducer gp130 is dimerized via a C-terminal disulfide bridge resulting from alternative mRNA splicing.	Disulfides	97-106	interleukin 6	Homo sapiens	22-35
26694608-6	2016	In particular, loop regions in SOD1 lose their restraint and become significantly disordered upon dissociation of metal ions and reduction of the disulfide bond.	Disulfides	146-155	superoxide dismutase 1	Homo sapiens	31-35
26890638-0	2016	T47D Cells Expressing Myeloperoxidase Are Able to Process, Traffic and Store the Mature Protein in Lysosomes: Studies in T47D Cells Reveal a Role for Cys319 in MPO Biosynthesis that Precedes Its Known Role in Inter-Molecular Disulfide Bond Formation.	Disulfides	225-234	myeloperoxidase	Homo sapiens	22-37
26890638-1	2016	Among the human heme-peroxidase family, myeloperoxidase (MPO) has a unique disulfide-linked oligomeric structure resulting from multi-step processing of the pro-protein monomer (proMPO) after it exits the endoplasmic reticulum (ER).	Disulfides	75-84	myeloperoxidase	Homo sapiens	40-55
26890638-1	2016	Among the human heme-peroxidase family, myeloperoxidase (MPO) has a unique disulfide-linked oligomeric structure resulting from multi-step processing of the pro-protein monomer (proMPO) after it exits the endoplasmic reticulum (ER).	Disulfides	75-84	myeloperoxidase	Homo sapiens	57-60
26890638-5	2016	However, only MPO undergoes both these proteolytic modifications and then is further oligomerized into a heterotetramer by a single inter-molecular disulfide bond.	Disulfides	148-157	myeloperoxidase	Homo sapiens	14-17
26890638-9	2016	Using this novel cell model we show that formation of MPO"s single inter-molecular disulfide bond can occur normally in the absence of the proteolytic events that lead to separation of the MPO heavy and light chains.	Disulfides	83-92	myeloperoxidase	Homo sapiens	54-57
26890638-10	2016	We further demonstrate that Cys319, which forms MPO"s unique inter-molecular disulfide bond, is important for events that precede this step.	Disulfides	77-86	myeloperoxidase	Homo sapiens	48-51
26846678-4	2016	In spite of the fact that the nitride group is multiply bound to two uranium and two or three Cs+ cations, these complexes transfer the nitride group to CS2 to afford SCN(-) and uranium(IV) disulfide.	Disulfides	190-199	chorionic somatomammotropin hormone 2	Homo sapiens	153-156
26890638-11	2016	Mutation of this residue alters the glycosylation and catalytic activity of MPO and blocks its entry into the endocytic pathway where proteolytic processing and disulfide bonding occur.	Disulfides	161-170	myeloperoxidase	Homo sapiens	76-79
26872211-3	2016	Peroxiredoxin 5 (Prdx5) is a thiol-dependent peroxidase that reduces oxidative stress by catalyzing intramolecular disulfide bonds.	Disulfides	115-124	peroxiredoxin 5	Rattus norvegicus	0-15
26694611-5	2016	Analyses by non-reducing SDS-PAGE, size exclusion chromatography, and sedimentation velocity revealed two native high Mr disulfide-bonded species that contain Golgi-modified forms of PMEL.	Disulfides	121-130	premelanosome protein	Homo sapiens	183-187
26694611-6	2016	These species correspond to disulfide bond-containing dimeric and monomeric PMEL isoforms that contain no other proteins as judged by two-dimensional PAGE of metabolically labeled/immunoprecipitated PMEL and by mass spectrometry of affinity-purified complexes.	Disulfides	28-37	premelanosome protein	Homo sapiens	76-80
26694611-6	2016	These species correspond to disulfide bond-containing dimeric and monomeric PMEL isoforms that contain no other proteins as judged by two-dimensional PAGE of metabolically labeled/immunoprecipitated PMEL and by mass spectrometry of affinity-purified complexes.	Disulfides	28-37	premelanosome protein	Homo sapiens	199-203
26694611-7	2016	Metabolic pulse-chase analyses, small molecule inhibitor treatments, and evaluation of site-directed mutants suggest that the PMEL dimer forms around the time of endoplasmic reticulum exit and is resolved by disulfide bond rearrangement into a monomeric form within the late Golgi or a post-Golgi compartment.	Disulfides	208-217	premelanosome protein	Homo sapiens	126-130
26694611-9	2016	Our data show that the Kringle-like domain facilitates the resolution of disulfide-bonded PMEL dimers and promotes PMEL functional amyloid formation, thereby suggesting that PMEL dimers must be resolved to monomers to generate functional amyloid fibrils.	Disulfides	73-82	premelanosome protein	Homo sapiens	90-94
26694611-9	2016	Our data show that the Kringle-like domain facilitates the resolution of disulfide-bonded PMEL dimers and promotes PMEL functional amyloid formation, thereby suggesting that PMEL dimers must be resolved to monomers to generate functional amyloid fibrils.	Disulfides	73-82	premelanosome protein	Homo sapiens	115-119
26694611-9	2016	Our data show that the Kringle-like domain facilitates the resolution of disulfide-bonded PMEL dimers and promotes PMEL functional amyloid formation, thereby suggesting that PMEL dimers must be resolved to monomers to generate functional amyloid fibrils.	Disulfides	73-82	premelanosome protein	Homo sapiens	115-119
26614766-11	2016	Notably the species with one disulfide and one hyperoxidized active site was decameric for Prx2 and dimeric for Prx3.	Disulfides	29-38	peroxiredoxin 2	Homo sapiens	91-95
26670609-5	2016	Importantly, ROS also inactivate Sb9 by oxidizing a highly conserved cysteine pair (P1-P1" in rodents and P1"-P2" in other mammals) in the reactive center loop to form a vicinal disulfide bond.	Disulfides	178-187	serpin family B member 9	Homo sapiens	33-36
26872211-3	2016	Peroxiredoxin 5 (Prdx5) is a thiol-dependent peroxidase that reduces oxidative stress by catalyzing intramolecular disulfide bonds.	Disulfides	115-124	peroxiredoxin 5	Rattus norvegicus	17-22
26304368-6	2016	The alpha-La:beta-lactoglobulin (beta-Lg) ratio greatly affected the nature of the interactions formed during gelation, where higher amounts of alpha-La lead to a gel more dependent on disulfide bonds.	Disulfides	185-194	lactalbumin alpha	Homo sapiens	4-12
26645455-8	2016	A disulfide bond introduced into the active center of the A": domain of GmPDIM was shown to be transferred to the active center of the A: domain of GmPDIM and the A: domain of GmPDIM directly oxidized the active centers of both the A: or A": domain of GmPDIL-2.	Disulfides	2-11	protein disulfide isomerse like protein	Glycine max	72-78
26645455-8	2016	A disulfide bond introduced into the active center of the A": domain of GmPDIM was shown to be transferred to the active center of the A: domain of GmPDIM and the A: domain of GmPDIM directly oxidized the active centers of both the A: or A": domain of GmPDIL-2.	Disulfides	2-11	protein disulfide isomerse like protein	Glycine max	148-154
26645455-8	2016	A disulfide bond introduced into the active center of the A": domain of GmPDIM was shown to be transferred to the active center of the A: domain of GmPDIM and the A: domain of GmPDIM directly oxidized the active centers of both the A: or A": domain of GmPDIL-2.	Disulfides	2-11	protein disulfide isomerse like protein	Glycine max	148-154
26645455-8	2016	A disulfide bond introduced into the active center of the A": domain of GmPDIM was shown to be transferred to the active center of the A: domain of GmPDIM and the A: domain of GmPDIM directly oxidized the active centers of both the A: or A": domain of GmPDIL-2.	Disulfides	2-11	protein disulfide isomerase-like protein	Glycine max	252-260
26695097-8	2016	Here we report the successful use of EC as a partial reduction approach in mapping of disulfide bonds of intact human insulin (HI) and lysozyme.	Disulfides	86-95	insulin	Homo sapiens	118-125
26319711-2	2016	As part of our efforts to understand ALS pathogenesis, in this study we found that reduction of the intramolecular disulfide bond destabilized the tertiary structure of metal free wild-type SOD1 and greatly enhanced fibril formation in vitro.	Disulfides	115-124	superoxide dismutase 1	Homo sapiens	190-194
26319711-6	2016	It was also revealed that by reducing the disulfide bond and causing a decrease in the structural stability, the amyloid fibril formation of a familial mutant SOD1 G93A was accelerated even under physiological conditions.	Disulfides	42-51	superoxide dismutase 1	Homo sapiens	159-163
26319711-7	2016	These results demonstrate that by destabilizing the structure of SOD1 by removing metal ions and breaking the intramolecular disulfide bridge, multiple fibril-forming core regions are exposed, which then interact with each another and form amyloid fibrils under physiological conditions.	Disulfides	125-134	superoxide dismutase 1	Homo sapiens	65-69
26620526-9	2016	The NTD has conserved intramolecular and intermolecular disulfide bonds for PDRP dimerization.	Disulfides	56-65	pyruvate, phosphate dikinase regulatory protein, chloroplastic	Zea mays	76-80
26304368-6	2016	The alpha-La:beta-lactoglobulin (beta-Lg) ratio greatly affected the nature of the interactions formed during gelation, where higher amounts of alpha-La lead to a gel more dependent on disulfide bonds.	Disulfides	185-194	lactalbumin alpha	Homo sapiens	144-152
26740011-8	2016	We provide here a better understanding of the mechanism by which disulfide bond-mediated PHD2 dimerization and inactivation result in the activation of HIF-1alpha and aerobic glycolysis in response to oxidative stress.	Disulfides	65-74	egl-9 family hypoxia inducible factor 1	Homo sapiens	89-93
26693734-3	2016	We have developed a novel vitamin B12 derivative suitably tailored for disulfide-based conjugation that can undergo cleavage in the presence of glutathione, the most abundant thiol in mammalian cells.	Disulfides	71-80	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	34-37
26702098-2	2016	Using site-specific disulfide crosslinking, compartment-specific chemical labeling, and mutational analysis, we found that activated integral membrane Bax proteins form a BH3-in-groove dimer interface on the MOM surface similar to that observed in crystals.	Disulfides	20-29	BCL2 associated X, apoptosis regulator	Homo sapiens	151-154
26612102-0	2016	Structural changes upon peroxynitrite-mediated nitration of peroxiredoxin 2; nitrated Prx2 resembles its disulfide-oxidized form.	Disulfides	105-114	peroxiredoxin 2	Homo sapiens	60-75
26612102-0	2016	Structural changes upon peroxynitrite-mediated nitration of peroxiredoxin 2; nitrated Prx2 resembles its disulfide-oxidized form.	Disulfides	105-114	peroxiredoxin 2	Homo sapiens	86-90
26612102-8	2016	Our results show that the reduced nitrated Prx2 structurally resembles the disulfide-oxidized native form of the enzyme favoring a locally unfolded conformation that facilitates disulfide formation.	Disulfides	75-84	peroxiredoxin 2	Homo sapiens	43-47
26612102-8	2016	Our results show that the reduced nitrated Prx2 structurally resembles the disulfide-oxidized native form of the enzyme favoring a locally unfolded conformation that facilitates disulfide formation.	Disulfides	178-187	peroxiredoxin 2	Homo sapiens	43-47
26740011-3	2016	Here, we identified disulfide bond-mediated PHD2 homo-dimer formation in response to oxidative stress caused by oxidizing agents and oncogenic H-ras(V12) signalling.	Disulfides	20-29	egl-9 family hypoxia inducible factor 1	Homo sapiens	44-48
26740011-5	2016	Furthermore, we demonstrated that disulfide bond-mediated PHD2 dimerization is associated with the stabilization and activation of HIF-1alpha under oxidative stress.	Disulfides	34-43	egl-9 family hypoxia inducible factor 1	Homo sapiens	58-62
26740011-5	2016	Furthermore, we demonstrated that disulfide bond-mediated PHD2 dimerization is associated with the stabilization and activation of HIF-1alpha under oxidative stress.	Disulfides	34-43	hypoxia inducible factor 1 subunit alpha	Homo sapiens	131-141
26693734-0	2016	Vitamin B12 Suitably Tailored for Disulfide-Based Conjugation.	Disulfides	34-43	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	8-11
26783049-5	2016	Nevertheless, introduction of a disulfide bridge in the interface of a psychrophilic DERA did confer increased thermostability, suggesting a strategy for rational design of more durable enzyme variants.	Disulfides	32-41	deoxyribose-phosphate aldolase	Homo sapiens	85-89
26740011-8	2016	We provide here a better understanding of the mechanism by which disulfide bond-mediated PHD2 dimerization and inactivation result in the activation of HIF-1alpha and aerobic glycolysis in response to oxidative stress.	Disulfides	65-74	hypoxia inducible factor 1 subunit alpha	Homo sapiens	152-162
26597547-2	2016	Pyridyl disulfide functionalized silica particles are prepared by surface chemical reactions, and thiol-terminated poly(oligo(ethylene glycol) monomethyl ether methacrylate) (POEGMA) and bovine serum albumin (BSA) molecules are grafted to the silica particles by thiol-disulfide exchange reactions.	Disulfides	8-17	albumin	Homo sapiens	194-207
26538256-4	2016	Spectroscopic analyses revealed the presence of thiol (-SH)/thione, disulfide (-S-S-), and sulfonate groups in ETB.	Disulfides	68-77	endothelin receptor type B	Homo sapiens	111-114
26599622-5	2016	Stimulated by the high content glutathione (GSH) in cytoplasm, the cleavage of disulfide bond resulted in the liberation of proapoptosis peptide C-KLA(TPP) and the p53 gene, which exerted the combined tumor therapy by regulating both intrinsic and extrinsic apoptotic pathways.	Disulfides	79-88	tumor protein p53	Homo sapiens	164-167
28128754-3	2016	While it has been well-established that the TF-VIIa complex is efficiently blocked by factor Xa associated with tissue factor pathway inhibitor (TFPI), it was uncovered during the last decade that TF contains an intramolecular allosteric disulfide, which is prone to reduction and is crucial for TF"s procoagulant and prothrombotic function.	Disulfides	238-247	coagulation factor III	Mus musculus	44-46
28128754-4	2016	The compromised integrity of the allosteric TF disulfide pair Cys186/Cys209 was demonstrated to be responsible for the cryptic nature of TF procoagulant activity on monocytes and other cell types as well as in mouse thrombosis models.	Disulfides	47-56	coagulation factor III	Mus musculus	44-46
28128754-4	2016	The compromised integrity of the allosteric TF disulfide pair Cys186/Cys209 was demonstrated to be responsible for the cryptic nature of TF procoagulant activity on monocytes and other cell types as well as in mouse thrombosis models.	Disulfides	47-56	coagulation factor III	Mus musculus	137-139
26631309-0	2016	Effect of disulfide bonding and multimerization on proteoglycan 4"s cartilage boundary lubricating ability and adsorption.	Disulfides	10-19	proteoglycan 4	Homo sapiens	51-65
26631309-1	2016	PURPOSE: The objectives of this study were to assess the cartilage boundary lubricating ability of (1) nonreduced (NR) disulfide-bonded proteoglycan 4 (PRG4) multimers versus PRG4 monomers and (2) NR versus reduced and alkylated (R/A) PRG4 monomers and to assess (3) the ability of NR PRG4 multimers versus monomers to adsorb to an articular cartilage surface.	Disulfides	119-128	proteoglycan 4	Homo sapiens	136-150
26631309-11	2016	CONCLUSIONS: These results demonstrate that the intermolecular disulfide-bonded multimeric structure of PRG4 is important for its ability to adsorb to a cartilage surface and function as a boundary lubricant.	Disulfides	63-72	proteoglycan 4	Homo sapiens	104-108
26547218-6	2016	In the patient group, a positive correlation was determined between c-reactive protein (r = 325, p = 0.007; r = 316, p = 0.010, respectively), fasting blood glucose (r = 279, p = 0.018; r = 251, p = 0.035, respectively), and glycosylated hemoglobin (r = 341, p = 0.004; r = 332, p = 0.005, respectively) and rates of disulfide/native thiol and disulfide/total thiol.	Disulfides	317-326	C-reactive protein	Homo sapiens	68-86
26547218-6	2016	In the patient group, a positive correlation was determined between c-reactive protein (r = 325, p = 0.007; r = 316, p = 0.010, respectively), fasting blood glucose (r = 279, p = 0.018; r = 251, p = 0.035, respectively), and glycosylated hemoglobin (r = 341, p = 0.004; r = 332, p = 0.005, respectively) and rates of disulfide/native thiol and disulfide/total thiol.	Disulfides	344-353	C-reactive protein	Homo sapiens	68-86
26864548-0	2016	ERp57 as a novel cellular factor controlling prion protein biosynthesis: Therapeutic potential of protein disulfide isomerases.	Disulfides	106-115	protein disulfide isomerase family A member 3	Homo sapiens	0-5
26254483-3	2016	In this study, the disulfide bonds within the IgG1 trastuzumab (TRA), which is specific for HER2, were cleaved by mild S-sulfonation or by mild reduction followed by S-alkylation with three different reagents.	Disulfides	19-28	erb-b2 receptor tyrosine kinase 2	Homo sapiens	92-96
26864548-2	2016	The protein disulfide isomerase ERp57 is a stress-responsive ER chaperone up-regulated in the brain of Creutzfeldt-Jakob disease patients.	Disulfides	12-21	protein disulfide isomerase family A member 3	Homo sapiens	32-37
26719252-8	2015	We demonstrated that this disulfide pair prevented CD4 induced-conformational rearrangements in NFL trimers derived from the prototypic subtype A, B, and C representatives.	Disulfides	26-35	CD4 molecule	Homo sapiens	51-54
26902251-6	2016	Functional assays showed that locking apoE(201-299) in an inter-molecular disulfide-bonded state at position 209, 223, 255, or 277 significantly decreases its ability to interact with lipids, especially when tethered towards the ends; this could be restored by reduction.	Disulfides	74-83	apolipoprotein E	Homo sapiens	38-42
27251471-10	2016	Moreover, oxidative stress can increase RyR2 activity by forming disulfide bonds between two neighboring subunits (intersubunit cross-linking).	Disulfides	65-74	ryanodine receptor 2	Homo sapiens	40-44
26581637-1	2016	INTRODUCTION: von Willebrand factor (VWF) is rich in cysteine; next to important structural disulfide bonds, free thiol groups are present.	Disulfides	92-101	von Willebrand factor	Homo sapiens	37-40
26719252-9	2015	Coupling the TD-based design with the engineered disulfide linkage, CC, increased the propensity of Env to form soluble highly stable spike mimics that are resistant to CD4-induced changes.	Disulfides	49-58	CD4 molecule	Homo sapiens	169-172
26116226-2	2015	GILT facilitates the presentation of a subset of epitopes from disulfide bond-containing antigens.	Disulfides	63-72	IFI30 lysosomal thiol reductase	Homo sapiens	0-4
26655737-4	2015	The carrier protein and enzyme interact only weakly, but we have trapped their complex by using a "suicide enzyme" strategy in which an engineered cysteine in the SoxB active site forms a disulfide bond with the incoming carrier arm cysteine.	Disulfides	188-197	SRY-box transcription factor 3	Homo sapiens	163-167
26511321-0	2015	The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.	Disulfides	4-13	superoxide dismutase 1	Homo sapiens	128-154
26511321-0	2015	The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.	Disulfides	4-13	superoxide dismutase 1	Homo sapiens	156-160
26511321-2	2015	Mature SOD1 owes its exceptional stability to a number of post-translational modifications as follows: formation of the intramolecular disulfide bond, binding of copper and zinc, and dimerization.	Disulfides	135-144	superoxide dismutase 1	Homo sapiens	7-11
26511321-4	2015	Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated.	Disulfides	49-58	superoxide dismutase 1	Homo sapiens	67-71
26511321-4	2015	Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated.	Disulfides	49-58	superoxide dismutase 1	Homo sapiens	99-103
26511321-4	2015	Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated.	Disulfides	199-208	superoxide dismutase 1	Homo sapiens	67-71
26511321-4	2015	Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated.	Disulfides	199-208	superoxide dismutase 1	Homo sapiens	99-103
26515416-9	2015	The specific HMGB1 isoform known to activate TLR4 signaling (disulfide HMGB1) stimulates smooth muscle cell to migrate and produce monocyte chemotactic protein 1/CCL2) via TLR4.	Disulfides	61-70	toll-like receptor 4	Mus musculus	45-49
26116226-1	2015	Gamma-interferon-inducible lysosomal thiol reductase (GILT) is the only enzyme known to catalyze disulfide bond reduction in the endocytic pathway.	Disulfides	97-106	IFI30 lysosomal thiol reductase	Homo sapiens	0-52
26116226-1	2015	Gamma-interferon-inducible lysosomal thiol reductase (GILT) is the only enzyme known to catalyze disulfide bond reduction in the endocytic pathway.	Disulfides	97-106	IFI30 lysosomal thiol reductase	Homo sapiens	54-58
26560632-1	2015	Insulin aggregates under storage conditions via disulfide interchange reaction.	Disulfides	48-57	insulin	Homo sapiens	0-7
26560632-5	2015	We explored the aggregation kinetics of insulin at pH 7.2 and 37  C in the presence of disulfide-reducing agent dithiothreitol (DTT), using spectroscopy (UV-visible, fluorescence, and Fourier transform infrared spectroscopy) and microscopy (scanning electron microscopy, atomic force microscopy) techniques.	Disulfides	87-96	insulin	Homo sapiens	40-47
26560632-6	2015	We prepared insulin "seeds" by incubating disulfide-reduced insulin at pH 7.2 and 37  C for varying lengths of time (10 min to 12 h).	Disulfides	42-51	insulin	Homo sapiens	12-19
26560632-6	2015	We prepared insulin "seeds" by incubating disulfide-reduced insulin at pH 7.2 and 37  C for varying lengths of time (10 min to 12 h).	Disulfides	42-51	insulin	Homo sapiens	60-67
26560632-9	2015	Interestingly, intermediate seeds (30 min to 4 h incubation) resulted in formation of transient fibrils in 4 h that converted to amorphous aggregates upon longer incubation of 24 h. Overall, the results show that insulin under disulfide reducing conditions at pH and temperature close to physiological favors amorphous aggregate formation and seed "maturity" plays an important role in nucleation dependent aggregation kinetics.	Disulfides	227-236	insulin	Homo sapiens	213-220
26515416-9	2015	The specific HMGB1 isoform known to activate TLR4 signaling (disulfide HMGB1) stimulates smooth muscle cell to migrate and produce monocyte chemotactic protein 1/CCL2) via TLR4.	Disulfides	61-70	toll-like receptor 4	Mus musculus	172-176
26515416-10	2015	Macrophages produce smooth muscle cell mitogens in response to disulfide HMGB1 also in a TLR4/myeloid differentiation primary response gene (88)/Trif-dependent manner.	Disulfides	63-72	toll-like receptor 4	Mus musculus	89-93
26421484-8	2015	Chemically conjugating IFN-gamma to silk films through disulfide bonds allowed for longer-term release to 10 days.	Disulfides	55-64	interferon gamma	Homo sapiens	23-32
26349060-4	2015	Here we report that the first-generation HIV-PI saquinavir (SQV), as well as a newly identified mammalian protease inhibitor STO33438 (334), potently block disulfide HMGB1-induced TLR4 activation, as assayed by the production of TNF-alpha by human monocyte-derived macrophages (THP-1).	Disulfides	156-165	tumor necrosis factor	Homo sapiens	229-238
26349060-4	2015	Here we report that the first-generation HIV-PI saquinavir (SQV), as well as a newly identified mammalian protease inhibitor STO33438 (334), potently block disulfide HMGB1-induced TLR4 activation, as assayed by the production of TNF-alpha by human monocyte-derived macrophages (THP-1).	Disulfides	156-165	GLI family zinc finger 2	Homo sapiens	278-283
26349060-11	2015	Cell-based screening identified the mammalian protease cathepsin V as a novel therapeutic target to inhibit TLR4-mediated inflammation induced by extracellular HMGB1 (disulfide form).	Disulfides	167-176	cathepsin V	Homo sapiens	55-66
26644781-4	2015	UV-activation in combination with ECD allowed the three disulfide bonds of insulin to be cleaved and the overall sequence coverage to be increased.	Disulfides	56-65	insulin	Homo sapiens	75-82
26854591-3	2015	Upon diamide treatment of the cells, Grx1 forms an active site disulfide bridge that is rapidly re-reduced after stress removal; Cys76, a conserved non-active site Cys remains in the thiol state.	Disulfides	63-72	glutaredoxin	Mus musculus	37-41
26513173-2	2015	The ER resident thiol oxidoreductase ERp57 plays an important role in disulfide bond formation.	Disulfides	70-79	protein disulfide isomerase family A member 3	Homo sapiens	37-42
26555695-6	2015	Using a combination of molecular design, phage-display, and medicinal chemistry, disulfide-rich peptides (DRPs) directed against IL-6 were developed with low nanomolar potency in inhibiting IL-6-induced pSTAT3 in U937 monocytic cells.	Disulfides	81-90	interleukin 6	Homo sapiens	129-133
26431872-2	2015	This process is associated with disulfide-bonded GAPDH aggregation.	Disulfides	32-41	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	49-54
26555695-6	2015	Using a combination of molecular design, phage-display, and medicinal chemistry, disulfide-rich peptides (DRPs) directed against IL-6 were developed with low nanomolar potency in inhibiting IL-6-induced pSTAT3 in U937 monocytic cells.	Disulfides	81-90	interleukin 6	Homo sapiens	190-194
26540198-1	2015	Thioredoxin-2 (Trx2) is a mitochondrial protein using a dithiol active site to reduce protein disulfides.	Disulfides	94-104	thioredoxin 2	Gallus gallus	0-13
26540198-1	2015	Thioredoxin-2 (Trx2) is a mitochondrial protein using a dithiol active site to reduce protein disulfides.	Disulfides	94-104	thioredoxin 2	Gallus gallus	15-19
26207449-3	2015	This study found, using amide hydrogen/deuterium (H/D) exchange, capillary electrophoresis, and lysine-acetyl protein charge ladders, that ALS-linked A4V SOD1 rapidly monomerizes and partially unfolds in an external electric field (of physiological strength), without loss of metal ions, exposure to disulfide-reducing agents, or Joule heating.	Disulfides	300-309	superoxide dismutase 1	Homo sapiens	139-142
26367307-0	2015	Toll-like receptor 4 signaling: A common pathway for interactions between prooxidants and extracellular disulfide high mobility group box 1 (HMGB1) protein-coupled activation.	Disulfides	104-113	toll-like receptor 4	Mus musculus	0-20
26446990-3	2015	Here, we show that NPGPx forms a disulfide bond with the translational regulator cytoplasmic polyadenylation element-binding protein 2 (CPEB2) that results in negative regulation of hypoxia-inducible factor 1-alpha (HIF-1alpha) RNA translation.	Disulfides	33-42	hypoxia inducible factor 1 subunit alpha	Homo sapiens	182-214
26446990-3	2015	Here, we show that NPGPx forms a disulfide bond with the translational regulator cytoplasmic polyadenylation element-binding protein 2 (CPEB2) that results in negative regulation of hypoxia-inducible factor 1-alpha (HIF-1alpha) RNA translation.	Disulfides	33-42	hypoxia inducible factor 1 subunit alpha	Homo sapiens	216-226
26382042-0	2015	The road to the first, fully active and more stable human insulin variant with an additional disulfide bond.	Disulfides	93-102	insulin	Homo sapiens	58-65
26382042-3	2015	All known insulin variants in vertebrates consist of two peptide chains and have six cysteine residues, which form three disulfide bonds, two of them link the two chains and a third is an intra-chain bond in the A-chain.	Disulfides	121-130	insulin	Homo sapiens	10-17
26382042-5	2015	We addressed the question whether a human insulin variant with four disulfide bonds could exist and be fully functional.	Disulfides	68-77	insulin	Homo sapiens	42-49
26382042-6	2015	In this review, we give an overview of the road to engineering four-disulfide bonded insulin analogs.	Disulfides	68-77	insulin	Homo sapiens	85-92
26382042-7	2015	During our journey, we discovered several active four disulfide bonded insulin analogs with markedly improved stability and gained insights into the instability of analogs with seven cysteine residues, importance of dimerization for stability, insulin fibril formation process, and the conformation of insulin binding to its receptor.	Disulfides	54-63	insulin	Homo sapiens	71-78
26382042-7	2015	During our journey, we discovered several active four disulfide bonded insulin analogs with markedly improved stability and gained insights into the instability of analogs with seven cysteine residues, importance of dimerization for stability, insulin fibril formation process, and the conformation of insulin binding to its receptor.	Disulfides	54-63	insulin	Homo sapiens	244-251
26382042-7	2015	During our journey, we discovered several active four disulfide bonded insulin analogs with markedly improved stability and gained insights into the instability of analogs with seven cysteine residues, importance of dimerization for stability, insulin fibril formation process, and the conformation of insulin binding to its receptor.	Disulfides	54-63	insulin	Homo sapiens	244-251
26207449-3	2015	This study found, using amide hydrogen/deuterium (H/D) exchange, capillary electrophoresis, and lysine-acetyl protein charge ladders, that ALS-linked A4V SOD1 rapidly monomerizes and partially unfolds in an external electric field (of physiological strength), without loss of metal ions, exposure to disulfide-reducing agents, or Joule heating.	Disulfides	300-309	superoxide dismutase 1	Homo sapiens	154-158
26464514-0	2015	Cyclic thrombospondin-1 mimetics: grafting of a thrombospondin sequence into circular disulfide-rich frameworks to inhibit endothelial cell migration.	Disulfides	86-95	thrombospondin 1	Homo sapiens	7-23
25895046-5	2015	We developed ssSM3E/800CW, a novel CEA-targeted near-infrared fluorescent (NIRF) tracer, based on a disulfide-stabilized single-chain antibody fragment (ssScFv), to visualize colorectal and pancreatic tumors in a clinically translatable setting.	Disulfides	100-109	CEA cell adhesion molecule 3	Homo sapiens	35-38
26464514-3	2015	The primary aim of the present study was to design cyclic thrombospondin-1 (TSP-1) mimetics using disulfide-rich frameworks for anti-angiogenesis therapies and to determine whether these peptides have better potency than the linear parent peptide.	Disulfides	98-107	thrombospondin 1	Homo sapiens	58-74
26464514-3	2015	The primary aim of the present study was to design cyclic thrombospondin-1 (TSP-1) mimetics using disulfide-rich frameworks for anti-angiogenesis therapies and to determine whether these peptides have better potency than the linear parent peptide.	Disulfides	98-107	thrombospondin 1	Homo sapiens	76-81
26051415-6	2015	The amino acid sequences equivalent to human mature GILT are well conserved, including the GILT signature and nine of the ten cysteine residues that potentially form 5 disulfide bonds in human GILT, across the animal kingdom.	Disulfides	168-177	IFI30 lysosomal thiol reductase	Homo sapiens	52-56
26387864-6	2015	In the presence of the disulfide bond, MICU1-MICU2 heterodimer binding to MCU is controlled by Ca(2+) levels: the dimer associates with MCU at low levels of Ca(2+) and dissociates upon high Ca(2+) concentrations.	Disulfides	23-32	mitochondrial calcium uniporter	Homo sapiens	74-77
26387864-6	2015	In the presence of the disulfide bond, MICU1-MICU2 heterodimer binding to MCU is controlled by Ca(2+) levels: the dimer associates with MCU at low levels of Ca(2+) and dissociates upon high Ca(2+) concentrations.	Disulfides	23-32	mitochondrial calcium uniporter	Homo sapiens	136-139
26690492-2	2015	The three-dimensional functional structure of gp120 contains intramolecular disulfide bonds, which are critical for the interaction with the CD4 receptor.	Disulfides	76-85	CD4 molecule	Homo sapiens	141-153
26170458-2	2015	PrP is a glycosylated and disulfide-bonded protein synthesized at the endoplasmic reticulum (ER).	Disulfides	26-35	prion protein	Homo sapiens	0-3
26269577-5	2015	Surprisingly, we find that protein disulfide isomerase (PDI), the major protein oxidase of the ER lumen, engages Akita proinsulin in a novel way, reducing proinsulin disulfide bonds and priming the Akita protein for ERAD.	Disulfides	35-44	insulin	Homo sapiens	119-129
26269577-5	2015	Surprisingly, we find that protein disulfide isomerase (PDI), the major protein oxidase of the ER lumen, engages Akita proinsulin in a novel way, reducing proinsulin disulfide bonds and priming the Akita protein for ERAD.	Disulfides	35-44	insulin	Homo sapiens	155-165
25761904-0	2015	When an Intramolecular Disulfide Bridge Governs the Interaction of DUOX2 with Its Partner DUOXA2.	Disulfides	23-32	dual oxidase 2	Homo sapiens	67-72
25761904-6	2015	RESULTS: We report the identification and the characterization of an intramolecular disulfide bond between cys-124 of the N-terminal ectodomain and cys-1162 of an extracellular loop of DUOX2, which has important functional implications in both export and activity of DUOX2.	Disulfides	84-93	dual oxidase 2	Homo sapiens	185-190
25761904-6	2015	RESULTS: We report the identification and the characterization of an intramolecular disulfide bond between cys-124 of the N-terminal ectodomain and cys-1162 of an extracellular loop of DUOX2, which has important functional implications in both export and activity of DUOX2.	Disulfides	84-93	dual oxidase 2	Homo sapiens	267-272
26214018-9	2015	The sulfhydryl oxidase Erv1 generates the disulfide pairs de novo using either molecular oxygen or, cytochrome c and other proteins as terminal electron acceptors that eventually link this folding process to respiration.	Disulfides	42-51	cytochrome c, somatic	Homo sapiens	100-112
26361352-1	2015	ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle.	Disulfides	51-60	calreticulin	Mus musculus	157-169
25985912-1	2015	In this paper, a redox and enzyme dual-stimuli responsive delivery system (MSN-SS-HA) based on mesoporous silica nanoparticles (MSN) for targeted drug delivery has been developed, in which hyaluronic acid (HA) was conjugated on the surface of silica by cleavable disulfide (SS) bonds.	Disulfides	263-272	moesin	Homo sapiens	75-78
25985912-1	2015	In this paper, a redox and enzyme dual-stimuli responsive delivery system (MSN-SS-HA) based on mesoporous silica nanoparticles (MSN) for targeted drug delivery has been developed, in which hyaluronic acid (HA) was conjugated on the surface of silica by cleavable disulfide (SS) bonds.	Disulfides	263-272	moesin	Homo sapiens	128-131
25960419-3	2015	The LTBPs were first identified as forming latent complexes with TGFbeta by covalently binding the TGFbeta propeptide (LAP) via disulfide bonds in the endoplasmic reticulum.	Disulfides	128-137	transforming growth factor beta 1	Homo sapiens	65-72
25960419-3	2015	The LTBPs were first identified as forming latent complexes with TGFbeta by covalently binding the TGFbeta propeptide (LAP) via disulfide bonds in the endoplasmic reticulum.	Disulfides	128-137	transforming growth factor beta 1	Homo sapiens	99-106
26203648-11	2015	The level of GAPDH-AP DNA adduct formation depends on oxidation of the protein SH-groups; disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA.	Disulfides	90-99	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	13-18
26203648-11	2015	The level of GAPDH-AP DNA adduct formation depends on oxidation of the protein SH-groups; disulfide bond reduction in GAPDH leads to the loss of its ability to form the adducts with AP DNA.	Disulfides	90-99	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	118-123
26367870-3	2015	This study presents data testing two main hypotheses: 1) that specific thiol-disulfide exchange in AtSS1 influences its catalytic function 2) that each conserved Cys residue has an impact on AtSS1 catalysis.	Disulfides	77-86	Glycogen/starch synthases, ADP-glucose type	Arabidopsis thaliana	99-104
26249042-5	2015	We have optimized the electrochemical reduction efficiency during HDX-MS analysis of two particularly challenging disulfide stabilized proteins: a therapeutic IgG1-antibody and nerve growth factor-beta (NGF).	Disulfides	114-123	nerve growth factor	Homo sapiens	203-206
26249042-8	2015	The presented results demonstrate the successful electrochemical reduction during HDX-MS analysis of both a small exceptional tightly disulfide-bonded protein (NGF) as well as the largest protein attempted to date (IgG1-antibody).	Disulfides	134-143	nerve growth factor	Homo sapiens	160-163
26201258-5	2015	On the one hand, TFF2 binds to MUC6 via non-covalent lectin interactions with the glycotope GlcNAcalpha1 4Galbeta1 R. On the other hand, TFF2 is probably also covalently bound to MUC6 via disulfide bridges.	Disulfides	188-197	trefoil factor 2	Homo sapiens	17-21
26201258-5	2015	On the one hand, TFF2 binds to MUC6 via non-covalent lectin interactions with the glycotope GlcNAcalpha1 4Galbeta1 R. On the other hand, TFF2 is probably also covalently bound to MUC6 via disulfide bridges.	Disulfides	188-197	trefoil factor 2	Homo sapiens	137-141
25720945-1	2015	BACKGROUND: The thiol protein peroxiredoxin 2 (Prx2) is a major red blood cell (RBC) antioxidant that breaks down hydroperoxides and in the process is converted to an oxidized disulfide.	Disulfides	176-185	peroxiredoxin 2	Homo sapiens	30-45
26075496-10	2015	This highly conserved pseudogene-derived variant in the TNX fibrinogen-like domain is predicted to be deleterious and disulfide bonded, results in reduced dermal elastin and fibrillin-1 staining and altered TGF-beta1 binding, and represents a novel TNXA/TNXB chimera.	Disulfides	118-127	transforming growth factor beta 1	Homo sapiens	207-216
26126825-3	2015	GARP forms disulfide bonds with proTGF-beta1, favors its cleavage into latent inactive TGF-beta1, induces the secretion and surface presentation of GARP latent TGF-beta1 complexes, and is required for activation of the cytokine in Tregs.	Disulfides	11-20	transforming growth factor beta 1	Homo sapiens	35-44
26126825-3	2015	GARP forms disulfide bonds with proTGF-beta1, favors its cleavage into latent inactive TGF-beta1, induces the secretion and surface presentation of GARP latent TGF-beta1 complexes, and is required for activation of the cytokine in Tregs.	Disulfides	11-20	transforming growth factor beta 1	Homo sapiens	87-96
25720945-1	2015	BACKGROUND: The thiol protein peroxiredoxin 2 (Prx2) is a major red blood cell (RBC) antioxidant that breaks down hydroperoxides and in the process is converted to an oxidized disulfide.	Disulfides	176-185	peroxiredoxin 2	Homo sapiens	47-51
26218428-5	2015	Sequence analysis of zebrafish ca10a and ca10b reveals strongly predicted signal peptides, N-glycosylation sites, and a potential disulfide, all of which are conserved, suggesting that all of CARP X and XI are secretory proteins and potentially dimeric.	Disulfides	130-139	carbonic anhydrase Xb	Danio rerio	41-46
26186140-0	2015	Structural Basis of IgE Binding to alpha- and gamma-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains.	Disulfides	78-87	Gli-G1	Triticum aestivum	35-60
26119103-4	2015	The consequences of beta1-beta2 contacts are evaluated by disulfide engineering, biophysical techniques, and cell viability assays.	Disulfides	58-67	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	20-25
26119103-5	2015	The double-cysteine mutant alpha-synCC, with a disulfide linking beta1 and beta2, is aggregation-incompetent and inhibits aggregation and toxicity of wild-type alpha-syn.	Disulfides	47-56	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	65-70
26013822-6	2015	To develop an LRP1 inhibitor that does not dissociate at low pH, we introduced a disulfide bond between the second and third helices in the RAP D3 domain.	Disulfides	81-90	LDL receptor related protein 1	Homo sapiens	14-18
25935706-2	2015	For selective cancer cell targeting, here the coupling of a synthetic cytolysin to the hY1-receptor preferring peptide [F(7),P(34)]-neuropeptide Y (NPY) using a labile disulfide linker is described.	Disulfides	168-177	RNA, Ro60-associated Y1	Homo sapiens	87-90
26193081-0	2015	Formation and reshuffling of disulfide bonds in bovine serum albumin demonstrated using tandem mass spectrometry with collision-induced and electron-transfer dissociation.	Disulfides	29-38	albumin	Homo sapiens	55-68
26101955-7	2015	SA suppresses both the chemoattractant activity of fully reduced HMGB1 and the increased expression of proinflammatory cytokine genes and cyclooxygenase 2 (COX-2) induced by disulfide HMGB1.	Disulfides	174-183	prostaglandin-endoperoxide synthase 2	Homo sapiens	138-154
26198801-3	2015	mSLLP1 monomer adopts a structural fold similar to that of chicken/mouse lysozymes retaining all four canonical disulfide bonds.	Disulfides	112-121	sperm acrosome associated 3	Mus musculus	0-6
25957407-4	2015	But the sequences and innate properties of ABri and Abeta are quite different, notably ABri contains two cysteine residues that can form disulfide bonds.	Disulfides	137-146	amyloid beta precursor protein	Homo sapiens	52-57
26099845-8	2015	Production of Von Willebrand factor is constrained by its large size, complex structure, and the need for extensive glycosylation and disulfide-bonded oligomerization.	Disulfides	134-143	von Willebrand factor	Homo sapiens	14-35
26101955-7	2015	SA suppresses both the chemoattractant activity of fully reduced HMGB1 and the increased expression of proinflammatory cytokine genes and cyclooxygenase 2 (COX-2) induced by disulfide HMGB1.	Disulfides	174-183	prostaglandin-endoperoxide synthase 2	Homo sapiens	156-161
26035642-7	2015	We find that linking the anti-parallel coiled-coils of the adjacent Orai1 C-termini through disulfide cross-links diminishes STIM1-Orai1 interaction, as assessed by FRET.	Disulfides	92-101	Stromal interaction molecule	Drosophila melanogaster	125-130
25944298-5	2015	In this study, three gp120 (strain JR-FL) variants were constructed, in which deletions of single outer-domain disulfide bonds were expected to introduce local conformational flexibility and promote presentation of additional CD4(+) T-cell epitopes.	Disulfides	111-120	CD4 molecule	Homo sapiens	226-229
25978680-0	2015	Probing the Conformational and Functional Consequences of Disulfide Bond Engineering in Growth Hormone by Hydrogen-Deuterium Exchange Mass Spectrometry Coupled to Electron Transfer Dissociation.	Disulfides	58-67	growth hormone 1	Homo sapiens	88-102
25917086-5	2015	In this study, we demonstrate that, after hTLR7 proteolytic processing, the liberated amino (N)-terminal fragment remains bound to the C terminus through disulfide bonds and provides key trafficking information that ensures correct delivery of the complex to endosomal compartments.	Disulfides	154-163	toll like receptor 7	Homo sapiens	42-47
25651816-3	2015	ERO1 function is essential for disulfide bond formation in yeast, whereas in mammals its function is compensated for by alternative pathways.	Disulfides	31-40	ER oxidoreductin	Saccharomyces cerevisiae S288C	0-4
25938783-3	2015	PKG1alpha can also be directly oxidized, forming a disulfide bond between homodimer subunits at cysteine 42 to enhance oxidant-stimulated vasorelaxation; however, the impact of PKG1alpha oxidation on myocardial regulation is unknown.	Disulfides	51-60	superoxide dismutase 1	Homo sapiens	74-83
25866208-0	2015	Structures of the Ets Protein DNA-binding Domains of Transcription Factors Etv1, Etv4, Etv5, and Fev: DETERMINANTS OF DNA BINDING AND REDOX REGULATION BY DISULFIDE BOND FORMATION.	Disulfides	154-163	ETS variant transcription factor 1	Homo sapiens	75-79
25635711-4	2015	Linker-drugs were evaluated as ADCs by conjugation to the anti-HER2 antibody trastuzumab via reduced interchain disulfides.	Disulfides	112-122	erb-b2 receptor tyrosine kinase 2	Homo sapiens	63-67
25866208-0	2015	Structures of the Ets Protein DNA-binding Domains of Transcription Factors Etv1, Etv4, Etv5, and Fev: DETERMINANTS OF DNA BINDING AND REDOX REGULATION BY DISULFIDE BOND FORMATION.	Disulfides	154-163	FEV transcription factor, ETS family member	Homo sapiens	97-100
25961806-0	2015	The Pediocin PA-1 Accessory Protein Ensures Correct Disulfide Bond Formation in the Antimicrobial Peptide Pediocin PA-1.	Disulfides	52-61	PAXIP1 associated glutamate rich protein 1	Homo sapiens	13-17
25961806-0	2015	The Pediocin PA-1 Accessory Protein Ensures Correct Disulfide Bond Formation in the Antimicrobial Peptide Pediocin PA-1.	Disulfides	52-61	PAXIP1 associated glutamate rich protein 1	Homo sapiens	115-119
25961806-6	2015	Pediocin PA-1 and sakacin P[N24C+44C] with correct disulfide bonds were the main products when they were secreted by the pediocin PA-1 ABC transporter and accessory protein, but when they were secreted by the corresponding secretion machinery for sakacin A, a pediocin-like bacteriocin with one disulfide bond (two cysteines), peptides with all three possible disulfide bonds were produced in approximately equal amounts.	Disulfides	51-60	PAXIP1 associated glutamate rich protein 1	Homo sapiens	9-13
25961806-6	2015	Pediocin PA-1 and sakacin P[N24C+44C] with correct disulfide bonds were the main products when they were secreted by the pediocin PA-1 ABC transporter and accessory protein, but when they were secreted by the corresponding secretion machinery for sakacin A, a pediocin-like bacteriocin with one disulfide bond (two cysteines), peptides with all three possible disulfide bonds were produced in approximately equal amounts.	Disulfides	51-60	PAXIP1 associated glutamate rich protein 1	Homo sapiens	130-134
25961806-6	2015	Pediocin PA-1 and sakacin P[N24C+44C] with correct disulfide bonds were the main products when they were secreted by the pediocin PA-1 ABC transporter and accessory protein, but when they were secreted by the corresponding secretion machinery for sakacin A, a pediocin-like bacteriocin with one disulfide bond (two cysteines), peptides with all three possible disulfide bonds were produced in approximately equal amounts.	Disulfides	295-304	PAXIP1 associated glutamate rich protein 1	Homo sapiens	9-13
25961806-6	2015	Pediocin PA-1 and sakacin P[N24C+44C] with correct disulfide bonds were the main products when they were secreted by the pediocin PA-1 ABC transporter and accessory protein, but when they were secreted by the corresponding secretion machinery for sakacin A, a pediocin-like bacteriocin with one disulfide bond (two cysteines), peptides with all three possible disulfide bonds were produced in approximately equal amounts.	Disulfides	295-304	PAXIP1 associated glutamate rich protein 1	Homo sapiens	9-13
25961806-8	2015	The Cys86Ser mutation in the accessory protein caused a 2-fold decrease in the amount of pediocin PA-1 with correct disulfide bonds, while the Cys83Ser mutation nearly abolished the production of pediocin PA-1 and resulted in the production of all three disufide bond variants in equal amounts.	Disulfides	116-125	PAXIP1 associated glutamate rich protein 1	Homo sapiens	98-102
25961806-11	2015	These results indicate that the pediocin PA-1 accessory protein has a chaperone-like activity in that it ensures the formation of the correct disulfide bond in pediocin PA-1.	Disulfides	142-151	PAXIP1 associated glutamate rich protein 1	Homo sapiens	41-45
25961806-11	2015	These results indicate that the pediocin PA-1 accessory protein has a chaperone-like activity in that it ensures the formation of the correct disulfide bond in pediocin PA-1.	Disulfides	142-151	PAXIP1 associated glutamate rich protein 1	Homo sapiens	169-173
25945585-0	2015	The structure of a dual-specificity tyrosine phosphorylation-regulated kinase 1A-PKC412 complex reveals disulfide-bridge formation with the anomalous catalytic loop HRD(HCD) cysteine.	Disulfides	104-113	dual specificity tyrosine phosphorylation regulated kinase 1A	Homo sapiens	19-87
25945585-3	2015	This replacement, along with the proximity of a potential disulfide-bridge partner from the activation segment, implies a potential for redox control of DYRK family activities.	Disulfides	58-67	dual specificity tyrosine phosphorylation regulated kinase 1A	Homo sapiens	153-157
25945585-4	2015	Here, the crystal structure of DYRK1A bound to PKC412 is reported, showing the formation of the disulfide bridge and associated conformational changes of the activation loop.	Disulfides	96-105	dual specificity tyrosine phosphorylation regulated kinase 1A	Homo sapiens	31-37
25666897-6	2015	In the present study, we observed the fibrillation of one of the premature forms of SOD1 (SOD1 with reduced disulfide) in the presence of curcumin.	Disulfides	108-117	superoxide dismutase 1	Homo sapiens	84-88
25666897-6	2015	In the present study, we observed the fibrillation of one of the premature forms of SOD1 (SOD1 with reduced disulfide) in the presence of curcumin.	Disulfides	108-117	superoxide dismutase 1	Homo sapiens	90-94
25934939-3	2015	Induction of disulfide linkage with oxidants such as copper (II)(1,10-phenanthroline)3 (CuPhe) and chemical cross-linking with cell-permeable homobifunctional maleimide reagents are convenient ways to investigate Bak and Bax oligomerization in cells or isolated mitochondria.	Disulfides	13-22	BCL2 associated X, apoptosis regulator	Homo sapiens	221-224
26222594-3	2015	It was found that, after internalization by cancer cells, the xPolyR8-KLA(TPP)/p53 complex released the C-KLA(TPP) moiety and the p53 gene in the cytoplasm due to its reducible disulfide bonds.	Disulfides	177-186	tumor protein p53	Homo sapiens	79-82
26222594-3	2015	It was found that, after internalization by cancer cells, the xPolyR8-KLA(TPP)/p53 complex released the C-KLA(TPP) moiety and the p53 gene in the cytoplasm due to its reducible disulfide bonds.	Disulfides	177-186	tumor protein p53	Homo sapiens	130-133
25716754-0	2015	Identification of reduction-susceptible disulfide bonds in transferrin by differential alkylation using O(16)/O(18) labeled iodoacetic acid.	Disulfides	40-49	transferrin	Homo sapiens	59-70
25628337-6	2015	The lack of the disulfide bridge in the Cx26C169Y protein causes a spatial rearrangement of two important residues, Asn176 and Thr177.	Disulfides	16-25	gap junction protein beta 2	Homo sapiens	40-49
25716754-7	2015	Application of this method to a cysteine-rich protein transferrin allows the majority of its native disulfide bonds to be measured for their reduction susceptibility, which appears to reflect both solvent accessibility and bond strain energy.	Disulfides	100-109	transferrin	Homo sapiens	54-65
25769921-0	2015	The C-terminal disulfide bonds of Helicobacter pylori GroES are critical for IL-8 secretion via the TLR4-dependent pathway in gastric epithelial cells.	Disulfides	15-24	toll-like receptor 4	Mus musculus	100-104
25865227-3	2015	EGFR family members contain conserved extracellular structures that are stabilized by disulfide bonds.	Disulfides	86-95	epidermal growth factor receptor	Homo sapiens	0-4
25865227-4	2015	Compounds that disrupt extracellular disulfide bonds could inactivate EGFR, HER2, and HER3 in unison.	Disulfides	37-46	epidermal growth factor receptor	Homo sapiens	70-74
25865227-4	2015	Compounds that disrupt extracellular disulfide bonds could inactivate EGFR, HER2, and HER3 in unison.	Disulfides	37-46	erb-b2 receptor tyrosine kinase 2	Homo sapiens	76-80
25627966-0	2015	Additional disulfide bonds in insulin: Prediction, recombinant expression, receptor binding affinity, and stability.	Disulfides	11-20	insulin	Homo sapiens	30-37
25627966-1	2015	The structure of insulin, a glucose homeostasis-controlling hormone, is highly conserved in all vertebrates and stabilized by three disulfide bonds.	Disulfides	132-141	insulin	Homo sapiens	17-24
25627966-2	2015	Recently, we designed a novel insulin analogue containing a fourth disulfide bond located between positions A10-B4.	Disulfides	67-76	insulin	Homo sapiens	30-37
25627966-4	2015	We examined how well disulfide bond predictions algorithms could identify disulfide bonds in this region of insulin.	Disulfides	21-30	insulin	Homo sapiens	108-115
25627966-4	2015	We examined how well disulfide bond predictions algorithms could identify disulfide bonds in this region of insulin.	Disulfides	74-83	insulin	Homo sapiens	108-115
25627966-5	2015	In order to identify stable insulin analogues with additional disulfide bonds, which could be expressed, the Cbeta cut-off distance had to be increased in many instances and single X-ray structures as well as structures from MD simulations had to be used.	Disulfides	62-71	insulin	Homo sapiens	28-35
25627966-7	2015	In contrast, addition of the fourth disulfide bond rendered all analogues resistant to fibrillation under stress conditions and all stable analogues bound to the insulin receptor with picomolar affinities.	Disulfides	36-45	insulin	Homo sapiens	162-169
25627966-9	2015	Statement: A fourth disulfide bond has recently been introduced into insulin, a small two-chain protein containing three native disulfide bonds.	Disulfides	20-29	insulin	Homo sapiens	69-76
25627966-9	2015	Statement: A fourth disulfide bond has recently been introduced into insulin, a small two-chain protein containing three native disulfide bonds.	Disulfides	128-137	insulin	Homo sapiens	69-76
25627966-10	2015	Here we show that a prediction algorithm predicts four additional four disulfide insulin analogues which could be expressed.	Disulfides	71-80	insulin	Homo sapiens	81-88
25627966-11	2015	Although the location of the additional disulfide bonds is only slightly shifted, this shift impacts both stability and activity of the resulting insulin analogues.	Disulfides	40-49	insulin	Homo sapiens	146-153
25739441-2	2015	We previously reported that adiponectin multimerization and stability are promoted by the disulfide bond A oxidoreductase-like protein (DsbA-L) in cells and in vivo.	Disulfides	90-99	adiponectin, C1Q and collagen domain containing	Homo sapiens	28-39
25880232-4	2015	Moreover, disulfide tethering of alpha1 to alpha2 or alpha6 blocks cytochrome c release, suggesting that alpha1 dissociation is required for further conformational changes during apoptosis.	Disulfides	10-19	cytochrome c, somatic	Homo sapiens	67-79
25769921-9	2015	We conclude that HpGroES, in which a unique conformational structure, domain B, is generated by these two disulfide bonds, induces IL-8 secretion via a TLR4-dependent mechanism.	Disulfides	106-115	toll-like receptor 4	Mus musculus	152-156
25691624-0	2015	Cys18-Cys137 disulfide bond in mouse angiotensinogen does not affect AngII-dependent functions in vivo.	Disulfides	13-22	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	37-52
25853513-4	2015	The three characteristics of cystatins, the cystatin-like domain (G, QxVxG, PW), a signal peptide, and one or two conserved disulfide bonds, were observed in platyhelminths, with the exception of cestodes, which lacked the conserved disulfide bond.	Disulfides	233-242	cystatin C	Gallus gallus	29-37
25853513-7	2015	Although no conserved disulfide bond was found in T. solium cystatin, the models of T. solium cystatin and chicken cystatin corresponded at the site of the first disulfide bridge of the chicken cystatin.	Disulfides	162-171	cystatin C	Gallus gallus	94-102
25853513-7	2015	Although no conserved disulfide bond was found in T. solium cystatin, the models of T. solium cystatin and chicken cystatin corresponded at the site of the first disulfide bridge of the chicken cystatin.	Disulfides	162-171	cystatin C	Gallus gallus	94-102
25853513-7	2015	Although no conserved disulfide bond was found in T. solium cystatin, the models of T. solium cystatin and chicken cystatin corresponded at the site of the first disulfide bridge of the chicken cystatin.	Disulfides	162-171	cystatin C	Gallus gallus	94-102
25853513-8	2015	However, the two models were not similar regarding the location of the second disulfide bridge of chicken cystatin.	Disulfides	78-87	cystatin C	Gallus gallus	106-114
25694424-0	2015	Formation of disulfide bridges drives oligomerization, membrane pore formation, and translocation of fibroblast growth factor 2 to cell surfaces.	Disulfides	13-22	fibroblast growth factor 2	Homo sapiens	101-127
25694424-12	2015	We propose that the formation of disulfide bridges drives membrane insertion of FGF2 oligomers as intermediates in unconventional secretion of FGF2.	Disulfides	33-42	fibroblast growth factor 2	Homo sapiens	80-84
25694424-12	2015	We propose that the formation of disulfide bridges drives membrane insertion of FGF2 oligomers as intermediates in unconventional secretion of FGF2.	Disulfides	33-42	fibroblast growth factor 2	Homo sapiens	143-147
25794267-2	2015	A trivalent arsenous acid (As(III)) derivative (1) obtained from p-arsanilic acid (As(V)) was shown to readily undergo conjugation to the therapeutic peptide salmon calcitonin (sCT) via bridging of the Cys(1)-Cys(7) disulfide, which was verified by RP-HPLC and MALDI-ToF-MS. Conjugation was shown to proceed rapidly (t &lt; 2 min) in situ and stoichiometrically through sequential reduction-conjugation protocols, therefore exhibiting conjugation efficiencies equivalent to those reported for the current leading disulfide-bond targeting strategies.	Disulfides	216-225	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	83-88
25794267-2	2015	A trivalent arsenous acid (As(III)) derivative (1) obtained from p-arsanilic acid (As(V)) was shown to readily undergo conjugation to the therapeutic peptide salmon calcitonin (sCT) via bridging of the Cys(1)-Cys(7) disulfide, which was verified by RP-HPLC and MALDI-ToF-MS. Conjugation was shown to proceed rapidly (t &lt; 2 min) in situ and stoichiometrically through sequential reduction-conjugation protocols, therefore exhibiting conjugation efficiencies equivalent to those reported for the current leading disulfide-bond targeting strategies.	Disulfides	513-522	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	83-88
25735823-5	2015	Both glycosylated and nonglycosylated forms were synthesized by Fmoc solid-phase peptide synthesis and NMR analysis identified an alpha-helix within the disulfide ring containing the putative pharmacophore for NPR-A.	Disulfides	153-162	natriuretic peptide receptor 1	Homo sapiens	210-215
25631887-0	2015	Thiol-disulfide exchange in peptides derived from human growth hormone during lyophilization and storage in the solid state.	Disulfides	6-15	growth hormone 1	Homo sapiens	56-70
25691624-2	2015	It has been suggested recently that redox regulation of a disulfide bond in AGT involving Cys18-Cys137 may be important to its renin cleavage efficiency in vivo.	Disulfides	58-67	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	76-79
25691624-12	2015	These data indicate that the Cys18-Cys137 disulfide bond in AGT is dispensable for AngII production and AngII-dependent functions in mice.	Disulfides	42-51	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	60-63
25579745-3	2015	This puts pressure on the beta cell secretory pathway, especially the endoplasmic reticulum (ER), where proinsulin undergoes its initial folding, including the formation of three evolutionarily conserved disulfide bonds.	Disulfides	204-213	insulin	Homo sapiens	104-114
25821118-1	2015	The inherently present seventeen disulfide bonds of the circulatory protein, human serum albumin (HSA) provide the necessary structural stability.	Disulfides	33-42	albumin	Homo sapiens	83-96
25688043-7	2015	Our data show for the first time that a disulfide bridge between Cys243 and Cys249 on PRK is required to form the PRK-GAPDH-CP12 complex.	Disulfides	40-49	uncharacterized protein	Chlamydomonas reinhardtii	124-128
24859801-0	2015	Extracellular disulfide bridges stabilize TRPC5 dimerization, trafficking, and activity.	Disulfides	14-23	transient receptor potential cation channel subfamily C member 5	Homo sapiens	42-47
24859801-4	2015	Here, we examine the functional importance of the extracellular disulfide bond in TRPC5 in modulating channel gating and trafficking.	Disulfides	64-73	transient receptor potential cation channel subfamily C member 5	Homo sapiens	82-87
24859801-6	2015	Using reducing agents, we determined that a disulfide linkage mediates the tetrameric formation of the TRPC5 channel.	Disulfides	44-53	transient receptor potential cation channel subfamily C member 5	Homo sapiens	103-108
24859801-13	2015	These results indicated that the disulfide bond between conserved extracellular cysteines, especially C553, is essential for functional TRPC5 activity by channel multimerization and trafficking.	Disulfides	33-42	transient receptor potential cation channel subfamily C member 5	Homo sapiens	136-141
25821118-1	2015	The inherently present seventeen disulfide bonds of the circulatory protein, human serum albumin (HSA) provide the necessary structural stability.	Disulfides	33-42	albumin	Homo sapiens	98-101
25613923-5	2015	AalphaC472S fibrinogen indicated the presence of additional disulfide-bonded molecules, and markedly impaired lateral aggregation of protofibrils in spite of slightly lower functional plasma fibrinogen levels.	Disulfides	60-69	fibrinogen beta chain	Homo sapiens	12-22
25613923-7	2015	Recombinant variant fibrinogen-producing cells demonstrated that destruction of the Aalpha442C-472C disulfide bond did not prevent the synthesis or secretion of fibrinogen, whereas the variant Aalpha chain of the secreted protein was degraded faster than that of the normal control.	Disulfides	100-109	fibrinogen beta chain	Homo sapiens	20-30
26182355-5	2015	Loss of the Tim9 inner disulfide bond led to a temperature-sensitive phenotype and degradation of both Tim9 and Tim10.	Disulfides	23-32	protein transporter TIM10	Saccharomyces cerevisiae S288C	112-117
25613923-9	2015	The destruction and steric hindrance of the alphaC-domain of variant fibrinogen led to the impaired lateral aggregation of protofibrils and t-PA and plasminogen-mediated fibrinolysis, as well as several previously reported variants located in the alphaC-domain, and demonstrated the presence of disulfide-bonded molecules.	Disulfides	295-304	fibrinogen beta chain	Homo sapiens	69-79
25785690-0	2015	Human beta-defensin 4 with non-native disulfide bridges exhibit antimicrobial activity.	Disulfides	38-47	defensin beta 104B	Homo sapiens	6-21
25785690-4	2015	In this study, we have explored the antimicrobial activity of human beta-defensin 4 (HBD4) analogs that differ in the number and connectivity of disulfide bridges.	Disulfides	145-154	defensin beta 104B	Homo sapiens	68-83
25785690-4	2015	In this study, we have explored the antimicrobial activity of human beta-defensin 4 (HBD4) analogs that differ in the number and connectivity of disulfide bridges.	Disulfides	145-154	defensin beta 104B	Homo sapiens	85-89
25775568-4	2015	We report the X-ray crystal structure of long form PDE4B containing UCR1, UCR2, and the catalytic domain, crystallized as a dimer in which a disulfide bond cross-links cysteines engineered into UCR2 and the catalytic domain.	Disulfides	141-150	phosphodiesterase 4B	Homo sapiens	51-56
26182355-7	2015	Formation of both disulfide bonds is not essential for Tim9 function, but it can facilitate the formation and improve the stability of the hexameric Tim9-Tim10 complex.	Disulfides	18-27	protein transporter TIM10	Saccharomyces cerevisiae S288C	154-159
25554517-5	2015	We show that interferon alpha2b, human growth hormone (hGH) and two antibody fragments are exported with high efficiency; surprisingly, however, they are efficiently exported even in the absence of cytoplasmic disulfide formation.	Disulfides	210-219	growth hormone 1	Homo sapiens	39-53
25666947-3	2015	Here, we report for the first time detailed structural modulation about the wild-type CP12 and its site-specific N-terminal and C-terminal disulfide bridge mutants upon interaction with GAPDH and PRK by Forster resonance energy transfer (FRET).	Disulfides	139-148	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	186-191
25689578-0	2015	Disulfide-bond scrambling promotes amorphous aggregates in lysozyme and bovine serum albumin.	Disulfides	0-9	albumin	Homo sapiens	79-92
25689578-3	2015	In this study, we report the effect of disulfide-reducing agent dithiothreitol (DTT) on hen egg white lysozyme (lysozyme) and bovine serum albumin (BSA) aggregation at pH 7.2 and 37  C. BSA and lysozyme proteins treated with disulfide-reducing agents form very distinct amorphous aggregates as observed by scanning electron microscope.	Disulfides	39-48	albumin	Homo sapiens	133-146
25758790-1	2015	The insulin receptor (IR) and insulin-like growth factor-1 receptor (IGF1R) are highly related receptor tyrosine kinases with a disulfide-linked homodimeric architecture.	Disulfides	128-137	insulin	Homo sapiens	4-11
25758790-1	2015	The insulin receptor (IR) and insulin-like growth factor-1 receptor (IGF1R) are highly related receptor tyrosine kinases with a disulfide-linked homodimeric architecture.	Disulfides	128-137	insulin	Homo sapiens	30-37
25661824-1	2015	A nickel-catalyzed thiolation of unactivated C(sp(2))-H bonds with disulfides employing the PIP directing group was described.	Disulfides	67-77	prolactin induced protein	Homo sapiens	92-95
25776511-2	2015	In this wok, epidermal growth factor receptor (EGFR) antagonist peptide GE11 was introduced into DOX structure via a disulfide bond which can be cleaved by reduced glutathione (GSH).	Disulfides	117-126	epidermal growth factor receptor	Homo sapiens	13-45
25776511-2	2015	In this wok, epidermal growth factor receptor (EGFR) antagonist peptide GE11 was introduced into DOX structure via a disulfide bond which can be cleaved by reduced glutathione (GSH).	Disulfides	117-126	epidermal growth factor receptor	Homo sapiens	47-51
25677339-1	2015	Biodegradable and biocompatible poly(d,l-lactic-co-glycolic acid) (PLGA)was conjugated to the 5"-thiol end of signal transducer and activator of transcription 3 (STAT3) small interfering RNA (STAT3-siRNA) via a disulfide bond.	Disulfides	211-220	signal transducer and activator of transcription 3	Homo sapiens	110-160
25677339-1	2015	Biodegradable and biocompatible poly(d,l-lactic-co-glycolic acid) (PLGA)was conjugated to the 5"-thiol end of signal transducer and activator of transcription 3 (STAT3) small interfering RNA (STAT3-siRNA) via a disulfide bond.	Disulfides	211-220	signal transducer and activator of transcription 3	Homo sapiens	162-167
25568315-9	2015	Moreover, the formation of this unique structure is critically dependent on the finely tuned interplay between disulfide bonding and N-glycosylation in the membrane processed NBCe1-A dimer.	Disulfides	111-120	solute carrier family 4 member 4	Homo sapiens	175-182
25617045-9	2015	The structure contains a disulfide bond, and redox titration of CrCAH3 function with dithiothreitol suggested a possible redox regulation of the enzyme.	Disulfides	25-34	uncharacterized protein	Chlamydomonas reinhardtii	64-70
25196942-7	2015	RESULTS: At 21 days of storage, we demonstrated that cytosolic GAPDH undergoes temporary inactivation due to the formation of an intramolecular disulfide bond between the active-site Cys-152 and nearby Cys-156, a mechanism to rerouting glucose flux toward the pentose phosphate pathway.	Disulfides	144-153	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	63-68
25680077-2	2015	The peptides of the insulin family are disulfide-linked single or dual-chain proteins, while receptors are ligand-activated transmembrane glycoproteins of the receptor tyrosine kinase (RTK) superfamily.	Disulfides	39-48	insulin	Homo sapiens	20-27
25387803-5	2015	In each expression system, mutation of cysteines in GPIHBP1"s Ly6 domain (including mutants identified in patients with chylomicronemia) led to the formation of disulfide-linked dimers and multimers.	Disulfides	161-170	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	52-59
25518935-0	2015	Identification of protein disulfide isomerase 1 as a key isomerase for disulfide bond formation in apolipoprotein B100.	Disulfides	26-35	apolipoprotein B	Rattus norvegicus	99-118
25518935-2	2015	ApoB100 contains 25 cysteine residues and eight disulfide bonds.	Disulfides	48-57	apolipoprotein B	Rattus norvegicus	0-7
25518935-3	2015	Although these disulfide bonds were suggested to be important in maintaining apoB100 function, neither the specific oxidoreductase involved nor the direct role of these disulfide bonds in apoB100-lipidation is known.	Disulfides	15-24	apolipoprotein B	Rattus norvegicus	77-84
25556652-7	2015	In addition to the four disulfide bond-forming cysteine residues that define the traditional chemokine fold, CCL28 possesses two additional cysteine residues that form a third disulfide bond.	Disulfides	24-33	C-C motif chemokine ligand 28	Homo sapiens	109-114
25556652-7	2015	In addition to the four disulfide bond-forming cysteine residues that define the traditional chemokine fold, CCL28 possesses two additional cysteine residues that form a third disulfide bond.	Disulfides	176-185	C-C motif chemokine ligand 28	Homo sapiens	109-114
25556652-8	2015	If all disulfide bonds are disrupted, recombinant human CCL28 is no longer able to drive mouse CD4+ T-cell chemotaxis or in vivo airway hyper-reactivity, indicating that the conserved chemokine fold is necessary for its biologic activity.	Disulfides	7-16	C-C motif chemokine ligand 28	Homo sapiens	56-61
25450808-2	2015	The 36-40-residue ectodomains of avian reovirus (ARV) and Nelson Bay reovirus (NBV) p10 contain an essential intramolecular disulfide bond required for both cell-cell fusion and lipid mixing between liposomes.	Disulfides	124-133	S100 calcium binding protein A10	Homo sapiens	84-87
25699251-4	2015	Using a peptide-protein binding assay, we found that Nox2 peptides containing a (369)CysGlyCys(371) triad (CGC) bound p67 (phox) with high affinity, dependent upon the establishment of a disulfide bond between the two cysteines.	Disulfides	187-196	CD33 molecule	Homo sapiens	118-121
25699251-7	2015	This led to the hypothesis that Nox2 establishes disulfide bonds with p67 (phox) via a thiol-dilsulfide exchange reaction and, thus, functions as a PDI.	Disulfides	49-58	CD33 molecule	Homo sapiens	70-73
25699251-9	2015	We propose a model of oxidase assembly in which binding of p67 (phox) to Nox2 via disulfide bonds, by virtue of the intrinsic PDI activity of Nox2, stabilizes the primary interaction between the two components.	Disulfides	82-91	CD33 molecule	Homo sapiens	59-62
25603346-1	2015	ShK, from the sea anemone Stichodactyla helianthus, is a 35-residue disulfide-rich peptide that blocks the voltage-gated potassium channel Kv1.3 at ca.	Disulfides	68-77	potassium voltage-gated channel, shaker-related subfamily, member 3	Mus musculus	139-144
25288022-4	2015	Mutations C137S and C14S in the HA2 and HA1 subunits, respectively, were introduced to prevent any possible disulfide linkage between the two subunit proteins.	Disulfides	108-117	Rho GTPase activating protein 45	Mus musculus	40-43
26028988-5	2015	With charge enhancement upon the addition of sulfolane to the analyte solution, improved protein fragmentation and disulfide bond cleavage efficiency was observed for proteins including bovine beta-lactoglobulin, soybean trypsin inhibitor, human proinsulin, and chicken lysozyme.	Disulfides	115-124	kunitz trypsin protease inhibitor	Glycine max	221-238
25370824-1	2015	Mature transforming growth factor beta1 (TGF-beta1) is a homodimeric protein with a single disulfide bridge between Cys77 on the respective monomers.	Disulfides	91-100	transforming growth factor beta 1	Homo sapiens	41-50
25673329-7	2015	In a further test, we introduced two mutations into Cx26, K125C and R104C, to allow disulfide bridge formation across the inter-subunit boundary.	Disulfides	84-93	gap junction protein beta 2	Homo sapiens	52-56
25392066-8	2015	Co-immunoprecipitation assays showed that FUT1 forms a homocomplex through disulfide bonds, and formation of the heterocomplexes does not involve covalent interactions.	Disulfides	75-84	fucosyltransferase 1	Arabidopsis thaliana	42-46
25584637-0	2015	Oxidation of p53 through DNA charge transport involves a network of disulfides within the DNA-binding domain.	Disulfides	68-78	tumor protein p53	Homo sapiens	13-16
25584637-11	2015	On the basis of these data, it is proposed that disulfide formation involving C275 is critical for inducing oxidative dissociation of p53 from DNA.	Disulfides	48-57	tumor protein p53	Homo sapiens	134-137
25433341-1	2015	The functional and structural significance of the intrasubunit disulfide bond in copper-zinc superoxide dismutase (SOD1) was studied by characterizing mutant forms of human SOD1 (hSOD) and yeast SOD1 lacking the disulfide bond.	Disulfides	63-72	superoxide dismutase 1	Homo sapiens	115-119
25433341-1	2015	The functional and structural significance of the intrasubunit disulfide bond in copper-zinc superoxide dismutase (SOD1) was studied by characterizing mutant forms of human SOD1 (hSOD) and yeast SOD1 lacking the disulfide bond.	Disulfides	63-72	superoxide dismutase 1	Homo sapiens	173-177
25433341-1	2015	The functional and structural significance of the intrasubunit disulfide bond in copper-zinc superoxide dismutase (SOD1) was studied by characterizing mutant forms of human SOD1 (hSOD) and yeast SOD1 lacking the disulfide bond.	Disulfides	212-221	superoxide dismutase 1	Homo sapiens	115-119
25433341-6	2015	Using pulse radiolysis, we determined SOD activities of yeast and human SOD1s lacking disulfide bonds and found that they were enzymatically active at ~10% of the wild type rate.	Disulfides	86-95	superoxide dismutase 1	Homo sapiens	72-76
25433341-7	2015	These results are contrary to earlier reports that the intrasubunit disulfide bonds in SOD1 are essential for SOD activity.	Disulfides	68-77	superoxide dismutase 1	Homo sapiens	87-91
25487639-3	2015	Upon covalent oligomerisation, the disulfide-bridged peptide has previously shown similar behaviour to that of TNF-related apoptosis inducing ligand (TRAIL), by selectively triggering the DR5 cell death pathway.	Disulfides	35-44	TNF superfamily member 10	Homo sapiens	111-148
25487639-3	2015	Upon covalent oligomerisation, the disulfide-bridged peptide has previously shown similar behaviour to that of TNF-related apoptosis inducing ligand (TRAIL), by selectively triggering the DR5 cell death pathway.	Disulfides	35-44	TNF superfamily member 10	Homo sapiens	150-155
25352602-8	2014	We show that Cstn3 ectodomains form monomers as well as tetramers that are stabilized by disulfide bonds and Ca(2+), and both are probably flexible in solution.	Disulfides	89-98	calsyntenin 3	Homo sapiens	13-18
25559892-0	2015	MD-2 is required for disulfide HMGB1-dependent TLR4 signaling.	Disulfides	21-30	toll-like receptor 4	Mus musculus	47-51
25559892-4	2015	Here we demonstrate that the extracellular TLR4 adaptor, myeloid differentiation factor 2 (MD-2), binds specifically to the cytokine-inducing disulfide isoform of HMGB1, to the exclusion of other isoforms.	Disulfides	142-151	toll-like receptor 4	Mus musculus	43-47
25568124-10	2015	Intracerebral disulfide HMGB-1 mimicked the effect of the stressor, because microglia isolated from HMGB-1-treated rats expressed exaggerated NLRP3 and proinflammatory cytokine expression after LPS treatment, whereas fully reduced HMGB-1 had no effect.	Disulfides	14-23	NLR family, pyrin domain containing 3	Rattus norvegicus	142-147
25069953-9	2015	INNOVATION AND CONCLUSION: IPO7 and IPO8 control the nuclear import of FOXO3, but not FOXO4, in a redox-sensitive and disulfide-dependent manner.	Disulfides	118-127	importin 7	Homo sapiens	27-31
25069953-9	2015	INNOVATION AND CONCLUSION: IPO7 and IPO8 control the nuclear import of FOXO3, but not FOXO4, in a redox-sensitive and disulfide-dependent manner.	Disulfides	118-127	importin 8	Homo sapiens	36-40
25069953-9	2015	INNOVATION AND CONCLUSION: IPO7 and IPO8 control the nuclear import of FOXO3, but not FOXO4, in a redox-sensitive and disulfide-dependent manner.	Disulfides	118-127	forkhead box O3	Homo sapiens	71-76
25306968-5	2015	Wild-type SOD1 is also highly unstructured upon reduction of disulfides and depletion of zinc.	Disulfides	61-71	superoxide dismutase 1	Homo sapiens	10-14
25523746-7	2015	Clumping was eliminated when additional disulfide bonds were incorporated into the scFv components of the BsAbs, but this resulted in lower BsAb expression.	Disulfides	40-49	immunglobulin heavy chain variable region	Homo sapiens	83-87
25402766-6	2015	The redox relay generates disulfide-linked STAT3 oligomers with attenuated transcriptional activity.	Disulfides	26-35	signal transducer and activator of transcription 3	Homo sapiens	43-48
26494386-1	2015	Calcitonin (CTN) is a polypeptide hormone consisting of 32 amino acids with a disulfide bridge between position 1 and 7 that is mainly produced by the C-cells of thyroid gland.	Disulfides	78-87	calcitonin related polypeptide alpha	Homo sapiens	0-10
26494386-1	2015	Calcitonin (CTN) is a polypeptide hormone consisting of 32 amino acids with a disulfide bridge between position 1 and 7 that is mainly produced by the C-cells of thyroid gland.	Disulfides	78-87	calcitonin related polypeptide alpha	Homo sapiens	12-15
25512553-4	2014	We previously reported that an endoplasmic reticulum chaperone, ERp44, binds to Cys200 and Cys209 residues of SERT to build a disulfide bond.	Disulfides	126-135	endoplasmic reticulum protein 44	Homo sapiens	64-69
25512553-4	2014	We previously reported that an endoplasmic reticulum chaperone, ERp44, binds to Cys200 and Cys209 residues of SERT to build a disulfide bond.	Disulfides	126-135	solute carrier family 6 member 4	Homo sapiens	110-114
25283130-2	2015	GSTO1 has been assayed spectrophotometrically by measuring the disappearance of its substrate, S-(4-nitrophenacyl)glutathione (4-NPG), in the presence of 2-mercaptoethanol that regenerates GSTO1 from its mixed disulfide.	Disulfides	210-219	glutathione S-transferase omega 1	Rattus norvegicus	0-5
24895182-6	2015	We showed that the VH-VL orientation, the (GGGGS)3 linker, disulfide bond stabilization of scFv, when combined with an affinity matured mutation provided the most efficient BsAb to direct T cells to lyse GD2-positive tumor cells.	Disulfides	59-68	immunglobulin heavy chain variable region	Homo sapiens	91-95
25069953-7	2015	The nuclear import receptors Importin-7 (IPO7) and Importin-8 (IPO8) form a disulfide-dependent heterodimer with FOXO3, which is required for its reactive oxygen species-induced nuclear translocation.	Disulfides	76-85	importin 7	Homo sapiens	29-39
25069953-7	2015	The nuclear import receptors Importin-7 (IPO7) and Importin-8 (IPO8) form a disulfide-dependent heterodimer with FOXO3, which is required for its reactive oxygen species-induced nuclear translocation.	Disulfides	76-85	importin 7	Homo sapiens	41-45
25069953-7	2015	The nuclear import receptors Importin-7 (IPO7) and Importin-8 (IPO8) form a disulfide-dependent heterodimer with FOXO3, which is required for its reactive oxygen species-induced nuclear translocation.	Disulfides	76-85	importin 8	Homo sapiens	51-61
25069953-7	2015	The nuclear import receptors Importin-7 (IPO7) and Importin-8 (IPO8) form a disulfide-dependent heterodimer with FOXO3, which is required for its reactive oxygen species-induced nuclear translocation.	Disulfides	76-85	importin 8	Homo sapiens	63-67
25069953-7	2015	The nuclear import receptors Importin-7 (IPO7) and Importin-8 (IPO8) form a disulfide-dependent heterodimer with FOXO3, which is required for its reactive oxygen species-induced nuclear translocation.	Disulfides	76-85	forkhead box O3	Homo sapiens	113-118
25327890-0	2015	Cytoglobin ligand binding regulated by changing haem-co-ordination in response to intramolecular disulfide bond formation and lipid interaction.	Disulfides	97-106	cytoglobin	Homo sapiens	0-10
25327890-6	2015	Furthermore, monomeric Cygb with an intramolecular disulfide bond has significantly different properties, oxidizing lipid membranes and binding ligands more rapidly as compared with the other forms of the protein.	Disulfides	51-60	cytoglobin	Homo sapiens	23-27
25514977-5	2015	The disulfide-bonded CTLA-2alpha/cathepsin L complex was isolated from mouse tissue.	Disulfides	4-13	cytotoxic T lymphocyte-associated protein 2 alpha	Mus musculus	21-32
25362663-1	2014	Glutaredoxin 2 (Grx2) is an isozyme of glutaredoxin1 (thioltransferase) present in the mitochondria and nucleus with disulfide reductase and peroxidase activities, and it controls thiol/disulfide balance in cells.	Disulfides	117-126	glutaredoxin	Mus musculus	39-52
25478966-3	2014	To further improve the bioactivity of scFv, we constructed a plasmid to express scFv-linker-matrilin-6xHis fusion proteins that could self-assemble into the scFv dimers by disulfide bonds in matrilin under non-reducing conditions.	Disulfides	172-181	immunglobulin heavy chain variable region	Homo sapiens	38-42
25390821-3	2014	Additionally, we present evidence that diphenyl disulfide ((PhS)2) operates on a common catalytic cycle with thiophenol (PhSH) by way of photolytic cleaveage of the disulfide bond.	Disulfides	48-57	prostaglandin-endoperoxide synthase 2	Homo sapiens	60-65
25478966-3	2014	To further improve the bioactivity of scFv, we constructed a plasmid to express scFv-linker-matrilin-6xHis fusion proteins that could self-assemble into the scFv dimers by disulfide bonds in matrilin under non-reducing conditions.	Disulfides	172-181	immunglobulin heavy chain variable region	Homo sapiens	80-84
25478966-3	2014	To further improve the bioactivity of scFv, we constructed a plasmid to express scFv-linker-matrilin-6xHis fusion proteins that could self-assemble into the scFv dimers by disulfide bonds in matrilin under non-reducing conditions.	Disulfides	172-181	immunglobulin heavy chain variable region	Homo sapiens	80-84
25256416-3	2014	Here, we described that co-expression of appropriate disulfide bonds (Dsb) proteins known to catalyze the formation and isomerization of Dsb can markedly recover the soluble expression of target scFv in E. coli.	Disulfides	53-62	immunglobulin heavy chain variable region	Homo sapiens	195-199
25289458-6	2014	We confirmed that adenanthin underwent Michael addition to isolated Prx2, thereby inhibiting oxidation to a disulfide-linked dimer.	Disulfides	108-117	peroxiredoxin 2	Homo sapiens	68-72
25001182-8	2014	Y141C-RDS formed strikingly abnormal disulfide-linked complexes which were localized to the outer segment (OS) where they impaired the formation of proper OS structure.	Disulfides	37-46	peripherin 2	Mus musculus	6-9
25363360-7	2014	The inner layer of LSZ is assumed to bind firmly to silver via disulfide bridges, which makes it irreversibly adsorbed with respect to dilution.	Disulfides	63-72	lysozyme	Homo sapiens	19-22
25419565-3	2014	As the ligands and receptors each contain disulfide bonds, a regulatory role for the cell surface protein disulfide isomerase (PDI) was investigated.	Disulfides	42-51	protein disulfide isomerase family A member 2	Homo sapiens	127-130
24968724-7	2014	Mia40 was in the oxidized, functional state, while SOD1 disulfide bond formation was promoted by increasing the level of the SOD1 chaperone, CCS, in the IMS.	Disulfides	56-65	superoxide dismutase 1	Homo sapiens	51-55
25253686-4	2014	Assessment of phagosomal disulfide reduction upon internalization of IgG-opsonized experimental particles confirmed a major role for GILT in phagosomal disulfide reduction in both resting and interferon-gamma-activated macrophages.	Disulfides	152-161	interferon gamma	Mus musculus	192-208
24684506-11	2014	INNOVATION AND CONCLUSION: H2S directly targets some disulfide bonds in EGFR, which activates the EGFR/gab1/PI3K/Akt pathway and subsequent Na(+)/K(+)-ATPase endocytosis and inhibition in renal tubular epithelial cells.	Disulfides	53-62	AKT serine/threonine kinase 1	Rattus norvegicus	113-116
25259849-6	2014	Biochemical data support that CRP molecules are secreted into the spinning dope and assembled into macromolecular complexes via disulfide bond linkages.	Disulfides	128-137	C-reactive protein	Homo sapiens	30-33
25237187-8	2014	Here, we showed by chromatography and a 1.9 A crystal structure that stable BMP9 dimers could form either with (D-form) or without (M-form) an intermolecular disulfide bond.	Disulfides	158-167	growth differentiation factor 2	Homo sapiens	76-80
32261800-6	2014	Bioreduction-triggered polymer degradation revealed that diselenide bonds are more stable than disulfide bonds with a lower redox potential (i.e. 10 muM GSH).	Disulfides	95-104	latexin	Homo sapiens	149-152
24968724-7	2014	Mia40 was in the oxidized, functional state, while SOD1 disulfide bond formation was promoted by increasing the level of the SOD1 chaperone, CCS, in the IMS.	Disulfides	56-65	superoxide dismutase 1	Homo sapiens	125-129
25036722-8	2014	Thus, the active form of BCRP, at least a dimer or a larger oligomer is maintained by intramolecular disulfide bridge that involves Cys(603) residues.	Disulfides	101-110	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	25-29
25294806-5	2014	This mechanism suggests a design for immunotoxins comprising a GUCY2C-directed monoclonal antibody conjugated through a reducible disulfide linkage to ricin A chain, which is activated to a potent cytotoxin in lysosomes.	Disulfides	130-139	guanylate cyclase 2c	Mus musculus	63-69
25142936-3	2014	eNPP 6 consists of two identical monomers of 55 kDa joined by a disulfide bridge, and possesses four N-glycans in each monomer.	Disulfides	64-73	ectonucleotide pyrophosphatase/phosphodiesterase 6	Bos taurus	0-6
26339260-1	2014	Human Insulin-like growth factor 1 (hIGF-1) consists of 70 amino acids in a single chain with three intermolecular disulfide bridges possessing valuable therapeutic effects.	Disulfides	115-124	insulin like growth factor 1	Homo sapiens	36-42
25299596-7	2014	Furthermore, we demonstrate that thiol/disulfide exchange in CD4 requires force for exposure of cryptic disulfide bonds.	Disulfides	39-48	CD4 molecule	Homo sapiens	61-64
25299596-7	2014	Furthermore, we demonstrate that thiol/disulfide exchange in CD4 requires force for exposure of cryptic disulfide bonds.	Disulfides	104-113	CD4 molecule	Homo sapiens	61-64
24094148-0	2014	Disulfide-containing high mobility group box-1 promotes N-methyl-D-aspartate receptor function and excitotoxicity by activating Toll-like receptor 4-dependent signaling in hippocampal neurons.	Disulfides	0-9	toll-like receptor 4	Mus musculus	128-148
25282523-3	2014	Both possess the unique three-disulfide heterodimeric peptide structure of insulin.	Disulfides	30-39	insulin	Homo sapiens	75-82
25127531-0	2014	Aberrant hetero-disulfide bond formation by the hypertriglyceridemia-associated p.Gly185Cys APOA5 variant (rs2075291).	Disulfides	16-25	apolipoprotein A5	Homo sapiens	92-97
25127531-6	2014	Nonreducing SDS-PAGE immunoblot analysis provided evidence that G162C apoA-V present in the lipoprotein-free fraction, but not that portion associated with lipoproteins, displayed altered electrophoretic mobility consistent with disulfide-linked heterodimer formation.	Disulfides	229-238	apolipoprotein A5	Homo sapiens	70-76
25127531-8	2014	CONCLUSIONS: Substitution of Cys for Gly at position 162 of mature apoA-V introduces a free cysteine that forms disulfide bonds with plasma proteins such that its lipoprotein-binding and triacylglycerol-modulation functions are compromised.	Disulfides	112-121	apolipoprotein A5	Homo sapiens	67-73
26461315-7	2014	Further, the inhibition extends the range where the concentrations of potential redox signaling readouts - H2O2, Prx2 sulfenic acid, Prx2 disulfide and Trx disulfide- show a proportional response to changes in H2O2 supply, covering practically the whole physiological range of the latter.	Disulfides	138-147	peroxiredoxin 2	Homo sapiens	133-137
25086035-2	2014	GAPDH normally exists in a soluble form; however, following necrosis, GAPDH and numerous other intracellular proteins convert into an insoluble disulfide-cross-linked state via the process of "nucleocytoplasmic coagulation."	Disulfides	144-153	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	0-5
24958171-2	2014	When the redox-sensitive oligomerization state of PTX3 was further investigated, PTX3 accumulated as an octamer as a result of disulfide-bond formation in heart, kidney, and lung-common organ dysfunctions seen in patients with sepsis.	Disulfides	127-136	pentraxin 3	Homo sapiens	81-85
25086035-4	2014	Despite the fact that disulfide cross-linking is a prominent feature of GAPDH aggregation, our data show that it is not a primary rate-determining step.	Disulfides	22-31	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	72-77
25086035-9	2014	Hence, methionine 46 represents a "linchpin" whereby its oxidation is a primary event permissive for the subsequent misfolding, aggregation, and disulfide cross-linking of GAPDH.	Disulfides	145-154	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	172-177
25122762-4	2014	Peroxiredoxin 4 (Prdx4), an ER-specific antioxidative peroxidase can utilize luminal H2O2 as driving force for reoxidizing protein disulfide isomerase family members, thus efficiently contributing to disulfide bond formation.	Disulfides	131-140	peroxiredoxin 4	Rattus norvegicus	0-15
25130463-2	2014	The interaction of ERp57 with calreticulin is believed to assist disulfide bond formation of nascent glycoprotein in the ER.	Disulfides	65-74	protein disulfide isomerase family A member 3	Homo sapiens	19-24
25122762-4	2014	Peroxiredoxin 4 (Prdx4), an ER-specific antioxidative peroxidase can utilize luminal H2O2 as driving force for reoxidizing protein disulfide isomerase family members, thus efficiently contributing to disulfide bond formation.	Disulfides	131-140	peroxiredoxin 4	Rattus norvegicus	17-22
25121341-6	2014	These copolymers were further conjugated through disulfide bonds to a Her-2 targeting moiety, Her-2 affibody.	Disulfides	49-58	erb-b2 receptor tyrosine kinase 2	Homo sapiens	70-75
25121341-6	2014	These copolymers were further conjugated through disulfide bonds to a Her-2 targeting moiety, Her-2 affibody.	Disulfides	49-58	erb-b2 receptor tyrosine kinase 2	Homo sapiens	94-99
25086035-11	2014	Furthermore, because disulfide-cross-linked aggregates of GAPDH arise in many disorders and because methionine 46 is irrelevant to native GAPDH function, mutation of methionine 46 in models of disease should allow the unequivocal assessment of whether GAPDH aggregation influences disease progression.	Disulfides	21-30	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	58-63
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	35-44	superoxide dismutase 1	Homo sapiens	9-13
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	35-44	superoxide dismutase 1	Homo sapiens	15-20
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	111-120	superoxide dismutase 1	Homo sapiens	9-13
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	111-120	superoxide dismutase 1	Homo sapiens	15-20
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	154-164	superoxide dismutase 1	Homo sapiens	9-13
25096579-4	2014	In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation.	Disulfides	154-164	superoxide dismutase 1	Homo sapiens	15-20
25096579-6	2014	Here, we adapt recently developed single-bond chemistry techniques to study individual disulfide isomerization reactions in hSOD1.	Disulfides	87-96	superoxide dismutase 1	Homo sapiens	124-129
25096579-7	2014	Mechanical unfolding of hSOD1 leads to the formation of a polypeptide loop held by the disulfide.	Disulfides	87-96	superoxide dismutase 1	Homo sapiens	24-29
24800789-10	2014	Structural and mutation analyses suggest that the formation of an intramolecular disulfide bridge regulates AtTPPD activity.	Disulfides	81-90	Haloacid dehalogenase-like hydrolase (HAD) superfamily protein	Arabidopsis thaliana	108-114
25130463-2	2014	The interaction of ERp57 with calreticulin is believed to assist disulfide bond formation of nascent glycoprotein in the ER.	Disulfides	65-74	calreticulin	Homo sapiens	30-42
25179308-8	2014	The linker connecting the polymer to the protein nanoparticle contained a disulfide bond thus allowing polymer shedding and subsequent Cytochrome c release under intracellular reducing conditions.	Disulfides	74-83	cytochrome c, somatic	Homo sapiens	135-147
25053414-0	2014	Cysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity.	Disulfides	144-153	ATP binding cassette subfamily B member 1	Homo sapiens	63-77
25026075-3	2014	One of the key challenges in the development of an effective HIV vaccine is the presence of the complex set of post-translational modifications (PTMs) on Env, namely, glycosylation and disulfide bonds, that affect protein folding, epitope accessibility, and immunogenecity.	Disulfides	185-194	endogenous retrovirus group W member 1, envelope	Homo sapiens	154-157
25026075-9	2014	The finding that disulfide bonding is consistently heterogeneous in these proteins is perhaps the most significant outcome of these studies; this disulfide heterogeneity has been reported for multiple other recombinant gp140s, and it is likely present in most recombinantly expressed Env immunogens.	Disulfides	17-26	endogenous retrovirus group W member 1, envelope	Homo sapiens	284-287
25026075-9	2014	The finding that disulfide bonding is consistently heterogeneous in these proteins is perhaps the most significant outcome of these studies; this disulfide heterogeneity has been reported for multiple other recombinant gp140s, and it is likely present in most recombinantly expressed Env immunogens.	Disulfides	146-155	endogenous retrovirus group W member 1, envelope	Homo sapiens	284-287
25138527-4	2014	Without any protein separation, the disulfide linkages of several cytotoxins and PLA2 could be solved, including more than 20 disulfide bonds.	Disulfides	36-45	phospholipase A2 group IB	Homo sapiens	81-85
25138527-4	2014	Without any protein separation, the disulfide linkages of several cytotoxins and PLA2 could be solved, including more than 20 disulfide bonds.	Disulfides	126-135	phospholipase A2 group IB	Homo sapiens	81-85
24941337-7	2014	This effect was completely reversed by treatment with the reducing agent dithiothreitol, indicating that S-glutathionylation of STAT3 was related to formation of protein-mixed disulfides.	Disulfides	176-186	signal transducer and activator of transcription 3	Homo sapiens	128-133
24954167-8	2014	Importantly, only HMGB1 in its partially oxidized isoform (disulfide HMGB1), which activates toll-like receptor 4 (TLR4), but not in its fully reduced or fully oxidized isoforms, evoked mechanical hypersensitivity upon i.t.	Disulfides	59-68	toll-like receptor 4	Mus musculus	93-113
24954167-8	2014	Importantly, only HMGB1 in its partially oxidized isoform (disulfide HMGB1), which activates toll-like receptor 4 (TLR4), but not in its fully reduced or fully oxidized isoforms, evoked mechanical hypersensitivity upon i.t.	Disulfides	59-68	toll-like receptor 4	Mus musculus	115-119
24998777-3	2014	TIMP-1 is an N-glycosylated protein that folds into two functional domains, a C- and an N-terminal domain, with six disulfide bonds.	Disulfides	116-125	TIMP metallopeptidase inhibitor 1	Homo sapiens	0-6
25135935-6	2014	Cotranslational N-glycosylation by the STT3A isoform of the OST, which lacks MagT1, allows efficient modification of acceptor sites in cysteine-rich protein domains before disulfide bond formation.	Disulfides	172-181	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	60-63
24814218-0	2014	Type AII lantibiotic bovicin HJ50 with a rare disulfide bond: structure, structure-activity relationships and mode of action.	Disulfides	46-55	NLR family pyrin domain containing 3	Homo sapiens	5-8
24962346-1	2014	Disulfide-containing IgG-, Fc-, or albumin-based prodrugs that rely on FcRn-trafficking by endothelial cells for prolonged circulation in the body might be hampered by premature bio-reduction processes during FcRn-mediated recycling events.	Disulfides	0-9	Fc gamma receptor and transporter	Homo sapiens	71-75
24962346-1	2014	Disulfide-containing IgG-, Fc-, or albumin-based prodrugs that rely on FcRn-trafficking by endothelial cells for prolonged circulation in the body might be hampered by premature bio-reduction processes during FcRn-mediated recycling events.	Disulfides	0-9	Fc gamma receptor and transporter	Homo sapiens	209-213
25017908-8	2014	However, this segment of coelacanth C-peptide possesses a unique Cys distribution, capable of forming a disulfide-stabilized turn.	Disulfides	104-113	insulin	Homo sapiens	36-45
24997578-4	2014	The bicyclic tetrapeptides disulfide showed potent HDAC1 and HDAC4 inhibition and p21 promoting activity.	Disulfides	27-36	histone deacetylase 1	Homo sapiens	51-56
25109988-7	2014	The consequences of the regulation of the FOXO4 (forkhead box O4) transcription factor by formation of intermolecular disulfides with both TNPO1 (transportin 1) and p300/CBP [CREB (cAMP-response-element-binding protein)-binding protein] are discussed in more detail.	Disulfides	118-128	CREB binding protein	Homo sapiens	170-173
24957739-0	2014	2-nitroveratryl as a photocleavable thiol-protecting group for directed disulfide bond formation in the chemical synthesis of insulin.	Disulfides	72-81	insulin	Homo sapiens	126-133
24661926-6	2014	The disulfide loop and the basic amino acids in the LPS-binding domain (LBD) of ALF played key roles in its antibacterial activities.	Disulfides	4-13	general transcription factor IIA subunit 1 like	Homo sapiens	80-83
25073928-2	2014	To critically examine the widely held assumption that reduced ER glutathione fuels disulfide reduction, we expressed a modified form of a cytosolic glutathione-degrading enzyme, ChaC1, in the ER lumen.	Disulfides	83-92	ChaC glutathione specific gamma-glutamylcyclotransferase 1	Homo sapiens	178-183
24973725-11	2014	These results suggest that thiol groups of hemoglobin cause splitting of the disulfide bonds of insulin which immediately leads to the formation of new intramolecular disulfide bridges, a reaction which occurs in hemolytic blood and may explain the gradual loss of insulin in postmortem blood samples.	Disulfides	77-86	insulin	Homo sapiens	96-103
24973725-11	2014	These results suggest that thiol groups of hemoglobin cause splitting of the disulfide bonds of insulin which immediately leads to the formation of new intramolecular disulfide bridges, a reaction which occurs in hemolytic blood and may explain the gradual loss of insulin in postmortem blood samples.	Disulfides	77-86	insulin	Homo sapiens	265-272
24973725-11	2014	These results suggest that thiol groups of hemoglobin cause splitting of the disulfide bonds of insulin which immediately leads to the formation of new intramolecular disulfide bridges, a reaction which occurs in hemolytic blood and may explain the gradual loss of insulin in postmortem blood samples.	Disulfides	167-176	insulin	Homo sapiens	96-103
24973725-11	2014	These results suggest that thiol groups of hemoglobin cause splitting of the disulfide bonds of insulin which immediately leads to the formation of new intramolecular disulfide bridges, a reaction which occurs in hemolytic blood and may explain the gradual loss of insulin in postmortem blood samples.	Disulfides	167-176	insulin	Homo sapiens	265-272
24847059-8	2014	An insect cell GPIHBP1 expression system confirmed the propensity of GPIHBP1-S107C to form disulfide-linked dimers and to form multimers.	Disulfides	91-100	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	69-76
24731058-6	2014	Cyt c was chemically conjugated to galactosylated albumin with a reducible disulfide linker in order to release Cyt c from the carrier inside cells.	Disulfides	75-84	cytochrome c, somatic	Homo sapiens	0-5
24847059-2	2014	The ability of GPIHBP1 to bind LPL depends on the Ly6 domain, a three-fingered structure containing 10 cysteines and a conserved pattern of disulfide bond formation.	Disulfides	140-149	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	15-22
24847059-7	2014	However, nearly all of the GPIHBP1-S107C on the cell surface was in the form of disulfide-linked dimers and multimers, whereas wild-type GPIHBP1 was predominantly monomeric.	Disulfides	80-89	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	27-34
24927250-5	2014	We report here the design and synthesis of new pro-drugs, derived from co-drugs combining a NEP and an APN inhibitor through a disulfide bond with side chains improving oral bioavailability.	Disulfides	127-136	membrane metalloendopeptidase	Homo sapiens	92-95
25120086-1	2014	The chemical structure of lipoprotein (a) is similar to that of LDL, from which it differs due to the presence of apolipoprotein (a) bound to apo B100 via one disulfide bridge.	Disulfides	159-168	apolipoprotein B	Homo sapiens	142-150
24636884-2	2014	Peroxiredoxin 2 (Prx2) is a major antioxidant enzyme that requires NADPH to recycle its oxidized (disulfide-bonded) form.	Disulfides	98-107	peroxiredoxin 2	Homo sapiens	0-15
24636884-2	2014	Peroxiredoxin 2 (Prx2) is a major antioxidant enzyme that requires NADPH to recycle its oxidized (disulfide-bonded) form.	Disulfides	98-107	peroxiredoxin 2	Homo sapiens	17-21
24731058-6	2014	Cyt c was chemically conjugated to galactosylated albumin with a reducible disulfide linker in order to release Cyt c from the carrier inside cells.	Disulfides	75-84	cytochrome c, somatic	Homo sapiens	112-117
24805286-2	2014	PhA molecules were chemically conjugated with biarmed linkages at one end of the mPEG molecule via disulfide bonds.	Disulfides	99-108	lamin B receptor	Homo sapiens	0-3
24805286-5	2014	However, the dissociation of the NP structure was effectively induced by the cleavage of the disulfide bonds in response to intracellular reductive conditions, triggering the rapid release of PhA molecules in a photoactive form.	Disulfides	93-102	lamin B receptor	Homo sapiens	192-195
24632414-0	2014	Disulfide bonds regulate binding of exogenous ligand to human cytoglobin.	Disulfides	0-9	cytoglobin	Homo sapiens	62-72
24856301-0	2014	An iodine-free and directed-disulfide-bond-forming route to insulin analogues.	Disulfides	28-37	insulin	Homo sapiens	60-67
24856301-1	2014	An iodine-free synthetic route to insulin analogues has been established via a directed disulfide bond formation strategy.	Disulfides	88-97	insulin	Homo sapiens	34-41
24820935-4	2014	In this work, the dissociation of disulfide-linked peptide dimers produced by peptic digestion of the 80 kDa glycoprotein transferrin in the course of HDX MS experiments is carried out using electron capture dissociation (ECD).	Disulfides	34-43	transferrin	Homo sapiens	122-133
24632414-10	2014	We concluded that polymerization could be a mechanism that triggers the exertion of various physiological functions of this protein and that an appropriate disulfide bond between the two cysteine residues was critical for regulating the binding affinity of Cgb, which can act as a ROS scavenger, for exogenous ligands.	Disulfides	156-165	cytoglobin	Homo sapiens	257-260
24855952-6	2014	We provide evidence that mCRY1/mPER2 complex formation is modulated by an interplay of zinc binding and mCRY1 disulfide bond formation, which may be influenced by the redox state of the cell.	Disulfides	110-119	period circadian clock 2	Mus musculus	31-36
24719319-7	2014	Mass spectrometry analysis revealed that treatment of disulfide-oxidized Prx2 with excess peroxynitrite renders mainly mononitrated and dinitrated species.	Disulfides	54-63	peroxiredoxin 2	Homo sapiens	73-77
24569069-6	2014	Additionally, the binding of PAC induced the conformational changes of disulfide bridges of HSA with the decrease of alpha-helix content.	Disulfides	71-80	albumin	Homo sapiens	92-95
24456905-10	2014	Two types of targets of disulfide stress were identified: redox buffers, such as ribonuclease inhibitor or albumin, and redox-signaling thiols, which include thioredoxin 1, APE1/Ref1, Keap1, tyrosine and serine/threonine phosphatases, and protein disulfide isomerase.	Disulfides	24-33	kelch like ECH associated protein 1	Homo sapiens	184-189
24084572-4	2014	The affected cysteine is highly conserved across vertebrates and its mutation is predicted to abolish a disulfide bond that defines the tertiary structure of fibulin-1.	Disulfides	104-113	fibulin 1	Homo sapiens	158-167
24793051-0	2014	Study on the disulfide bond and disulfide loop of native and mutated SOD1 protein.	Disulfides	13-22	superoxide dismutase 1	Homo sapiens	69-73
24793051-0	2014	Study on the disulfide bond and disulfide loop of native and mutated SOD1 protein.	Disulfides	32-41	superoxide dismutase 1	Homo sapiens	69-73
24793051-2	2014	The disulfide bond in SOD1 is essential to maintain the structural stability of protein and its proper folding.	Disulfides	4-13	superoxide dismutase 1	Homo sapiens	22-26
24615765-1	2014	The chemical synthesis of insulin has been a longstanding challenge, mainly because of the notorious hydrophobicity of the A chain and the complicated topology of this 51-mer peptide hormone consisting of two chains and three disulfide bonds.	Disulfides	226-235	insulin	Homo sapiens	26-33
23900850-8	2014	Zebrafish CXL1 (zCXL1) has three disulfides that appear to be important for a stable structure.	Disulfides	33-43	CX chemokine ligand 34b, duplicate 11	Danio rerio	10-14
23900850-8	2014	Zebrafish CXL1 (zCXL1) has three disulfides that appear to be important for a stable structure.	Disulfides	33-43	CX chemokine ligand 34b, duplicate 11	Danio rerio	16-21
24755153-8	2014	Functional significance of glutathionylation in intact vessels was supported by Ang II-induced impairment of endothelium-dependent vasorelaxation that was abolished by the disulfide reducing agent, dithiothreitol.	Disulfides	172-181	angiotensinogen	Homo sapiens	80-86
24685145-4	2014	Here, we show that N33/Tusc3 possesses a membrane-anchored N-terminal thioredoxin domain located in the ER lumen that may form transient mixed disulfide complexes with OST substrates.	Disulfides	143-152	dolichyl-diphosphooligosaccharide--protein glycosyltransferase non-catalytic subunit	Homo sapiens	168-171
24439038-8	2014	While the association with keratin as well as the cohesive self-assembly of Krtap11-1 appeared to be stabilized by disulfide cross-links, the biotinylated Krtap11-1 probe enabled the adherence to certain type I keratins in the hair cortex, including K31, 33 and 34, in the absence of disulfide formation.	Disulfides	115-124	keratin associated protein 11-1	Mus musculus	76-85
27919037-1	2014	In the ER (endoplasmic reticulum) of human cells, disulfide bonds are predominantly generated by the two isoforms of Ero1 (ER oxidoreductin-1): Ero1alpha and Ero1beta.	Disulfides	50-59	endoplasmic reticulum oxidoreductase 1 beta	Homo sapiens	158-166
27919037-4	2014	Ero1beta contains an additional cysteine residue (Cys262), which has been suggested to engage in an isoform-specific regulatory disulfide bond with Cys100 However, we show that the two regulatory disulfide bonds in Ero1alpha are likely conserved in Ero1beta (Cys90-Cys130 and Cys95-Cys100).	Disulfides	128-137	endoplasmic reticulum oxidoreductase 1 beta	Homo sapiens	0-8
27919037-4	2014	Ero1beta contains an additional cysteine residue (Cys262), which has been suggested to engage in an isoform-specific regulatory disulfide bond with Cys100 However, we show that the two regulatory disulfide bonds in Ero1alpha are likely conserved in Ero1beta (Cys90-Cys130 and Cys95-Cys100).	Disulfides	128-137	endoplasmic reticulum oxidoreductase 1 beta	Homo sapiens	249-257
27919037-4	2014	Ero1beta contains an additional cysteine residue (Cys262), which has been suggested to engage in an isoform-specific regulatory disulfide bond with Cys100 However, we show that the two regulatory disulfide bonds in Ero1alpha are likely conserved in Ero1beta (Cys90-Cys130 and Cys95-Cys100).	Disulfides	196-205	endoplasmic reticulum oxidoreductase 1 beta	Homo sapiens	0-8
27919037-4	2014	Ero1beta contains an additional cysteine residue (Cys262), which has been suggested to engage in an isoform-specific regulatory disulfide bond with Cys100 However, we show that the two regulatory disulfide bonds in Ero1alpha are likely conserved in Ero1beta (Cys90-Cys130 and Cys95-Cys100).	Disulfides	196-205	endoplasmic reticulum oxidoreductase 1 beta	Homo sapiens	249-257
27919037-8	2014	We propose that features other than a distinct pattern of regulatory disulfide bonds determine the loose redox regulation of Ero1beta relative to Ero1alpha.	Disulfides	69-78	endoplasmic reticulum oxidoreductase 1 beta	Homo sapiens	125-133
24439038-8	2014	While the association with keratin as well as the cohesive self-assembly of Krtap11-1 appeared to be stabilized by disulfide cross-links, the biotinylated Krtap11-1 probe enabled the adherence to certain type I keratins in the hair cortex, including K31, 33 and 34, in the absence of disulfide formation.	Disulfides	284-293	keratin associated protein 11-1	Mus musculus	155-164
26989723-2	2014	VEGF is a highly conserved, disulfide-bonded dimeric glycoprotein of 34 to 45 kDa produced by several cell types including fibroblasts, neutrophils, endothelial cells, and peripheral blood mononuclear cells, particularly T lymphocytes and macrophages.	Disulfides	28-37	vascular endothelial growth factor A	Homo sapiens	0-4
24486813-14	2014	AMS-modification and far-UV CD spectroscopic analyses suggested that ESP4 has an intramolecular disulfide bridge and a helical structure, respectively.	Disulfides	96-105	exocrine gland secreted peptide 4	Mus musculus	69-73
24549831-0	2014	Thiol-disulfide exchange in peptides derived from human growth hormone.	Disulfides	6-15	growth hormone 1	Homo sapiens	56-70
24549831-4	2014	Here, we present experimental data for the mechanism of thiol-disulfide exchange in tryptic peptides derived from human growth hormone in aqueous solution.	Disulfides	62-71	growth hormone 1	Homo sapiens	120-134
24501222-0	2014	Crystal structure of histidine-rich glycoprotein N2 domain reveals redox activity at an interdomain disulfide bridge: implications for angiogenic regulation.	Disulfides	100-109	histidine-rich glycoprotein	Oryctolagus cuniculus	21-48
24412276-11	2014	Disulfide cross-linking analysis of cysteines W356C(TM6) and W1145C(TM12) suggest that the V232D mutation inhibits maturation by trapping CFTR as a partially folded intermediate.	Disulfides	0-9	CF transmembrane conductance regulator	Homo sapiens	138-142
24337902-1	2014	In hyperhomocysteinemic patients, after reaction with homocysteine-albumin mixed disulfides (HSS-ALB), mesna (MSH) forms the mixed disulfide with Hcy (HSSM) which can be removed by renal clearance, thus reducing the plasma concentration of total homocysteine (tHcy).	Disulfides	81-91	msh homeobox 2	Homo sapiens	110-113
24412408-7	2014	Non-denaturing electrophoresis and MALDI-TOF MS analysis demonstrated that the purified rhEpo had two intra-disulfide bonds identical to those of the native hEpo.	Disulfides	108-117	erythropoietin	Homo sapiens	89-93
24241534-5	2014	Mechanistically, XBP1s promotes adiponectin multimerization rather than activating its transcription, likely through a direct regulation of the expression of several ER chaperones involved in adiponectin maturation, including glucose-regulated protein 78 kDa, protein disulfide isomerase family A, member 6, ER protein 44, and disulfide bond oxidoreductase A-like protein.	Disulfides	268-277	X-box binding protein 1	Mus musculus	17-21
24337902-1	2014	In hyperhomocysteinemic patients, after reaction with homocysteine-albumin mixed disulfides (HSS-ALB), mesna (MSH) forms the mixed disulfide with Hcy (HSSM) which can be removed by renal clearance, thus reducing the plasma concentration of total homocysteine (tHcy).	Disulfides	81-90	msh homeobox 2	Homo sapiens	110-113
24311274-2	2014	DEF5, a 32-residue peptide adopting a three-stranded beta-sheet fold stabilized by three internal disulfide bonds, is not efficiently produced by recombinant expression techniques and is, therefore, an interesting goal for chemical synthesis.	Disulfides	98-107	defensin alpha 5	Homo sapiens	0-4
24257748-3	2014	CD4 is a type I transmembrane glycoprotein, with four extracellular immunoglobulin-like domains containing three intrachain disulfide bridges.	Disulfides	124-133	CD4 molecule	Homo sapiens	0-3
24283831-2	2014	It has been suggested that these free thiols function to regulate the self-association of VWF through thiol-disulfide exchange (J Biol Chem, 7, 2007, 35604; Blood, 118, 5312).	Disulfides	108-117	von Willebrand factor	Homo sapiens	90-93
24341642-4	2014	The chemically modified IL-4 analogues consist of (1) mixed disulfides created by refolding IL-4 cysteine muteins in the presence of different thiol compounds or (2) maleimide conjugates created by modifying cysteine muteins with maleimide derivatives.	Disulfides	60-70	interleukin 4	Homo sapiens	24-28
24494201-7	2014	Neither metabolic stress nor UA supplementation altered mRNA or protein levels of glutaredoxin-1, the principal enzyme responsible for the reduction of mixed disulfides between glutathione and protein thiols in these cells.	Disulfides	158-168	glutaredoxin	Mus musculus	82-96
24409188-3	2014	Thioredoxin interacting protein (Txnip/thioredoxin binding protein-2/vitamin D3 upregulated protein) directly binds to Trx1 and Trx2 (Trx) and inhibit the reducing activity of Trx through their disulfide exchange.	Disulfides	194-203	thioredoxin interacting protein	Homo sapiens	33-38
24409188-3	2014	Thioredoxin interacting protein (Txnip/thioredoxin binding protein-2/vitamin D3 upregulated protein) directly binds to Trx1 and Trx2 (Trx) and inhibit the reducing activity of Trx through their disulfide exchange.	Disulfides	194-203	thioredoxin interacting protein	Homo sapiens	39-68
24300993-1	2014	The thylakoid protein LTO1/AtVKOR-DsbA is recently found to be an oxidoreductase involved in disulfide bond formation and the assembly of photosystem II (PSII) in Arabidopsis thaliana.	Disulfides	93-102	oxidoreductase	Arabidopsis thaliana	66-80
24268202-0	2014	p53 mediated apoptosis by reduction sensitive shielding ternary complexes based on disulfide linked PEI ternary complexes.	Disulfides	83-92	tumor protein p53	Homo sapiens	0-3
23978514-10	2014	Subsequently, use of another low pH labeling reagent, 4,4-dithiopyridine (4-DTP) helped identify novel disulfide linkages providing evidence that hYVH1 utilizes a disulfide exchange mechanism to prevent irreversible oxidation of the catalytic Cys residue in the active site.	Disulfides	103-112	dual specificity phosphatase 12	Homo sapiens	146-151
23978514-10	2014	Subsequently, use of another low pH labeling reagent, 4,4-dithiopyridine (4-DTP) helped identify novel disulfide linkages providing evidence that hYVH1 utilizes a disulfide exchange mechanism to prevent irreversible oxidation of the catalytic Cys residue in the active site.	Disulfides	163-172	dual specificity phosphatase 12	Homo sapiens	146-151
24257748-6	2014	We found that CD4 retro-translocates with oxidized intrachain disulfide bridges, and only upon proteasomal inhibition does it accumulate in the cytosol as already reduced and deglycosylated molecules.	Disulfides	62-71	CD4 molecule	Homo sapiens	14-17
24101560-7	2014	The conserved region of Delta6-fatty acid desaturase included three conserved histidine-rich domain, hydropathy profile, and was rich in disulfide bonds.	Disulfides	137-146	fatty acid desaturase 2	Homo sapiens	30-52
25307213-7	2014	Since redox-sensitive processes may be involved in signaling disassembly of higher-order structures of P-gp, we feel that manipulating redox signaling, via specific protein targeting at the BBB, may protect disulfide bond integrity of P-gp reservoirs and control trafficking to the membrane surface, providing improved CNS drug delivery.	Disulfides	207-216	ATP binding cassette subfamily B member 1	Homo sapiens	103-107
25307213-7	2014	Since redox-sensitive processes may be involved in signaling disassembly of higher-order structures of P-gp, we feel that manipulating redox signaling, via specific protein targeting at the BBB, may protect disulfide bond integrity of P-gp reservoirs and control trafficking to the membrane surface, providing improved CNS drug delivery.	Disulfides	207-216	ATP binding cassette subfamily B member 1	Homo sapiens	235-239
25818000-2	2014	The effects of PRG4 disulfide-bonded structure on viscosity and viscosity of newly available full-length recombinant human PRG4 (rhPRG4) have not previously been reported.	Disulfides	20-29	proteoglycan 4	Homo sapiens	123-127
24210874-3	2014	VEGF was successfully encapsulated into microcrystals derived from insect cypovirus with overexpression of protein disulfide bond isomerase.	Disulfides	115-124	vascular endothelial growth factor A	Homo sapiens	0-4
25483965-5	2014	A combination of biochemical assays, redox titrations, and site-directed mutagenesis revealed that Atg4 is regulated by oxidoreduction of a single disulfide bond between Cys338 and Cys394.	Disulfides	147-156	cysteine protease ATG4	Saccharomyces cerevisiae S288C	99-103
25483965-6	2014	This disulfide has a low redox potential and is very efficiently reduced by thioredoxin, suggesting that this oxidoreductase plays an important role in Atg4 regulation.	Disulfides	5-14	cysteine protease ATG4	Saccharomyces cerevisiae S288C	152-156
25818000-5	2014	RESULTS: PRG4 demonstrated shear-dependent viscosity at high concentrations, but Newtonian behaviour at low concentrations and when disulfide-bonded/multimeric structure was disrupted by R/A.	Disulfides	132-141	proteoglycan 4	Homo sapiens	9-13
25818000-9	2014	Effects of PRG4 on HA solution viscosity were dependent on PRG4"s disulfide-bonded structure.	Disulfides	66-75	proteoglycan 4	Homo sapiens	11-15
25818000-9	2014	Effects of PRG4 on HA solution viscosity were dependent on PRG4"s disulfide-bonded structure.	Disulfides	66-75	proteoglycan 4	Homo sapiens	59-63
25412899-1	2014	The Arabidopsis thylakoid membrane bimodular oxidoreductase, AtVKOR, could catalyze disulfide bond formation, and its direct functional domain (thioredoxin-like domain) is located in the thylakoid lumen according to the topological structure.	Disulfides	84-93	oxidoreductase	Arabidopsis thaliana	45-59
25045530-4	2014	The CTLA-2alpha monomer was converted to a disulfide-bonded dimer in vitro and in vivo.	Disulfides	43-52	cytotoxic T lymphocyte-associated protein 2 alpha	Mus musculus	4-15
25045530-6	2014	A disulfide-bonded CTLA-2alpha/cathepsin L complex was isolated, and a cathepsin L subunit with a molecular weight of 24,000 was identified as the interactive enzyme protein.	Disulfides	2-11	cytotoxic T lymphocyte-associated protein 2 alpha	Mus musculus	19-30
25359082-6	2014	MALDI-TOF/TOF revealed that papain degraded LYS, giving rise to three IgE-binding fragments: LYS (22-129), LYS (34-96) and LYS (62-128) that likely remained linked through the disulfide bonds present in the LYS molecule.	Disulfides	176-185	lysozyme	Homo sapiens	44-47
24203231-7	2014	Besides, a monomeric glutathionylated form and a dimeric disulfide-bridged form of BolA2 can be preferentially reduced by the nucleo-cytoplasmic GrxS17.	Disulfides	57-66	BolA-like family protein	Arabidopsis thaliana	83-88
24559913-3	2014	Preproinsulin is cleaved by signal peptidase to form proinsulin that folds on the luminal side of the ER, forming three evolutionarily conserved disulfide bonds.	Disulfides	145-154	insulin	Homo sapiens	0-13
24559913-3	2014	Preproinsulin is cleaved by signal peptidase to form proinsulin that folds on the luminal side of the ER, forming three evolutionarily conserved disulfide bonds.	Disulfides	145-154	insulin	Homo sapiens	3-13
24256422-4	2013	By exposing disulfide-stabilized poly(methacrylic acid) nanoporous polymer particles (PMASH NPPs) to complete cell growth media containing 10% fetal bovine serum, a protein corona, with the most abundant component being bovine serum albumin, was characterized.	Disulfides	12-21	albumin	Homo sapiens	227-240
24308268-5	2013	This study reports the conformation of lipid-free human apoA-I using lysine-to-lysine chemical cross-linking in conjunction with disulfide cross-linking achieved using selective cysteine mutations.	Disulfides	129-138	apolipoprotein A1	Homo sapiens	56-62
24279864-1	2013	Copper thiolate/disulfide interconversions are related to the functions of several important proteins such as human Sco1, Cu-Zn superoxide dismutase (SOD1), and mammalian zinc-bonded metallothionein.	Disulfides	16-25	synthesis of cytochrome C oxidase 1	Homo sapiens	116-120
24279864-1	2013	Copper thiolate/disulfide interconversions are related to the functions of several important proteins such as human Sco1, Cu-Zn superoxide dismutase (SOD1), and mammalian zinc-bonded metallothionein.	Disulfides	16-25	superoxide dismutase 1	Homo sapiens	122-148
24279864-1	2013	Copper thiolate/disulfide interconversions are related to the functions of several important proteins such as human Sco1, Cu-Zn superoxide dismutase (SOD1), and mammalian zinc-bonded metallothionein.	Disulfides	16-25	superoxide dismutase 1	Homo sapiens	150-154
24299064-9	2013	The AChE-catalyzed hydrolysis of acetylthiocholine to the thiol-functionalized thiocholine enabled the probing of the enzymatic activity of AChE through the hemin/G-quadruplex-catalyzed aerobic oxidation of thiocholine to the respective disulfide and the concomitant generation of the fluorescent resorufin product.	Disulfides	237-246	acetylcholinesterase (Cartwright blood group)	Homo sapiens	4-8
24299064-9	2013	The AChE-catalyzed hydrolysis of acetylthiocholine to the thiol-functionalized thiocholine enabled the probing of the enzymatic activity of AChE through the hemin/G-quadruplex-catalyzed aerobic oxidation of thiocholine to the respective disulfide and the concomitant generation of the fluorescent resorufin product.	Disulfides	237-246	acetylcholinesterase (Cartwright blood group)	Homo sapiens	140-144
24188028-1	2013	Insulin-like peptide 5 (INSL5) is a complex two-chain peptide hormone constrained by three disulfide bonds in a pattern identical to insulin.	Disulfides	91-100	insulin like 5	Homo sapiens	0-22
24188028-1	2013	Insulin-like peptide 5 (INSL5) is a complex two-chain peptide hormone constrained by three disulfide bonds in a pattern identical to insulin.	Disulfides	91-100	insulin like 5	Homo sapiens	24-29
24188028-7	2013	Given these difficulties, we have developed a highly active INSL5 analogue that has a much simpler structure with two disulfide bonds and is thus easier to assemble compared to native INSL5.	Disulfides	118-127	insulin like 5	Homo sapiens	60-65
24409177-5	2013	GILT reduces protein disulfide bonds in the endocytic compartment, exposing additional epitopes for binding to MHC class II and facilitating antigen presentation.	Disulfides	21-30	IFI30 lysosomal thiol reductase	Homo sapiens	0-4
24349312-1	2013	Human relaxin-3 is a neuropeptide that is structurally similar to human insulin with two chains (A and B) connected by three disulfide bonds.	Disulfides	125-134	insulin	Homo sapiens	72-79
24236702-7	2013	In vitro digestion indicated that MDA could induce non-disulfide covalent polymer of SPI, which could not be digested by pepsin and pancreatin.	Disulfides	55-64	chromogranin A	Homo sapiens	85-88
24409178-2	2013	Gamma-interferon-inducible lysosomal thiol reductase (GILT) reduces protein disulfide bonds in the endocytic compartment, thereby exposing buried epitopes for MHC class II binding and presentation.	Disulfides	76-85	IFI30 lysosomal thiol reductase	Homo sapiens	0-52
24409178-2	2013	Gamma-interferon-inducible lysosomal thiol reductase (GILT) reduces protein disulfide bonds in the endocytic compartment, thereby exposing buried epitopes for MHC class II binding and presentation.	Disulfides	76-85	IFI30 lysosomal thiol reductase	Homo sapiens	54-58
24490732-2	2013	The ability of both AGR2 and ERp57/GRP58 to catalyze the formation of disulfide bonds in proteins is the parameter most important for assigning them to a PDI family.	Disulfides	70-79	protein disulfide isomerase family A member 3	Homo sapiens	29-34
24490732-2	2013	The ability of both AGR2 and ERp57/GRP58 to catalyze the formation of disulfide bonds in proteins is the parameter most important for assigning them to a PDI family.	Disulfides	70-79	protein disulfide isomerase family A member 3	Homo sapiens	35-40
24008134-0	2013	Reduction of the internal disulfide bond between Cys 38 and 83 switches the ligand migration pathway in cytoglobin.	Disulfides	26-35	cytoglobin	Homo sapiens	104-114
24008134-3	2013	Photo-acoustic and transient absorption data show that disulfide bond formation alters the ligand migration pathway(s) as evident from the distinct geminate quantum yields (Phigem=0.35 for Cygb(ox) and Phigem=0.63 for Cygb(red)) and rate constants for bimolecular CO rebinding.	Disulfides	55-64	cytoglobin	Homo sapiens	189-193
24008134-3	2013	Photo-acoustic and transient absorption data show that disulfide bond formation alters the ligand migration pathway(s) as evident from the distinct geminate quantum yields (Phigem=0.35 for Cygb(ox) and Phigem=0.63 for Cygb(red)) and rate constants for bimolecular CO rebinding.	Disulfides	55-64	cytoglobin	Homo sapiens	218-222
24008134-5	2013	These results demonstrate that the disulfide bond connecting helix E and helix B modulates the conformational dynamics in Cygb including the size and energy barrier between the internal hydrophobic sites.	Disulfides	35-44	cytoglobin	Homo sapiens	122-126
24206272-5	2013	We find these two cysteines (C98 and C107) form a disulfide in heterologously expressed human CB1, and this C98-C107 disulfide is much more accessible to reducing agents than the previously known disulfide in extracellular loop 2 (EL2).	Disulfides	50-59	cannabinoid receptor 1	Homo sapiens	94-97
24312339-7	2013	Based on a Sclerostin variant found in a Turkish family suffering from Sclerosteosis we generated a Sclerostin mutant with cysteines 84 and 142 exchanged thereby removing the third disulfide bond of the cystine-knot.	Disulfides	181-190	sclerostin	Homo sapiens	100-110
24106275-4	2013	As a complementary approach, we superimposed this panel of ADRP mutants onto a rhodopsin background containing a juxtaposed cysteine pair (N2C/D282C) that forms a disulfide bond.	Disulfides	163-172	rhodopsin	Homo sapiens	79-88
23604598-8	2013	We found that two cysteine residues, C87 and C320, in the ATD of the GluN2A subunit were required for the formation of disulfide bonds and GluN2A ATD homodimers.	Disulfides	119-128	glutamate ionotropic receptor NMDA type subunit 2A	Homo sapiens	69-75
24161674-3	2013	A disulfide dimer peptide of CXCL14(51-77) bound to CXCR4 with comparable affinity to full length CXCL14, and exhibited CXCL12 inhibitor activity.	Disulfides	2-11	C-X-C motif chemokine ligand 14	Homo sapiens	29-35
24161674-3	2013	A disulfide dimer peptide of CXCL14(51-77) bound to CXCR4 with comparable affinity to full length CXCL14, and exhibited CXCL12 inhibitor activity.	Disulfides	2-11	C-X-C motif chemokine ligand 14	Homo sapiens	98-104
24206272-5	2013	We find these two cysteines (C98 and C107) form a disulfide in heterologously expressed human CB1, and this C98-C107 disulfide is much more accessible to reducing agents than the previously known disulfide in extracellular loop 2 (EL2).	Disulfides	117-126	cannabinoid receptor 1	Homo sapiens	94-97
24206272-7	2013	The C98-C107 disulfide also alters the effects of allosteric ligands for CB1, Org 27569 and PSNCBAM-1.	Disulfides	13-22	cannabinoid receptor 1	Homo sapiens	73-76
24085763-4	2013	THPO has 4 conserved cysteines in its RBD that form 2 disulfide bonds.	Disulfides	54-63	thrombopoietin	Homo sapiens	0-4
24224005-0	2013	Novel disulfide bond-mediated dimerization of the CARD domain was revealed by the crystal structure of CARMA1 CARD.	Disulfides	6-15	caspase recruitment domain family member 11	Homo sapiens	103-109
24224005-4	2013	Here, we report the dimeric structure of CARMA1 CARD at a resolution of 3.2 A. Interestingly, although CARMA1 CARD has a canonical six helical-bundles structural fold similar to other CARDs, CARMA1 CARD shows the first homo-dimeric structure of CARD formed by a disulfide bond and reveals a possible biologically important homo-dimerization mechanism.	Disulfides	262-271	caspase recruitment domain family member 11	Homo sapiens	41-47
24224005-4	2013	Here, we report the dimeric structure of CARMA1 CARD at a resolution of 3.2 A. Interestingly, although CARMA1 CARD has a canonical six helical-bundles structural fold similar to other CARDs, CARMA1 CARD shows the first homo-dimeric structure of CARD formed by a disulfide bond and reveals a possible biologically important homo-dimerization mechanism.	Disulfides	262-271	caspase recruitment domain family member 11	Homo sapiens	103-109
24224005-4	2013	Here, we report the dimeric structure of CARMA1 CARD at a resolution of 3.2 A. Interestingly, although CARMA1 CARD has a canonical six helical-bundles structural fold similar to other CARDs, CARMA1 CARD shows the first homo-dimeric structure of CARD formed by a disulfide bond and reveals a possible biologically important homo-dimerization mechanism.	Disulfides	262-271	caspase recruitment domain family member 11	Homo sapiens	103-109
24077854-8	2013	By adjusting the settings, the EC reaction efficiency was gradually changed from partial to full disulfide bonds reduction in alpha-lactalbumin, and the expected shift in charge state distribution has been demonstrated.	Disulfides	97-106	lactalbumin alpha	Homo sapiens	126-143
24037759-2	2013	The current model for insulin receptor activation is that two distinct surfaces of insulin monomer engage sequentially with two distinct binding sites on the extracellular surface of the insulin receptor, which is itself a disulfide-linked (alphabeta)2 homodimer.	Disulfides	223-232	insulin	Homo sapiens	22-29
24146662-2	2013	After biosynthesis, POMC undergoes several posttranslational modifications, including proteolytic cleavage, acetylation, amidation, phosphorylation, glycosylation, and disulfide linkage formation, which generate mature POMC-derived peptides.	Disulfides	168-177	proopiomelanocortin	Homo sapiens	20-24
23943880-4	2013	Interestingly, N-terminus tetramerization mediated by endogenous disulfide bond formation occurs in native RyR2, but notably not in RyR1.	Disulfides	65-74	ryanodine receptor 2	Homo sapiens	107-111
23883583-4	2013	Disulfide is the major product of MPO-mediated KYC oxidation.	Disulfides	0-9	myeloperoxidase	Homo sapiens	34-37
23571504-2	2013	We demonstrated recently that hBD-1 shows activity against enteric commensals and Candida species only after its disulfide bonds have been reduced by thioredoxin (TRX) or a reducing environment.	Disulfides	113-122	defensin beta 1	Homo sapiens	30-35
24022479-7	2013	Indeed, using three different variants of Ero1alpha, we find that expression of either wild-type or an Ero1alpha variant lacking regulatory disulfides can rescue mutant proinsulin-G(B23)V, in parallel with its ability to provide an oxidizing environment in the ER lumen, whereas beneficial effects were less apparent for a redox-inactive form of Ero1.	Disulfides	140-150	insulin	Homo sapiens	169-179
24101517-0	2013	Mitochondrial disulfide relay mediates translocation of p53 and partitions its subcellular activity.	Disulfides	14-23	tumor protein p53	Homo sapiens	56-59
24101517-2	2013	Here we report that the mammalian homolog of the yeast mitochondrial disulfide relay protein Mia40 (CHCHD4) is necessary for the respiratory-dependent translocation of p53 into the mitochondria.	Disulfides	69-78	tumor protein p53	Homo sapiens	168-171
24101517-5	2013	Thus, the mitochondrial disulfide relay system allows p53 to regulate two spatially segregated genomes depending on oxidative metabolic activity.	Disulfides	24-33	tumor protein p53	Homo sapiens	54-57
24167603-4	2013	By performing Raman spectroscopic measurements on purified insulin and glucagon, we showed that the 520 cm(-1) band assigned to disulfide bridges in insulin, and the 1552 cm(-1) band assigned to tryptophan in glucagon are mutually exclusive and could therefore be used as indirect markers for the label-free distinction between both hormones.	Disulfides	128-137	insulin	Homo sapiens	59-66
24167603-4	2013	By performing Raman spectroscopic measurements on purified insulin and glucagon, we showed that the 520 cm(-1) band assigned to disulfide bridges in insulin, and the 1552 cm(-1) band assigned to tryptophan in glucagon are mutually exclusive and could therefore be used as indirect markers for the label-free distinction between both hormones.	Disulfides	128-137	insulin	Homo sapiens	149-156
24167603-5	2013	High-resolution hyperspectral Raman imaging for these bands showed the distribution of disulfide bridges and tryptophan at sub-micrometer scale, which correlated with the location of insulin and glucagon as revealed by conventional immunohistochemistry.	Disulfides	87-96	insulin	Homo sapiens	183-190
24167603-7	2013	Although the use of separate microscope systems with different spatial resolution and the use of indirect Raman markers cause some image mismatch, our findings indicate that Raman bands for disulfide bridges and tryptophan can be used as distinctive markers for the label-free detection of insulin and glucagon in human islets of Langerhans.	Disulfides	190-199	insulin	Homo sapiens	290-297
24146829-6	2013	We found that a single disulfide bond strategically inserted between the highly conserved layers 1 and 2 (C65-C115) is able to "lock" gp120 in a CD4 receptor bound conformation (in the absence of CD4), as indicated by the lower dissociation constant (Kd) for the CD4-induced (CD4i) epitope binding 17b antibody.	Disulfides	23-32	CD4 molecule	Homo sapiens	145-157
24146829-6	2013	We found that a single disulfide bond strategically inserted between the highly conserved layers 1 and 2 (C65-C115) is able to "lock" gp120 in a CD4 receptor bound conformation (in the absence of CD4), as indicated by the lower dissociation constant (Kd) for the CD4-induced (CD4i) epitope binding 17b antibody.	Disulfides	23-32	CD4 molecule	Homo sapiens	145-148
24146829-6	2013	We found that a single disulfide bond strategically inserted between the highly conserved layers 1 and 2 (C65-C115) is able to "lock" gp120 in a CD4 receptor bound conformation (in the absence of CD4), as indicated by the lower dissociation constant (Kd) for the CD4-induced (CD4i) epitope binding 17b antibody.	Disulfides	23-32	CD4 molecule	Homo sapiens	196-199
24146829-7	2013	When disulfide-stabilized monomeric (gp120) and trimeric (gp140) Envs were used to immunize rabbits, they were found to elicit a higher proportion of antibodies directed against both CD4i and CD4 binding site epitopes than the wild-type proteins.	Disulfides	5-14	CD4 molecule	Homo sapiens	183-186
23895568-1	2013	These acyloxy nitroso compounds inhibit glyceraldehyde 3-phosphate dehydrogenase (GAPDH) by forming a reduction reversible active site disulfide and a reduction irreversible sulfinic acid or sulfinamide modification at Cys244.	Disulfides	135-144	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	40-80
24143259-0	2013	Disulfide scrambling in superoxide dismutase 1 reduces its cytotoxic effect in cultured cells and promotes protein aggregation.	Disulfides	0-9	superoxide dismutase 1	Homo sapiens	24-46
24143259-11	2013	Disulfide scrambling thus appears to be an important event for misfolding and aggregation of SOD1, but may also be significant for protein function involving cysteines, e.g. mitochondrial import and copper loading.	Disulfides	0-9	superoxide dismutase 1	Homo sapiens	93-97
23919584-11	2013	In cardiomyocytes, HNO achieved this effect by stabilizing PLN in an oligomeric disulfide bond-dependent configuration, decreasing the amount of free inhibitory monomeric PLN available.	Disulfides	80-89	phospholamban	Mus musculus	59-62
23802566-2	2013	Sod1 requires its specific chaperone Ccs1 and disulfide bond formation in order to be retained in the intermembrane space.	Disulfides	46-55	superoxide dismutase 1	Homo sapiens	0-4
24081982-0	2013	Orai3 TM3 point mutation G158C alters kinetics of 2-APB-induced gating by disulfide bridge formation with TM2 C101.	Disulfides	74-83	ORAI calcium release-activated calcium modulator 3	Homo sapiens	0-5
24081982-8	2013	We suggest that a disulfide bridge, formed between the introduced cysteine at TM3 position 158 and the endogenous cysteine at TM2 position 101, hinders transitions between Orai3 open and closed states.	Disulfides	18-27	ORAI calcium release-activated calcium modulator 3	Homo sapiens	172-177
23625804-0	2013	Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants.	Disulfides	115-124	superoxide dismutase 1	Homo sapiens	23-28
23838530-6	2013	On the basis of these observations, we designed and synthesized a YwlE inhibitor, denoted cyc-SeCN-amidine, that irreversibly inhibits YwlE (kinact/KI = 310 M(-1) min(-1)) by inducing disulfide bond formation between the two active site cysteine residues.	Disulfides	184-193	cytochrome c, somatic	Homo sapiens	90-93
23841778-1	2013	Human defensin 5 (HD5) is a 32-residue cysteine-rich host-defense peptide that exhibits three disulfide bonds in the oxidized form (HD5ox).	Disulfides	94-103	defensin alpha 5	Homo sapiens	6-16
23841778-1	2013	Human defensin 5 (HD5) is a 32-residue cysteine-rich host-defense peptide that exhibits three disulfide bonds in the oxidized form (HD5ox).	Disulfides	94-103	defensin alpha 5	Homo sapiens	18-21
23324801-8	2013	We suggest that efficient disulfide bond formation using the P. pastoris expression system improves the covalent dimer anti-TNF-VHH-Fc neutralizing activity.	Disulfides	26-35	tumor necrosis factor	Homo sapiens	124-127
24098777-4	2013	Stimulated Tregs, which naturally express GARP, and Th cells transfected with GARP secrete a previously unknown form of latent TGF-beta1 that is disulfide-linked to GARP.	Disulfides	145-154	transforming growth factor beta 1	Homo sapiens	127-136
23895568-1	2013	These acyloxy nitroso compounds inhibit glyceraldehyde 3-phosphate dehydrogenase (GAPDH) by forming a reduction reversible active site disulfide and a reduction irreversible sulfinic acid or sulfinamide modification at Cys244.	Disulfides	135-144	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	82-87
23798702-9	2013	Thus, physiological redox regulation of RyR1 by endogenously generated hydrogen peroxide is exerted through dynamic disulfide formation involving multiple Cys residues.	Disulfides	116-125	ryanodine receptor 1	Homo sapiens	40-44
23827315-2	2013	ER-60, which has been implicated in apoB degradation, is a protein disulfide isomerase (PDI) that forms or rearranges disulfide bonds in substrate proteins and also possesses cysteine protease activity.	Disulfides	67-76	protein disulfide isomerase family A member 3	Homo sapiens	0-5
23827315-2	2013	ER-60, which has been implicated in apoB degradation, is a protein disulfide isomerase (PDI) that forms or rearranges disulfide bonds in substrate proteins and also possesses cysteine protease activity.	Disulfides	67-76	apolipoprotein B	Homo sapiens	36-40
23780345-2	2013	It has been shown that a reduced intra-subunit disulfide bridge apo-SOD1 can rapidly initiate fibrillation forming an inter-subunits disulfide under mild, physiologically accessible conditions.	Disulfides	47-56	superoxide dismutase 1	Homo sapiens	68-72
23689258-8	2013	The soluble DsbA-like domain of LTO1 was found to have reduction, oxidation and isomerization activities, and could promote the formation of disulfide bonds in a lumenal protein, FKBP13.	Disulfides	141-150	FK506-binding protein 13	Arabidopsis thaliana	179-185
23780345-2	2013	It has been shown that a reduced intra-subunit disulfide bridge apo-SOD1 can rapidly initiate fibrillation forming an inter-subunits disulfide under mild, physiologically accessible conditions.	Disulfides	133-142	superoxide dismutase 1	Homo sapiens	68-72
23780345-3	2013	Once initiated, elongation can proceed via recruitment of either apo or partially metallated disulfide-intact SOD1 and the presence of copper, but not zinc, ions inhibit fibrillation.	Disulfides	93-102	superoxide dismutase 1	Homo sapiens	110-114
23756812-2	2013	Vertebrate glutaredoxin 2 is characterized by two extra cysteines that form an intra-molecular disulfide bridge.	Disulfides	95-104	glutaredoxin 2	Danio rerio	11-25
23713588-6	2013	The complex involved a stable non-covalent interaction that was disassociated by the reduction of intramolecular disulfides in ERp46, or by disruption of the decameric structure of hyperoxidized Prx2.	Disulfides	113-123	peroxiredoxin 2	Homo sapiens	195-199
23624384-0	2013	Effect of two synthetic disulfide bond variants of a 13-mer toxin from Conus californicus on the transcription of pro-inflammatory cytokines induced by LPS.	Disulfides	24-33	toll-like receptor 4	Mus musculus	152-155
23979894-1	2013	Thioredoxin h (Trxh) is a ubiquitous protein that reduces disulfides in target proteins, and is itself reduced by NADPH-thioredoxin reductase.	Disulfides	58-68	thioredoxin H4-2	Triticum aestivum	0-11
23979894-1	2013	Thioredoxin h (Trxh) is a ubiquitous protein that reduces disulfides in target proteins, and is itself reduced by NADPH-thioredoxin reductase.	Disulfides	58-68	thioredoxin H4-2	Triticum aestivum	120-131
23760509-9	2013	Increases in SOD1 disulfide bonding and maturation with increased copper chaperone for SOD1 expression caused a decrease in wtSOD1 palmitoylation.	Disulfides	18-27	superoxide dismutase 1, soluble	Mus musculus	13-17
23677799-0	2013	Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines.	Disulfides	51-60	claudin 2	Canis lupus familiaris	0-9
23677799-5	2013	Immunoblotting showed a higher molecular mass band in the mutants with a single cysteine mutation, consistent with a claudin-2 dimer, suggesting that the two conserved cysteines normally form an intramolecular disulfide bond in wild-type claudin-2.	Disulfides	210-219	claudin 2	Canis lupus familiaris	117-126
23677799-5	2013	Immunoblotting showed a higher molecular mass band in the mutants with a single cysteine mutation, consistent with a claudin-2 dimer, suggesting that the two conserved cysteines normally form an intramolecular disulfide bond in wild-type claudin-2.	Disulfides	210-219	claudin 2	Canis lupus familiaris	238-247
23677799-9	2013	We conclude that the disulfide bond between the conserved extracellular cysteines in claudin-2 is necessary for pore formation, probably by stabilizing the ECL1 fold, but is not required for correct protein trafficking.	Disulfides	21-30	claudin 2	Canis lupus familiaris	85-94
23446849-0	2013	Essential role for Toll-like receptor 7 (TLR7)-unique cysteines in an intramolecular disulfide bond, proteolytic cleavage and RNA sensing.	Disulfides	85-94	toll like receptor 7	Homo sapiens	19-39
23702800-1	2013	[RuCl(PPh3)2(3-phenylindenyl)] (1) has been shown to be an efficient catalyst in thiol dehydrogenative coupling to give disulfides.	Disulfides	120-130	caveolin 1	Homo sapiens	6-10
23825428-6	2013	Here we show that human beta1 and beta2 subunits alter interactions between bound Mg2+ and gating charge R213 and disrupt the disulfide bond formation at the VSD-CTD interface of mouse Slo1, indicating that the beta subunits alter the VSD-CTD interface.	Disulfides	126-135	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	24-29
23446849-0	2013	Essential role for Toll-like receptor 7 (TLR7)-unique cysteines in an intramolecular disulfide bond, proteolytic cleavage and RNA sensing.	Disulfides	85-94	toll like receptor 7	Homo sapiens	41-45
23567256-4	2013	R-CRT (arginylated calreticulin) forms disulfide-bridged dimers that are increased in low Ca(2+) conditions at physiological temperatures, a similar condition to the cellular environment that it required for arginylation of CRT.	Disulfides	39-48	calreticulin	Homo sapiens	2-5
23567256-4	2013	R-CRT (arginylated calreticulin) forms disulfide-bridged dimers that are increased in low Ca(2+) conditions at physiological temperatures, a similar condition to the cellular environment that it required for arginylation of CRT.	Disulfides	39-48	calreticulin	Homo sapiens	19-31
23446849-4	2013	We here show that TLR7N remains associated with TLR7C through a disulfide bond.	Disulfides	64-73	toll like receptor 7	Homo sapiens	48-53
23567256-7	2013	Thus, R-CRT disulfide-bridged dimers (through Cys146) are essential for the scaffolding of larger SGs under heat shock, although these dimers are not required for R-CRT association to SGs.	Disulfides	12-21	calreticulin	Homo sapiens	8-11
23446849-7	2013	TLR7N in endolysosomes was linked with TLR7C by a disulfide bond.	Disulfides	50-59	toll like receptor 7	Homo sapiens	39-44
23398327-6	2013	In these severely stressed cells, biochemical alterations of TDP-43, such as increased insolubility and disulfide bond formation, were irreversible.	Disulfides	104-113	TAR DNA binding protein	Homo sapiens	61-67
23525969-5	2013	Two cysteines (Cys176 and Cys185) within the extracellular loop of the NET have been proposed to form a disulfide bond.	Disulfides	104-113	solute carrier family 6 member 2	Homo sapiens	71-74
23319267-5	2013	Gel electrophoresis under reducing conditions of CCCP-induced PIMT multimers led to PIMT monomers accumulation, indicating that multimers resulted from disulfide-linked PIMT monomers.	Disulfides	152-161	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	62-66
23319267-5	2013	Gel electrophoresis under reducing conditions of CCCP-induced PIMT multimers led to PIMT monomers accumulation, indicating that multimers resulted from disulfide-linked PIMT monomers.	Disulfides	152-161	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	84-88
23319267-5	2013	Gel electrophoresis under reducing conditions of CCCP-induced PIMT multimers led to PIMT monomers accumulation, indicating that multimers resulted from disulfide-linked PIMT monomers.	Disulfides	152-161	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	84-88
23319267-8	2013	This indicated that PIMT monomers have lower enzymatic activity following CCCP treatments and that activation of PIMT multimers is essentially dependent on the formation of disulfide-linked monomers of PIMT.	Disulfides	173-182	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	113-117
23319267-8	2013	This indicated that PIMT monomers have lower enzymatic activity following CCCP treatments and that activation of PIMT multimers is essentially dependent on the formation of disulfide-linked monomers of PIMT.	Disulfides	173-182	protein-L-isoaspartate (D-aspartate) O-methyltransferase	Homo sapiens	113-117
23455544-2	2013	We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 oxidizes the SOD1 intrasubunit disulfide bond through both copper-dependent and copper-independent mechanisms.	Disulfides	161-170	superoxide dismutase 1	Homo sapiens	125-129
23685074-3	2013	Here we unveil how ERp44 cycles between cisGolgi and ER in a pH-regulated manner, patrolling assembly of disulfide-linked oligomers such as IgM and adiponectin.	Disulfides	105-114	endoplasmic reticulum protein 44	Homo sapiens	19-24
23685074-3	2013	Here we unveil how ERp44 cycles between cisGolgi and ER in a pH-regulated manner, patrolling assembly of disulfide-linked oligomers such as IgM and adiponectin.	Disulfides	105-114	adiponectin, C1Q and collagen domain containing	Homo sapiens	148-159
23741766-1	2004	VEGF-A is composed of VEGF121, VEGF165, and VEGF189 isoforms, which are secreted by most cell types and are active as homodimers linked by disulfide bonds.	Disulfides	139-148	vascular endothelial growth factor A	Homo sapiens	0-6
23478141-0	2013	The role of human growth hormone"s C-terminal disulfide bridge.	Disulfides	46-55	growth hormone 1	Homo sapiens	18-32
23478141-1	2013	OBJECTIVE: Human growth hormone (hGH), as well as the other members of the same polypeptide hormone family, have a four-helix bundle structure linked by two disulfide bridges, C53-C165 and C182-C189 in hGH.	Disulfides	157-166	growth hormone 1	Homo sapiens	17-31
23478141-2	2013	The C-terminal disulfide bridge of growth hormone is evolutionally conserved but its role is unknown.	Disulfides	15-24	growth hormone 1	Homo sapiens	35-49
23474148-1	2013	Interferon-gamma-inducible-lysosomal thiol reductase (GILT) plays a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction, thus unfolding native protein Ag and facilitating subsequent cleavage by proteases.	Disulfides	166-175	IFI30, lysosomal thiol reductase	Gallus gallus	0-52
23474148-1	2013	Interferon-gamma-inducible-lysosomal thiol reductase (GILT) plays a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction, thus unfolding native protein Ag and facilitating subsequent cleavage by proteases.	Disulfides	166-175	IFI30, lysosomal thiol reductase	Gallus gallus	54-58
23806332-2	2013	(2013) show that a pH-induced conformational change in the quality control protein ERp44 allows retrieval of secretory proteins that contain free thiols via a disulfide linkage from postendoplasmic reticulum compartments to prevent their premature secretion.	Disulfides	159-168	endoplasmic reticulum protein 44	Homo sapiens	83-88
23629649-4	2013	In the present investigation, we use redox experiments of monomeric cystatin C, stabilized against domain swapping by an intramolecular disulfide bond, to generate stable oligomers (dimers, trimers, tetramers, decamers, and high molecular weight oligomers).	Disulfides	136-145	cystatin-C	Oryctolagus cuniculus	68-78
23519916-1	2013	To assure efficient MHC class I (MHC-I) peptide loading, the peptide loading complex (PLC) recruits the peptide-receptive form of MHC-I, and in this process, tapasin (tpn) connects MHC-I with the peptide transporter TAP and forms a stable disulfide bond with ERp57.	Disulfides	239-248	TAP binding protein	Homo sapiens	158-165
23519916-4	2013	Exon 3 includes Cys-95, which is responsible for the disulfide bond formation with ERp57 and, consequently, interaction of the DeltaExon3 variant with ERp57 was strongly impaired.	Disulfides	53-62	protein disulfide isomerase family A member 3	Homo sapiens	83-88
23543738-4	2013	We determined rate constants for disulfide formation and hyperoxidation for human recombinant Prx2 and Prx3 by analyzing the relative proportions of hyperoxidized and dimeric products using mass spectrometry as a function of H2O2 concentration (in the absence of reductive cycling) and in competition with catalase at a fixed concentration of H2O2.	Disulfides	33-42	peroxiredoxin 2	Homo sapiens	94-98
23543738-5	2013	This gave a second order rate constant for hyperoxidation of 12,000 M(-1) s(-1) and a rate constant for disulfide formation of 2 s(-1) for Prx2.	Disulfides	104-113	peroxiredoxin 2	Homo sapiens	139-143
23594119-1	2013	We have previously shown that human extracellular superoxide dismutase (EC-SOD) exists as two variants with differences in their disulfide bridge patterns: one form is the active enzyme (aEC-SOD), and the other is inactive (iEC-SOD).	Disulfides	129-138	superoxide dismutase 3	Homo sapiens	36-70
23594119-1	2013	We have previously shown that human extracellular superoxide dismutase (EC-SOD) exists as two variants with differences in their disulfide bridge patterns: one form is the active enzyme (aEC-SOD), and the other is inactive (iEC-SOD).	Disulfides	129-138	superoxide dismutase 3	Homo sapiens	72-78
23455544-2	2013	We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 oxidizes the SOD1 intrasubunit disulfide bond through both copper-dependent and copper-independent mechanisms.	Disulfides	161-170	superoxide dismutase 1	Homo sapiens	143-147
23614004-4	2013	The structure adopts a thioredoxin-like fold stabilized by a structural disulfide bridge with a positively charged binding surface for interactions with the ER chaperones, calreticulin and ERp72.	Disulfides	72-81	calreticulin	Homo sapiens	172-184
23482565-0	2013	Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase.	Disulfides	25-34	malonyl-CoA decarboxylase	Homo sapiens	89-114
23614004-4	2013	The structure adopts a thioredoxin-like fold stabilized by a structural disulfide bridge with a positively charged binding surface for interactions with the ER chaperones, calreticulin and ERp72.	Disulfides	72-81	protein disulfide isomerase family A member 4	Homo sapiens	189-194
23290930-6	2013	Interestingly, HQ directly targeted and bound to the sulfhydryl group of cysteine-483 (C483) and C400 residues of Src, potentially leading to disruption of intracellular disulfide bonds.	Disulfides	170-179	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	114-117
23463512-1	2013	TGF-beta1 is a disulfide-bonded homodimeric protein produced by platelets and other cells that plays a role in many physiologic and pathologic processes.	Disulfides	15-24	transforming growth factor beta 1	Homo sapiens	0-9
23463512-10	2013	We conclude that thiol isomerases and thiol-disulfide exchange contribute to TGF-beta1 activation and identify a number of molecules that may participate in the process.	Disulfides	44-53	transforming growth factor beta 1	Homo sapiens	77-86
23516120-11	2013	Targets of Trx, such as phosphoribulokinase, glyceraldehyde-3-phosphate dehydrogenase, transketolase, and sedoheptulose-1,7-bisphosphatase have at least one regulatory disulfide bridge which supports the conclusion that the identified proteins undergo reversible thiol oxidation.	Disulfides	168-177	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	45-85
23184636-10	2013	CONCLUSION: Specific modifications of the disulfide bond within the lipoic-acid-conjugated PDC-E2 moiety, i.e., by an electrophilic agent renders PDC-E2 immunogenic in a genetically susceptible host.	Disulfides	42-51	dihydrolipoamide S-acetyltransferase	Homo sapiens	91-97
23184636-10	2013	CONCLUSION: Specific modifications of the disulfide bond within the lipoic-acid-conjugated PDC-E2 moiety, i.e., by an electrophilic agent renders PDC-E2 immunogenic in a genetically susceptible host.	Disulfides	42-51	dihydrolipoamide S-acetyltransferase	Homo sapiens	146-152
23360541-7	2013	Thiolated siRNA targeting glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was directly conjugated to the polymeric micelles via thiol exchange reactions with the pyridal disulfide groups present in the micelle corona.	Disulfides	171-180	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	26-66
23360541-7	2013	Thiolated siRNA targeting glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was directly conjugated to the polymeric micelles via thiol exchange reactions with the pyridal disulfide groups present in the micelle corona.	Disulfides	171-180	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	68-73
23534080-1	2004	VEGF-A is composed of VEGF121, VEGF165, and VEGF189 isoforms, which are secreted by most cell types and are active as homodimers linked by disulfide bonds.	Disulfides	139-148	vascular endothelial growth factor A	Homo sapiens	0-6
23396533-0	2013	Human serum albumin (HSA) nanoparticles stabilized with intermolecular disulfide bonds.	Disulfides	71-80	albumin	Homo sapiens	6-19
23329142-0	2013	Cu/Zn incorporation during purification of soluble human EC-SOD from E. coli stabilizes proper disulfide bond formation.	Disulfides	95-104	superoxide dismutase 3	Homo sapiens	57-63
23291526-6	2013	Intriguingly, we found that disulfide reduction mechanically stabilizes apo-SOD1 monomer, underscoring the differences between native basin mechanical properties and equilibrium thermodynamic stabilities and elucidating the presence of internal stress in the apo state.	Disulfides	28-37	superoxide dismutase 1	Homo sapiens	76-80
23291526-9	2013	As well, several mutants were more susceptible to loss of metals and monomerization than the disulfide-reduced or apo forms of SOD1.	Disulfides	93-102	superoxide dismutase 1	Homo sapiens	127-131
24843647-1	2013	AIMS/INTRODUCTION: The human insulin gene/preproinsulin protein mutation C43G disrupts disulfide bond formation and causes diabetes in humans.	Disulfides	87-96	insulin	Homo sapiens	29-36
24843647-1	2013	AIMS/INTRODUCTION: The human insulin gene/preproinsulin protein mutation C43G disrupts disulfide bond formation and causes diabetes in humans.	Disulfides	87-96	insulin	Homo sapiens	42-55
23329142-9	2013	Therefore, the enzymatic activity of hEC-SOD is associated with metal incorporation and protein folding via disulfide bond.	Disulfides	108-117	superoxide dismutase 3	Homo sapiens	37-44
23281053-6	2013	Addition of the disulfide bond also resulted in a 34.6 C increase in melting temperature and prevented insulin fibril formation under high physical stress even though the C-terminus of the B-chain thought to be directly involved in fibril formation was not modified.	Disulfides	16-25	insulin	Homo sapiens	103-110
23076707-7	2013	The major portion of misfolded superoxide dismutase-1 was shown to be monomers lacking the C57-C146 disulfide bond with large hydrodynamic volume, indicating a severely disordered structure.	Disulfides	100-109	superoxide dismutase 1	Homo sapiens	31-53
23281053-0	2013	Insulin analog with additional disulfide bond has increased stability and preserved activity.	Disulfides	31-40	insulin	Homo sapiens	0-7
23281053-2	2013	All known vertebrate insulin analogs have a classical structure with three 100% conserved disulfide bonds that are essential for structural stability and thus the function of insulin.	Disulfides	90-99	insulin	Homo sapiens	21-28
23314241-0	2013	Nitric oxide activates intradomain disulfide bond formation in the kinase             loop of Akt1/PKBalpha after burn injury.	Disulfides	35-44	AKT serine/threonine kinase 1	Rattus norvegicus	94-98
23314241-0	2013	Nitric oxide activates intradomain disulfide bond formation in the kinase             loop of Akt1/PKBalpha after burn injury.	Disulfides	35-44	AKT serine/threonine kinase 1	Rattus norvegicus	99-107
23322773-2	2013	Crystallographic studies of APSK from Arabidopsis thaliana revealed the presence of a regulatory intersubunit disulfide bond (Cys(86)-Cys(119)).	Disulfides	110-119	APS-kinase 2	Arabidopsis thaliana	28-32
23322773-5	2013	Formation of the disulfide bond in A. thaliana APSK (AtAPSK) inverts the binding affinities at the ATP/ADP and APS/PAPS sites from those observed in the reduced enzyme, consistent with initial binding of APS as inhibitory, and suggests a role for the N-terminal domain in guiding nucleotide binding order.	Disulfides	17-26	APS-kinase 2	Arabidopsis thaliana	47-51
23281053-3	2013	It might be hypothesized that an additional disulfide bond may enhance insulin structural stability which would be highly desirable in a pharmaceutical use.	Disulfides	44-53	insulin	Homo sapiens	71-78
23281053-8	2013	Furthermore, the additional disulfide bond prevented this insulin analog from adopting the R-state conformation and thus showing that the R-state conformation is not a prerequisite for binding to insulin receptor as previously suggested.	Disulfides	28-37	insulin	Homo sapiens	58-65
23281053-9	2013	In summary, this is the first example of an insulin analog featuring a fourth disulfide bond with increased structural stability and retained function.	Disulfides	78-87	insulin	Homo sapiens	44-51
23122227-1	2013	XK is a putative transporter of unknown function that is ubiquitously expressed and linked through disulfide bonds to Kell protein, an endothelin-3 (ET-3)-converting enzyme.	Disulfides	99-108	endothelin 3	Mus musculus	135-147
23264618-0	2013	Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis.	Disulfides	0-9	superoxide dismutase 1	Homo sapiens	79-83
23264618-2	2013	Wild-type SOD1 forms a highly conserved intra-molecular disulfide bond, whereas pathological SOD1 proteins are cross-linked via intermolecular disulfide bonds and form insoluble oligomers.	Disulfides	56-65	superoxide dismutase 1	Homo sapiens	10-14
23264618-2	2013	Wild-type SOD1 forms a highly conserved intra-molecular disulfide bond, whereas pathological SOD1 proteins are cross-linked via intermolecular disulfide bonds and form insoluble oligomers.	Disulfides	143-152	superoxide dismutase 1	Homo sapiens	93-97
23264618-3	2013	A thiol-disulfide status in SOD1 will thus play a regulatory role in determining its folding/misfolding pathways; however, it remains unknown how pathogenic mutations in SOD1 affect the thiol-disulfide status to facilitate the protein misfolding.	Disulfides	8-17	superoxide dismutase 1	Homo sapiens	28-32
23264618-3	2013	A thiol-disulfide status in SOD1 will thus play a regulatory role in determining its folding/misfolding pathways; however, it remains unknown how pathogenic mutations in SOD1 affect the thiol-disulfide status to facilitate the protein misfolding.	Disulfides	192-201	superoxide dismutase 1	Homo sapiens	28-32
23264618-3	2013	A thiol-disulfide status in SOD1 will thus play a regulatory role in determining its folding/misfolding pathways; however, it remains unknown how pathogenic mutations in SOD1 affect the thiol-disulfide status to facilitate the protein misfolding.	Disulfides	192-201	superoxide dismutase 1	Homo sapiens	170-174
23264618-4	2013	Here, we show that the structural destabilization of SOD1 scrambles a disulfide bond among four Cys residues in an SOD1 molecule.	Disulfides	70-79	superoxide dismutase 1	Homo sapiens	53-57
23264618-4	2013	Here, we show that the structural destabilization of SOD1 scrambles a disulfide bond among four Cys residues in an SOD1 molecule.	Disulfides	70-79	superoxide dismutase 1	Homo sapiens	115-119
23264618-5	2013	The disulfide scrambling produces SOD1 monomers with distinct electrophoretic mobility and also reproduces the formation of disulfide-linked oligomers.	Disulfides	4-13	superoxide dismutase 1	Homo sapiens	34-38
23264618-5	2013	The disulfide scrambling produces SOD1 monomers with distinct electrophoretic mobility and also reproduces the formation of disulfide-linked oligomers.	Disulfides	124-133	superoxide dismutase 1	Homo sapiens	34-38
23264618-6	2013	We have also found that the familial form of amyotrophic lateral sclerosis-causing mutations facilitate the disulfide scrambling in SOD1.	Disulfides	108-117	superoxide dismutase 1	Homo sapiens	132-136
23264618-7	2013	Based upon our results, therefore, scrambling of the conserved disulfide bond will be a key event to cause the pathological changes in disease-associated mutant SOD1 proteins.	Disulfides	63-72	superoxide dismutase 1	Homo sapiens	161-165
23327656-3	2013	For example, Trx activates extracellular transglutaminase 2 (TG2) via reduction of an intramolecular disulfide bond.	Disulfides	101-110	transglutaminase 2	Homo sapiens	41-59
23327656-3	2013	For example, Trx activates extracellular transglutaminase 2 (TG2) via reduction of an intramolecular disulfide bond.	Disulfides	101-110	transglutaminase 2	Homo sapiens	61-64
23442914-1	2013	Protegrin is an antimicrobial peptide with a beta-hairpin structure stabilized by a pair of disulfide bonds.	Disulfides	92-101	amyloid beta precursor protein	Homo sapiens	43-49
22867017-0	2013	Disulfide bond as a switch for copper-zinc superoxide dismutase activity in asthma.	Disulfides	0-9	superoxide dismutase 1	Homo sapiens	43-63
23312470-6	2013	Vasopressin and oxytocin contain a disulfide linkage leaving them particularly vulnerable to deactivation from the reducing environment inside the cell.	Disulfides	35-44	arginine vasopressin	Homo sapiens	0-11
22406071-4	2013	This includes the evolution of two unique outer membrane import receptors, plant Translocase of outer membrane 20 kDa subunit (TOM20) and Outer membrane protein of 64 kDa (OM64), the loss of a receptor domain from an ancestral import component, Translocase of outer membrane 22 kDa subunit (TOM22), evolution of unique features in the disulfide relay system of the inter membrane space, and the addition of an extra membrane spanning domain to another ancestral component of the inner membrane, Translocase of inner membrane 17 kDa subunit (TIM17).	Disulfides	335-344	translocase of outer mitochondrial membrane 20	Homo sapiens	127-132
23340690-1	2013	The purpose of this work is to characterize the interactions of two disulfide-constrained cyclic tetrapeptides [c(Ac-Cys-Pro-Phe-Cys-NH(2)), SS1; c(Ac-Cys-Pro-Gly-Cys-NH(2)), SS2] with Cu(2+) ions in order to facilitate the design of cyclic peptides as sensors for metal ions.	Disulfides	68-77	major histocompatibility complex, class II, DR beta 1	Homo sapiens	141-144
23353556-2	2013	Using a new genetic mouse model to track and isolate myofibroblasts, we performed gene expression profiling followed by biological validation to identify HE4 (encoding human epididymis protein 4, also known as WAP 4-disulfide core domain-2 or Wfdc2) as the most upregulated gene in fibrosis-associated myofibroblasts.	Disulfides	216-225	WAP four-disulfide core domain 2	Mus musculus	154-157
23353556-2	2013	Using a new genetic mouse model to track and isolate myofibroblasts, we performed gene expression profiling followed by biological validation to identify HE4 (encoding human epididymis protein 4, also known as WAP 4-disulfide core domain-2 or Wfdc2) as the most upregulated gene in fibrosis-associated myofibroblasts.	Disulfides	216-225	secretory leukocyte peptidase inhibitor	Homo sapiens	210-215
23537207-3	2013	Peptide ligands specific for the VEGFA binding site on neuropilin-1 were identified by screening a library of disulfide-rich peptides derived from the thermostable, protease-resistant cyclotide kalata B1.	Disulfides	110-119	vascular endothelial growth factor A	Homo sapiens	33-38
23219881-4	2013	Here, we report the crystal structure of HBeAg, which clarifies how the short N-terminal propeptide of HBeAg induces a radically altered mode of dimerization relative to HBcAg (~140  rotation), locked into place through formation of intramolecular disulfide bridges.	Disulfides	248-257	capsid protein;pre-capsid protein	Hepatitis B virus	41-46
23219881-4	2013	Here, we report the crystal structure of HBeAg, which clarifies how the short N-terminal propeptide of HBeAg induces a radically altered mode of dimerization relative to HBcAg (~140  rotation), locked into place through formation of intramolecular disulfide bridges.	Disulfides	248-257	capsid protein;pre-capsid protein	Hepatitis B virus	103-108
22702224-4	2013	RECENT ADVANCES: Human cytosolic/nuclear Trx1 in the disulfide form can be nitrosylated at Cys73 and transnitrosylate target proteins, including caspase 3.	Disulfides	53-62	caspase 3	Homo sapiens	145-154
22801966-0	2013	Murine tissue factor coagulant activity is critically dependent on the presence of an intact allosteric disulfide.	Disulfides	104-113	coagulation factor III	Mus musculus	7-20
23167757-6	2013	Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer.	Disulfides	95-104	protein disulfide isomerase family A member 2	Homo sapiens	112-117
24246976-6	2013	Reduction of disulfide bonds is an important mechanism activating HBD-1.	Disulfides	13-22	defensin beta 1	Homo sapiens	66-71
22801966-1	2013	Tissue factor activation (decryption) has been proposed to be dependent on the cysteine 186-cysteine 209 allosteric disulfide in the tissue factor extracellular domain.	Disulfides	116-125	coagulation factor III	Mus musculus	0-13
22801966-1	2013	Tissue factor activation (decryption) has been proposed to be dependent on the cysteine 186-cysteine 209 allosteric disulfide in the tissue factor extracellular domain.	Disulfides	116-125	coagulation factor III	Mus musculus	133-146
22801966-2	2013	Tissue factor procoagulant activity is under the control of protein disulfide isomerase-dependent modulation and nitrosylation of this disulfide.	Disulfides	68-77	coagulation factor III	Mus musculus	0-13
22801966-11	2013	Mouse tissue factor procoagulant function is dependent on the Cys190-Cys213 disulfide bond and is modulated by nitrosylation.	Disulfides	76-85	coagulation factor III	Mus musculus	6-19
22801966-12	2013	The murine model of disulfide-mutated tissue factor is more suitable for studying tissue factor decryption than are human tissue factor mutants.	Disulfides	20-29	coagulation factor III	Mus musculus	38-51
22801966-12	2013	The murine model of disulfide-mutated tissue factor is more suitable for studying tissue factor decryption than are human tissue factor mutants.	Disulfides	20-29	coagulation factor III	Mus musculus	82-95
24489546-4	2013	By virtue of the same cysteine, unassembled secretory IgM subunits are recognized and retained (via mixed disulfide bonds) by members of the protein disulfide isomerase family, in particular ERp44.	Disulfides	106-115	endoplasmic reticulum protein 44	Homo sapiens	191-196
23247967-7	2013	Using these methods, we could resolve the relative contributions of copper and zinc binding, as well as disulfide reduction to intact SOD1 protein present from &lt;100 mug of the lumbar spinal cord of a transgenic, SOD1 overexpressing mouse.	Disulfides	104-113	superoxide dismutase 1, soluble	Mus musculus	134-138
24220679-3	2013	Here we demonstrate that the intrinsic propensity of TDP-43 to aggregate drives the assembly of TDP-43-positive stress granules and soluble toxic TDP-43 oligomers in response to a ROS insult via a disulfide crosslinking-independent mechanism.	Disulfides	197-206	TAR DNA binding protein	Homo sapiens	53-59
23329479-5	2013	Using recombinant MHC class I molecules bearing monoglucosylated N-linked glycans, calreticulin, and disulfide-linked tapasin/ERp57 heterodimers, this soluble PLC subcomplex can be employed to study the mechanism of peptide loading or the principles governing peptide selection for particular MHC class I alleles.	Disulfides	101-110	TAP binding protein	Homo sapiens	118-125
23329479-5	2013	Using recombinant MHC class I molecules bearing monoglucosylated N-linked glycans, calreticulin, and disulfide-linked tapasin/ERp57 heterodimers, this soluble PLC subcomplex can be employed to study the mechanism of peptide loading or the principles governing peptide selection for particular MHC class I alleles.	Disulfides	101-110	protein disulfide isomerase family A member 3	Homo sapiens	126-131
24220679-3	2013	Here we demonstrate that the intrinsic propensity of TDP-43 to aggregate drives the assembly of TDP-43-positive stress granules and soluble toxic TDP-43 oligomers in response to a ROS insult via a disulfide crosslinking-independent mechanism.	Disulfides	197-206	TAR DNA binding protein	Homo sapiens	96-102
24220679-3	2013	Here we demonstrate that the intrinsic propensity of TDP-43 to aggregate drives the assembly of TDP-43-positive stress granules and soluble toxic TDP-43 oligomers in response to a ROS insult via a disulfide crosslinking-independent mechanism.	Disulfides	197-206	TAR DNA binding protein	Homo sapiens	96-102
23176598-4	2012	Disulfide-linked dimers produced by Cu(2+) oxidation of the free-thiol form of the protein demonstrated picomolar affinity for VEGF in solution, comparable to that of a D2-Fc fusion (sFLT01) and ~50-fold higher than monomeric D2, suggesting the 26 a.a. tag length between the two D2 domains permits simultaneous interaction of both faces of the VEGF homodimer.	Disulfides	0-9	vascular endothelial growth factor A	Homo sapiens	127-131
23738035-5	2013	Immunoblots from buffered solutions or suction blister fluid reveal that propagation of photooxidative damage to other residues such as Tyr or disulfide bonds produces intra- and intermolecular bonds in apolipoproteins A-I, A-II, and B100.	Disulfides	143-152	apolipoprotein A1	Homo sapiens	203-238
23536797-5	2013	To enable the development of a potential drug product with a once-daily dosing profile, in a preserved, multi-use formulation, an additional disulfide bond was introduced in FGF21 through Leu118Cys and Ala134Cys mutations.	Disulfides	141-150	fibroblast growth factor 21	Homo sapiens	174-179
23383248-7	2013	This example for mFIZZ1 should encourage the design of an appropriate thiol/disulfide oxidoreductase-tuned cell free expression system for other challenging disulfide rich proteins.	Disulfides	76-85	resistin like alpha	Mus musculus	17-23
23949117-3	2013	Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides.	Disulfides	168-177	protein disulfide isomerase family A member 2	Homo sapiens	75-78
23949117-3	2013	Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides.	Disulfides	238-248	protein disulfide isomerase family A member 2	Homo sapiens	75-78
23949117-4	2013	Remarkably, the Prx4-dependent formation of native disulfide bonds was accelerated when PDI was combined with ERp46 or P5, suggesting that PDIs work synergistically to increase the rate and fidelity of oxidative protein folding.	Disulfides	51-60	protein disulfide isomerase family A member 2	Homo sapiens	88-91
23176598-4	2012	Disulfide-linked dimers produced by Cu(2+) oxidation of the free-thiol form of the protein demonstrated picomolar affinity for VEGF in solution, comparable to that of a D2-Fc fusion (sFLT01) and ~50-fold higher than monomeric D2, suggesting the 26 a.a. tag length between the two D2 domains permits simultaneous interaction of both faces of the VEGF homodimer.	Disulfides	0-9	vascular endothelial growth factor A	Homo sapiens	345-349
23141538-1	2012	PDI catalyzes the oxidative folding of disulfide-containing proteins.	Disulfides	39-48	protein disulfide isomerase family A member 2	Homo sapiens	0-3
22964495-3	2012	This phenomenon was dependent on ABCC1-mediated GSH extrusion, along with GCL inhibition and, to a minor extent, the formation of GSH-protein mixed disulfides that synergistically contributed to the modulation of autophagy by shifting the intracellular redox state toward more oxidizing conditions.	Disulfides	148-158	ATP binding cassette subfamily C member 1	Homo sapiens	33-38
23123197-4	2012	Subsequently, the formation of the disulfide bond between Cys41 and Cys420 of GRP78 enhances its chaperone activity.	Disulfides	35-44	heat shock protein family A (Hsp70) member 5	Homo sapiens	78-83
22982242-7	2012	Our observation from this study reveals that SelW activated CDC25B by promoting the dissociation of 14-3-3 from CDC25B through the reduction of the intramolecular disulfide bond during recovery.	Disulfides	163-172	selenoprotein W	Homo sapiens	45-49
22982242-7	2012	Our observation from this study reveals that SelW activated CDC25B by promoting the dissociation of 14-3-3 from CDC25B through the reduction of the intramolecular disulfide bond during recovery.	Disulfides	163-172	cell division cycle 25B	Homo sapiens	60-66
22939972-9	2012	Evidence was found that STAT3 is more resistant than STAT1 to intermolecular disulfide bond formation under oxidizing conditions and more likely to retain the monomeric form, suggesting that conformational differences explain the differential effect of GSH depletion on STAT1 and STAT3.	Disulfides	77-86	signal transducer and activator of transcription 3	Homo sapiens	24-29
23070980-1	2012	EPPIN (epididymal protease inhibitor; SPINLW1), an antimicrobial cysteine-rich protein containing both Kunitz and whey acidic protein (WAP)-type four disulfide core protease inhibitor consensus sequences, is a target for male contraception because of its critical role in sperm motility.	Disulfides	150-159	whey acidic protein	Rattus norvegicus	135-138
23000475-0	2012	Antimicrobial activity of human beta-defensin 4 analogs: insights into the role of disulfide linkages in modulating activity.	Disulfides	83-92	defensin beta 104B	Homo sapiens	32-47
23066897-0	2012	Incorporation of disulfide containing protein modules into multivalent antigenic conjugates: generation of antibodies against the thrombin-sensitive region of murine protein S. Antigenic peptide conjugates can be used as vaccines and for the production of antibodies for clinical and research use.	Disulfides	17-26	coagulation factor II	Mus musculus	130-138
23141538-5	2012	In contrast, a PDI domain favors native disulfides by catalyzing oxidation at a late stage of folding.	Disulfides	40-50	protein disulfide isomerase family A member 2	Homo sapiens	15-18
22948901-2	2012	In combination with m-nitrobenzyl alcohol, molecular ion charge states that are greater than the number of basic sites in the protein can be produced from these native solutions, even for lysozyme, which is conformationally constrained by four intramolecular disulfide bonds.	Disulfides	259-268	lysozyme	Homo sapiens	188-196
23041369-3	2012	Here, we show that NPP1 forms homodimers via intramembrane disulfide bonding, but is also processed intracellularly to a secreted monomer.	Disulfides	59-68	ectonucleotide pyrophosphatase/phosphodiesterase 1	Homo sapiens	19-23
22899364-1	2012	The role of the 17 disulfide (S-S) bridges in preserving the native conformation of human serum albumin (HSA) is investigated by performing classical molecular dynamics (MD) simulations on protein structures with intact and, respectively, reduced S-S bridges.	Disulfides	19-28	albumin	Homo sapiens	90-103
22988250-4	2012	EGF and kinase inhibitors stimulate formation of identical dimer interfaces in the EGFR transmembrane domain, as shown by disulfide cross-linking.	Disulfides	122-131	epidermal growth factor receptor	Homo sapiens	83-87
22982335-1	2012	In mammals, interferon-gamma-inducible-lysosomal thiol reductase (GILT) has been demonstrated to play a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction, thus unfolding native protein Ag and facilitating subsequent cleavage by proteases.	Disulfides	202-211	IFI30 lysosomal thiol reductase	Danio rerio	12-64
22982335-1	2012	In mammals, interferon-gamma-inducible-lysosomal thiol reductase (GILT) has been demonstrated to play a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction, thus unfolding native protein Ag and facilitating subsequent cleavage by proteases.	Disulfides	202-211	IFI30 lysosomal thiol reductase	Danio rerio	66-70
22994388-5	2012	Only the reducible disulfide-linked Cyt c-MAP conjugate, and not free Cyt c or thioether-linked Cyt c-MAP, initiated apoptosis in proteasome-inhibited cells which correlated with the cytosolic localization profiles of the proteins.	Disulfides	19-28	cytochrome c, somatic	Homo sapiens	36-41
23044006-14	2012	It formed when the disulfide bonds between A-chain and B-chain of human insulin were cut by beta-mercaptoethanol, followed by cleavage of the B-chain by trypsin and carboxypeptidase B.	Disulfides	19-28	insulin	Homo sapiens	72-79
22994388-6	2012	The co-treatment of disulfide-linked Cyt c-MAP with a disulfide reduction inhibitor decreased the amount of Cyt c delivered to the cytosol, which correlated with a lack of apoptotic activity.	Disulfides	20-29	cytochrome c, somatic	Homo sapiens	37-42
22994388-6	2012	The co-treatment of disulfide-linked Cyt c-MAP with a disulfide reduction inhibitor decreased the amount of Cyt c delivered to the cytosol, which correlated with a lack of apoptotic activity.	Disulfides	20-29	cytochrome c, somatic	Homo sapiens	108-113
22994388-6	2012	The co-treatment of disulfide-linked Cyt c-MAP with a disulfide reduction inhibitor decreased the amount of Cyt c delivered to the cytosol, which correlated with a lack of apoptotic activity.	Disulfides	54-63	cytochrome c, somatic	Homo sapiens	37-42
22994388-6	2012	The co-treatment of disulfide-linked Cyt c-MAP with a disulfide reduction inhibitor decreased the amount of Cyt c delivered to the cytosol, which correlated with a lack of apoptotic activity.	Disulfides	54-63	cytochrome c, somatic	Homo sapiens	108-113
22764321-6	2012	Within the unique quaternary structural arrangement, the FAD-binding pocket and the characteristic CXXC motif from each monomer is 35 A (3.5 nm) away from that of its corresponding molecule, which suggests that BmNPV ORF75 might adopt a deviant mechanism from that of QSOX to catalyse disulfide bond formation.	Disulfides	285-294	AcMNPV orf92	Bombyx mori nucleopolyhedrovirus	217-222
23017013-2	2012	A fluorescence off-on change is induced by disulfide cleavage of the probe, resulting from a reaction with Trx and subsequent intramolecular cyclization by the released thiolate to give a fluorescent product.	Disulfides	43-52	thioredoxin 1	Rattus norvegicus	107-110
23017013-5	2012	In vitro kinetic analysis of the disulfide bond cleavage revealed that the second-order rate constant for Trx is (4.04 +- 0.26) x 10(3) (M s)(-1), approximately 5000 times faster than that for GSH.	Disulfides	33-42	thioredoxin 1	Rattus norvegicus	106-109
22464987-2	2012	For this purpose disulfide stabilized scFv domains of the EGFR/ADCC antibody GA201 were fused via serine-glycine connectors to the C-terminus of the heavy (XGFR2) or light chain (XGFR4), or the N-termini of the light (XGFR5) or heavy chain (XGFR3) of the IGF-1R antibody R1507 as parental IgG1 antibody.	Disulfides	17-26	immunglobulin heavy chain variable region	Homo sapiens	38-42
22464987-2	2012	For this purpose disulfide stabilized scFv domains of the EGFR/ADCC antibody GA201 were fused via serine-glycine connectors to the C-terminus of the heavy (XGFR2) or light chain (XGFR4), or the N-termini of the light (XGFR5) or heavy chain (XGFR3) of the IGF-1R antibody R1507 as parental IgG1 antibody.	Disulfides	17-26	epidermal growth factor receptor	Homo sapiens	58-62
23067373-4	2012	The self-association of vWF is also supported by a rapidly expanding reservoir of novel evidences that the thiol/disulfide exchange regulates vWF multimer size in the blood circulation.	Disulfides	113-122	von Willebrand factor	Homo sapiens	24-27
23067373-4	2012	The self-association of vWF is also supported by a rapidly expanding reservoir of novel evidences that the thiol/disulfide exchange regulates vWF multimer size in the blood circulation.	Disulfides	113-122	von Willebrand factor	Homo sapiens	142-145
22963549-4	2012	Effects of DMSO-specific solvation and conformation-restricting covalent structure of insulin (including the three intact disulfide bridges) are argued to play important roles in stabilizing the disordered state of the protein.	Disulfides	122-131	insulin	Homo sapiens	86-93
22714274-1	2012	We have developed a NH(3)/H(2)O(2) two-step method for the recovery of insulin monomers from amyloid fibrils by modulating the cleavage and regeneration of disulfide bonds.	Disulfides	156-165	insulin	Homo sapiens	71-78
22902630-6	2012	These data imply that Prdx1 can function as a peroxide receptor in response to extracellular H(2)O(2), receiving the peroxide signal and transducing it into a disulfide bond that is subsequently transmitted to the substrate, ASK1, resulting in p38 phosphorylation.	Disulfides	159-168	mitogen-activated protein kinase 14	Homo sapiens	244-247
22842048-6	2012	These results suggest a model where the molecular interactions guiding the protein recognition between Mia40 and the disulfide-reduced CHCHD5 and CHCHD7 substrates occurs in vivo when the latter proteins are partially embedded in the protein import pore of the outer membrane of mitochondria.	Disulfides	117-126	coiled-coil-helix-coiled-coil-helix domain containing 7	Homo sapiens	146-152
22871361-5	2012	MDK is a cysteine-rich 13kDa protein containing five disulfide bonds and PTN is 19kDa protein containing ten disulphide bonds.	Disulfides	53-62	midkine	Homo sapiens	0-3
22913736-3	2012	Time-resolved dynamic light scattering (DLS), disk centrifuge photosedimentometry (DCP), and circular dichroism (CD) spectroscopy studies confirm that bovine serum albumin (BSA) adsorbs rapidly onto the cationic poly(vinyl amine)-stabilized polypyrrole nanoparticles and suggest that the initial well-defined protein coronal is subsequently cross-linked via thiol-disulfide exchange.	Disulfides	364-373	albumin	Homo sapiens	158-171
22776248-5	2012	Cells over-expressing Keap1 were treated with TNBS or SFN and the formation of disulfide bonds among Keap1 molecules were determined.	Disulfides	79-88	kelch like ECH associated protein 1	Homo sapiens	22-27
22776248-5	2012	Cells over-expressing Keap1 were treated with TNBS or SFN and the formation of disulfide bonds among Keap1 molecules were determined.	Disulfides	79-88	kelch like ECH associated protein 1	Homo sapiens	101-106
22776248-6	2012	SFN promoted intramolecular disulfide formation whereas TNBS promoted intermolecular disulfide formation of Keap1.	Disulfides	85-94	kelch like ECH associated protein 1	Homo sapiens	108-113
22610276-5	2012	Biochemical analyses of recombinant vWFA2 domain of cochlin carrying the p.F527C mutation revealed that the mutation increases propensity of the protein to form covalent disulfide-bonded dimers and affects the structural stability but not the collagen-affinity of the vWFA2 domain.	Disulfides	170-179	cochlin	Homo sapiens	52-59
22949505-5	2012	Here we reveal that, in contrast to other ubiquitin pathway E2 enzymes, Cdc34 is particularly sensitive to oxidative inactivation, through sequestration of the catalytic cysteine in a disulfide complex with Uba1, by levels of oxidant that do not reduce global ubiquitinylation of proteins.	Disulfides	184-193	E1 ubiquitin-activating protein UBA1	Saccharomyces cerevisiae S288C	207-211
22976197-1	2012	We have designed bispecific antibodies that bind one target (anti-Her3) in a bivalent IgG-like manner and contain one additional binding entity (anti-cMet) composed of one V(H) and one V(L) domain connected by a disulfide bond.	Disulfides	212-221	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	150-154
22928725-5	2012	Comparisons of two matched thiol and disulfide forms reveal that the active site conformational change required for disulfide formation involves a transition of ~20 residues from a pair of alpha-helices to a beta-hairpin and 3(10)-helix.	Disulfides	37-46	amyloid beta precursor protein	Homo sapiens	206-212
22928725-5	2012	Comparisons of two matched thiol and disulfide forms reveal that the active site conformational change required for disulfide formation involves a transition of ~20 residues from a pair of alpha-helices to a beta-hairpin and 3(10)-helix.	Disulfides	116-125	amyloid beta precursor protein	Homo sapiens	206-212
22843683-6	2012	These results provide important new information on the three-dimensional structure of the outer mouth of the cystic fibrosis transmembrane conductance regulator channel pore: TMs 6 and 11 are close enough together to form disulfide bonds in both open and closed channels.	Disulfides	222-231	CF transmembrane conductance regulator	Homo sapiens	109-160
22764321-8	2012	These data suggest that the thiol oxidase activity of BmNPV ORF75 could be critical to catalyse the formation of the disulfide bonds of certain BmNPV proteins essential for BmNPV virion assembly.	Disulfides	117-126	AcMNPV orf92	Bombyx mori nucleopolyhedrovirus	60-65
23089196-4	2012	In addition, using conditions which preserve the tapasin-ERp57 disulfide-bonded conjugate, we demonstrated that beta 2-microglobulin increases tapasin-containing protein complexes, and reduces the level of MHC class I/ERp57 complexes lacking tapasin.	Disulfides	63-72	TAP binding protein	Homo sapiens	49-56
22908275-3	2012	These ERBB2 extracellular domain mutants were activated by two distinct mechanisms, characterized by elevated C-terminal tail phosphorylation or by covalent dimerization mediated by intermolecular disulfide bond formation.	Disulfides	197-206	erb-b2 receptor tyrosine kinase 2	Homo sapiens	6-11
22738645-2	2012	This MSN system demonstrates controlled release of fluorescein molecules under disulfide reducing conditions.	Disulfides	79-88	moesin	Homo sapiens	5-8
23089196-4	2012	In addition, using conditions which preserve the tapasin-ERp57 disulfide-bonded conjugate, we demonstrated that beta 2-microglobulin increases tapasin-containing protein complexes, and reduces the level of MHC class I/ERp57 complexes lacking tapasin.	Disulfides	63-72	protein disulfide isomerase family A member 3	Homo sapiens	57-62
22595939-7	2012	Genotype-phenotype and SOD1 structural model analysis revealed the effects of the Cys57-Cys146 disulfide bond formation and the C-terminal dimer contact region on the disease phenotypes.	Disulfides	95-104	superoxide dismutase 1	Homo sapiens	23-27
22789714-1	2012	Thioredoxin domain-containing protein 12 (Txndc12) belongs to the thioredoxin superfamily, and has roles in redox regulation, defense against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors.	Disulfides	173-182	thioredoxin domain containing 12 (endoplasmic reticulum)	Mus musculus	42-49
22476940-9	2012	These data implicate thiol-disulfide exchange reactions in the initial tethering of apoptotic cells to macrophage and establish P2X7 as one of the scavenger receptors involved in the recognition and removal of apoptotic cells in the absence of extracellular ATP and serum.	Disulfides	27-36	purinergic receptor P2X 7	Homo sapiens	128-132
22819772-4	2012	Acra3 is a 7620Da molecular weight peptide, with 66 amino acid residues crosslinked by four disulfide bridges.	Disulfides	92-101	cholinergic receptor, nicotinic, alpha polypeptide 3	Mus musculus	0-5
22899260-8	2012	LC-MS/MS analysis of the disulfide-linked proteins correctly identified haptoglobin (Hp), a disulfide-linked protein usually found as a heterotetramer or as a disulfide-linked heteropolymer.	Disulfides	25-34	haptoglobin	Homo sapiens	72-83
22869735-6	2012	Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57-Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer.	Disulfides	80-89	superoxide dismutase 1	Homo sapiens	59-64
22869735-6	2012	Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57-Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer.	Disulfides	145-154	superoxide dismutase 1	Homo sapiens	59-64
22651090-0	2012	Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1.	Disulfides	24-33	superoxide dismutase 1	Homo sapiens	48-74
22651090-1	2012	The intramolecular disulfide bond in hSOD1 [human SOD1 (Cu,Zn superoxide dismutase 1)] plays a key role in maintaining the protein"s stability and quaternary structure.	Disulfides	19-28	superoxide dismutase 1	Homo sapiens	37-42
22651090-1	2012	The intramolecular disulfide bond in hSOD1 [human SOD1 (Cu,Zn superoxide dismutase 1)] plays a key role in maintaining the protein"s stability and quaternary structure.	Disulfides	19-28	superoxide dismutase 1	Homo sapiens	38-42
22651090-1	2012	The intramolecular disulfide bond in hSOD1 [human SOD1 (Cu,Zn superoxide dismutase 1)] plays a key role in maintaining the protein"s stability and quaternary structure.	Disulfides	19-28	superoxide dismutase 1	Homo sapiens	56-82
22651090-2	2012	In mutant forms of SOD1 that cause familial ALS (amyotrophic lateral sclerosis), this disulfide bond is more susceptible to chemical reduction, which may lead to destabilization of the dimer and aggregation.	Disulfides	86-95	superoxide dismutase 1	Homo sapiens	19-23
22651090-3	2012	During hSOD1 maturation, disulfide formation is catalysed by CCS1 (copper chaperone for SOD1).	Disulfides	25-34	superoxide dismutase 1	Homo sapiens	7-12
22651090-3	2012	During hSOD1 maturation, disulfide formation is catalysed by CCS1 (copper chaperone for SOD1).	Disulfides	25-34	superoxide dismutase 1	Homo sapiens	8-12
22651090-4	2012	Previous studies in yeast demonstrate that the yeast GSH/Grx (glutaredoxin) redox system promotes reduction of the hSOD1 disulfide in the absence of CCS1.	Disulfides	121-130	superoxide dismutase 1	Homo sapiens	115-120
22651090-5	2012	In the present study, we probe further the interaction between hSOD1, GSH and Grxs to provide mechanistic insight into the redox kinetics and thermodynamics of the hSOD1 disulfide.	Disulfides	170-179	superoxide dismutase 1	Homo sapiens	63-68
22651090-5	2012	In the present study, we probe further the interaction between hSOD1, GSH and Grxs to provide mechanistic insight into the redox kinetics and thermodynamics of the hSOD1 disulfide.	Disulfides	170-179	superoxide dismutase 1	Homo sapiens	164-169
22651090-6	2012	We demonstrate that hGrx1 (human Grx1) uses a monothiol mechanism to reduce the hSOD1 disulfide, and the GSH/hGrx1 system reduces ALS mutant SOD1 at a faster rate than WT (wild-type) hSOD1.	Disulfides	86-95	superoxide dismutase 1	Homo sapiens	80-85
22651090-6	2012	We demonstrate that hGrx1 (human Grx1) uses a monothiol mechanism to reduce the hSOD1 disulfide, and the GSH/hGrx1 system reduces ALS mutant SOD1 at a faster rate than WT (wild-type) hSOD1.	Disulfides	86-95	superoxide dismutase 1	Homo sapiens	81-85
22899260-8	2012	LC-MS/MS analysis of the disulfide-linked proteins correctly identified haptoglobin (Hp), a disulfide-linked protein usually found as a heterotetramer or as a disulfide-linked heteropolymer.	Disulfides	92-101	haptoglobin	Homo sapiens	72-83
22899260-8	2012	LC-MS/MS analysis of the disulfide-linked proteins correctly identified haptoglobin (Hp), a disulfide-linked protein usually found as a heterotetramer or as a disulfide-linked heteropolymer.	Disulfides	92-101	haptoglobin	Homo sapiens	72-83
22686939-5	2012	Four cysteine residues of WhiB2 form two intramolecular disulfide bonds; however, chaperone function was unaffected by the redox state of the cysteines.	Disulfides	56-65	transcriptional regulator WhiB2	Mycobacterium tuberculosis H37Rv	26-31
22899503-5	2012	In contrast, although the milk protein alpha-lactalbumin has several disulfide bridges, only one phenylarsenic moiety was bound under strongly denaturing conditions.	Disulfides	69-78	lactalbumin alpha	Homo sapiens	39-56
22746182-1	2012	Insulin-like growth factor 1 (IGF-1) is a 70-residue hormone containing three intramolecular disulfide bridges.	Disulfides	93-102	insulin like growth factor 1	Homo sapiens	0-28
22665445-7	2012	Additionally, coimmunoprecipitation of XXT2YFP and XXT5HA proteins from Arabidopsis protoplasts indicated that while the formation of the XXT2-XXT2 homocomplex involves disulfide bonds, the formation of the XXT2-XXT5 heterocomplex does not involve covalent interactions.	Disulfides	169-178	xyloglucan xylosyltransferase 5	Arabidopsis thaliana	51-55
22706041-2	2012	Cyclopeptide C*HSDGIC* (CHC), which results from the cyclization of PACAP (1-5) with disulfide, has been demonstrated to represent a potent agonist for the PACAP-specific receptor PAC1 which mediates the majority of PACAP"s effects.	Disulfides	85-94	adenylate cyclase activating polypeptide 1	Mus musculus	68-73
22706041-2	2012	Cyclopeptide C*HSDGIC* (CHC), which results from the cyclization of PACAP (1-5) with disulfide, has been demonstrated to represent a potent agonist for the PACAP-specific receptor PAC1 which mediates the majority of PACAP"s effects.	Disulfides	85-94	adenylate cyclase activating polypeptide 1	Mus musculus	156-161
22706041-2	2012	Cyclopeptide C*HSDGIC* (CHC), which results from the cyclization of PACAP (1-5) with disulfide, has been demonstrated to represent a potent agonist for the PACAP-specific receptor PAC1 which mediates the majority of PACAP"s effects.	Disulfides	85-94	adenylate cyclase activating polypeptide 1	Mus musculus	156-161
22746182-1	2012	Insulin-like growth factor 1 (IGF-1) is a 70-residue hormone containing three intramolecular disulfide bridges.	Disulfides	93-102	insulin like growth factor 1	Homo sapiens	30-35
22521946-3	2012	Two cysteines, Cys232 and Cys66, nanometer away from each other and from the enzyme active site were proposed to form disulfide bond to regulate the activity of rSULT1A1.	Disulfides	118-127	sulfotransferase family 1A member 1	Rattus norvegicus	161-169
22664107-0	2012	Dissecting the role of disulfide bonds on the amyloid formation of insulin.	Disulfides	23-32	insulin	Homo sapiens	67-74
22490677-9	2012	Homologies of domains in VWF to domains in other proteins allow many disulfide bonds to be tentatively assigned, which may have functional implications.	Disulfides	69-78	von Willebrand factor	Homo sapiens	25-28
22583869-0	2012	A highly conserved tryptophan in the N-terminal variable domain regulates disulfide bond formation and oligomeric assembly of adiponectin.	Disulfides	74-83	adiponectin, C1Q and collagen domain containing	Homo sapiens	126-137
22138455-5	2012	METHODS AND MATERIALS: A recombinant ScFv 18-2 derivative was conjugated to folate via a scissile disulfide linker.	Disulfides	98-107	immunglobulin heavy chain variable region	Homo sapiens	37-41
22537912-2	2012	It is understood that the physiologically functional state of peroxiredoxin 2 is the monomer, and that its role in scavenging low levels of H(2)O(2) results in the formation of disulfide-linked dimers, which are reversibly reduced to monomers by the thioredoxin-thioredoxin reductase system.	Disulfides	177-186	peroxiredoxin 2	Homo sapiens	62-77
22664107-2	2012	Here, we used insulin as a model system, to investigate the role of its individual disulfide bond during the amyloid formation of insulin.	Disulfides	83-92	insulin	Homo sapiens	14-21
22664107-2	2012	Here, we used insulin as a model system, to investigate the role of its individual disulfide bond during the amyloid formation of insulin.	Disulfides	83-92	insulin	Homo sapiens	130-137
22664107-4	2012	Three disulfide bond-modified insulin analogs, INS-2 (lack of A6-A11), INS-3 (lack of A7-B7) and INS-6 (lack of both A6-A11 and A7-B7), were obtained.	Disulfides	6-15	insulin	Homo sapiens	30-37
22451649-1	2012	In heterologous and endogenous expression systems, we studied the role of ERp44 and its complex partner endoplasmic reticulum (ER) oxidase 1-alpha (Ero1-Lalpha) in mechanisms regulating disulfide bond formation for serotonin transporter (SERT), an oligomeric glycoprotein.	Disulfides	186-195	endoplasmic reticulum protein 44	Homo sapiens	74-79
22978166-1	2012	In order to explore the potential influences of the disulfide bridge on the physical and chemical properties of PrP protein, the expressed recombinant human wild-type PrP protein was purified for using in an established redox process for the reduction and oxidation of the ethanethiol group within PrP.	Disulfides	52-61	prion protein	Homo sapiens	112-115
22978166-6	2012	Those data indicates that the formation of the disulfide bridge induces the alteration of the secondary structure and enhances the progresses of aggregation and fibrillization of PrP protein.	Disulfides	47-56	prion protein	Homo sapiens	179-182
22443713-5	2012	The structural model of AtDIR6 was supported experimentally by confirmation of a predicted disulfide bridge and by the characterization of two N-linked glycans at the solvent-exposed protein surface.	Disulfides	91-100	Disease resistance-responsive (dirigent-like protein) family protein	Arabidopsis thaliana	24-30
22207689-3	2012	We hypothesize that disruption of either intra- or interchain disulfide bonds by cysteine mutations in von Willebrand factor has different effects on the biogenesis of Weibel-Palade bodies.	Disulfides	62-71	von Willebrand factor	Homo sapiens	103-124
22484442-0	2012	Effects of alcohol on the solubility and structure of native and disulfide-modified bovine serum albumin.	Disulfides	65-74	albumin	Homo sapiens	91-104
22442152-5	2012	Insertion of ED-B appears to stabilize overall head-to-tail dimerization of two separate Fn chains, which, together with alternating homodimer formation via disulfide bridges at the C-terminal Fn tail, should lead to the known macromolecular fibril formation.	Disulfides	157-166	fibronectin 1	Homo sapiens	13-17
22514274-5	2012	Initially, a CP12 conformation characterized by a circular structural motif including the C-terminal disulfide is selected by GAPDH.	Disulfides	101-110	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	126-131
22577854-4	2012	To that effect, a monoclonal antibody, C219, directed against the intracellular ATP-binding site of the membrane-anchored MDR transporter ABCB1 [P-glycoprotein (P-gp), MDR1], was conjugated to human immunodeficiency virus [HIV(37-72)Tat] translocator peptide through a disulfide bridge.	Disulfides	269-278	ATP-binding cassette, sub-family B (MDR/TAP), member 1B	Mus musculus	138-143
22354542-8	2012	A disulfide bond between Cys6 and Cys113 was identified in 3-morpholinosydnonimine hydrochloride (SIN-1)-treated SR monomer and dimer.	Disulfides	2-11	MAPK associated protein 1	Homo sapiens	98-103
22484084-6	2012	To enhance its stability and neutralizing potency, a disulfide-stabilized scFv, ds-FV57, was also derived by introduction of cysteines at V(H)44 and V(L)100.	Disulfides	53-62	immunglobulin heavy chain variable region	Homo sapiens	74-78
22451649-13	2012	Based on these collective findings, we hypothesize that ERp44 together with Ero1-Lalpha plays an important role in disulfide formation of SERT, which may be a prerequisite step for the assembly of SERT molecules in oligomeric form.	Disulfides	115-124	solute carrier family 6 member 4	Homo sapiens	197-201
22451649-2	2012	ERp44 is an ER lumenal chaperone protein that favors the maturation of disulfide-linked oligomeric proteins.	Disulfides	71-80	endoplasmic reticulum protein 44	Homo sapiens	0-5
22451649-12	2012	These interactions with the chaperone may reflect the inability of Cys-200 and Cys-209 SERT mutants to form a disulfide bond and self-association as evidenced by immunoprecipitation assays.	Disulfides	110-119	solute carrier family 6 member 4	Homo sapiens	87-91
22451649-13	2012	Based on these collective findings, we hypothesize that ERp44 together with Ero1-Lalpha plays an important role in disulfide formation of SERT, which may be a prerequisite step for the assembly of SERT molecules in oligomeric form.	Disulfides	115-124	endoplasmic reticulum protein 44	Homo sapiens	56-61
22451649-13	2012	Based on these collective findings, we hypothesize that ERp44 together with Ero1-Lalpha plays an important role in disulfide formation of SERT, which may be a prerequisite step for the assembly of SERT molecules in oligomeric form.	Disulfides	115-124	solute carrier family 6 member 4	Homo sapiens	138-142
22220984-6	2012	A specific protein-protein interaction between either isoform and protein disulfide isomerase (PDI) facilitates the propagation of disulfides from Ero1 via PDI to nascent polypeptides, and inbuilt oxidative shutdown mechanisms in Ero1alpha and Ero1beta prevent excessive oxidation of PDI.	Disulfides	131-141	endoplasmic reticulum oxidoreductase 1 beta	Homo sapiens	244-252
22083516-9	2012	Retained mutant matrilin 3 formed disulfide-bonded aggregates and caused the co-retention of matrilin 1.	Disulfides	34-43	matrilin 3	Mus musculus	16-26
22427660-0	2012	Human cyclin-dependent kinase 2-associated protein 1 (CDK2AP1) is dimeric in its disulfide-reduced state, with natively disordered N-terminal region.	Disulfides	81-90	cyclin dependent kinase 2 associated protein 1	Homo sapiens	6-52
22427660-0	2012	Human cyclin-dependent kinase 2-associated protein 1 (CDK2AP1) is dimeric in its disulfide-reduced state, with natively disordered N-terminal region.	Disulfides	81-90	cyclin dependent kinase 2 associated protein 1	Homo sapiens	54-61
22503819-5	2012	In vivo disulfide mapping provided additional validation for the crosslinking-derived arrangement as the definitive TRiC topology.	Disulfides	8-17	MARVEL domain containing 2	Homo sapiens	116-120
22503978-12	2012	The molecule resides in the lumen of the endoplasmic reticulum and participates in disulfide bond formation during protein folding by interacting with calnexin and calreticulin.	Disulfides	83-92	calreticulin	Bos taurus	164-176
22083516-11	2012	Mutant matrilin 3 oligomers form non-native disulfide-bonded aggregates through the misfolded A domain.	Disulfides	44-53	matrilin 3	Mus musculus	7-17
22371254-7	2012	MEGF10 contains 17 atypical epidermal growth factor-like domains, each of which contains eight cysteine residues that likely form disulfide bonds.	Disulfides	130-139	multiple EGF like domains 10	Homo sapiens	0-6
23586828-7	2012	In this study, we selected three candidate epitopes within the extra membrane loop of hCD20 with the aid of five immunoinformatics predictor web servers and evaluated mouse humoral response to keyhole-limpet-hemocyaninconjugated peptides, and P4 and P5 peptides (the extracellular loop of hCD20 without and with a disulfide bond, respectively).	Disulfides	314-323	keratin 20	Homo sapiens	86-91
22406321-7	2012	Similarly, a more reduced redox state of the cytosol, but not of the ER, is observed during oxidative protein folding in the ER without UPR induction, as demonstrated by overexpressing genes of disulfide bond-rich secretory proteins such as porcine trypsinogen or protein disulfide isomerase (PDI1) and ER oxidase (ERO1).	Disulfides	194-203	ER oxidoreductin	Saccharomyces cerevisiae S288C	315-319
22326886-3	2012	We find that among the five members of the Grx family and two members of the thioredoxin (Trx) family (Trx1 and Trx2), Grx5 alone interacts with SPT10 via an intermolecular disulfide linkage between Cys60 of Grx5 and Cys385 of SPT10.	Disulfides	173-182	thioredoxin TRX2	Saccharomyces cerevisiae S288C	112-116
22326886-3	2012	We find that among the five members of the Grx family and two members of the thioredoxin (Trx) family (Trx1 and Trx2), Grx5 alone interacts with SPT10 via an intermolecular disulfide linkage between Cys60 of Grx5 and Cys385 of SPT10.	Disulfides	173-182	monothiol glutaredoxin GRX5	Saccharomyces cerevisiae S288C	119-123
22326886-6	2012	From this study, we suggest an interaction between Grx5 and SPT10 via intermolecular disulfide linkage and propose a model for a role of Grx5 in the regulation of protein expression under the control of SPT10.	Disulfides	85-94	monothiol glutaredoxin GRX5	Saccharomyces cerevisiae S288C	51-55
22225540-2	2012	Conjugation of Cyt c with either the amphipathic peptide model amphipathic peptide (MAP) or the cationic peptide oligoarginine via a disulfide linkage significantly increased the total internalization and nuclear localization of Cyt c in both cell lines, though to a greater extent following conjugation with MAP.	Disulfides	133-142	cytochrome c, somatic	Homo sapiens	15-20
22225540-2	2012	Conjugation of Cyt c with either the amphipathic peptide model amphipathic peptide (MAP) or the cationic peptide oligoarginine via a disulfide linkage significantly increased the total internalization and nuclear localization of Cyt c in both cell lines, though to a greater extent following conjugation with MAP.	Disulfides	133-142	cytochrome c, somatic	Homo sapiens	229-234
22401798-2	2012	TF contains a surface exposed allosteric disulfide bond that stabilizes the carboxyl-terminal domain involved in ligand interactions with coagulation factors VIIa and X.	Disulfides	41-50	coagulation factor III	Mus musculus	0-2
22401798-4	2012	However, thiol modifying agents, without suppressing phosphatidylserine exposure, can prevent TF activation, implicating thiol-disulfide exchange reactions in the regulation of TF procoagulant activity of primary cells.	Disulfides	127-136	coagulation factor III	Mus musculus	177-179
22503683-0	2012	Antagonistic effect of disulfide-rich peptide aptamers selected by cDNA display on interleukin-6-dependent cell proliferation.	Disulfides	23-32	interleukin 6	Homo sapiens	83-96
22503683-2	2012	We previously identified peptide aptamers containing one or two disulfide-bonds as an alternative ligand to the interleukin-6 receptor (IL-6R).	Disulfides	64-73	interleukin 6 receptor	Homo sapiens	112-134
22503683-2	2012	We previously identified peptide aptamers containing one or two disulfide-bonds as an alternative ligand to the interleukin-6 receptor (IL-6R).	Disulfides	64-73	interleukin 6 receptor	Homo sapiens	136-141
22503683-5	2012	The results revealed that a disulfide-rich peptide aptamer inhibited IL-6-dependent cell proliferation with similar efficacy to an anti-IL-6R monoclonal antibody.	Disulfides	28-37	interleukin 6	Homo sapiens	69-73
22503683-5	2012	The results revealed that a disulfide-rich peptide aptamer inhibited IL-6-dependent cell proliferation with similar efficacy to an anti-IL-6R monoclonal antibody.	Disulfides	28-37	interleukin 6 receptor	Homo sapiens	136-141
22351773-8	2012	In vitro, secreted myonectin forms disulfide-linked oligomers, and when co-expressed, forms heteromeric complexes with other members of the C1q/TNF-related protein family.	Disulfides	35-44	erythroferrone	Mus musculus	19-28
22471402-1	2012	cis-Diamminedichloroplatinum(II) (cisplatin) is able to interact with human superoxide dismutase (hSOD1) in the disulfide oxidized apo form with a dissociation constant of 37 +- 3 muM through binding cysteine 111 (Cys111) located at the edge of the subunit interface.	Disulfides	112-121	superoxide dismutase 1	Homo sapiens	98-103
22425777-0	2012	Identification of an intra-molecular disulfide bond in the sodium channel beta1-subunit.	Disulfides	37-46	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	74-79
22425777-4	2012	This mutation changed a conserved cysteine residue in position 121 into a tryptophan, putatively disrupting a disulfide bridge that should normally maintain the beta1 extracellular immunoglobulin-like fold.	Disulfides	110-119	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	161-166
22425777-5	2012	Using the 2-D-diagonal-SDS-PAGE technique, we demonstrated the existence of this putative disulfide bridge in the Ig-like extracellular domain of the beta1 subunit and its disruption in the epileptogenic C121W mutant.	Disulfides	90-99	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	150-155
22181833-1	2012	The LRP (low-density lipoprotein receptor-related protein) can bind a wide range of structurally diverse ligands to regions composed of clusters of ~40 residue Ca2+-dependent, disulfide-rich, CRs (complement-like repeats).	Disulfides	176-185	LDL receptor related protein 1	Homo sapiens	4-7
22357757-2	2012	Here we show that the testis-specific protein disulfide isomerase homolog (PDILT) cooperates with the testis-specific calreticulin-like chaperone, calsperin (CALR3), in the endoplasmic reticulum and plays an indispensable role in the disulfide-bond formation and folding of ADAM3.	Disulfides	46-55	protein disulfide isomerase like, testis expressed	Homo sapiens	75-80
22266140-0	2012	Disulfide bonds are critical for tissue-nonspecific alkaline phosphatase function revealed by analysis of mutant proteins bearing a C(201)-Y or C(489)-S substitution associated with severe hypophosphatasia.	Disulfides	0-9	alkaline phosphatase, placental	Homo sapiens	52-72
22219129-0	2012	Oxidative modification of cysteine 111 promotes disulfide bond-independent aggregation of SOD1.	Disulfides	48-57	superoxide dismutase 1	Homo sapiens	90-94
22219129-7	2012	This oxidative modification of cysteine 111 therefore promotes the formation of disulfide bond-independent aggregation of SOD1.	Disulfides	80-89	superoxide dismutase 1	Homo sapiens	122-126
22105604-5	2012	Using tandem mass spectrometric analysis, we now have established that the C106 thiol and the C23-C45 disulfide bond are required for HMGB1 to induce nuclear NF-kappaB translocation and tumor necrosis factor (TNF) production in macrophages.	Disulfides	102-111	tumor necrosis factor	Mus musculus	186-207
22105604-5	2012	Using tandem mass spectrometric analysis, we now have established that the C106 thiol and the C23-C45 disulfide bond are required for HMGB1 to induce nuclear NF-kappaB translocation and tumor necrosis factor (TNF) production in macrophages.	Disulfides	102-111	tumor necrosis factor	Mus musculus	209-212
22244853-4	2012	Cyc[60-70] was formed by disulfide cross-linking of cysteine residues added to the termini of the fibrillogenic peptide comprising apoC-II residues 60-70.	Disulfides	25-34	cytochrome c, somatic	Homo sapiens	0-3
22244853-7	2012	Reduction of the disulfide bond or scrambling the amino acid sequence within cyc[60-70] significantly impaired its inhibitory activity.	Disulfides	17-26	cytochrome c, somatic	Homo sapiens	77-80
22470188-1	2012	Proinsulin C-peptide, released in equimolar amounts with insulin by pancreatic beta cells, since its discovery in 1967 has been thought to be devoid of biological functions apart from correct insulin processing and formation of disulfide bonds between A and B chains.	Disulfides	228-237	insulin	Homo sapiens	11-20
22357757-2	2012	Here we show that the testis-specific protein disulfide isomerase homolog (PDILT) cooperates with the testis-specific calreticulin-like chaperone, calsperin (CALR3), in the endoplasmic reticulum and plays an indispensable role in the disulfide-bond formation and folding of ADAM3.	Disulfides	46-55	calreticulin 3	Homo sapiens	147-156
22357757-2	2012	Here we show that the testis-specific protein disulfide isomerase homolog (PDILT) cooperates with the testis-specific calreticulin-like chaperone, calsperin (CALR3), in the endoplasmic reticulum and plays an indispensable role in the disulfide-bond formation and folding of ADAM3.	Disulfides	46-55	calreticulin 3	Homo sapiens	158-163
22357757-2	2012	Here we show that the testis-specific protein disulfide isomerase homolog (PDILT) cooperates with the testis-specific calreticulin-like chaperone, calsperin (CALR3), in the endoplasmic reticulum and plays an indispensable role in the disulfide-bond formation and folding of ADAM3.	Disulfides	46-55	ADAM metallopeptidase domain 3A (pseudogene)	Homo sapiens	274-279
22063273-6	2012	We reasoned that if identical residues in the double belt juxtapositions were mutated to a cysteine and kept under reducing conditions during disc formation, we would have a precise method for determining registration in discoidal HDL by formation of a disulfide-linked apoA-I homodimer.	Disulfides	253-262	apolipoprotein A1	Homo sapiens	270-276
22340500-3	2012	Here, we show that Furin and SKI-1 combine with autocatalytic cleavage and a disulfide bridge to generate four membrane-bound and three soluble forms of the repulsive guidance molecule (RGMa).	Disulfides	77-86	repulsive guidance molecule BMP co-receptor a	Homo sapiens	186-190
22002549-2	2012	Wild-type HspB1 and Cys mutants of HspB5, HspB6 and HspB8 containing a single Cys residue in position homologous to that of Cys137 of human HspB1 were able to generate heterodimers cross-linked by disulfide bond.	Disulfides	197-206	heat shock protein family B (small) member 6	Homo sapiens	42-47
22002549-2	2012	Wild-type HspB1 and Cys mutants of HspB5, HspB6 and HspB8 containing a single Cys residue in position homologous to that of Cys137 of human HspB1 were able to generate heterodimers cross-linked by disulfide bond.	Disulfides	197-206	heat shock protein family B (small) member 8	Homo sapiens	52-57
22278742-2	2012	We find that Cys-192 and Cys-331 of GARP disulfide link to the TGFbeta1 prodomain and that GARP with C192A and C331A mutations can also noncovalently associate with proTGFbeta1.	Disulfides	41-50	transforming growth factor beta 1	Homo sapiens	63-71
22207756-0	2012	Productive recognition of factor IX by factor XIa exosites requires disulfide linkage between heavy and light chains of factor XIa.	Disulfides	68-77	coagulation factor IX	Homo sapiens	26-35
22201548-10	2012	The thermal stability of alpha-La stabilized emulsions in the presence of salt is a combined effect of the electrostatic repulsion and the lack of covalent disulfide interchange reactions.	Disulfides	156-165	lactalbumin alpha	Homo sapiens	25-33
22117064-0	2012	Defining the disulfide bonds of insulin-like growth factor-binding protein-5 by tandem mass spectrometry with electron transfer dissociation and collision-induced dissociation.	Disulfides	13-22	insulin like growth factor binding protein 5	Homo sapiens	32-76
22004669-0	2012	Identification of persulfide-binding and disulfide-forming cysteine residues in the NifS-like domain of the molybdenum cofactor sulfurase ABA3 by cysteine-scanning mutagenesis.	Disulfides	41-50	molybdenum cofactor sulfurase (LOS5) (ABA3)	Arabidopsis thaliana	108-137
22004669-0	2012	Identification of persulfide-binding and disulfide-forming cysteine residues in the NifS-like domain of the molybdenum cofactor sulfurase ABA3 by cysteine-scanning mutagenesis.	Disulfides	41-50	molybdenum cofactor sulfurase (LOS5) (ABA3)	Arabidopsis thaliana	138-142
22013897-5	2012	Interestingly, N60 derived from thrombin cleavage of rsTEM5 was covalently linked to C50 by disulfide bonds, whereas N60 shed from thrombin-treated cells was not associated with its membrane-bound C-terminal counterpart.	Disulfides	92-101	coagulation factor II, thrombin	Homo sapiens	32-40
22013897-9	2012	We conclude that PDI regulates thrombin-induced shedding of N60 and exposure of the TEM5 RGD motif by catalysing the reduction of crucial disulfide bonds of TEM5 on the cell surface.	Disulfides	138-147	coagulation factor II, thrombin	Homo sapiens	31-39
22013897-9	2012	We conclude that PDI regulates thrombin-induced shedding of N60 and exposure of the TEM5 RGD motif by catalysing the reduction of crucial disulfide bonds of TEM5 on the cell surface.	Disulfides	138-147	adhesion G protein-coupled receptor A2	Homo sapiens	84-88
22013897-9	2012	We conclude that PDI regulates thrombin-induced shedding of N60 and exposure of the TEM5 RGD motif by catalysing the reduction of crucial disulfide bonds of TEM5 on the cell surface.	Disulfides	138-147	adhesion G protein-coupled receptor A2	Homo sapiens	157-161
22190736-5	2012	Through the use of a yeast expression system for apolipoprotein B (ApoB), which is disulfide rich, we discovered that Pdi1 interacts with ApoB and facilitates degradation through its chaperone activity.	Disulfides	83-92	apolipoprotein B	Homo sapiens	67-71
22014003-2	2012	Previously, we discovered an allosteric site at the dimer interface of caspases-3, -7, and -1 using disulfide trapping.	Disulfides	100-109	caspase 3	Homo sapiens	71-93
22131165-8	2012	The feasibility of this method is demonstrated for bovine pancreatic trypsin inhibitor, which has three disulfide bonds.	Disulfides	104-113	trophoblast Kunitz domain protein 1	Bos taurus	69-86
22093877-1	2012	TFF1 is a cysteine-rich protein that forms a characteristic trefoil domain through disulfide bonds, which render it resistant to vigorous conditions and it involves in maintaining the integrity of the gastric mucosa.	Disulfides	83-92	trefoil factor 1	Homo sapiens	0-4
22117064-5	2012	In addition, in conjunction with ab initio molecular modeling we are able to assign the other 4 disulfide linkages to within a GCGCCXXC motif that is conserved in five IGFBPs.	Disulfides	96-105	insulin like growth factor binding protein 5	Homo sapiens	168-174
22117064-7	2012	Our results not only establish a disulfide bond map of IGFBP-5 but also define a general approach that takes advantage of the specificity of ETD and the scalability of tandem MS, and the predictive power of ab initio molecular modeling to characterize unknown disulfide linkages in proteins.	Disulfides	33-42	insulin like growth factor binding protein 5	Homo sapiens	55-62
22105075-1	2012	For insulin synthesis, the proinsulin precursor is translated at the endoplasmic reticulum (ER), folds to include its three native disulfide bonds, and is exported to secretory granules for processing and secretion.	Disulfides	131-140	insulin	Homo sapiens	27-37
22117064-7	2012	Our results not only establish a disulfide bond map of IGFBP-5 but also define a general approach that takes advantage of the specificity of ETD and the scalability of tandem MS, and the predictive power of ab initio molecular modeling to characterize unknown disulfide linkages in proteins.	Disulfides	260-269	insulin like growth factor binding protein 5	Homo sapiens	55-62
22105075-4	2012	The data establish that upon PDI-KD, oxidation of proinsulin to form native disulfide bonds is unimpaired and in fact enhanced.	Disulfides	76-85	insulin	Homo sapiens	50-60
22062630-4	2012	We have determined the redox potential of this disulfide bridge and show that both EC-SOD dimers and EC-SOD monomers are present within the intracellular space.	Disulfides	47-56	superoxide dismutase 3	Homo sapiens	83-89
23132570-6	2012	Im-2 consists of 68 amino acids cross-linked by 4 disulfide bonds, and has sequence similarity to scorpion beta-toxins that have been reported to affect the sodium channels of both insects and mammals.	Disulfides	50-59	immunoregulatory 2	Mus musculus	0-4
23339308-0	2012	SOD1 aggregation and ALS: role of metallation states and disulfide status.	Disulfides	57-66	superoxide dismutase 1	Homo sapiens	0-4
23339308-5	2012	We here review the recent studies on the role of metallation states and disulfide status in the unfolding, misfolding, and aggregation of SOD1.	Disulfides	72-81	superoxide dismutase 1	Homo sapiens	138-142
22062630-4	2012	We have determined the redox potential of this disulfide bridge and show that both EC-SOD dimers and EC-SOD monomers are present within the intracellular space.	Disulfides	47-56	superoxide dismutase 3	Homo sapiens	101-107
22907349-4	2012	Irreversible scFv denaturation, which is a prerequisite for efficient selection, is achieved by combining denaturation with reduction of the intradomain disulfide bonds.	Disulfides	153-162	immunglobulin heavy chain variable region	Homo sapiens	13-17
21982971-7	2012	Transient expression of chicken endoglin allowed the identification of a 180-kDa disulfide linked homodimer similar to the mammalian homologues.	Disulfides	81-90	endoglin	Gallus gallus	32-40
22645657-0	2012	Interleukin-2 signalling is modulated by a labile disulfide bond in the CD132 chain of its receptor.	Disulfides	50-59	interleukin 2	Homo sapiens	0-13
22094809-4	2012	Here we present a detailed protocol for the selection of disulfide-rich peptide aptamers against interleukin 6 receptor (IL-6R) from a 35-amino acid peptide library containing 32 amino acids in the random region, which is linked to its genotype by cDNA display.	Disulfides	57-66	interleukin 6 receptor	Homo sapiens	97-119
22094809-4	2012	Here we present a detailed protocol for the selection of disulfide-rich peptide aptamers against interleukin 6 receptor (IL-6R) from a 35-amino acid peptide library containing 32 amino acids in the random region, which is linked to its genotype by cDNA display.	Disulfides	57-66	interleukin 6 receptor	Homo sapiens	121-126
22645657-3	2012	Recent studies have shown that a wide range of membrane proteins have labile disulfide bonds including CD132, the common gamma chain of the receptors for several cytokines including interleukin-2 and interleukin-4 (IL-2 and IL-4).	Disulfides	77-86	interleukin 2	Homo sapiens	182-195
22645657-3	2012	Recent studies have shown that a wide range of membrane proteins have labile disulfide bonds including CD132, the common gamma chain of the receptors for several cytokines including interleukin-2 and interleukin-4 (IL-2 and IL-4).	Disulfides	77-86	interleukin 4	Homo sapiens	200-213
22645657-3	2012	Recent studies have shown that a wide range of membrane proteins have labile disulfide bonds including CD132, the common gamma chain of the receptors for several cytokines including interleukin-2 and interleukin-4 (IL-2 and IL-4).	Disulfides	77-86	interleukin 4	Homo sapiens	224-228
22645657-6	2012	Conditions that lead to the reduction of the Cys(183)-Cys(232) disulfide bond in CD132 inhibit proliferation of an IL-2-dependent T cell clone and concomitant inhibition of the STAT-5 signalling pathway.	Disulfides	63-72	interleukin 2	Homo sapiens	115-119
22645657-7	2012	The same reducing conditions had no effect on the proliferation of an IL-2-independent T cell clone, nor did they reduce disulfide bonds in IL-2 itself.	Disulfides	121-130	interleukin 2	Homo sapiens	140-144
22645657-8	2012	We postulate that reduction of the Cys(183)-Cys(232) disulfide in CD132 inhibits IL-2 binding to the receptor complex.	Disulfides	53-62	interleukin 2	Homo sapiens	81-85
22645657-9	2012	Published data show that the Cys(183)-Cys(232) disulfide bond is exposed at the surface of CD132 and in close contact with IL-2 and IL-4 in their respective receptor complexes.	Disulfides	47-56	interleukin 2	Homo sapiens	123-127
22645657-9	2012	Published data show that the Cys(183)-Cys(232) disulfide bond is exposed at the surface of CD132 and in close contact with IL-2 and IL-4 in their respective receptor complexes.	Disulfides	47-56	interleukin 4	Homo sapiens	132-136
22848655-8	2012	RON Sema domain adopts a seven-bladed beta-propeller fold, followed by disulfide bond rich, cysteine-knot PSI motif.	Disulfides	71-80	semaphorin 3B	Homo sapiens	4-8
22916297-5	2012	We sequenced and recombinantly expressed two ~25 kDa polypeptides (BgAChBP1 and BgAChBP2) with a specific active site, N-glycan site and disulfide bridge variation.	Disulfides	137-146	acetylcholine-binding protein-like	Biomphalaria glabrata	67-75
21748537-0	2012	Photolysis of recombinant human insulin in the solid state: formation of a dithiohemiacetal product at the C-terminal disulfide bond.	Disulfides	118-127	insulin	Homo sapiens	32-39
21748537-5	2012	RESULTS: UV-exposure of solid human insulin results in photodissociation of the C-terminal intrachain disulfide bond, leading to formation of a CysS( ) thiyl radical pair which ultimately disproportionates into thiol and thioaldehyde species.	Disulfides	102-111	insulin	Homo sapiens	36-43
23118898-0	2012	Role of disulfide cross-linking of mutant SOD1 in the formation of inclusion-body-like structures.	Disulfides	8-17	superoxide dismutase 1	Homo sapiens	42-46
23118898-1	2012	BACKGROUND: Pathologic aggregates of superoxide dismutase 1 (SOD1) harboring mutations linked to familial amyotrophic lateral sclerosis (fALS) have been shown to contain aberrant intermolecular disulfide cross-links.	Disulfides	194-203	superoxide dismutase 1	Homo sapiens	37-59
23118898-1	2012	BACKGROUND: Pathologic aggregates of superoxide dismutase 1 (SOD1) harboring mutations linked to familial amyotrophic lateral sclerosis (fALS) have been shown to contain aberrant intermolecular disulfide cross-links.	Disulfides	194-203	superoxide dismutase 1	Homo sapiens	61-65
23118898-6	2012	CONCLUSIONS/SIGNIFICANCE: Overall, this study is an extension of previous work demonstrating that cysteine residues in mutant SOD1 play a role in modulating aggregation and that intermolecular disulfide bonds are not required to produce large intracellular inclusion-like structures.	Disulfides	193-202	superoxide dismutase 1	Homo sapiens	126-130
22879932-3	2012	Recently, we demonstrated that engineering an additional disulfide bond and removing seven N-terminal residues results in an engineered antibody domain (eAd) (m01s) with highly increased stability and enhanced binding to human neonatal Fc receptor (FcRn) (Gong et al, JBC, 2009 and 2011).	Disulfides	57-66	Fc gamma receptor and transporter	Homo sapiens	227-247
22879932-3	2012	Recently, we demonstrated that engineering an additional disulfide bond and removing seven N-terminal residues results in an engineered antibody domain (eAd) (m01s) with highly increased stability and enhanced binding to human neonatal Fc receptor (FcRn) (Gong et al, JBC, 2009 and 2011).	Disulfides	57-66	Fc gamma receptor and transporter	Homo sapiens	249-253
22675475-5	2012	All three disulfide bonds of native insulin remained intact during the aggregation process, withstanding scrambling.	Disulfides	10-19	insulin	Homo sapiens	36-43
22675475-7	2012	In addition, using all-atom MD simulations, the disulfide bonds were confirmed to remain intact in the insulin dimer, which mimics the fibrillar form of insulin.	Disulfides	48-57	insulin	Homo sapiens	103-110
22675475-7	2012	In addition, using all-atom MD simulations, the disulfide bonds were confirmed to remain intact in the insulin dimer, which mimics the fibrillar form of insulin.	Disulfides	48-57	insulin	Homo sapiens	153-160
22586462-2	2012	They consist of a conserved three-dimensional (3D) structure, so-called IL8-like chemokine fold, which is supported by disulfide bridges characteristic of this protein family.	Disulfides	119-128	C-X-C motif chemokine ligand 8	Homo sapiens	72-75
22272277-6	2012	Additionally, we have introduced the intradomain disulfide bonds into an IgG Fc fragment engineered in C-terminal loops of the CH3 domain for binding to Her2/neu, and observed an increase of the T(m) of the CH3 domain for 7.5 C for CysP4, 15.5 C for CysP2 and 19 C for the CysP2 and CysP4 disulfide bonds combined in one molecule.	Disulfides	49-58	erb-b2 receptor tyrosine kinase 2	Homo sapiens	153-161
22389684-5	2012	In the current study, we generated a panel of Cys-to-Ser mutants to interrogate the potential for disulfide bond formation in AAV capsids.	Disulfides	98-107	adeno-associated virus integration site 1	Homo sapiens	126-129
22050912-9	2011	These results suggest that the HMP is a disulfide-linked protein complex involving mtMGST1, ANT, CypD and function as a MPT pore in PON-induced swelling, in which the Ca(2+) released by PON might play an important role in the complex formation.	Disulfides	40-49	peptidylprolyl isomerase F	Homo sapiens	97-101
22291921-4	2012	A CD4-mimetic miniprotein, miniCD4 (M64U1-SH), was produced and covalently complexed to recombinant, trimeric gp140 envelope glycoprotein (gp140) using site-specific disulfide linkages.	Disulfides	166-175	CD4 molecule	Homo sapiens	2-5
21911017-2	2011	Two novel linker molecules, containing an ester bond and/or a disulfide bond for temporary immobilization, were synthesized and conjugated to lysozyme.	Disulfides	62-71	lysozyme	Homo sapiens	142-150
21911017-7	2011	Upon hydrolysis of the ester bonds or incubation with glutathione to reduce disulfide bonds of the linker molecules that conjugate the lysozyme to the gel network, the modified lysozyme was mobilized and released from the hydrogel to the same extent as native lysozyme.	Disulfides	76-85	lysozyme	Homo sapiens	135-143
21911017-7	2011	Upon hydrolysis of the ester bonds or incubation with glutathione to reduce disulfide bonds of the linker molecules that conjugate the lysozyme to the gel network, the modified lysozyme was mobilized and released from the hydrogel to the same extent as native lysozyme.	Disulfides	76-85	lysozyme	Homo sapiens	177-185
21911017-7	2011	Upon hydrolysis of the ester bonds or incubation with glutathione to reduce disulfide bonds of the linker molecules that conjugate the lysozyme to the gel network, the modified lysozyme was mobilized and released from the hydrogel to the same extent as native lysozyme.	Disulfides	76-85	lysozyme	Homo sapiens	177-185
22023352-7	2011	We use MAPS to illustrate in silico the propagation of a local perturbation over medium- to long-range distances across a disulfide bridge linking loops L1 and L2, which constitute the binding interface of BPTI.	Disulfides	122-131	L1 cell adhesion molecule	Homo sapiens	153-162
21898342-4	2011	METHODS: Conformational changes in beta(2)GPI were studied using various techniques, either upon binding to cardiolipin or after disruption of the internal disulfide bonds.	Disulfides	156-165	apolipoprotein H	Mus musculus	35-45
22007786-2	2011	As a proof-of-concept demonstration, Au-MSNs are shown to release luciferin from the interior pores of MSN upon AuNP uncapping in response to disulfide-reducing antioxidants and codeliver bioactive luciferase from the PEGylated exterior surface of Au-MSN to Hela cells.	Disulfides	142-151	moesin	Homo sapiens	40-43
22007786-2	2011	As a proof-of-concept demonstration, Au-MSNs are shown to release luciferin from the interior pores of MSN upon AuNP uncapping in response to disulfide-reducing antioxidants and codeliver bioactive luciferase from the PEGylated exterior surface of Au-MSN to Hela cells.	Disulfides	142-151	moesin	Homo sapiens	103-106
22051117-1	2011	Transglutaminase 2 (TG2; EC 2.3.2.13) is the most abundantly expressed member of the transglutaminase family and exerts opposing effects on cell growth, differentiation and apoptosis via multiple activities, including transamidase, GTPase, cell adhesion, protein disulfide isomerase, kinase and scaffold activities.	Disulfides	263-272	transglutaminase 2	Homo sapiens	0-18
21949131-9	2011	Next, we introduced disulfide mutations into full-length FN.	Disulfides	20-29	fibronectin 1	Homo sapiens	57-59
21835919-6	2011	Prx IV-L was detected in spermatids but not in mature sperm, it could form disulfide-linked dimers but not higher order oligomers via oxidation, and it was resistant to hyperoxidation unless additional reductant was added, suggesting that its peroxidase activity is limited in vivo.	Disulfides	75-84	peroxiredoxin 4	Mus musculus	0-6
22098737-3	2011	We studied how a disulfide bond in the obligatory GluN1 subunit-the sole site of redox modulation in NMDA receptors-controls this activation gating mechanism.	Disulfides	17-26	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	50-55
21930702-6	2011	Furthermore, L-homocysteine covalently bound hnRNP-E1 via multiple protein-cysteine-S-S-homocysteine mixed disulfide bonds within K-homology domains known to interact with mRNA.	Disulfides	107-116	poly(rC) binding protein 1	Homo sapiens	45-53
21949131-11	2011	When we tested the disulfide mutants in cell culture, only the disulfide bond in (III)2 reduced the FN matrix.	Disulfides	63-72	fibronectin 1	Homo sapiens	100-102
21880711-9	2011	The most interesting aspect of the structure was the unexpected disulfide bond between Cys-8 and Cys-108, which might be important for regulation of the activity of NALP3 by redox potential.	Disulfides	64-73	NLR family pyrin domain containing 3	Homo sapiens	165-170
21911836-0	2011	Lateral self-association of VWF involves the Cys2431-Cys2453 disulfide/dithiol in the C2 domain.	Disulfides	61-70	von Willebrand factor	Homo sapiens	28-31
21911836-3	2011	Fiber formation has been shown to involve thiol/disulfide exchange between VWF molecules.	Disulfides	48-57	von Willebrand factor	Homo sapiens	75-78
21911836-5	2011	The VWF C2 domain Cys2431-Cys2453 disulfide bond was shown to be reduced in approximately 75% of the molecules.	Disulfides	34-43	von Willebrand factor	Homo sapiens	4-7
21911836-8	2011	Our present findings imply that lateral VWF dimers form when a Cys2431 thiolate anion attacks the Cys2431 sulfur atom of the Cys2431-Cys2453 disulfide bond of another VWF molecule, whereas the Cys2451-Cys2468 disulfide/dithiol mediates formation of trimers and higher-order oligomers.	Disulfides	141-150	von Willebrand factor	Homo sapiens	40-43
21911836-8	2011	Our present findings imply that lateral VWF dimers form when a Cys2431 thiolate anion attacks the Cys2431 sulfur atom of the Cys2431-Cys2453 disulfide bond of another VWF molecule, whereas the Cys2451-Cys2468 disulfide/dithiol mediates formation of trimers and higher-order oligomers.	Disulfides	141-150	von Willebrand factor	Homo sapiens	167-170
21911836-8	2011	Our present findings imply that lateral VWF dimers form when a Cys2431 thiolate anion attacks the Cys2431 sulfur atom of the Cys2431-Cys2453 disulfide bond of another VWF molecule, whereas the Cys2451-Cys2468 disulfide/dithiol mediates formation of trimers and higher-order oligomers.	Disulfides	209-218	von Willebrand factor	Homo sapiens	40-43
21911836-8	2011	Our present findings imply that lateral VWF dimers form when a Cys2431 thiolate anion attacks the Cys2431 sulfur atom of the Cys2431-Cys2453 disulfide bond of another VWF molecule, whereas the Cys2451-Cys2468 disulfide/dithiol mediates formation of trimers and higher-order oligomers.	Disulfides	209-218	von Willebrand factor	Homo sapiens	167-170
21831887-5	2011	Deficiency in oxidoreductase ERp57 results in impaired folding and function of P0, a disulfide bond-containing protein, but does not have any effect on folding or function of PMP22 (a protein that does not contain a disulfide bond).	Disulfides	85-94	protein disulfide isomerase family A member 3	Homo sapiens	29-34
21831887-5	2011	Deficiency in oxidoreductase ERp57 results in impaired folding and function of P0, a disulfide bond-containing protein, but does not have any effect on folding or function of PMP22 (a protein that does not contain a disulfide bond).	Disulfides	216-225	protein disulfide isomerase family A member 3	Homo sapiens	29-34
21987804-4	2011	Treatment with diamide, a thiol-oxidizing agent, induced formation of disulfide bonds between R91C residues in adjacent Orai1 subunits and rapidly blocked STIM1-operated Ca(2+) current.	Disulfides	70-79	stromal interaction molecule 1	Homo sapiens	155-160
21441428-3	2011	Our laboratory has described EPPIN (epididymal protease inhibitor) as  a novel gene on human chromosome 20q12-13.2 that encodes a cysteine-rich  protein containing both Kunitz-type and WAP-type 4-disulfide core consensus  sequences that characterize it as a protease inhibitor.	Disulfides	196-205	epididymal peptidase inhibitor	Homo sapiens	29-34
21441428-3	2011	Our laboratory has described EPPIN (epididymal protease inhibitor) as  a novel gene on human chromosome 20q12-13.2 that encodes a cysteine-rich  protein containing both Kunitz-type and WAP-type 4-disulfide core consensus  sequences that characterize it as a protease inhibitor.	Disulfides	196-205	epididymal peptidase inhibitor	Homo sapiens	36-65
21855639-7	2011	The state of the disulfide bridge has further structural consequences for one face of the enzyme that suggest UPP2 may have additional functions in sensing and initiating cellular responses to oxidative stress.	Disulfides	17-26	uridine phosphorylase 2	Homo sapiens	110-114
21862690-5	2011	Protein sequence comparison among zebrafish GPR81s, mammalian GPR81s, GPR109a, and GPR109b identified a common structure (six Cys residues at the extracellular domains that potentially form three disulfide bonds) in this subfamily of receptors.	Disulfides	196-205	hydroxycarboxylic acid receptor 2	Homo sapiens	70-77
21763105-5	2011	Our results demonstrate that AMA-positive PBC sera demonstrate marked reactivity against 6,8-bis(acetylthio)octanoic acid, implying that chemical modification of the lipoyl ring, i.e. disruption of the S-S disulfide, renders lipoic acid to its reduced form that will promote xenobiotic modification.	Disulfides	206-215	dihydrolipoamide S-acetyltransferase	Homo sapiens	42-45
21763105-6	2011	This observation is particularly significant in light of the function of the lipoyl moiety in electron transport of which the catalytic disulfide constantly opens and closes and, thus, raises the intriguing thesis that common electrophilic agents, i.e. acetaminophen or non-steroidal anti-inflammatory drugs (NSAIDs), may lead to xenobiotic modification in genetically susceptible individuals that results in the generation of AMAs and ultimately clinical PBC.	Disulfides	136-145	dihydrolipoamide S-acetyltransferase	Homo sapiens	456-459
21908620-2	2011	Earlier investigations have highlighted the role of a disulfide bond formed by vicinal Cys residues in maintaining calcium-bound TG2 in an inactive state.	Disulfides	54-63	transglutaminase 2	Homo sapiens	129-132
21816778-13	2011	Our results highlight the crucial role of C65-C89 disulfide bond in LPL binding by GPIHBP1 Ly6 domain.	Disulfides	50-59	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	83-90
21978460-1	2011	BACKGROUND: Alpha 2 macroglobulin (A2M; also known as ovostatin), a homotetrameric protein with four disulfide-linked subunits, has the unique feature of inactivating/inhibiting most known proteases including serine-, threonine-, cysteine-, aspartic- and metalloproteases.	Disulfides	101-110	ovostatin	Gallus gallus	54-63
21936829-1	2011	SLPI (secretory leucoprotease inhibitor) and elafin represent the archetypal members of the WFDC [WAP (whey acidic protein) four disulfide core] family of proteins, and were originally characterized as protease inhibitors but have since been shown to possess a wider repertoire of activities.	Disulfides	129-138	secretory leukocyte peptidase inhibitor	Homo sapiens	0-4
21936829-1	2011	SLPI (secretory leucoprotease inhibitor) and elafin represent the archetypal members of the WFDC [WAP (whey acidic protein) four disulfide core] family of proteins, and were originally characterized as protease inhibitors but have since been shown to possess a wider repertoire of activities.	Disulfides	129-138	secretory leukocyte peptidase inhibitor	Homo sapiens	6-39
21936831-1	2011	Our laboratory has characterized EPPIN [epididymal protease inhibitor; SPINLW1] as a novel gene on human chromosome 20q12-13.2, which encodes a cysteine-rich protein of 133 amino acids with a calculated molecular mass of 15.283 kDa, containing both Kunitz-type and WAP (whey acidic protein)-type four-disulfide core consensus sequences.	Disulfides	301-310	epididymal peptidase inhibitor	Homo sapiens	33-38
21936831-1	2011	Our laboratory has characterized EPPIN [epididymal protease inhibitor; SPINLW1] as a novel gene on human chromosome 20q12-13.2, which encodes a cysteine-rich protein of 133 amino acids with a calculated molecular mass of 15.283 kDa, containing both Kunitz-type and WAP (whey acidic protein)-type four-disulfide core consensus sequences.	Disulfides	301-310	epididymal peptidase inhibitor	Homo sapiens	40-69
21936831-1	2011	Our laboratory has characterized EPPIN [epididymal protease inhibitor; SPINLW1] as a novel gene on human chromosome 20q12-13.2, which encodes a cysteine-rich protein of 133 amino acids with a calculated molecular mass of 15.283 kDa, containing both Kunitz-type and WAP (whey acidic protein)-type four-disulfide core consensus sequences.	Disulfides	301-310	epididymal peptidase inhibitor	Homo sapiens	71-78
21936833-1	2011	The present evaluates the key features of the WFDC1 [WAP (whey acidic protein) four disulfide core 1] gene that encodes ps20 (20 kDa prostate stromal protein), a member of the WAP family.	Disulfides	84-93	WAP four-disulfide core domain 1	Homo sapiens	46-51
21936833-1	2011	The present evaluates the key features of the WFDC1 [WAP (whey acidic protein) four disulfide core 1] gene that encodes ps20 (20 kDa prostate stromal protein), a member of the WAP family.	Disulfides	84-93	WAP four-disulfide core domain 1	Homo sapiens	120-124
21824290-4	2011	Here we review recent studies in which protein engineering, and in particular disulfide engineering, has been applied to stabilize different Abeta aggregates.	Disulfides	78-87	amyloid beta precursor protein	Homo sapiens	141-146
21824290-6	2011	Disulfide engineering has also revealed structural properties of neurotoxic aggregates, for instance that Abeta in protofibrils and globular oligomers adopts a beta-hairpin conformation that is similar to, but topologically distinct from, the conformation of Abeta in mature amyloid fibrils.	Disulfides	0-9	amyloid beta precursor protein	Homo sapiens	106-111
21824290-6	2011	Disulfide engineering has also revealed structural properties of neurotoxic aggregates, for instance that Abeta in protofibrils and globular oligomers adopts a beta-hairpin conformation that is similar to, but topologically distinct from, the conformation of Abeta in mature amyloid fibrils.	Disulfides	0-9	amyloid beta precursor protein	Homo sapiens	259-264
21865594-2	2011	Active Sod1 is a homodimer containing one zinc ion, one copper ion, and one disulfide bond per subunit.	Disulfides	76-85	superoxide dismutase 1	Homo sapiens	7-11
21844193-7	2011	H(2)O(2) exposure triggers formation of a dual disulfide bonded Yap1 that is catalyzed by the presence of Gpx3 and Ybp1.	Disulfides	47-56	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	64-68
21781282-3	2011	In the present study, we characterized an oxidoreductase, AtVKOR-DsbA, encoded by the gene At4g35760 as a potential disulfide bond oxidant in Arabidopsis.	Disulfides	116-125	oxidoreductase	Arabidopsis thaliana	42-56
21930926-3	2011	Expression of the enzymatically inactive, natural familial ALS SOD1 mutations G127X and G85R in human mesenchymal and neural cell lines induces misfolding of wild-type natively structured SOD1, as indicated by: acquisition of immunoreactivity with SOD1 misfolding-specific monoclonal antibodies; markedly enhanced protease sensitivity suggestive of structural loosening; and nonnative disulfide-linked oligomer and multimer formation.	Disulfides	385-394	superoxide dismutase 1	Homo sapiens	63-67
21930926-3	2011	Expression of the enzymatically inactive, natural familial ALS SOD1 mutations G127X and G85R in human mesenchymal and neural cell lines induces misfolding of wild-type natively structured SOD1, as indicated by: acquisition of immunoreactivity with SOD1 misfolding-specific monoclonal antibodies; markedly enhanced protease sensitivity suggestive of structural loosening; and nonnative disulfide-linked oligomer and multimer formation.	Disulfides	385-394	superoxide dismutase 1	Homo sapiens	188-192
21930926-3	2011	Expression of the enzymatically inactive, natural familial ALS SOD1 mutations G127X and G85R in human mesenchymal and neural cell lines induces misfolding of wild-type natively structured SOD1, as indicated by: acquisition of immunoreactivity with SOD1 misfolding-specific monoclonal antibodies; markedly enhanced protease sensitivity suggestive of structural loosening; and nonnative disulfide-linked oligomer and multimer formation.	Disulfides	385-394	superoxide dismutase 1	Homo sapiens	188-192
21802428-4	2011	Our model is upain-1 (CSWRGLENHRMC), a disulfide-bond-constrained competitive inhibitor of human urokinase-type plasminogen activator with a noncanonical inhibitory mechanism and an unusually high specificity.	Disulfides	39-48	plasminogen activator, urokinase	Homo sapiens	97-133
21892159-4	2011	In most cases, these IL7R mutations introduce an unpaired cysteine in the extracellular juxtamembrane-transmembrane region and promote de novo formation of intermolecular disulfide bonds between mutant IL-7Ralpha subunits, thereby driving constitutive signaling via JAK1 and independently of IL-7, gammac or JAK3.	Disulfides	171-180	interleukin 7	Homo sapiens	202-206
21670067-2	2011	Here, we have identified the intrasubunit disulfide bond as a conserved switch that controls the structure and functions of CRP.	Disulfides	42-51	C-reactive protein	Homo sapiens	124-127
21670067-8	2011	Therefore, expression of proinflammatory properties of CRP on endothelial cells requires sequential conformational changes, i.e., loss of pentameric symmetry followed by reduction of the intrasubunit disulfide bond.	Disulfides	200-209	C-reactive protein	Homo sapiens	55-58
21787789-2	2011	It shows the architecture of the three disulfide-linked polypeptide chains (alpha, beta, and gamma) of the acidic subunit CA noncovalently complexed with the basic phospholipase A(2) (PLA(2)) subunit CB.	Disulfides	39-48	phospholipase A2 group IB	Homo sapiens	164-182
21787789-2	2011	It shows the architecture of the three disulfide-linked polypeptide chains (alpha, beta, and gamma) of the acidic subunit CA noncovalently complexed with the basic phospholipase A(2) (PLA(2)) subunit CB.	Disulfides	39-48	phospholipase A2 group IB	Homo sapiens	184-190
22048691-0	2011	The improvement of an anti-CD22 immunotoxin: conversion to single-chain and disulfide stabilized form and affinity maturation by alanine scan.	Disulfides	76-85	CD22 molecule	Homo sapiens	27-31
21598303-8	2011	To determine if an interaction between the rel homology binding domain in ERp57 and the nuclear factor-kappaB subunit, p65, occurred after TNF-alpha treatment and could account for nuclear movement, co-immunoprecipitation was performed under control and conditions that stabilized labile disulfide bonds.	Disulfides	288-297	protein disulfide isomerase family A member 3	Homo sapiens	74-79
21615106-6	2011	In addition, the knottin variant mediated 20-fold enhanced affinity for thrombin, when compared to the same seven residue binding epitope constrained by a single disulfide bond.	Disulfides	162-171	coagulation factor II, thrombin	Homo sapiens	72-80
21631431-11	2011	An activating deletion mutation of IL27R enhanced homodimerization of the receptor by a mechanism that may involve disulfide bonding.	Disulfides	115-124	interleukin 27 receptor, alpha	Mus musculus	35-40
21666221-8	2011	Protein thiyl radical formation leads to oxidation or modification of cysteine with either disulfide bond formation or S-glutathionylation, which induces eNOS uncoupling.	Disulfides	91-100	nitric oxide synthase 3	Homo sapiens	154-158
21688771-4	2011	The potential role of a disulfide bond between two conserved Cys residues, Cys(105) in TM3 and Cys(182) in EC2, is necessary for proper folding and trafficking in VCOP.	Disulfides	24-33	tropomyosin 3 L homeolog	Xenopus laevis	87-90
21459789-0	2011	The natural occurrence of human fibrinogen variants disrupting inter-chain disulfide bonds (A{alpha}Cys36Gly, A{alpha}Cys36Arg and A{alpha}Cys45Tyr) confirms the role of N-terminal A{alpha} disulfide bonds in protein assembly and secretion.	Disulfides	75-84	fibrinogen beta chain	Homo sapiens	32-42
21459789-0	2011	The natural occurrence of human fibrinogen variants disrupting inter-chain disulfide bonds (A{alpha}Cys36Gly, A{alpha}Cys36Arg and A{alpha}Cys45Tyr) confirms the role of N-terminal A{alpha} disulfide bonds in protein assembly and secretion.	Disulfides	190-199	fibrinogen beta chain	Homo sapiens	32-42
21459789-1	2011	Analyses of site-directed fibrinogen mutants expressed in several recombinant models have previously shown that both inter- and intra-chain disulfide bonds are critical for fibrinogen assembly and secretion.	Disulfides	140-149	fibrinogen beta chain	Homo sapiens	26-36
21459789-1	2011	Analyses of site-directed fibrinogen mutants expressed in several recombinant models have previously shown that both inter- and intra-chain disulfide bonds are critical for fibrinogen assembly and secretion.	Disulfides	140-149	fibrinogen beta chain	Homo sapiens	173-183
21459789-3	2011	This confirms the main role of the AalphaCys36-BbetaCys65 and AalphaCys45-gammaCys23 disulfide bonds in reaching a normal fibrinogen plasma level.	Disulfides	85-94	fibrinogen beta chain	Homo sapiens	122-132
22417479-6	2011	Our results also suggested that the formation of intermolecular disulfide bonds together with noncovalent interactions are the main mechanisms resulting in the moisture-induced aggregation of alpha-lactalbumin in model systems.	Disulfides	64-73	lactalbumin alpha	Homo sapiens	192-209
22103127-2	2011	Branched polyethylenimine cross-linked via disulfide bonds (ssPEI) complexed with vascular endothelial growth factor (VEGF) were immobilized on electrospun polycaprolactone (PCL)/polyethylenimine (PEI) nanofibers for the local expression of VEGF angiogenic factor.	Disulfides	43-52	vascular endothelial growth factor A	Homo sapiens	82-116
21673386-7	2011	Therefore, human serum albumin can be fabricated into nanoparticles by breaking the disulfide bonds and these nanoparticles exhibit high tumor targeting ability.	Disulfides	84-93	albumin	Homo sapiens	17-30
21724266-6	2011	A Western blot analysis using an anti-DPEP3 polyclonal antibody established in this study showed that this molecule was glycosylated and formed a disulfide-linked homodimer within the testis.	Disulfides	146-155	dipeptidase 3	Mus musculus	38-43
21664938-4	2011	Based on our previous research, a GLP-1 analog that contained an intra-disulfide bond exhibited a prolonged biological half-life.	Disulfides	71-80	glucagon	Homo sapiens	34-39
21568348-7	2011	Our results suggest that 6-TGNP can also react with the redox-sensitive GXXXCGK(S/T)C and GXXXXGK(S/T)C motif of RhoA and Rac, respectively, to produce a 6-TGNP-RhoA and 6-TGNP-Rac disulfide adduct.	Disulfides	181-190	AKT serine/threonine kinase 1	Homo sapiens	122-125
21568348-7	2011	Our results suggest that 6-TGNP can also react with the redox-sensitive GXXXCGK(S/T)C and GXXXXGK(S/T)C motif of RhoA and Rac, respectively, to produce a 6-TGNP-RhoA and 6-TGNP-Rac disulfide adduct.	Disulfides	181-190	AKT serine/threonine kinase 1	Homo sapiens	177-180
21591667-0	2011	Crystallographic snapshots of Tom20-mitochondrial presequence interactions with disulfide-stabilized peptides.	Disulfides	80-89	translocase of outer mitochondrial membrane 20	Homo sapiens	30-35
21714924-8	2011	We found that U24 is isolated with an intramolecular disulfide bond under these conditions, and we probed whether this disulfide bond was critical to high yield expression of full-length protein.	Disulfides	53-62	small nucleolar RNA, C/D box 24	Homo sapiens	14-17
21714924-8	2011	We found that U24 is isolated with an intramolecular disulfide bond under these conditions, and we probed whether this disulfide bond was critical to high yield expression of full-length protein.	Disulfides	119-128	small nucleolar RNA, C/D box 24	Homo sapiens	14-17
21714924-9	2011	Expression analysis of a C21SC37S cysteine-free mutant U24 demonstrated that this disulfide was not critical for full-length protein expression, but it is more likely that strained metabolic conditions favour factors which promote protein expression.	Disulfides	82-91	small nucleolar RNA, C/D box 24	Homo sapiens	55-58
21591667-4	2011	The successful crystallization involved tethering the presequence to Tom20 through an intermolecular disulfide bond with an optimized linker.	Disulfides	101-110	translocase of outer mitochondrial membrane 20	Homo sapiens	69-74
21634027-3	2011	During episodes of crisis, ISCs accumulate C284-C373 intramolecularly disulfide bonded actin, which reduces actin filament dynamics.	Disulfides	70-79	actin	Saccharomyces cerevisiae S288C	87-92
21561146-9	2011	ELISA analyses of homocysteinylated fibronectin with three monoclonal antibodies demonstrated structural changes in the disulfide-containing FNI domains FNI(2), FNI(4), and FNI(9).	Disulfides	120-129	fibronectin 1	Homo sapiens	36-47
21507408-3	2011	Thiol groups of beta-Lg underwent a dynamic sulfhydryl/disulfide exchange that is probably essential in accomplishing specific physiological requirements in which proteins may alternatively act either as a trigger or as a target.	Disulfides	55-64	beta-lactoglobulin	Bubalus bubalis	16-23
21507943-6	2011	Thus, for the first time, we demonstrated that GP Ibbeta/GP IX mediates the disulfide-linked GP Ibalpha localization to the GEMs, which is critical for vWf interaction at high shear.	Disulfides	76-85	von Willebrand factor	Homo sapiens	152-155
21235355-5	2011	The net effect of Abeta treatment was an oxidative shift in the intracellular glutathione/glutathione disulfide redox potential in contrast to a reductive shift in response to peroxide.	Disulfides	102-111	amyloid beta precursor protein	Homo sapiens	18-23
21270431-7	2011	ProMBP specifically forms disulfide-mediated, covalent complexes with the metzincin metalloproteinase pregnancy-associated plasma protein A (PAPPA) and the prohormone angiotensinogen (AGT).	Disulfides	26-35	angiotensinogen	Homo sapiens	167-182
21270431-7	2011	ProMBP specifically forms disulfide-mediated, covalent complexes with the metzincin metalloproteinase pregnancy-associated plasma protein A (PAPPA) and the prohormone angiotensinogen (AGT).	Disulfides	26-35	angiotensinogen	Homo sapiens	184-187
21401803-0	2011	A new disulfide-linked dimer of a single-chain antibody fragment against human CD47 induces apoptosis in lymphoid malignant cells via the hypoxia inducible factor-1alpha pathway.	Disulfides	6-15	hypoxia inducible factor 1 subunit alpha	Homo sapiens	138-169
21634027-3	2011	During episodes of crisis, ISCs accumulate C284-C373 intramolecularly disulfide bonded actin, which reduces actin filament dynamics.	Disulfides	70-79	actin	Saccharomyces cerevisiae S288C	108-113
21355045-8	2011	Distinct disulfide-linked TDP-43 dimers and oligomers were detected.	Disulfides	9-18	TAR DNA binding protein	Homo sapiens	26-32
21619930-2	2011	PTX3 is a multimeric protein consisting of eight identical protomers held together by a combination of non-covalent interactions and disulfide bonds.	Disulfides	133-142	pentraxin 3	Homo sapiens	0-4
21515323-0	2011	GLP-1 analogs containing disulfide bond exhibited prolonged half-life in vivo than GLP-1.	Disulfides	25-34	glucagon	Homo sapiens	0-5
21515323-4	2011	In this study, we developed a cluster of GLP-1 mutants containing an inter-disulfide bond that is predicted to increase the half-life of GLP-1 in vivo.	Disulfides	75-84	glucagon	Homo sapiens	41-46
21515323-4	2011	In this study, we developed a cluster of GLP-1 mutants containing an inter-disulfide bond that is predicted to increase the half-life of GLP-1 in vivo.	Disulfides	75-84	glucagon	Homo sapiens	137-142
21515323-8	2011	These results suggest that GLP-1 and exendin-4 mutants containing disulfide bonds might be utilized as possible potent anti-diabetic drugs in the treatment of type 2 diabetes mellitus.	Disulfides	66-75	glucagon	Homo sapiens	27-32
21110117-1	2011	The interferon-gamma-inducible lysosomal thiol reductase enzymes (GILT) have been shown to play an important role in the processing of exogenous antigens by catalyzing disulfide bond reduction, that facilitates unfolding of the native protein antigen to simplify further cleavage by cellular proteases.	Disulfides	168-177	IFI30 lysosomal thiol reductase	Homo sapiens	66-70
21316742-0	2011	Homocysteinylated fibrinogen forms disulfide-linked complexes with albumin.	Disulfides	35-44	fibrinogen beta chain	Homo sapiens	18-28
21316742-6	2011	In those cases the new cysteine mediates disulfide formation between the mutant fibrinogen and albumin.	Disulfides	41-50	fibrinogen beta chain	Homo sapiens	80-90
21316742-7	2011	We now report that Hcys-fibrinogen similarly forms disulfides with albumin in vitro, specifically through sites in its D-domain.	Disulfides	51-61	fibrinogen beta chain	Homo sapiens	24-34
21474446-7	2011	Mutation of Cys(632) alone abolished dimerization in these mutants, indicating that it was the critical residue mediating disulfide bond formation between PC2 monomers.	Disulfides	122-131	polycystin 2, transient receptor potential cation channel	Homo sapiens	155-158
21600065-4	2011	RESULTS: We previously reported that trimers assemble into HMW adiponectin via intermediates stabilized by disulfide bonds, and complete oxidation of available cysteines locks adiponectin in hexameric conformation.	Disulfides	107-116	adiponectin, C1Q and collagen domain containing	Homo sapiens	63-74
21600065-6	2011	Reassembly of adiponectin under oxidizing conditions accelerated disulfide bonding but favored formation of hexamers over the HMW species.	Disulfides	65-74	adiponectin, C1Q and collagen domain containing	Homo sapiens	14-25
21600065-7	2011	Increased ratios of HMW to hexameric adiponectin could be achieved rapidly under oxidizing conditions by promoting disulfide rearrangement.	Disulfides	115-124	adiponectin, C1Q and collagen domain containing	Homo sapiens	37-48
21600065-8	2011	CONCLUSIONS: Based upon these observations, we propose oxidative assembly of multi-subunit adiponectin complexes in a defined and stable redox environment is favored under oxidizing conditions coupled with high rates of disulfide rearrangement.	Disulfides	220-229	adiponectin, C1Q and collagen domain containing	Homo sapiens	91-102
22778868-3	2011	Using computational chemistry, we designed conservative cysteine substitutions in Abeta aiming at accelerating and stabilizing assembly of Abeta dimers by an intermolecular disulfide bond without changing its folding.	Disulfides	173-182	amyloid beta precursor protein	Homo sapiens	82-87
22778868-3	2011	Using computational chemistry, we designed conservative cysteine substitutions in Abeta aiming at accelerating and stabilizing assembly of Abeta dimers by an intermolecular disulfide bond without changing its folding.	Disulfides	173-182	amyloid beta precursor protein	Homo sapiens	139-144
21338337-1	2011	The colonic human MUC2 mucin forms a polymeric gel by covalent disulfide bonds in its N- and C-termini.	Disulfides	63-72	mucin 2, oligomeric mucus/gel-forming	Homo sapiens	18-22
21345800-4	2011	Reduction of the disulfide bond restored the ability of the mutant to reduce its redox partners, demonstrating that a conformational change is essential for CYPOR function.	Disulfides	17-26	cytochrome p450 oxidoreductase	Homo sapiens	157-162
21393238-4	2011	Asbestos-induced translocation of Cu,Zn-SOD to the IMS was unique to macrophages and dependent on functional mitochondrial respiration and the presence of at least one of the conserved cysteines required for disulfide bond formation.	Disulfides	208-217	superoxide dismutase 1, soluble	Mus musculus	34-43
21377473-4	2011	We identified two previously undocumented disulfide bridges in the crystal structure of properly folded S100A3: one disulfide bridge is between Cys30 in the N-terminal pseudo-EF-hand and Cys68 in the C-terminal EF-hand (SS1), and another disulfide bridge attaches Cys99 in the C-terminal coil structure to Cys81 in helix IV (SS2).	Disulfides	42-51	major histocompatibility complex, class II, DR beta 1	Homo sapiens	220-223
21377473-4	2011	We identified two previously undocumented disulfide bridges in the crystal structure of properly folded S100A3: one disulfide bridge is between Cys30 in the N-terminal pseudo-EF-hand and Cys68 in the C-terminal EF-hand (SS1), and another disulfide bridge attaches Cys99 in the C-terminal coil structure to Cys81 in helix IV (SS2).	Disulfides	116-125	major histocompatibility complex, class II, DR beta 1	Homo sapiens	220-223
20872260-6	2011	Then, the regioselective formation of the two disulfide bridges of hPTN 60-110 was successfully achieved by a two-step procedure, involving an oxidative folding step in dimethylsulfoxide (DMSO) to form the Cys(77)-Cys(109) bond, followed by iodine oxidation to form the Cys(67)-Cys(99) bond.	Disulfides	46-55	pleiotrophin	Homo sapiens	67-71
21296671-6	2011	Comparison of these results with the structure and backbone dynamics previously determined for bovine apo-S100A1 protein modified by disulfide formation with beta-mercaptoethanol at Cys 85 revealed that the secondary structure of both these proteins was almost identical, whereas the global structure of the latter was much more mobile than that of human apo-S100 protein.	Disulfides	133-142	S100 calcium binding protein A1	Homo sapiens	106-112
21296671-6	2011	Comparison of these results with the structure and backbone dynamics previously determined for bovine apo-S100A1 protein modified by disulfide formation with beta-mercaptoethanol at Cys 85 revealed that the secondary structure of both these proteins was almost identical, whereas the global structure of the latter was much more mobile than that of human apo-S100 protein.	Disulfides	133-142	S100 calcium binding protein A1	Homo sapiens	106-110
21377473-4	2011	We identified two previously undocumented disulfide bridges in the crystal structure of properly folded S100A3: one disulfide bridge is between Cys30 in the N-terminal pseudo-EF-hand and Cys68 in the C-terminal EF-hand (SS1), and another disulfide bridge attaches Cys99 in the C-terminal coil structure to Cys81 in helix IV (SS2).	Disulfides	116-125	major histocompatibility complex, class II, DR beta 1	Homo sapiens	220-223
21544205-3	2011	Here we studied the organization of the amino terminal domain (ATD) of the rat GluN1/GluN2A and GluN1/GluN2B NMDA receptors by cysteine-directed, disulfide bond-mediated cross-linking.	Disulfides	146-155	glutamate ionotropic receptor NMDA type subunit 2A	Rattus norvegicus	85-91
21357685-9	2011	PDI catalyzes the reduction of the PABP disulfide bond resulting in specific binding of PABP to the insulin 5" UTR.	Disulfides	40-49	insulin	Homo sapiens	100-107
21521879-3	2011	Sema3A stimulation generated hydrogen peroxide (H2O2) through MICAL (molecule interacting with CasL) and oxidized CRMP2, enabling it to form a disulfide-linked homodimer through cysteine-504.	Disulfides	143-152	dihydropyrimidinase like 2	Homo sapiens	114-119
21521879-4	2011	Oxidized CRMP2 then formed a transient disulfide-linked complex with TRX, which stimulated CRMP2 phosphorylation by glycogen synthase kinase-3, leading to growth cone collapse.	Disulfides	39-48	dihydropyrimidinase like 2	Homo sapiens	9-14
21521879-4	2011	Oxidized CRMP2 then formed a transient disulfide-linked complex with TRX, which stimulated CRMP2 phosphorylation by glycogen synthase kinase-3, leading to growth cone collapse.	Disulfides	39-48	dihydropyrimidinase like 2	Homo sapiens	91-96
21544205-4	2011	We found that GluN1 ATDs and GluN2 ATDs spontaneously formed disulfide bond-mediated dimers after introducing cysteines into the L1 interface of GluN2A or GluN2B ATD.	Disulfides	61-70	glutamate ionotropic receptor NMDA type subunit 2A	Rattus norvegicus	145-151
21329361-9	2011	Analysis of the cysteine reactivity of the compound shows that compound binding to Cys(107) in RGS8 inhibits Galpha binding in a manner that can be reversed by cleavage of the compound-RGS disulfide bond.	Disulfides	189-198	paired like homeodomain 2	Homo sapiens	95-98
21182835-4	2011	By using various heterologous protein expression systems, we demonstrated that murine IL-31 was secreted as inter-molecularly disulfide-bonded covalent aggregates.	Disulfides	126-135	interleukin 31	Mus musculus	86-91
21428412-1	2011	The disulfides in three monoclonal antibodies (mAb), the anti-HER2, anti-CD11a, and GLP-1 with IgG4-Fc fusion protein, were completely mapped by LC-MS with the combination of electron-transfer dissociation (ETD) and collision induced dissociation (CID) fragmentation.	Disulfides	4-14	erb-b2 receptor tyrosine kinase 2	Homo sapiens	62-66
24843467-12	2011	Mutations at the cysteine residue or creating a new cysteine will disturb the correct disulfide bonding and proper conformation, and finally will lead to misfolded proinsulin accumulation, endoplasmic reticulum stress and apoptosis of pancreatic beta-cells.	Disulfides	86-95	insulin	Homo sapiens	164-174
21381664-6	2011	A reporter assay showed that three disulfides increased GSTP enhancer I (GPE I) activity (P &lt; 0.05) in the order DADS &gt; DPDS &gt;= PMDS.	Disulfides	35-45	glutathione S-transferase pi 1	Rattus norvegicus	56-60
21391575-7	2011	In the case of L1 and L2, this gives rise to complexes with silver at low concentration, enhancing the signals observed, while for the tricarbonylbromorhenium complexes of these ligands, the presence of the disulfide tether allows an enhancement in the limits of detection of these surface-borne species of 20 times in the case of [ReL2(CO)(3)Br] over [Re(bipy)(CO)(3)Br].	Disulfides	207-216	L1 cell adhesion molecule	Homo sapiens	15-24
21238616-0	2011	Both PDI and PDIp can attack the native disulfide bonds in thermally-unfolded RNase and form stable disulfide-linked complexes.	Disulfides	40-49	protein disulfide isomerase family A member 2	Homo sapiens	13-17
21238616-0	2011	Both PDI and PDIp can attack the native disulfide bonds in thermally-unfolded RNase and form stable disulfide-linked complexes.	Disulfides	100-109	protein disulfide isomerase family A member 2	Homo sapiens	13-17
21238616-1	2011	Protein disulfide isomerase (PDI) and its pancreatic homolog (PDIp) are folding catalysts for the formation, reduction, and/or isomerization of disulfide bonds in substrate proteins.	Disulfides	8-17	protein disulfide isomerase family A member 2	Homo sapiens	62-66
21238616-2	2011	However, the question as to whether PDI and PDIp can directly attack the native disulfide bonds in substrate proteins is still not answered, which is the subject of the present study.	Disulfides	80-89	protein disulfide isomerase family A member 2	Homo sapiens	44-48
21238616-6	2011	In support of this suggestion, we show that both PDI and PDIp form stable disulfide-linked complexes only with thermally-unfolded RNase, and RNase in the complexes can be released and reactivated dependently of the redox conditions used.	Disulfides	74-83	protein disulfide isomerase family A member 2	Homo sapiens	57-61
21238616-8	2011	These data indicate that PDI and PDIp can perform thiol-disulfide exchange reactions with native disulfide bonds in unfolded RNase via formation of stable disulfide-linked complexes, and from these complexes RNase is further released.	Disulfides	56-65	protein disulfide isomerase family A member 2	Homo sapiens	33-37
21238616-8	2011	These data indicate that PDI and PDIp can perform thiol-disulfide exchange reactions with native disulfide bonds in unfolded RNase via formation of stable disulfide-linked complexes, and from these complexes RNase is further released.	Disulfides	97-106	protein disulfide isomerase family A member 2	Homo sapiens	33-37
21238616-8	2011	These data indicate that PDI and PDIp can perform thiol-disulfide exchange reactions with native disulfide bonds in unfolded RNase via formation of stable disulfide-linked complexes, and from these complexes RNase is further released.	Disulfides	97-106	protein disulfide isomerase family A member 2	Homo sapiens	33-37
21458670-3	2011	We constrained Bax in its native cytosolic conformation within cells using intramolecular disulfide tethers.	Disulfides	90-99	BCL2 associated X, apoptosis regulator	Homo sapiens	15-18
21220411-6	2011	These data rule out disulfide bonding Cys412-Cys413, which would substantially deform the inner helix, suggest a clash of Cys413 with the para-methoxy group, and provide a distance constraint to dock phenylalkylamines in a Kv1.2-based homology model.	Disulfides	20-29	potassium voltage-gated channel subfamily A member 2	Homo sapiens	223-228
21322034-2	2011	They present a conserved 3D structure, so-called IL8-like chemokine fold, which is supported by conserved cysteines forming intra-molecular disulfide bonds.	Disulfides	140-149	C-X-C motif chemokine ligand 8	Homo sapiens	49-52
21322034-4	2011	However, it has been shown that different patterns can provide disulfide bonds fitting into an IL8-like architecture, which has been the key to identify new remote homologues of the IL8-like chemokine family.	Disulfides	63-72	C-X-C motif chemokine ligand 8	Homo sapiens	95-98
21322034-4	2011	However, it has been shown that different patterns can provide disulfide bonds fitting into an IL8-like architecture, which has been the key to identify new remote homologues of the IL8-like chemokine family.	Disulfides	63-72	C-X-C motif chemokine ligand 8	Homo sapiens	182-185
21171964-6	2011	The discrepancy between these K(d) values may be rationalized by recognizing that cytoglobin is a disulfide-linked dimer and invoking co-operativity in oleate binding.	Disulfides	98-107	cytoglobin	Homo sapiens	82-92
21433411-1	2004	VEGF-A is composed of VEGF121, VEGF165, and VEGF189 isoforms, which are secreted by most cell types and are active as homodimers linked by disulfide bonds.	Disulfides	139-148	vascular endothelial growth factor A	Homo sapiens	0-6
21110786-0	2011	Genetic selection for enhanced folding in vivo targets the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor.	Disulfides	71-80	trophoblast Kunitz domain protein 1	Bos taurus	107-124
21110786-3	2011	This trypsin inhibitor contains three disulfides that contribute to its extreme stability and protease resistance.	Disulfides	38-48	trophoblast Kunitz domain protein 1	Bos taurus	5-22
21308844-0	2011	Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity.	Disulfides	8-17	insulin	Homo sapiens	75-85
20963501-8	2011	Alignment of Izumo1 protein sequences among 15 mammalian species displayed several highly conserved regions, including LDC and YRC motifs with cysteine residues for potential disulfide bridge formation, CPNKCG motif upstream of the Ig-like domain, GLTDYSFYRVW motif upstream of the putative N-linked glycosylation site, and a number of scattered cysteine residues.	Disulfides	175-184	izumo sperm-egg fusion 1	Homo sapiens	13-19
21197958-7	2011	Furthermore, electrolytic reduction of proteins (e.g., alpha-lactalbumin) leads to increased charges on the detected protein ions, revealing the role of disulfide bonds on maintaining protein conformation.	Disulfides	153-162	lactalbumin alpha	Homo sapiens	55-72
21269829-1	2011	Ero1p, using molecular oxygen as its preferred terminal electron acceptor, promotes disulfide bond formation by interaction with protein disulfide isomerase.	Disulfides	84-93	ER oxidoreductin	Saccharomyces cerevisiae S288C	0-5
21091435-6	2011	Our results reveal that Ero1beta oxidase activity is regulated by long-range disulfide bonds and that Cys130 plays a critical role in feedback regulation.	Disulfides	77-86	endoplasmic reticulum oxidoreductase 1 beta	Homo sapiens	24-32
21455494-7	2011	Furthermore, such structural destruction was prevented by inter-hexamer crosslinking using P207C/T216C mutant CA with disulfide bonds at the CTD-CTD trimer interface of capsid assemblies, but not by intra-hexamer crosslinking via A14C/E45C at the NTD-NTD interface.	Disulfides	118-127	CTD	Homo sapiens	141-144
21455494-7	2011	Furthermore, such structural destruction was prevented by inter-hexamer crosslinking using P207C/T216C mutant CA with disulfide bonds at the CTD-CTD trimer interface of capsid assemblies, but not by intra-hexamer crosslinking via A14C/E45C at the NTD-NTD interface.	Disulfides	118-127	CTD	Homo sapiens	145-148
21329881-2	2011	ERdj5 was recently discovered to be a key ER-resident PDI family member protein that accelerates ERAD by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1.	Disulfides	124-133	ER degradation enhancing alpha-mannosidase like protein 1	Homo sapiens	181-186
21949740-13	2011	A dimer of ARTS 266-274 formed by oxidation of the Cys residues into a disulfide bond bound with similar affinity and was probably required for the interaction with Bir3.	Disulfides	71-80	septin 4	Homo sapiens	11-15
21257910-2	2011	Recent studies have suggested that destabilization and aggregation of the most immature form of SOD1, the disulfide-reduced, unmetallated (apo) protein is particularly important in causing ALS.	Disulfides	106-115	superoxide dismutase 1	Homo sapiens	96-100
21266777-3	2011	vWF protein forms long multimers from homodimers that first form through C-terminal disulfide bonds and then join through their N termini by further disulfide bonding.	Disulfides	84-93	von Willebrand factor	Homo sapiens	0-3
21266777-3	2011	vWF protein forms long multimers from homodimers that first form through C-terminal disulfide bonds and then join through their N termini by further disulfide bonding.	Disulfides	149-158	von Willebrand factor	Homo sapiens	0-3
21415529-5	2011	Similarly, the activation of MGST1 by diamide or diamide plus glutathione through disulfide-bond formation was also disturbed in the presence of CL.	Disulfides	82-91	microsomal glutathione S-transferase 1	Homo sapiens	29-34
20971184-2	2011	H(2)O(2) activates Yap1 through the Gpx3-mediated formation of a Yap1 Cys303-Cys598 intramolecular disulfide bond.	Disulfides	99-108	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	19-23
20971184-2	2011	H(2)O(2) activates Yap1 through the Gpx3-mediated formation of a Yap1 Cys303-Cys598 intramolecular disulfide bond.	Disulfides	99-108	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	65-69
21133413-7	2011	The truncated (-5)IDH1/IDH2 and tetrameric enzymes were much more sensitive than the wild-type enzyme to inhibition by the oxidant diamide and concomitant formation of a disulfide bond between IDH2 Cys-150 residues.	Disulfides	170-179	isocitrate dehydrogenase (NAD(+)) IDH1	Saccharomyces cerevisiae S288C	18-22
21133413-9	2011	These results suggest that the octameric structure of IDH has in part evolved for regulation of disulfide bond formation and activity by ensuring the proximity of the amino terminus of an IDH1 subunit of one tetramer to the IDH2 Cys-150 residues in the other tetramer.	Disulfides	96-105	isocitrate dehydrogenase (NAD(+)) IDH1	Saccharomyces cerevisiae S288C	188-192
21904647-4	2011	In addition, hydroxyl radicals can reduce disulfide bonds in proteins, specifically fibrinogen, resulting in their unfolding and scrambled refolding into abnormal spatial configurations.	Disulfides	42-51	fibrinogen beta chain	Homo sapiens	84-94
20974843-8	2010	Cleavage of the domain 2 disulfide bond is possibly involved in the conformational change in CD4 associated with fusion of the HIV and cell membranes.	Disulfides	25-34	CD4 molecule	Homo sapiens	93-96
20889503-2	2010	The dimerization of apoE3 by disulfide bonds between cysteine residues enhances apoE3 function to generate HDL.	Disulfides	29-38	apolipoprotein E	Homo sapiens	20-25
20858597-1	2010	Cysteine 150 of retinal degeneration slow protein (RDS) mediates the intermolecular disulfide bonding necessary for large RDS complex assembly and morphogenesis of the rim region of photoreceptor outer segments.	Disulfides	84-93	peripherin 2	Mus musculus	16-49
20858597-1	2010	Cysteine 150 of retinal degeneration slow protein (RDS) mediates the intermolecular disulfide bonding necessary for large RDS complex assembly and morphogenesis of the rim region of photoreceptor outer segments.	Disulfides	84-93	peripherin 2	Mus musculus	51-54
20858597-1	2010	Cysteine 150 of retinal degeneration slow protein (RDS) mediates the intermolecular disulfide bonding necessary for large RDS complex assembly and morphogenesis of the rim region of photoreceptor outer segments.	Disulfides	84-93	peripherin 2	Mus musculus	122-125
20858597-6	2010	Furthermore, our results suggest that RDS intermolecular disulfide bonding may be part of RDS inner-segment assembly in cones but not in rods.	Disulfides	57-66	peripherin 2	Mus musculus	38-41
20858597-6	2010	Furthermore, our results suggest that RDS intermolecular disulfide bonding may be part of RDS inner-segment assembly in cones but not in rods.	Disulfides	57-66	peripherin 2	Mus musculus	90-93
21077590-5	2010	The 17 disulfide bridges present in HSA provide the necessary structural rigidity to the protein.	Disulfides	7-16	albumin	Homo sapiens	36-39
21078955-0	2010	Oxidation-induced intramolecular disulfide bond inactivates mitogen-activated protein kinase kinase 6 by inhibiting ATP binding.	Disulfides	33-42	mitogen-activated protein kinase kinase 6	Homo sapiens	60-101
21078955-3	2010	Detailed mechanistic studies showed that cysteines 109 and 196, two of the six cysteines in MKK6, formed an intramolecular disulfide bond upon oxidation that inactivated MKK6 by inhibiting its ATP binding.	Disulfides	123-132	mitogen-activated protein kinase kinase 6	Homo sapiens	92-96
21078955-3	2010	Detailed mechanistic studies showed that cysteines 109 and 196, two of the six cysteines in MKK6, formed an intramolecular disulfide bond upon oxidation that inactivated MKK6 by inhibiting its ATP binding.	Disulfides	123-132	mitogen-activated protein kinase kinase 6	Homo sapiens	170-174
21339972-3	2010	With homology modeling and molecular docking, we designed a scFv containing an interdomain disulfide bond between the residues H44 and L100.	Disulfides	91-100	immunglobulin heavy chain variable region	Homo sapiens	60-64
21339972-4	2010	The stability of scFv (H4) increased from a GdnHCl(50) of 2.4 M to 4.2 M after addition of the H44-L100 disulfide bond.	Disulfides	104-113	immunglobulin heavy chain variable region	Homo sapiens	17-21
21339972-7	2010	Our results indicate that interdomain disulfide bonds could stabilize scFv without affecting affinity.	Disulfides	38-47	immunglobulin heavy chain variable region	Homo sapiens	70-74
20943653-1	2010	A functional disulfide bond in both the HIV envelope glycoprotein, gp120, and its immune cell receptor, CD4, is involved in viral entry, and compounds that block cleavage of the disulfide bond in these proteins inhibit HIV entry and infection.	Disulfides	13-22	CD4 molecule	Homo sapiens	104-107
20943653-1	2010	A functional disulfide bond in both the HIV envelope glycoprotein, gp120, and its immune cell receptor, CD4, is involved in viral entry, and compounds that block cleavage of the disulfide bond in these proteins inhibit HIV entry and infection.	Disulfides	178-187	CD4 molecule	Homo sapiens	104-107
20943653-4	2010	A single disulfide bond was cleaved in isolated and cell surface gp120, but not the gp160 precursor, and the extent of the reaction was enhanced when gp120 was bound to CD4.	Disulfides	9-18	CD4 molecule	Homo sapiens	169-172
20943653-6	2010	Considering that V3 sequences largely determine the chemokine receptor preference of HIV, we propose that cleavage of the V3 domain disulfide, which is facilitated by CD4 binding, regulates chemokine receptor binding.	Disulfides	132-141	CD4 molecule	Homo sapiens	167-170
20943653-7	2010	There are 20 possible disulfide bond configurations, and, notably, the V3 domain disulfide has the same unusual -RHStaple configuration as the functional disulfide bond cleaved in CD4.	Disulfides	81-90	CD4 molecule	Homo sapiens	180-183
20943653-7	2010	There are 20 possible disulfide bond configurations, and, notably, the V3 domain disulfide has the same unusual -RHStaple configuration as the functional disulfide bond cleaved in CD4.	Disulfides	81-90	CD4 molecule	Homo sapiens	180-183
21145486-1	2010	Endoplasmic reticulum (ER) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (PDI) and is essential for oxidative protein folding in simple eukaryotes such as yeast and worms.	Disulfides	56-66	ER oxidoreductin	Saccharomyces cerevisiae S288C	40-44
21145486-1	2010	Endoplasmic reticulum (ER) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (PDI) and is essential for oxidative protein folding in simple eukaryotes such as yeast and worms.	Disulfides	56-66	protein disulfide isomerase family A member 2	Homo sapiens	99-102
21145486-2	2010	Surprisingly, ERO1-deficient mammalian cells exhibit only a modest delay in disulfide bond formation.	Disulfides	76-85	ER oxidoreductin	Saccharomyces cerevisiae S288C	14-18
21145486-3	2010	To identify ERO1-independent pathways to disulfide bond formation, we purified PDI oxidants with a trapping mutant of PDI.	Disulfides	41-50	protein disulfide isomerase family A member 2	Homo sapiens	118-121
20889503-2	2010	The dimerization of apoE3 by disulfide bonds between cysteine residues enhances apoE3 function to generate HDL.	Disulfides	29-38	apolipoprotein E	Homo sapiens	80-85
20849982-10	2010	It was found that, while the disulfide/dithiol redox chemistry of AtTDX was not affected by increasing the temperature to 40 C, no redox transitions were observed at 50 C and higher temperatures.	Disulfides	29-38	tetraticopeptide domain-containing thioredoxin	Arabidopsis thaliana	66-71
21029072-4	2010	The interchain disulfide bond cleavage decreased the affinity much more for mouse FcgammaRIV than for mouse FcgammaRIIB.	Disulfides	15-24	Fc receptor, IgG, low affinity IIb	Mus musculus	108-119
21167011-1	2010	Lipoprotein (a), [Lp(a)] has many properties in common with low-density lipoprotein, (LDL) but contains a unique protein apolipoprotein(a), linked to apolipoprotein B-100 by a single disulfide bond.	Disulfides	183-192	apolipoprotein B	Homo sapiens	150-170
20878207-3	2010	The bulk of OLFM4 exists in a polymeric form which is held together by disulfide bonds and carbohydrate interactions.	Disulfides	71-80	olfactomedin 4	Homo sapiens	12-17
20826547-5	2010	Our results suggest that this binding involves formation of a disulfide bond with one of the eight cysteines in CYP2E1.	Disulfides	62-71	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	112-118
20946172-0	2010	Disulfide bond reduction of von Willebrand factor by ADAMTS-13.	Disulfides	0-9	von Willebrand factor	Homo sapiens	28-49
20946172-3	2010	Shear stress induces the exposed thiols to form disulfide bonds between laterally apposed plasma-type VWF multimers, leading to enhanced VWF binding to platelets.	Disulfides	48-57	von Willebrand factor	Homo sapiens	102-105
20946172-3	2010	Shear stress induces the exposed thiols to form disulfide bonds between laterally apposed plasma-type VWF multimers, leading to enhanced VWF binding to platelets.	Disulfides	48-57	von Willebrand factor	Homo sapiens	137-140
20946172-4	2010	OBJECTIVES: We tested a hypothesis that ADAMTS-13 has a disulfide bond reducing activity that regulates shear-induced thiol-disulfide exchange of VWF.	Disulfides	56-65	von Willebrand factor	Homo sapiens	146-149
20946172-4	2010	OBJECTIVES: We tested a hypothesis that ADAMTS-13 has a disulfide bond reducing activity that regulates shear-induced thiol-disulfide exchange of VWF.	Disulfides	124-133	von Willebrand factor	Homo sapiens	146-149
20946172-6	2010	RESULTS: ADAMTS-13 contains a disulfide bond reducing activity that primarily targets disulfide bonds in plasma-type VWF multimers induced by high shear stress or formed with thiol beads, but not disulfide bonds in native multimeric structures.	Disulfides	30-39	von Willebrand factor	Homo sapiens	117-120
20946172-6	2010	RESULTS: ADAMTS-13 contains a disulfide bond reducing activity that primarily targets disulfide bonds in plasma-type VWF multimers induced by high shear stress or formed with thiol beads, but not disulfide bonds in native multimeric structures.	Disulfides	86-95	von Willebrand factor	Homo sapiens	117-120
20946172-6	2010	RESULTS: ADAMTS-13 contains a disulfide bond reducing activity that primarily targets disulfide bonds in plasma-type VWF multimers induced by high shear stress or formed with thiol beads, but not disulfide bonds in native multimeric structures.	Disulfides	86-95	von Willebrand factor	Homo sapiens	117-120
20946172-7	2010	Cysteine thiols targeted by this activity are in the VWF C-domain and are known to participate in shear-induced thiol-disulfide exchange.	Disulfides	118-127	von Willebrand factor	Homo sapiens	53-56
20946172-11	2010	CONCLUSIONS: This novel disulfide-bond-reducing activity of ADAMTS-13 may prevent covalent lateral association and increased platelet adherence of plasma-type VWF multimers induced by high fluid shear stress.	Disulfides	24-33	von Willebrand factor	Homo sapiens	159-162
21047126-0	2010	Disulfide cyclized tripeptide analogues of angiotensin IV as potent and selective inhibitors of insulin-regulated aminopeptidase (IRAP).	Disulfides	0-9	leucyl and cystinyl aminopeptidase	Homo sapiens	96-128
20869417-0	2010	Functional coupling of Cys-226 and Cys-296 in the glucagon-like peptide-1 (GLP-1) receptor indicates a disulfide bond that is close to the activation pocket.	Disulfides	103-112	glucagon	Homo sapiens	50-73
21047126-0	2010	Disulfide cyclized tripeptide analogues of angiotensin IV as potent and selective inhibitors of insulin-regulated aminopeptidase (IRAP).	Disulfides	0-9	leucyl and cystinyl aminopeptidase	Homo sapiens	130-134
20949898-2	2010	The assay is based on a disulfide-thiol interchange reaction between the intramolecularly quenched dimeric dye BODIPY FL l-cystine and thiocholine generated by the AChE-catalyzed hydrolysis of acetylthiocholine (ATCh), which results in a brightly fluorescent monomeric product owing to the cleavage of the disulfide-coupled form of the dye.	Disulfides	24-33	acetylcholinesterase (Cartwright blood group)	Homo sapiens	164-168
20954716-2	2010	Introduction of specific disulfide bonds between Fd and FNR by engineering cysteines into the two proteins resulted in 13 different Fd-FNR cross-linked complexes displaying a broad range of activity to catalyze the NADPH-dependent cytochrome c reduction.	Disulfides	25-34	cytochrome c, somatic	Homo sapiens	231-243
20971072-4	2010	Mass spectrometry analysis indicated a greater number of disulfide bonds in the SLPI produced by the PDI overexpression strain compared to the SLPI produced in strains with normal PDI levels.	Disulfides	57-66	secretory leukocyte peptidase inhibitor	Homo sapiens	80-84
20949898-2	2010	The assay is based on a disulfide-thiol interchange reaction between the intramolecularly quenched dimeric dye BODIPY FL l-cystine and thiocholine generated by the AChE-catalyzed hydrolysis of acetylthiocholine (ATCh), which results in a brightly fluorescent monomeric product owing to the cleavage of the disulfide-coupled form of the dye.	Disulfides	306-315	acetylcholinesterase (Cartwright blood group)	Homo sapiens	164-168
20826822-8	2010	Grx2 catalyzes the reduction of insulin disulfide but not of ribonucleotide reductase and exerts deglutathionylation activity 10-fold lower than that of Grx1.	Disulfides	40-49	glutaredoxin 2	Homo sapiens	0-4
20832396-4	2010	Fractionation studies showed that sV23 incorporates into a large disulfide linked network well after its secretion ceases, suggesting that post-depositional mechanisms are in place to restrict disulfide bond formation until late oogenesis, when the oocyte no longer experiences large volume increases.	Disulfides	65-74	Vitelline membrane 26Ab	Drosophila melanogaster	34-38
20832396-4	2010	Fractionation studies showed that sV23 incorporates into a large disulfide linked network well after its secretion ceases, suggesting that post-depositional mechanisms are in place to restrict disulfide bond formation until late oogenesis, when the oocyte no longer experiences large volume increases.	Disulfides	193-202	Vitelline membrane 26Ab	Drosophila melanogaster	34-38
20832396-5	2010	Affinity chromatography utilizing histidine tagged sV23 alleles revealed small sV23 disulfide linked complexes during the early stages of eggshell formation that included other VMPs, namely sV17 and Vml.	Disulfides	84-93	Vitelline membrane 26Ab	Drosophila melanogaster	51-55
20832396-5	2010	Affinity chromatography utilizing histidine tagged sV23 alleles revealed small sV23 disulfide linked complexes during the early stages of eggshell formation that included other VMPs, namely sV17 and Vml.	Disulfides	84-93	Vitelline membrane 26Ab	Drosophila melanogaster	79-83
20832396-6	2010	The early presence but late loss of these associations in an sV23 double cysteine mutant suggests that reorganization of disulfide bonds may underlie the regulated growth of disulfide linked networks in the vitelline membrane.	Disulfides	121-130	Vitelline membrane 26Ab	Drosophila melanogaster	61-65
20832396-6	2010	The early presence but late loss of these associations in an sV23 double cysteine mutant suggests that reorganization of disulfide bonds may underlie the regulated growth of disulfide linked networks in the vitelline membrane.	Disulfides	174-183	Vitelline membrane 26Ab	Drosophila melanogaster	61-65
20832396-7	2010	Found within the context of a putative thioredoxin active site (CXXS) C131, the critical cysteine in sV23, may play an important enzymatic role in isomerizing intermolecular disulfide bonds during eggshell assembly.	Disulfides	174-183	Vitelline membrane 26Ab	Drosophila melanogaster	101-105
20801878-2	2010	One notable exception is the complex of ERp57 and calnexin that functions as part the calnexin cycle to direct disulfide bond formation in N-glycoproteins.	Disulfides	111-120	protein disulfide isomerase family A member 3	Homo sapiens	40-45
20383778-8	2010	Circular dichroism spectroscopic analysis and peptide mapping showed that the recombinant INSL5s adopted an insulin-like conformation and possessed the expected characteristic insulin-like disulfide linkages.	Disulfides	189-198	insulin like 5	Homo sapiens	90-95
20136511-6	2010	After disulfide transfer from Tim40/Mia40 to substrate proteins, Tim40/Mia40 is reoxidized again by Erv1, which is then oxidized by electron transfer to either cytochrome c or molecular oxygen.	Disulfides	6-15	cytochrome c, somatic	Homo sapiens	160-172
20367259-4	2010	IMS import of SOD1 involves its copper chaperone, CCS, whose mitochondrial distribution is regulated by the Mia40/Erv1 disulfide relay system in a redox-dependent manner: CCS promotes SOD1 maturation and retention in the IMS.	Disulfides	119-128	superoxide dismutase 1	Homo sapiens	14-18
20367259-4	2010	IMS import of SOD1 involves its copper chaperone, CCS, whose mitochondrial distribution is regulated by the Mia40/Erv1 disulfide relay system in a redox-dependent manner: CCS promotes SOD1 maturation and retention in the IMS.	Disulfides	119-128	superoxide dismutase 1	Homo sapiens	184-188
20367259-2	2010	Similar to other small IMS proteins, the import and retention of SOD1 in the IMS is linked to its folding and maturation, involving the formation of critical intra- and intermolecular disulfide bonds.	Disulfides	184-193	superoxide dismutase 1	Homo sapiens	65-69
20820534-1	2010	We report the facile synthesis of well defined, disulfide containing polymers via SET-LRP.	Disulfides	48-57	LDL receptor related protein 1	Homo sapiens	86-89
20693287-2	2010	The major C4BP isoform consists of 7 alpha-chains and 1 beta-chain (C4BPbeta(+)), the chains being linked by disulfide bridges.	Disulfides	109-118	complement component 4 binding protein alpha	Homo sapiens	10-14
20802036-7	2010	Our results indicate that C-terminal domains having an N-terminal alpha-helix and a beta-barrel constitute functional transport units for the translocation of peptides and immunoglobulin domains with disulfide bonds.	Disulfides	200-209	amyloid beta precursor protein	Homo sapiens	82-88
20873779-2	2010	These compounds are usually formed by a slow reaction of mercury salts with thiolates or disulfides to produce small (up to 1 mum), plate-like crystals of Hg(S-R)(2).	Disulfides	89-99	latexin	Homo sapiens	126-129
20981267-6	2010	In addition to the identified candidate nsSNPs for increased or reduced arsenic responsiveness, we observed i) a nsSNP that results in the breakage of a disulfide bond, as candidate marker for reduced arsenic responsiveness of KLK7, a secreted serine protease participate in normal shedding of the skin; and ii) 6 pairs of vicinal cysteines in KLK7 protein that could be binding sites for arsenic.	Disulfides	153-162	coagulation factor II, thrombin	Homo sapiens	244-259
20948967-5	2010	First, in the presence of MIDY mutants, an increased fraction of wild-type proinsulin becomes recruited into nonnative disulfide-linked protein complexes.	Disulfides	119-128	insulin	Homo sapiens	75-85
20214493-5	2010	Proteins destined to the intermembrane space are trapped by a disulfide relay mechanism that involves an electron cascade from the incoming substrate to Mia40, then on to Erv1, and finally to molecular oxygen via cytochrome c.	Disulfides	62-71	cytochrome c, somatic	Homo sapiens	213-225
20948967-9	2010	We conclude that the molecular pathogenesis of MIDY is initiated by perturbation of the disulfide-coupled folding pathway of wild-type proinsulin.	Disulfides	88-97	insulin	Homo sapiens	135-145
20486761-1	2010	Formation of disulfide bonds in the endoplasmic reticulum (ER) is catalyzed by the ER oxidoreductin (Ero1) family of sulfhydryl oxidases.	Disulfides	13-22	ER oxidoreductin	Saccharomyces cerevisiae S288C	101-105
20669236-0	2010	Steps in reductive activation of the disulfide-generating enzyme Ero1p.	Disulfides	37-46	ER oxidoreductin	Saccharomyces cerevisiae S288C	65-70
20486761-2	2010	Ero1 oxidizes protein disulfide isomerase (PDI), which, in turn, introduces disulfides into ER client proteins.	Disulfides	76-86	ER oxidoreductin	Saccharomyces cerevisiae S288C	0-4
20486761-3	2010	To maintain an oxidized state, Ero1 couples disulfide transfer to PDI with reduction of molecular oxygen, forming hydrogen peroxide.	Disulfides	44-53	ER oxidoreductin	Saccharomyces cerevisiae S288C	31-35
20486761-6	2010	Central to these mechanisms are noncatalytic cysteines, which form regulatory disulfides and influence catalytic activity of Ero1 in relation to local redox conditions.	Disulfides	78-88	ER oxidoreductin	Saccharomyces cerevisiae S288C	125-129
20486761-7	2010	Here we focus on the distinct regulatory disulfides modulating Ero1 activities in the yeast and mammalian ER.	Disulfides	41-51	ER oxidoreductin	Saccharomyces cerevisiae S288C	63-67
20499289-2	2010	The mature 34-38 kDa disulfide-linked homodimer protein plays a key role in the differentiation of mesenchymal cells into bone and cartilage.	Disulfides	21-30	superoxide dismutase 1	Homo sapiens	38-47
20669236-1	2010	Ero1p is the primary catalyst of disulfide bond formation in the yeast endoplasmic reticulum (ER).	Disulfides	33-42	ER oxidoreductin	Saccharomyces cerevisiae S288C	0-5
20669236-2	2010	Ero1p contains a pair of essential disulfide bonds that participate directly in the electron transfer pathway from substrate thiol groups to oxygen.	Disulfides	35-44	ER oxidoreductin	Saccharomyces cerevisiae S288C	0-5
20857183-0	2010	Mechanism of gemini disulfide detergent mediated oxidative refolding of lysozyme in a new artificial chaperone system.	Disulfides	20-29	lysozyme	Homo sapiens	72-80
20857183-4	2010	Using lysozyme as a model protein we could demonstrate that the disulfide gemini detergents allow oxidative refolding of the protein in the absence of any external redox system in an "artificial chaperone system".	Disulfides	64-73	lysozyme	Homo sapiens	6-14
20669236-3	2010	Remarkably, elimination of certain other Ero1p disulfides by mutation enhances enzyme activity.	Disulfides	47-57	ER oxidoreductin	Saccharomyces cerevisiae S288C	41-46
20857183-6	2010	The results point to an important role of the transiently formed mixed disulfides between the protein and the detergent (Prot-SS-Det) in the oxidative refolding process of lysozyme.	Disulfides	71-81	lysozyme	Homo sapiens	172-180
20669236-5	2010	Inhibitory disulfides of Ero1p are thus important for enzyme regulation.	Disulfides	11-21	ER oxidoreductin	Saccharomyces cerevisiae S288C	25-30
20669236-8	2010	To determine how the C150--C295 disulfide nonetheless participates in redox regulation of Ero1p, we analyzed using mass spectrometry the changes in Ero1p disulfide connectivity as a function of time after encounter with reducing substrates.	Disulfides	32-41	ER oxidoreductin	Saccharomyces cerevisiae S288C	90-95
20669236-8	2010	To determine how the C150--C295 disulfide nonetheless participates in redox regulation of Ero1p, we analyzed using mass spectrometry the changes in Ero1p disulfide connectivity as a function of time after encounter with reducing substrates.	Disulfides	154-163	ER oxidoreductin	Saccharomyces cerevisiae S288C	148-153
20595380-2	2010	The maturation of SOD1 is initiated by incorporation of zinc and copper ions followed by disulfide oxidation leading to the formation of enzymatically active homodimers.	Disulfides	89-98	superoxide dismutase 1	Homo sapiens	18-22
20705333-4	2010	Thrombospondin-1 (TSP1) is considered as a reductase of VWF (von Willebrand factor) which can mildly downregulate the size of VWF by targeting on disulfide bond between VWF dimers.	Disulfides	146-155	thrombospondin 1	Homo sapiens	0-16
20705333-4	2010	Thrombospondin-1 (TSP1) is considered as a reductase of VWF (von Willebrand factor) which can mildly downregulate the size of VWF by targeting on disulfide bond between VWF dimers.	Disulfides	146-155	thrombospondin 1	Homo sapiens	18-22
20705333-4	2010	Thrombospondin-1 (TSP1) is considered as a reductase of VWF (von Willebrand factor) which can mildly downregulate the size of VWF by targeting on disulfide bond between VWF dimers.	Disulfides	146-155	von Willebrand factor	Homo sapiens	56-59
20705333-4	2010	Thrombospondin-1 (TSP1) is considered as a reductase of VWF (von Willebrand factor) which can mildly downregulate the size of VWF by targeting on disulfide bond between VWF dimers.	Disulfides	146-155	von Willebrand factor	Homo sapiens	61-82
20705333-4	2010	Thrombospondin-1 (TSP1) is considered as a reductase of VWF (von Willebrand factor) which can mildly downregulate the size of VWF by targeting on disulfide bond between VWF dimers.	Disulfides	146-155	von Willebrand factor	Homo sapiens	126-129
20705333-4	2010	Thrombospondin-1 (TSP1) is considered as a reductase of VWF (von Willebrand factor) which can mildly downregulate the size of VWF by targeting on disulfide bond between VWF dimers.	Disulfides	146-155	von Willebrand factor	Homo sapiens	126-129
20862248-6	2010	Murine ADAMTSL2 containing the p.R221C mutation formed anomalous disulfide-bonded dimers when transiently expressed in COS-1, HEK293F and CHO cells, and was present in the medium of these cells at lower levels than wild-type ADAMTSL2 expressed in parallel.	Disulfides	65-74	ADAMTS-like 2	Mus musculus	7-15
20600836-3	2010	For instance, the antioxidant enzyme human superoxide dismutase 1 (hSod1) has been reported to undergo non-disulfide covalent dimerization and further oligomerization during its bicarbonate-dependent peroxidase activity.	Disulfides	107-116	superoxide dismutase 1	Homo sapiens	43-65
20600836-3	2010	For instance, the antioxidant enzyme human superoxide dismutase 1 (hSod1) has been reported to undergo non-disulfide covalent dimerization and further oligomerization during its bicarbonate-dependent peroxidase activity.	Disulfides	107-116	superoxide dismutase 1	Homo sapiens	67-72
20660153-3	2010	We show that PDI plays a predominant role in oxidative folding because its depletion delayed disulfide formation in all secretory proteins tested.	Disulfides	93-102	protein disulfide isomerase family A member 2	Homo sapiens	13-16
20697659-2	2010	Most attention was given to reductive desorption caused by insulin binding to the Au-surfaces via up to three disulfide groups per insulin monomer, presumably converted to single Au-S links.	Disulfides	110-119	insulin	Homo sapiens	59-66
20812761-0	2010	Human FEZ1 protein forms a disulfide bond mediated dimer: implications for cargo transport.	Disulfides	27-36	fasciculation and elongation protein zeta 1	Homo sapiens	6-10
20666415-5	2010	Herein, we investigate the structural determinants of the folding kinetics of a naturally occurring helical hairpin (porcine PYY) that is free of disulfide bonds and metal ion-induced cross-links using an infrared temperature-jump technique.	Disulfides	146-155	peptide YY	Homo sapiens	125-128
20812761-6	2010	This disulfide bond may be important for the FEZ1 role as a dimeric and bivalent transport adaptor molecule, since it establishes a strong link between the monomers, which could be a prerequisite for the simultaneous binding of two cargoes.	Disulfides	5-14	fasciculation and elongation protein zeta 1	Homo sapiens	45-49
20540164-0	2010	In vitro folding of methionine-arginine human lyspro-proinsulin S-sulfonate-disulfide formation pathways and factors controlling yield.	Disulfides	76-85	insulin	Homo sapiens	53-63
20540164-8	2010	At a cysteine-to-proinsulin-SH ratio of 3.5, all intermediates with the non-native disulfide bonds were converted to properly folded proinsulin via disulfide bond reshuffling, which was the slowest step.	Disulfides	148-157	insulin	Homo sapiens	133-143
20668223-3	2010	TRP1 contains internal disulfide bonds and is presented by MHC class II molecules.	Disulfides	23-32	tyrosinase related protein 1	Homo sapiens	0-4
20668223-4	2010	Gamma-IFN-inducible lysosomal thiol reductase (GILT) facilitates the generation of class II-binding peptides by the endocytic reduction of protein disulfide bonds.	Disulfides	147-156	IFI30 lysosomal thiol reductase	Homo sapiens	0-45
20668223-4	2010	Gamma-IFN-inducible lysosomal thiol reductase (GILT) facilitates the generation of class II-binding peptides by the endocytic reduction of protein disulfide bonds.	Disulfides	147-156	IFI30 lysosomal thiol reductase	Homo sapiens	47-51
20668223-8	2010	Given that many self and tumor Ags have disulfide bonds and are presented on MHC class II, GILT is likely to be important in the pathogenesis of other CD4(+) T cell-mediated autoimmune diseases and for the development of effective cancer immunotherapy.	Disulfides	40-49	IFI30 lysosomal thiol reductase	Homo sapiens	91-95
20666485-0	2010	A disulfide-linked amyloid-beta peptide dimer forms a protofibril-like oligomer through a distinct pathway from amyloid fibril formation.	Disulfides	2-11	amyloid beta precursor protein	Homo sapiens	19-31
20600430-3	2010	The native disulfide connectivity was found essential for the bactericidal activity of hBD-2, while sodium chloride concentration was reversely associated with its potency.	Disulfides	11-20	defensin beta 4A	Homo sapiens	87-92
20713699-3	2010	Here we show that this beta-hairpin is a building block of toxic Abeta oligomers by engineering a double-cysteine mutant (called Abetacc) in which the beta-hairpin is stabilized by an intramolecular disulfide bond.	Disulfides	199-208	amyloid beta precursor protein	Homo sapiens	65-70
20553742-7	2010	Additionally, we also revealed that nitric oxide, chemical compounds containing reactive disulfide, and inflammatory mediators directly activate the TRPC, TRPV, and TRPA subfamilies via oxidative modification of cysteine residues.	Disulfides	89-98	tryptase gamma 1	Homo sapiens	165-169
20518742-5	2010	Membrane-associated matriptase-2 is highly N-glycosylated and occurs in monomeric, as well as multimeric, forms covalently linked by disulfide bonds.	Disulfides	133-142	transmembrane serine protease 6	Homo sapiens	20-32
20518742-6	2010	Furthermore, matriptase-2 undergoes shedding into the conditioned medium as an activated two-chain form containing the catalytic domain, which is cleaved at the canonical activation motif, but is linked to a released portion of the stem region via a conserved disulfide bond.	Disulfides	260-269	transmembrane serine protease 6	Homo sapiens	13-25
20547769-7	2010	To investigate the role of each cysteine residue, we created alanine mutants and found that Cys(230) appears to promote oxidation and inactivation of TG2 by facilitating formation of Cys(370)-Cys(371) through formation of the Cys(230)-Cys(370) disulfide bond.	Disulfides	244-253	transglutaminase 2	Homo sapiens	150-153
20538591-0	2010	Stabilization of HIV-1 gp120-CD4 receptor complex through targeted interchain disulfide exchange.	Disulfides	78-87	CD4 molecule	Homo sapiens	29-32
20516062-5	2010	We therefore investigated whether distortion of the domain 1-domain 4 ligand-binding epitope in hbetac and the related mouse receptor, beta(IL-3), could account for the loss of receptor signaling when the domain 1 D-E loop disulfide is disrupted.	Disulfides	223-232	interleukin 3	Mus musculus	135-144
20538591-3	2010	In this study, we describe a novel recombinant CD4 protein designed to bind gp120 through a targeted disulfide-exchange mechanism.	Disulfides	101-110	CD4 molecule	Homo sapiens	47-50
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	186-195	CD4 molecule	Homo sapiens	44-47
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	186-195	CD4 molecule	Homo sapiens	97-100
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	186-195	CD4 molecule	Homo sapiens	97-100
20660758-4	2010	We show that erythrocytes can efficiently eliminate H(2)O(2) derived from urate oxidation to prevent cell injury in vitro; during therapy, disulfide-linked peroxiredoxin 2 dimer did not accumulate in red blood cells, indicating that their peroxidase capacity was not exceeded.	Disulfides	139-148	peroxiredoxin 2	Homo sapiens	156-171
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	377-386	CD4 molecule	Homo sapiens	44-47
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	377-386	CD4 molecule	Homo sapiens	97-100
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	377-386	CD4 molecule	Homo sapiens	97-100
20538591-6	2010	We show that 2dCD4-S60C binds HIV-1 gp120 with a significantly higher affinity than wild-type protein under conditions that facilitate disulfide exchange and that this translates into a corresponding increase in the efficacy of CD4-mediated viral entry inhibition.	Disulfides	135-144	CD4 molecule	Homo sapiens	15-18
20538591-7	2010	We propose that targeted redox exchange between conserved gp120 disulfides and nucleophilic moieties positioned strategically on CD4 (or CD4-like scaffolds) conceptualizes a new strategy in the development of high affinity HIV-1 Env ligands, with important implications for therapy and vaccine development.	Disulfides	64-74	CD4 molecule	Homo sapiens	129-132
20538591-7	2010	We propose that targeted redox exchange between conserved gp120 disulfides and nucleophilic moieties positioned strategically on CD4 (or CD4-like scaffolds) conceptualizes a new strategy in the development of high affinity HIV-1 Env ligands, with important implications for therapy and vaccine development.	Disulfides	64-74	CD4 molecule	Homo sapiens	137-140
20516062-8	2010	Our data are most consistent with a role for the domain 1 D-E loop disulfide of hbetac and beta(IL-3) in maintaining the precise positions of ligand-binding residues necessary for normal high affinity binding and signaling.	Disulfides	67-76	interleukin 3	Mus musculus	91-100
20220067-2	2010	The HLA-A*3014L variant has a disulfide bridge missing in the alpha2 domain which could affect peptide binding and presentation to T cells.	Disulfides	30-39	major histocompatibility complex, class I, A	Homo sapiens	4-9
20493921-7	2010	Data from mass spectrometry and comparative modeling showed that CA VII protein contains a single intramolecular disulfide bridge (Cys-56 to Cys-180) which is lacking in the short form.	Disulfides	113-122	carbonic anhydrase 7	Homo sapiens	65-71
20382254-7	2010	Truncated tilapia growth hormone lacking the helix 4 and two disulfide loops is still a bioactive hormone, suggesting that the disulfide bonds and the helix 4 are not essential for the biological activities examined in this work.	Disulfides	61-70	growth hormone 1	Homo sapiens	18-32
20382254-7	2010	Truncated tilapia growth hormone lacking the helix 4 and two disulfide loops is still a bioactive hormone, suggesting that the disulfide bonds and the helix 4 are not essential for the biological activities examined in this work.	Disulfides	127-136	growth hormone 1	Homo sapiens	18-32
20220067-10	2010	These results indicate that surface expression, as well as peptide-binding data of HLA variants with similar disulfide bridge variations (e.g. HLA-A*3211Q) need to be considered as functionally active in an allogeneic hematopoietic stem cell transplantation setting as long as the opposite has not been shown.	Disulfides	109-118	major histocompatibility complex, class I, A	Homo sapiens	143-148
20441567-6	2010	Moreover, by regulating the degree of disulfide linkages, we were able to investigate how oligomerization of kappa-casein influences its propensity for fibril formation under conditions of physiological pH and temperature.	Disulfides	38-47	casein kappa	Bos taurus	109-121
20472479-0	2010	Human growth hormone: 45-kDa isoform with extraordinarily stable interchain disulfide links has attenuated receptor-binding and cell-proliferative activities.	Disulfides	76-85	growth hormone 1	Homo sapiens	6-20
20472479-3	2010	Mercaptoethanol-resistant 45-kDa human growth hormone (MER-45 kDa hGH) is an extraordinarily stable disulfide-linked hGH homodimer whose biological significance is unknown.	Disulfides	100-109	growth hormone 1	Homo sapiens	39-53
20979592-8	2010	Reduced beta(2) GPI in vitro displays increased binding to VWF that is dependent on disulfide bond formation.	Disulfides	84-93	von Willebrand factor	Homo sapiens	59-62
20662138-17	2004	A truncated form of the agouti-related protein (AgRP), a 4-kDa knottin with four disulfide-bonds, was found to have high affinity for the alphavbeta3 integrin (17).	Disulfides	81-90	agouti related neuropeptide	Mus musculus	24-46
20662138-17	2004	A truncated form of the agouti-related protein (AgRP), a 4-kDa knottin with four disulfide-bonds, was found to have high affinity for the alphavbeta3 integrin (17).	Disulfides	81-90	agouti related neuropeptide	Mus musculus	48-52
20450932-6	2010	Additionally, we newly discovered an intramolecular disulfide bond between Cys230 and Cys370, which formation might regulate the enzymatic activity of TG2.	Disulfides	52-61	transglutaminase 2	Homo sapiens	151-154
20441567-7	2010	Thus, using fractions containing different proportions of multimeric species, we demonstrate that the propensity of the disulfide-linked multimers to form fibrils is inversely related to their size, with monomeric kappa-casein being the most aggregation prone.	Disulfides	120-129	casein kappa	Bos taurus	214-226
20557125-3	2010	As corroborated by electrophoresis analysis, both beta-lactoglobulin (beta-lg) and alpha-lactalbumin (alpha-la) were involved in the formation of aggregates via the thiol-disulfide interchange reaction and/or noncovalent interactions.	Disulfides	171-180	lactalbumin alpha	Homo sapiens	83-100
20557125-5	2010	In comparison with the control bar without Cys, the thiol-disulfide interchange reaction was significantly reduced by Cys (WPI/Cys = 0.05), increased by Cys (WPI/Cys = 0.25), and inhibited by NEM (WPI/NEM = 2).	Disulfides	58-67	actin alpha 1, skeletal muscle	Homo sapiens	201-208
20412382-6	2010	The aggregated hSOD1 was mainly composed of subunits that lacked the native stabilizing intra-subunit disulfide bond.	Disulfides	102-111	superoxide dismutase 1	Homo sapiens	15-20
20437224-8	2010	The feasability of this SNP identification methodology based on an MS-based disulfide barcode assay was demonstrated by applying it to genomic DNA samples representing all possible genotypes of the SNPs G2677T and C3435T in the human MDR1 gene.	Disulfides	76-85	ATP binding cassette subfamily B member 1	Homo sapiens	234-238
20417731-1	2010	Yeast glutaredoxins Grx1 and Grx2 catalyze the reduction of both inter- and intra-molecular disulfide bonds using glutathione (GSH) as the electron donor.	Disulfides	92-101	glutaredoxin 2	Homo sapiens	29-33
20615204-2	2010	This novel in vivo cleavable disulfide linker, based on a dithiocyclopeptide containing a thrombin-sensitive sequence and an intramolecular disulfide bond, was inserted between transferrin and granulocyte colony-stimulating factor (G-CSF) recombinant fusion protein domains.	Disulfides	29-38	coagulation factor II, thrombin	Homo sapiens	90-98
20615204-2	2010	This novel in vivo cleavable disulfide linker, based on a dithiocyclopeptide containing a thrombin-sensitive sequence and an intramolecular disulfide bond, was inserted between transferrin and granulocyte colony-stimulating factor (G-CSF) recombinant fusion protein domains.	Disulfides	29-38	transferrin	Homo sapiens	177-188
20615204-2	2010	This novel in vivo cleavable disulfide linker, based on a dithiocyclopeptide containing a thrombin-sensitive sequence and an intramolecular disulfide bond, was inserted between transferrin and granulocyte colony-stimulating factor (G-CSF) recombinant fusion protein domains.	Disulfides	140-149	transferrin	Homo sapiens	177-188
20615204-3	2010	After expression of the fusion protein, G-C-T, from HEK293 cells, thrombin treatment in vitro generated a fusion protein linked via a reversible disulfide bond that was quickly cleaved in vivo, separating the protein domains.	Disulfides	145-154	coagulation factor II, thrombin	Homo sapiens	66-74
23408156-1	2010	Tissue plasminogen activator (tPA) is a serine protease, which is composed of five distinct structural domains with 17 disulfide bonds, representing a model of high-disulfide proteins in human body.	Disulfides	119-128	plasminogen activator, tissue type	Homo sapiens	0-34
23408156-1	2010	Tissue plasminogen activator (tPA) is a serine protease, which is composed of five distinct structural domains with 17 disulfide bonds, representing a model of high-disulfide proteins in human body.	Disulfides	165-174	plasminogen activator, tissue type	Homo sapiens	0-34
20347046-9	2010	In another example the protein disulfide isomerase ERdj5 binds specifically to EDEM (which is probably a mannosidase) and a lectin OS9, and reduces the disulfide bonds of bound glycoproteins destined for ERAD.	Disulfides	31-40	OS9 endoplasmic reticulum lectin	Homo sapiens	131-134
20424732-0	2010	Signal sequence as a determinant in expressing disulfide-stabilized single chain antibody variable fragments (sc-dsFv) against human VEGF.	Disulfides	47-56	vascular endothelial growth factor A	Homo sapiens	133-137
20424732-7	2010	The utility of the phagemid systems was demonstrated in generating anti-VEGF sc-dsFv with VEGF-binding affinity one order of magnitude higher than the corresponding scFv, due only to the interface disulfide bond in the sc-dsFv.	Disulfides	197-206	vascular endothelial growth factor A	Homo sapiens	72-76
20424732-7	2010	The utility of the phagemid systems was demonstrated in generating anti-VEGF sc-dsFv with VEGF-binding affinity one order of magnitude higher than the corresponding scFv, due only to the interface disulfide bond in the sc-dsFv.	Disulfides	197-206	vascular endothelial growth factor A	Homo sapiens	90-94
20424732-7	2010	The utility of the phagemid systems was demonstrated in generating anti-VEGF sc-dsFv with VEGF-binding affinity one order of magnitude higher than the corresponding scFv, due only to the interface disulfide bond in the sc-dsFv.	Disulfides	197-206	immunglobulin heavy chain variable region	Homo sapiens	165-169
20347046-9	2010	In another example the protein disulfide isomerase ERdj5 binds specifically to EDEM (which is probably a mannosidase) and a lectin OS9, and reduces the disulfide bonds of bound glycoproteins destined for ERAD.	Disulfides	31-40	ER degradation enhancing alpha-mannosidase like protein 1	Homo sapiens	79-83
20348090-1	2010	The sulfhydryl oxidase Ero1 oxidizes protein disulfide isomerase (PDI), which in turn catalyzes disulfide formation in proteins folding in the endoplasmic reticulum (ER).	Disulfides	45-54	ER oxidoreductin	Saccharomyces cerevisiae S288C	23-27
20378753-7	2010	Structural and functional T-cell avidities of an accessory disulfide-linked scTCR gp100/Calpha were higher than those of a dcTCR.	Disulfides	59-68	premelanosome protein	Homo sapiens	82-87
20348090-9	2010	Overall, our results provide a rank order for the tendency of yeast ER oxidoreductases to acquire disulfides from Ero1p.	Disulfides	98-108	ER oxidoreductin	Saccharomyces cerevisiae S288C	114-119
20538950-1	2010	Gamma-interferon-inducible lysosomal thiolreductase (GILT) promotes major histocompatibility complex (MHC) class II-restricted presentation of exogenous antigens containing disulfide bonds.	Disulfides	173-182	IFI30 lysosomal thiol reductase	Homo sapiens	0-51
20354169-1	2010	The von Willebrand factor (VWF) A2 crystal structure has revealed the presence of a rare vicinal disulfide bond between C1669 and C1670, predicted to influence domain unfolding required for proteolysis by ADAMTS13.	Disulfides	97-106	von Willebrand factor	Homo sapiens	4-25
20354169-1	2010	The von Willebrand factor (VWF) A2 crystal structure has revealed the presence of a rare vicinal disulfide bond between C1669 and C1670, predicted to influence domain unfolding required for proteolysis by ADAMTS13.	Disulfides	97-106	von Willebrand factor	Homo sapiens	27-30
20538950-1	2010	Gamma-interferon-inducible lysosomal thiolreductase (GILT) promotes major histocompatibility complex (MHC) class II-restricted presentation of exogenous antigens containing disulfide bonds.	Disulfides	173-182	IFI30 lysosomal thiol reductase	Homo sapiens	53-57
20538950-5	2010	Efficient cross-presentation of disulfide-rich antigens requires a complex pathway involving GILT-mediated reduction, unfolding, and partial proteolysis, followed by translocation into the cytosol for proteasomal processing.	Disulfides	32-41	IFI30 lysosomal thiol reductase	Homo sapiens	93-97
20363749-3	2010	Here, biophysical analyses reveal that PTX3 is composed of eight identical protomers, associated through disulfide bonds, forming an elongated and asymmetric, molecule with two differently sized domains interconnected by a stalk.	Disulfides	105-114	pentraxin 3	Homo sapiens	39-43
20207738-8	2010	Structural comparisons revealed that the receptor-ligand pairing in the TGF-beta superfamily is dictated by unique insertions, deletions, and disulfide bonds rather than amino acid conservation at the interface.	Disulfides	142-151	transforming growth factor beta 1	Homo sapiens	72-80
20382709-5	2010	In both LNCaP prostate cancer cells and human semen, TMPRSS2 protein was detected predominantly as inactive zymogen forms as part of an array of multiple noncovalent and disulfide-linked complexes, suggesting that TMPRSS2 activity may be regulated by unconventional mechanisms.	Disulfides	170-179	transmembrane serine protease 2	Homo sapiens	53-60
20553503-7	2010	An internal disulfide bond may form which modifies the rate of dissociation of the distal histidine and apparently leads to different cytoglobin conformations, which may affect the observed oxygen affinity by an order of magnitude.	Disulfides	12-21	cytoglobin	Homo sapiens	134-144
21204007-8	2010	More than ten years" efforts on studying insulin disulfide intermediates by NMR have enabled us to decipher the whole picture of insulin folding coupled to disulfide pairing, especially at the initial stage that forms the nascent peptide.	Disulfides	49-58	insulin	Homo sapiens	41-48
21204007-8	2010	More than ten years" efforts on studying insulin disulfide intermediates by NMR have enabled us to decipher the whole picture of insulin folding coupled to disulfide pairing, especially at the initial stage that forms the nascent peptide.	Disulfides	49-58	insulin	Homo sapiens	129-136
21204007-8	2010	More than ten years" efforts on studying insulin disulfide intermediates by NMR have enabled us to decipher the whole picture of insulin folding coupled to disulfide pairing, especially at the initial stage that forms the nascent peptide.	Disulfides	156-165	insulin	Homo sapiens	41-48
21204007-8	2010	More than ten years" efforts on studying insulin disulfide intermediates by NMR have enabled us to decipher the whole picture of insulin folding coupled to disulfide pairing, especially at the initial stage that forms the nascent peptide.	Disulfides	156-165	insulin	Homo sapiens	129-136
20228064-5	2010	A full-length SP-D mutant lacking N-terminal cysteine residues and truncation mutants lacking the N-terminal domains were resistant to the oxidant-induced alterations in disulfide bonding.	Disulfides	170-179	surfactant associated protein D	Mus musculus	14-18
20485669-4	2010	Covalent Prm1p dimer formation occurs via intermolecular disulfide bonds of two cysteines, Cys-120 and Cys-545.	Disulfides	57-66	pheromone-regulated protein PRM1	Saccharomyces cerevisiae S288C	9-14
20485669-7	2010	Because prm1-C120S and prm1-C545S mutants can form covalent dimers when coexpressed with wild-type PRM1, an intermolecular C120-C545 disulfide linkage is inferred.	Disulfides	133-142	pheromone-regulated protein PRM1	Saccharomyces cerevisiae S288C	8-12
20485669-7	2010	Because prm1-C120S and prm1-C545S mutants can form covalent dimers when coexpressed with wild-type PRM1, an intermolecular C120-C545 disulfide linkage is inferred.	Disulfides	133-142	pheromone-regulated protein PRM1	Saccharomyces cerevisiae S288C	23-27
20485669-7	2010	Because prm1-C120S and prm1-C545S mutants can form covalent dimers when coexpressed with wild-type PRM1, an intermolecular C120-C545 disulfide linkage is inferred.	Disulfides	133-142	pheromone-regulated protein PRM1	Saccharomyces cerevisiae S288C	99-103
20485669-10	2010	The importance of intermolecular disulfide bonding informs models regarding the mechanism of Prm1-mediated cell-cell fusion.	Disulfides	33-42	pheromone-regulated protein PRM1	Saccharomyces cerevisiae S288C	93-97
20485683-1	2010	Gamma interferon Inducible Lysosomal Thiol reductase (GILT) is a unique lysosomal reductase that reduces disulfide bonds of endocytosed proteins.	Disulfides	105-114	IFI30 lysosomal thiol reductase	Homo sapiens	0-52
20485683-1	2010	Gamma interferon Inducible Lysosomal Thiol reductase (GILT) is a unique lysosomal reductase that reduces disulfide bonds of endocytosed proteins.	Disulfides	105-114	IFI30 lysosomal thiol reductase	Homo sapiens	54-58
20485683-2	2010	Lack of GILT clearly decreases CD4 T cell-antigen specific responses against some epitopes of antigens containing disulfide bonds, but not to proteins with few or no disulfide bridges.	Disulfides	114-123	IFI30 lysosomal thiol reductase	Homo sapiens	8-12
20459757-16	2010	The two proteins respond to differing cellular redox modulators, suggesting that the oxidized cysteine adduct is a disulfide bond(s) in Tat, but sulfenic acid in EBNA1.	Disulfides	115-124	EBNA-1	Human gammaherpesvirus 4	162-167
20423149-0	2010	Human intestinal TFF3 forms disulfide-linked heteromers with the mucus-associated FCGBP protein and is released by hydrogen sulfide.	Disulfides	28-37	trefoil factor 3	Homo sapiens	17-21
20423149-4	2010	Purification of this heteromer and characterization by LC-ESI-MS/MS analysis identified the IgG Fc binding protein (FCGBP) as the disulfide-linked partner protein of TFF3.	Disulfides	130-139	trefoil factor 3	Homo sapiens	166-170
20219242-0	2010	Biotinylated transferrin/avidin/biotinylated disulfide containing PEI bioconjugates mediated p53 gene delivery system for tumor targeted transfection.	Disulfides	45-54	tumor protein p53	Homo sapiens	93-96
20219242-2	2010	In this paper, biotinylated transferrin/avidin/biotinylated disulfide containing PEI bioconjugates (TABP-SS) mediated p53 gene delivery system was formed attributed to the "avidin-biotin bridge".	Disulfides	60-69	transferrin	Homo sapiens	28-39
20219242-2	2010	In this paper, biotinylated transferrin/avidin/biotinylated disulfide containing PEI bioconjugates (TABP-SS) mediated p53 gene delivery system was formed attributed to the "avidin-biotin bridge".	Disulfides	60-69	tumor protein p53	Homo sapiens	118-121
20299456-9	2010	Analysis suggested that a lid conformation similar to that of ECL2 in rhodopsin was induced upon binding both agonist and antagonist, but exposing different accessible segments delimited by the highly conserved disulfide bond.	Disulfides	211-220	rhodopsin	Homo sapiens	70-79
20235151-4	2010	Arsenic also increased extracellular domain-deleted RET-PTC1 kinase activity with promotion of disulfide bond-mediated dimerization of RET-PTC1 protein.	Disulfides	95-104	patched 1	Homo sapiens	139-143
20479580-2	2010	Lp(a) contains a unique protein, apolipoprotein(a), which is linked to the Apo B-100 through a disulfide bond that gives it a great structural homology with plasminogen, and confers it atherogenic and atherothrombotic properties.	Disulfides	95-104	apolipoprotein B	Homo sapiens	75-84
20184893-7	2010	With the exception of the S134N metal-binding variant, the Zn affinity of disulfide-oxidized SOD1 monomers showed little sensitivity to amino acid replacements.	Disulfides	74-83	superoxide dismutase 1	Homo sapiens	93-97
20824113-6	2010	Despite the presence of disulfide bonds within individual Fn1 modules that are presumed to prevent their extension, it is found that significant internal structural changes within individual modules are induced by the forces applied in our simulations.	Disulfides	24-33	fibronectin 1	Homo sapiens	58-61
20824113-10	2010	The results suggest that Fn1 modules in FN polymers do contribute to the overall extension caused by force-induced stretching of the polymer in the ECM, and that binding properties of Fn1 modules can be affected by mechanically induced internal protein conformational changes in spite of the presence of disulfide bonds which were presumed to completely abolish the capacity of Fn1 modules to undergo extension in response to external forces.	Disulfides	304-313	fibronectin 1	Homo sapiens	184-187
20824113-10	2010	The results suggest that Fn1 modules in FN polymers do contribute to the overall extension caused by force-induced stretching of the polymer in the ECM, and that binding properties of Fn1 modules can be affected by mechanically induced internal protein conformational changes in spite of the presence of disulfide bonds which were presumed to completely abolish the capacity of Fn1 modules to undergo extension in response to external forces.	Disulfides	304-313	fibronectin 1	Homo sapiens	184-187
19961363-2	2010	Although bacterial expression has been used for the preparation of recombinant mIL-3 for more than 20 years, the resultant cytokine is known to exhibit poor solubility, be prone to aggregation, and may contain mispaired disulfide bonds.	Disulfides	220-229	interleukin 3	Mus musculus	79-84
20013338-1	2010	Although the fission yeast Schizosaccharomyces pombe has been used for high-level heterologous protein production, the productivity of secreted human serum transferrin (hTF) has been low, presumably, because the protein harbors twenty disulfide bonds and two N-glycosylation sites.	Disulfides	235-244	transferrin	Homo sapiens	156-167
20453928-3	2010	The correct folding of apoB requires assistance from chaperone proteins in co-translational lipidation, disulfide bond formation, and glycosylation.	Disulfides	104-113	apolipoprotein B	Homo sapiens	23-27
20145245-3	2010	Recently, peroxiredoxin (Prx)-induced relays of disulfide bond formation have been identified in budding yeast, namely the disulfide bond formation of Yap1, a crucial transcription factor for oxidative stress response, by a specific Prx Gpx3 and by a major Prx Tsa1.	Disulfides	48-57	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	151-155
20145245-3	2010	Recently, peroxiredoxin (Prx)-induced relays of disulfide bond formation have been identified in budding yeast, namely the disulfide bond formation of Yap1, a crucial transcription factor for oxidative stress response, by a specific Prx Gpx3 and by a major Prx Tsa1.	Disulfides	123-132	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	151-155
20174897-6	2010	The mIL-3 construct used in the present study was engineered by eliminating residues 27-32 of the N-terminus (the first 26 residues of the primary sequence of mIL-3 are cleaved in vivo during secretion), the C-terminal 10 residues (157-166), and a disulfide bond between Cys105 and Cys166 that is poorly conserved in orthologue sequences.	Disulfides	248-257	interleukin 3	Mus musculus	4-9
20124439-3	2010	The mutation, p.C65Y, replaces a conserved cysteine in the GPIHBP1 lymphocyte antigen 6 domain with a tyrosine and is predicted to perturb protein structure by interfering with the formation of a disulfide bond.	Disulfides	196-205	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	59-66
20019028-1	2010	Here we present a bispecific antibody (bsAb) format in which a disulfide-stabilized scFv is fused to the C-terminus of the light chain of an IgG to create an IgG-scFv bifunctional antibody.	Disulfides	63-72	immunglobulin heavy chain variable region	Homo sapiens	84-88
20208522-0	2010	Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation.	Disulfides	0-9	DOT1 like histone lysine methyltransferase	Homo sapiens	64-70
20208522-2	2010	The disulfide-linked analog of mono-ubiquitylated H2B stimulated the H3K79 methyltransferase activity of hDot1L to a similar extent as the native isopeptide linkage.	Disulfides	4-13	DOT1 like histone lysine methyltransferase	Homo sapiens	105-111
19883768-2	2010	MDK is a cysteine-rich 13 kDa protein containing five disulfide bonds.	Disulfides	54-63	midkine	Homo sapiens	0-3
20019028-1	2010	Here we present a bispecific antibody (bsAb) format in which a disulfide-stabilized scFv is fused to the C-terminus of the light chain of an IgG to create an IgG-scFv bifunctional antibody.	Disulfides	63-72	immunglobulin heavy chain variable region	Homo sapiens	162-166
20019028-3	2010	The extension of the C-terminus of the light chain of an IgG with an scFv or even a smaller peptide does appear to disrupt disulfide bond formation between the light and heavy chains; however, this does not appear to affect binding, stability or in vivo properties of the IgG.	Disulfides	123-132	immunglobulin heavy chain variable region	Homo sapiens	69-73
20163832-3	2010	In this article we review PDI contribution to different models of TF decryption, namely the disulfide switch model and the phosphatidylserine dynamics, and hypothesize on PDI contribution to TF self-association and association with lipid domains.	Disulfides	92-101	protein disulfide isomerase family A member 2	Homo sapiens	26-29
20163832-4	2010	Experimental evidence debate the disulfide switch model of TF decryption and its regulation by PDI.	Disulfides	33-42	protein disulfide isomerase family A member 2	Homo sapiens	95-98
20061377-8	2010	A cysteine mutant preventing KEAP1 intermolecular disulfide formation also prevented NRF2 stabilization in response to oxidants, whereas those preventing intramolecular disulfide formation were functionally silent.	Disulfides	50-59	NFE2 like bZIP transcription factor 2	Homo sapiens	85-89
20178376-4	2010	Here we investigated the activation mechanism of botulinum neurotoxin type E upon nicking and subsequent reduction of disulfide bond.	Disulfides	118-127	neurotoxin	Clostridium botulinum	59-69
20068035-0	2010	Engineering anti-vascular endothelial growth factor single chain disulfide-stabilized antibody variable fragments (sc-dsFv) with phage-displayed sc-dsFv libraries.	Disulfides	65-74	vascular endothelial growth factor A	Homo sapiens	17-51
20068035-6	2010	Comparison of the scFv and sc-dsFv variants selected from the phage-displayed libraries for vascular endothelial growth factor binding revealed the sequence preference differences resulting from the interdomain disulfide bond.	Disulfides	211-220	immunglobulin heavy chain variable region	Homo sapiens	18-22
20068035-6	2010	Comparison of the scFv and sc-dsFv variants selected from the phage-displayed libraries for vascular endothelial growth factor binding revealed the sequence preference differences resulting from the interdomain disulfide bond.	Disulfides	211-220	vascular endothelial growth factor A	Homo sapiens	92-126
20194751-4	2010	Here we show that KACL is a non-disulfide-linked homodimeric surface receptor and stimulates cytotoxicity by human NK92MI cells.	Disulfides	32-41	C-type lectin domain family 2 member A	Homo sapiens	18-22
20061377-5	2010	We found that in untreated cells, a fraction of KEAP1 carried a long range disulfide linking Cys(226) and Cys(613).	Disulfides	75-84	kelch like ECH associated protein 1	Homo sapiens	48-53
20061377-6	2010	Exposing cells to hydrogen peroxide, to the nitric oxide donor spermine NONOate, to hypochlorous acid, or to S-nitrosocysteine further increased this disulfide and promoted formation of a disulfide linking two KEAP1 molecules via Cys(151).	Disulfides	150-159	kelch like ECH associated protein 1	Homo sapiens	210-215
20061377-6	2010	Exposing cells to hydrogen peroxide, to the nitric oxide donor spermine NONOate, to hypochlorous acid, or to S-nitrosocysteine further increased this disulfide and promoted formation of a disulfide linking two KEAP1 molecules via Cys(151).	Disulfides	188-197	kelch like ECH associated protein 1	Homo sapiens	210-215
20061377-10	2010	We propose that KEAP1 intermolecular disulfide formation via Cys(151) underlies the activation of NRF2 by reactive oxygen and nitrogen species.	Disulfides	37-46	kelch like ECH associated protein 1	Homo sapiens	16-21
20061377-10	2010	We propose that KEAP1 intermolecular disulfide formation via Cys(151) underlies the activation of NRF2 by reactive oxygen and nitrogen species.	Disulfides	37-46	NFE2 like bZIP transcription factor 2	Homo sapiens	98-102
19933274-0	2010	Prm1 functions as a disulfide-linked complex in yeast mating.	Disulfides	20-29	pheromone-regulated protein PRM1	Saccharomyces cerevisiae S288C	0-4
20106974-1	2010	The folding of proinsulin, the single-chain precursor of insulin, ensures native disulfide pairing in pancreatic beta-cells.	Disulfides	81-90	insulin	Homo sapiens	15-25
20106974-1	2010	The folding of proinsulin, the single-chain precursor of insulin, ensures native disulfide pairing in pancreatic beta-cells.	Disulfides	81-90	insulin	Homo sapiens	18-25
20124699-3	2010	NMR structures of human and porcine C5a have been reported; these revealed a four-helix bundle stabilized by three disulfide bonds.	Disulfides	115-124	complement C5a receptor 1	Homo sapiens	36-39
19950203-4	2010	Western blot analysis in the presence or absence of reducing agents, revealed that H(2)O(2) induces the rapid formation of an intermolecular disulfide bond between Twist1 homodimers and Twist/E2a proteins heterodimers.	Disulfides	141-150	twist family bHLH transcription factor 1	Homo sapiens	164-170
19950203-5	2010	The disulfide bond is first observed between Twist1 homodimers at 25 mM H(2)O(2) and between Twist1 heterodimers at 75 mM H(2)O(2).	Disulfides	4-13	twist family bHLH transcription factor 1	Homo sapiens	45-51
19950203-5	2010	The disulfide bond is first observed between Twist1 homodimers at 25 mM H(2)O(2) and between Twist1 heterodimers at 75 mM H(2)O(2).	Disulfides	4-13	twist family bHLH transcription factor 1	Homo sapiens	93-99
19950203-9	2010	Disulfide bond formation between Twist1 homodimers significantly reduced its ability to interact with two of its binding partners, Runx2 and HDAC4, indicating that disulfide dimerization in response to H(2)O(2) has functional significance.	Disulfides	0-9	twist family bHLH transcription factor 1	Homo sapiens	33-39
19950203-9	2010	Disulfide bond formation between Twist1 homodimers significantly reduced its ability to interact with two of its binding partners, Runx2 and HDAC4, indicating that disulfide dimerization in response to H(2)O(2) has functional significance.	Disulfides	0-9	RUNX family transcription factor 2	Homo sapiens	131-136
19950203-9	2010	Disulfide bond formation between Twist1 homodimers significantly reduced its ability to interact with two of its binding partners, Runx2 and HDAC4, indicating that disulfide dimerization in response to H(2)O(2) has functional significance.	Disulfides	164-173	twist family bHLH transcription factor 1	Homo sapiens	33-39
19950203-9	2010	Disulfide bond formation between Twist1 homodimers significantly reduced its ability to interact with two of its binding partners, Runx2 and HDAC4, indicating that disulfide dimerization in response to H(2)O(2) has functional significance.	Disulfides	164-173	RUNX family transcription factor 2	Homo sapiens	131-136
19950203-10	2010	These data support the conclusion that disulfide bond formation in response to an oxidative stimulus contributes to Twist1 homo- and heterodimerization and raises the possibility that the redox status of a cell may represent an important step in bHLH transcriptional regulation.	Disulfides	39-48	twist family bHLH transcription factor 1	Homo sapiens	116-122
19882737-2	2010	Mammalian protein disulfide isomerase (PDI) has previously been shown to have a role in the formation of disulfide bonds in immunoglobulins.	Disulfides	18-27	protein disulfide isomerase family A member 2	Homo sapiens	39-42
20070606-4	2010	The formation of disulfide-linked conjugates of tapasin with ERp57 is suggested to be crucial for tapasin function.	Disulfides	17-26	TAP binding protein	Homo sapiens	48-55
20070606-4	2010	The formation of disulfide-linked conjugates of tapasin with ERp57 is suggested to be crucial for tapasin function.	Disulfides	17-26	protein disulfide isomerase family A member 3	Homo sapiens	61-66
20070606-4	2010	The formation of disulfide-linked conjugates of tapasin with ERp57 is suggested to be crucial for tapasin function.	Disulfides	17-26	TAP binding protein	Homo sapiens	98-105
19959476-1	2010	Proinsulin exhibits a single structure, whereas insulin-like growth factors refold as two disulfide isomers in equilibrium.	Disulfides	90-99	insulin	Homo sapiens	0-10
19959476-3	2010	Studies of mini-domain models suggest that residue B5 (His in insulin and Thr in IGFs) governs the ambiguity or uniqueness of disulfide pairing.	Disulfides	126-135	insulin	Homo sapiens	62-69
19959476-9	2010	Whereas wild-type IGF-I undergoes thiol-catalyzed disulfide exchange to yield IGF-swap, His(B5)-IGF-I retains canonical pairing.	Disulfides	50-59	insulin like growth factor 1	Homo sapiens	18-23
19917265-5	2010	capsulatus, the non-functional low-potential forms of cytochrome c(1) which are devoid of the disulfide bond naturally present in this protein revert spontaneously by introducing a second-site suppression (mutation A181T) that brings the potential of heme c(1) back to the functionally high levels, yet maintains it some 100 mV lower from the native value.	Disulfides	94-103	cytochrome c, somatic	Homo sapiens	54-66
19916574-10	2010	HBD-1, without disulfide bridges, unfolds to a greater extent during the course of the MDS.	Disulfides	15-24	defensin beta 1	Homo sapiens	0-5
19933274-2	2010	HA-Prm1 migrates at twice its expected molecular weight on non-reducing SDS-PAGE gels and coprecipitates with Prm1-TAP, indicating that Prm1 is a disulfide-linked homodimer.	Disulfides	146-155	pheromone-regulated protein PRM1	Saccharomyces cerevisiae S288C	3-7
19933274-6	2010	Cys(120) in loop 1 and Cys(545) in loop 2 form disulfide cross-links in the Prm1 homodimer and are required for fusion activity.	Disulfides	47-56	pheromone-regulated protein PRM1	Saccharomyces cerevisiae S288C	76-80
21071845-1	2010	Since human serum albumin has one sulfhydryl group and 17 disulfides, reactive sulfhydryl groups give rise to heterogeneity.	Disulfides	58-68	albumin	Homo sapiens	12-25
19899791-6	2010	The changes in secondary structure and conformation of disulfide linkage (S-S) of lysozyme were investigated experimentally by circular dichroism analysis and micro-Raman spectra.	Disulfides	55-64	lysozyme	Homo sapiens	82-90
20238000-3	2010	While these cysteines are used only for intramolecular disulfide bonds in most tetraspanins, RDS expresses a seventh, unpaired cysteine (C150) used for intermolecular disulfide bonding in the formation of large RDS oligomers.	Disulfides	167-176	peripherin 2	Mus musculus	93-96
20150614-0	2010	Disulfide-linked liposomes: effective delivery vehicle for Bcl-2 antisense oligodeoxyribonucleotide G3139.	Disulfides	0-9	BCL2 apoptosis regulator	Homo sapiens	59-64
20150614-3	2010	Disulfide-linked ODN liposomes were characterized for their size, ODN intracellular delivery, Bcl-2 mRNA and protein expression, growth inhibition, and chemosensitization.	Disulfides	0-9	BCL2 apoptosis regulator	Homo sapiens	94-99
20150614-5	2010	Treatment of the cells with disulfide-linked ODN liposomes resulted in efficient Bcl-2 down-regulation greater than that with hydrophobized disulfide-linked ODN and consistent with that of cellular growth inhibition and the sensitization to daunorubicin in KB cells.	Disulfides	28-37	BCL2 apoptosis regulator	Homo sapiens	81-86
20410586-4	2010	When MGST1 and hepsin were incubated at room temperature, MGST1 activity was markedly increased and the increase was decreased to the control level by further incubation with disulfide bond reducing agent dithiothreitol.	Disulfides	175-184	microsomal glutathione S-transferase 1	Rattus norvegicus	5-10
20410586-4	2010	When MGST1 and hepsin were incubated at room temperature, MGST1 activity was markedly increased and the increase was decreased to the control level by further incubation with disulfide bond reducing agent dithiothreitol.	Disulfides	175-184	hepsin	Rattus norvegicus	15-21
20410586-4	2010	When MGST1 and hepsin were incubated at room temperature, MGST1 activity was markedly increased and the increase was decreased to the control level by further incubation with disulfide bond reducing agent dithiothreitol.	Disulfides	175-184	microsomal glutathione S-transferase 1	Rattus norvegicus	58-63
20410586-8	2010	These results clearly show that the protease hepsin stimulates disulfide-linked MGST1 dimer formation resulting in activation of MGST1 and preferential degradation of MGST1 dimer.	Disulfides	63-72	hepsin	Rattus norvegicus	45-51
20410586-8	2010	These results clearly show that the protease hepsin stimulates disulfide-linked MGST1 dimer formation resulting in activation of MGST1 and preferential degradation of MGST1 dimer.	Disulfides	63-72	microsomal glutathione S-transferase 1	Rattus norvegicus	80-85
20410586-8	2010	These results clearly show that the protease hepsin stimulates disulfide-linked MGST1 dimer formation resulting in activation of MGST1 and preferential degradation of MGST1 dimer.	Disulfides	63-72	microsomal glutathione S-transferase 1	Rattus norvegicus	129-134
20410586-8	2010	These results clearly show that the protease hepsin stimulates disulfide-linked MGST1 dimer formation resulting in activation of MGST1 and preferential degradation of MGST1 dimer.	Disulfides	63-72	microsomal glutathione S-transferase 1	Rattus norvegicus	129-134
20410586-9	2010	Since hepsin contains disulfide bonds in the scavenger receptor cysteine-rich (SRCR) domain, it was suggested that the SRCR domain interacts with MGST1 leading to thiol/disulfide exchange between the two enzymes followed by disulfide-linked MGST1 dimer formation.	Disulfides	22-31	hepsin	Rattus norvegicus	6-12
20410586-9	2010	Since hepsin contains disulfide bonds in the scavenger receptor cysteine-rich (SRCR) domain, it was suggested that the SRCR domain interacts with MGST1 leading to thiol/disulfide exchange between the two enzymes followed by disulfide-linked MGST1 dimer formation.	Disulfides	22-31	microsomal glutathione S-transferase 1	Rattus norvegicus	146-151
19901032-3	2010	They are characterized by a conserved two-disulfide bond framework, which gives rise to two intervening loops of extensively mutated amino acids that determine their selectivity for different nAChR subtypes.	Disulfides	42-51	cholinergic receptor nicotinic alpha 4 subunit	Homo sapiens	192-197
20410586-9	2010	Since hepsin contains disulfide bonds in the scavenger receptor cysteine-rich (SRCR) domain, it was suggested that the SRCR domain interacts with MGST1 leading to thiol/disulfide exchange between the two enzymes followed by disulfide-linked MGST1 dimer formation.	Disulfides	169-178	hepsin	Rattus norvegicus	6-12
20410586-9	2010	Since hepsin contains disulfide bonds in the scavenger receptor cysteine-rich (SRCR) domain, it was suggested that the SRCR domain interacts with MGST1 leading to thiol/disulfide exchange between the two enzymes followed by disulfide-linked MGST1 dimer formation.	Disulfides	169-178	microsomal glutathione S-transferase 1	Rattus norvegicus	146-151
20410586-9	2010	Since hepsin contains disulfide bonds in the scavenger receptor cysteine-rich (SRCR) domain, it was suggested that the SRCR domain interacts with MGST1 leading to thiol/disulfide exchange between the two enzymes followed by disulfide-linked MGST1 dimer formation.	Disulfides	169-178	hepsin	Rattus norvegicus	6-12
20410586-9	2010	Since hepsin contains disulfide bonds in the scavenger receptor cysteine-rich (SRCR) domain, it was suggested that the SRCR domain interacts with MGST1 leading to thiol/disulfide exchange between the two enzymes followed by disulfide-linked MGST1 dimer formation.	Disulfides	169-178	microsomal glutathione S-transferase 1	Rattus norvegicus	146-151
20069542-6	2010	The most effective method for formation of the disulfide bond in amylin was found to be iodine oxidation.	Disulfides	47-56	islet amyloid polypeptide	Mus musculus	65-71
20069542-7	2010	The highest purity amylin was obtained when the crude peptide was purified with HPLC before formation of the disulfide bond.	Disulfides	109-118	islet amyloid polypeptide	Mus musculus	19-25
20069636-0	2010	Synthesis of the proteinase inhibitor LEKTI domain 6 by the fragment condensation method and regioselective disulfide bond formation.	Disulfides	108-117	endogenous retrovirus group K member 25	Homo sapiens	17-27
21125805-2	2010	A very large glycoprotein, the apoprotein (a) (apoA) is firmly linked to apo-B-100 by two covalent disulfide bonds.	Disulfides	99-108	apolipoprotein B	Homo sapiens	73-82
20798521-8	2010	CaSR assembles in the endoplasmic reticulum as a covalent disulfide-linked dimer and we determined whether retention requires the presence of arginine-rich regions in both subunits.	Disulfides	58-67	calcium sensing receptor	Homo sapiens	0-4
20029959-4	2010	CANX along with ERP-57 promotes the formation of disulfide bond bridges in nascent proteins.	Disulfides	49-58	protein disulfide isomerase family A member 3	Homo sapiens	16-22
20609911-2	2010	The redox state of cysteine-34 of human albumin defines three fractions which allow to monitor albumin oxidation: mercaptalbumin with a free thiol group, nonmercaptalbumin1 containing a disulfide, and nonmercaptalbumin2 with a sulfinic or sulfonic acid group.	Disulfides	186-195	albumin	Homo sapiens	40-47
19696176-8	2010	Disulfide myocilin homoaggregates decreased as the proteolytic processing increased.	Disulfides	0-9	myocilin	Homo sapiens	10-18
20233500-4	2010	bFGF was loaded into freeze-dried poly(gamma-glutamic acid) hydrogels with disulfide cross-links (gamma-PGA-SS gels) as a template to enhance cell growth.	Disulfides	75-84	fibroblast growth factor 2	Homo sapiens	0-4
19687800-4	2010	We showed that a large disulfide-bonded complex was present in the mouse cells that included ERp57, tapasin, and K(d).	Disulfides	23-32	TAP binding protein	Mus musculus	100-107
20308796-5	2010	Disruption of kringle structures by reduction of disulfide bonds resulted in the loss of the inhibitory effect of AS on VEGF-stimulated NO production.	Disulfides	49-58	vascular endothelial growth factor A	Homo sapiens	120-124
20007289-5	2010	The mature form was a 45-amino-acid peptide (stomagen) with three intramolecular disulfide bonds.	Disulfides	81-90	stomagen	Arabidopsis thaliana	45-53
19686851-3	2010	Here, we produced a dual functioning protein, designated as CAtin that exhibits both specific binding and killing functions, by fusing a tumor-specific apoptosis-inducing molecular Apoptin to C-terminus of an anti-CEA single-chain disulfide-stabilized Fv antibody (scdsFv).	Disulfides	231-240	CEA cell adhesion molecule 3	Homo sapiens	214-217
19943704-0	2009	Disulfide-dependent self-assembly of adiponectin octadecamers from trimers and presence of stable octadecameric adiponectin lacking disulfide bonds in vitro.	Disulfides	0-9	adiponectin, C1Q and collagen domain containing	Homo sapiens	112-123
19943704-0	2009	Disulfide-dependent self-assembly of adiponectin octadecamers from trimers and presence of stable octadecameric adiponectin lacking disulfide bonds in vitro.	Disulfides	0-9	adiponectin, C1Q and collagen domain containing	Homo sapiens	37-48
19878651-0	2009	Regulation of interleukin-4 signaling by extracellular reduction of intramolecular disulfides.	Disulfides	83-93	interleukin 4	Homo sapiens	14-27
19878651-1	2009	Interleukin-4 (IL-4) contains three structurally important intramolecular disulfides that are required for the bioactivity of the cytokine.	Disulfides	74-84	interleukin 4	Homo sapiens	0-13
19878651-1	2009	Interleukin-4 (IL-4) contains three structurally important intramolecular disulfides that are required for the bioactivity of the cytokine.	Disulfides	74-84	interleukin 4	Homo sapiens	15-19
19878651-2	2009	We show that the cell surface of HeLa cells and endotoxin-activated monocytes can reduce IL-4 intramolecular disulfides in the extracellular space and inhibit binding of IL-4 to the IL-4Ralpha receptor.	Disulfides	109-119	interleukin 4	Homo sapiens	89-93
19878651-3	2009	IL-4 disulfides were in vitro reduced by thioredoxin 1 (Trx1) and protein disulfide isomerase (PDI).	Disulfides	5-15	interleukin 4	Homo sapiens	0-4
19878651-4	2009	Reduction of IL-4 disulfides by the cell surface of HeLa cells was inhibited by auranofin, an inhibitor of thioredoxin reductase that is an electron donor to both Trx1 and PDI.	Disulfides	18-28	interleukin 4	Homo sapiens	13-17
19878651-5	2009	Both Trx1 and PDI have been shown to be located at the cell surface and our data suggests that these enzymes are involved in catalyzing reduction of IL-4 disulfides.	Disulfides	154-164	interleukin 4	Homo sapiens	149-153
19943704-0	2009	Disulfide-dependent self-assembly of adiponectin octadecamers from trimers and presence of stable octadecameric adiponectin lacking disulfide bonds in vitro.	Disulfides	132-141	adiponectin, C1Q and collagen domain containing	Homo sapiens	112-123
19878651-6	2009	The pro-drug N-acetylcysteine (NAC) that promotes T-helper type 1 responses was also shown to mediate the reduction of IL-4 disulfides.	Disulfides	124-134	interleukin 4	Homo sapiens	119-123
19943704-9	2009	These findings indicate that while disulfide bonds help to maintain the mature octadecameric adiponectin structure, their more important function is to stabilize intermediates during the assembly of octadecamer.	Disulfides	35-44	adiponectin, C1Q and collagen domain containing	Homo sapiens	93-104
19857203-6	2009	Reversible conjugation by a disulfide bond of a carrier peptide bearing a penetration accelerating sequence to PRL, facilitated the cellular uptake of this peptide and significantly inhibited phosphorylation of tau by PKN1 at the PKN1-specific phosphorylation site in vivo.	Disulfides	28-37	prolactin	Homo sapiens	111-114
19958498-5	2009	We used the X-ray crystallographic structure of bovine lysosomal alpha-mannosidase as template, containing only two disulphide bonds and some ligands, to build structural models of wild-type structures with four disulfide linkages and all bound ligands.	Disulfides	212-221	mannosidase alpha class 2B member 1	Bos taurus	55-82
20006956-1	2009	Insulin, a small hormone protein comprising 51 residues in two disulfide-linked polypeptide chains, adopts a predominantly alpha-helical conformation in its native state.	Disulfides	63-72	insulin	Homo sapiens	0-7
20006956-3	2009	Insulin is a unique model system in which to study protein fibrillization, since its three disulfide bridges are retained in the fibrillar state and thus limit the conformational space available to the polypeptide chains during misfolding and fibrillization.	Disulfides	91-100	insulin	Homo sapiens	0-7
19850922-10	2009	Classical studies of insulin chain combination in vitro have illuminated the impact of off-pathway reactions on the efficiency of native disulfide pairing.	Disulfides	137-146	insulin	Homo sapiens	21-28
19873992-2	2009	This work reports the online coupling of a thin-layer electrochemical flow cell with liquid sample desorption electrospray ionization mass spectrometry (DESI-MS) and its applications in investigating various electrochemical reactions of biological molecules such as oxidative formation and reductive cleavage of disulfide bonds and online derivatization of peptides/proteins.	Disulfides	312-321	desumoylating isopeptidase 2	Homo sapiens	153-157
19873992-4	2009	More importantly, with the use of this new coupling apparatus, three disulfide bonds of insulin were fully cleaved by electrolytic reduction and both the A and B chains of the protein were successfully detected online by DESI-MS.	Disulfides	69-78	desumoylating isopeptidase 2	Homo sapiens	221-225
19909340-1	2009	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.	Disulfides	147-156	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	50-55
19909340-1	2009	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.	Disulfides	147-156	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	57-61
19909340-1	2009	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.	Disulfides	147-156	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	62-65
19909340-1	2009	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.	Disulfides	147-156	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	66-70
19909340-2	2009	We have recently reported that the intramolecular disulfide bond is a critical checkpoint for determining the degradation fates of ABCG2.	Disulfides	50-59	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	131-136
19817991-3	2009	We generated a full length mutant VWF featuring a homologous disulfide bond in A2 (N1493C and C1670S), in an attempt to lock A2 against unfolding.	Disulfides	61-70	von Willebrand factor	Homo sapiens	34-37
19788901-2	2009	In addition, hSOD1 maintains an intra-subunit disulfide bond formed in the reducing environment of the cytosol and is active under a variety of stringent denaturing conditions.	Disulfides	46-55	superoxide dismutase 1	Homo sapiens	13-18
19788901-3	2009	We report the expression of hSOD1 in a cell-free protein synthesis system constructed from Spodoptera frugiperda 21 (Sf21) insect cells, and its structural analysis including the status of the sole intra-subunit disulfide bond by mass spectrometry.	Disulfides	212-221	superoxide dismutase 1	Homo sapiens	28-33
19817991-5	2009	Interestingly, disulfide bonds in the adjacent and highly homologous VWF A1 and A3 domains obstruct their mechanical unfolding.	Disulfides	15-24	von Willebrand factor	Homo sapiens	69-72
19835355-1	2009	Here we report a proof-of-principle study demonstrating the efficient folding, with concomitant formation of the correct disulfides, of an isolated polypeptide insulin precursor of defined covalent structure.	Disulfides	121-131	insulin	Homo sapiens	160-167
19716412-3	2009	Prx2 was oxidized to a disulfide-linked dimer by HOCl, glycine chloramine (GlyCl), and monochloramine (NH(2)Cl) in a dose-dependent manner.	Disulfides	23-32	peroxiredoxin 2	Homo sapiens	0-4
19824668-2	2009	Here we report on the in vitro and in vivo immunostimulatory capabilities of LbL-assembled disulfide cross-linked poly(methacrylic acid) (PMA(SH)) hydrogel capsules as a delivery strategy for protein and peptide vaccines using robust transgenic mice models and ovalbumin (OVA) as a model vaccine.	Disulfides	91-100	serine (or cysteine) peptidase inhibitor, clade B, member 1, pseudogene	Mus musculus	261-270
19824668-2	2009	Here we report on the in vitro and in vivo immunostimulatory capabilities of LbL-assembled disulfide cross-linked poly(methacrylic acid) (PMA(SH)) hydrogel capsules as a delivery strategy for protein and peptide vaccines using robust transgenic mice models and ovalbumin (OVA) as a model vaccine.	Disulfides	91-100	serine (or cysteine) peptidase inhibitor, clade B, member 1, pseudogene	Mus musculus	272-275
19835355-2	2009	We used oxime-forming chemical ligation to introduce a temporary "chemical tether" to link the N-terminal residue of the insulin A chain to the C-terminal residue of the insulin B chain; the tether enabled us to fold/form disulfides with high efficiency.	Disulfides	222-232	insulin	Homo sapiens	121-128
19835355-2	2009	We used oxime-forming chemical ligation to introduce a temporary "chemical tether" to link the N-terminal residue of the insulin A chain to the C-terminal residue of the insulin B chain; the tether enabled us to fold/form disulfides with high efficiency.	Disulfides	222-232	insulin	Homo sapiens	170-177
19817801-2	2009	The mature insulin molecule is composed of two polypeptide chains designated as A and B that are joined by two pairs of disulfide bonds with an additional intramolecular disulfide bond in the A chain.	Disulfides	120-129	insulin	Homo sapiens	11-18
19902129-3	2009	The Fourier transformed infrared spectroscopy (FTIR), Raman spectroscopy, and circular dichroism (CD) experiment results implied that hTFPI-2/KD3C contained small contents of alpha-helix and beta-strand, but large amounts of random coil and two kinds of disulfide bonds, gauche-gauche-gauche (ggg) and trans-gauchetrans (tgt).	Disulfides	254-263	tissue factor pathway inhibitor 2	Homo sapiens	134-146
19817801-2	2009	The mature insulin molecule is composed of two polypeptide chains designated as A and B that are joined by two pairs of disulfide bonds with an additional intramolecular disulfide bond in the A chain.	Disulfides	170-179	insulin	Homo sapiens	11-18
19825939-0	2009	Dominant pro-vasopressin mutants that cause diabetes insipidus form disulfide-linked fibrillar aggregates in the endoplasmic reticulum.	Disulfides	68-77	arginine vasopressin	Homo sapiens	13-24
19825939-3	2009	Here, we show that several dominant pro-vasopressin mutants form disulfide-linked homo-oligomers and develop large aggregations visible by immunofluorescence and immunogold electron microscopy, both in a fibroblast and a neuronal cell line.	Disulfides	65-74	arginine vasopressin	Homo sapiens	40-51
19551705-11	2009	In addition, the disulfide arrangement was then "de novo" identified in the recombinant murine leukocyte receptor NKR-P1A and in the larger glycosylated proteins beta-N-acetylhexosaminidases from Aspergillus oryzae and Penicillium oxalicum.	Disulfides	17-26	killer cell lectin-like receptor subfamily B member 1A	Mus musculus	114-121
19703468-6	2009	Among these, three represent novel proteins, which we named Cmc2 to 4 (for Cx(9)C motif-containing protein) and which we demonstrated to be dependent for import on the Mia40-Erv1 disulfide relay.	Disulfides	179-188	Cmc2p	Saccharomyces cerevisiae S288C	60-64
19651777-3	2009	In this study we correlated the metal contents and disulfide bond status of purified wild-type (WT) and mutant SOD1 proteins to changes in electrophoretic mobility and surface hydrophobicity as detected by 1-anilinonaphthalene-8-sulfonic acid (ANS) fluorescence.	Disulfides	51-60	superoxide dismutase 1	Homo sapiens	111-115
19592043-1	2009	Vascular endothelial growth factor (VEGF) is a disulfide-linked dimeric glycoprotein that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells.	Disulfides	47-56	vascular endothelial growth factor A	Homo sapiens	0-34
19592043-1	2009	Vascular endothelial growth factor (VEGF) is a disulfide-linked dimeric glycoprotein that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells.	Disulfides	47-56	vascular endothelial growth factor A	Homo sapiens	36-40
19805157-4	2009	In LPS-stimulated murine splenocytes, pERp1 interacted covalently via a disulfide bond with IgM monomers and noncovalently with other Ig assembly intermediates.	Disulfides	72-81	marginal zone B and B1 cell-specific protein 1	Mus musculus	38-43
19651777-5	2009	However, upon disulfide reduction and demetallation at physiological pH, both WT and mutant SOD1s underwent a conformational change that produced a slower mobility indicative of partial unfolding.	Disulfides	14-23	superoxide dismutase 1	Homo sapiens	92-96
19651777-7	2009	This increased interaction with ANS was greater for the mutant SOD1s and could be reversed by the addition of metal ions, especially Cu(2+), even for SOD1 variants incapable of forming the disulfide bond.	Disulfides	189-198	superoxide dismutase 1	Homo sapiens	63-67
19770509-4	2009	Analysis of the P2(1) crystal form uncovered major conformational changes (i) in beta-strands B, C and D, (ii) in loops 1, 2 and 4 at the open end of the beta-barrel and (iii) in the extended C-terminal segment, which is attached to the beta-barrel via a disulfide bridge.	Disulfides	255-264	cyclin dependent kinase inhibitor 1A	Homo sapiens	16-21
19615735-3	2009	TMC-Cys/insulin nanoparticles (TMC-Cys NP) showed a 2.1-4.7-fold increase in mucoadhesion compared to TMC/insulin nanoparticles (TMC NP), which might be partly attributed to disulfide formation between TMC-Cys and mucin as evidenced by DSC measurement.	Disulfides	174-183	insulin	Homo sapiens	8-15
20641539-9	2004	Three isoforms of ET (ET-1, ET-2, and ET-3) exist in mammalian tissues, each of which has 21 amino acids with two disulfide bonds.	Disulfides	114-123	endothelin 1	Homo sapiens	22-26
19596823-4	2009	A critical step on the SOD1 folding pathway occurs when the copper chaperone for SOD1 (CCS) modifies the nascent SOD1 polypeptide by inserting the catalytic copper cofactor and oxidizing its intrasubunit disulfide bond.	Disulfides	204-213	superoxide dismutase 1, soluble	Mus musculus	23-27
19596823-4	2009	A critical step on the SOD1 folding pathway occurs when the copper chaperone for SOD1 (CCS) modifies the nascent SOD1 polypeptide by inserting the catalytic copper cofactor and oxidizing its intrasubunit disulfide bond.	Disulfides	204-213	superoxide dismutase 1, soluble	Mus musculus	81-85
19596823-4	2009	A critical step on the SOD1 folding pathway occurs when the copper chaperone for SOD1 (CCS) modifies the nascent SOD1 polypeptide by inserting the catalytic copper cofactor and oxidizing its intrasubunit disulfide bond.	Disulfides	204-213	superoxide dismutase 1, soluble	Mus musculus	81-85
19596823-5	2009	Recent studies reveal that pathogenic SOD1 proteins coming from cultured cells and from the spinal cords of transgenic mice tend to be metal-deficient and/or lacking the disulfide bond, raising the possibility that the disease-causing mutations may enhance levels of SOD1-folding intermediates by preventing or hindering CCS-mediated SOD1 maturation.	Disulfides	170-179	superoxide dismutase 1, soluble	Mus musculus	38-42
19361272-6	2009	Mutating Tyr13, Thr58, and/or Asp74 to alanine in E. coli Grx1 results in the glutaredoxin-peptide mixed disulfide being thermodynamically favored over the glutaredoxin-glutathione mixed disulfide in the first step of the reaction.	Disulfides	105-114	dithiol glutaredoxin GRX1	Saccharomyces cerevisiae S288C	58-62
19701894-0	2009	Functional significance of tapasin membrane association and disulfide linkage to ERp57 in MHC class I presentation.	Disulfides	60-69	protein disulfide isomerase family A member 3	Homo sapiens	81-86
19701894-1	2009	Tapasin is disulfide linked to ERp57 within the peptide loading complex.	Disulfides	11-20	TAP binding protein	Homo sapiens	0-7
19701894-1	2009	Tapasin is disulfide linked to ERp57 within the peptide loading complex.	Disulfides	11-20	protein disulfide isomerase family A member 3	Homo sapiens	31-36
19567874-0	2009	Redox regulation of the human dual specificity phosphatase YVH1 through disulfide bond formation.	Disulfides	72-81	dual specificity phosphatase 12	Homo sapiens	59-63
19567874-5	2009	Furthermore, using differential thiol labeling and mass spectrometry, it was determined that hYVH1 forms intramolecular disulfide bonds at the catalytic cleft as well as within the zinc binding domain to avoid irreversible inactivation during severe oxidative stress.	Disulfides	120-129	dual specificity phosphatase 12	Homo sapiens	93-98
19586921-3	2009	To date, two such activation pathways have been identified: one requiring the CCS copper chaperone and one that works independently of CCS to insert copper and activate SOD1 through oxidation of an intramolecular disulfide.	Disulfides	213-222	superoxide dismutase 1	Homo sapiens	169-173
19589785-2	2009	One of these fragments, 611-CTF, is a hyperactive form of HER2 that constitutively establishes homodimers maintained by disulfide bonds, making it an excellent model to study overactivation of HER2 during tumor progression and metastasis.	Disulfides	120-129	erb-b2 receptor tyrosine kinase 2	Homo sapiens	58-62
19482076-6	2009	Our data also reveal that 4-HPR-mediated ROS evoke Akt conformational change by forming an intramolecular disulfide bond; N-acetylcysteine and glutathione, as thiol antioxidants, significantly abate the ROS generation in 4-HPR-exposed cells.	Disulfides	106-115	AKT serine/threonine kinase 1	Homo sapiens	51-54
19528071-5	2009	Selection of a 32-residue random library against interleukin-6 receptor generated novel peptides containing multiple disulfide bonds with a unique linkage for its function.	Disulfides	117-126	interleukin 6	Homo sapiens	49-62
19639556-0	2009	Mass spectrometry study of PRL-3 phosphatase inactivation by disulfide bond formation and cysteine into glycine conversion.	Disulfides	61-70	protein tyrosine phosphatase 4A3	Homo sapiens	27-32
19639556-3	2009	By liquid chromatography combined with selective alkylation and mass spectrometry, we found two main PRL-3 inactivation pathways: a disulfide bond formation between the catalytic C104 and C49, blocking the enzyme in an inactive oxidized form, or the conversion of the catalytic C104 into glycine.	Disulfides	132-141	protein tyrosine phosphatase 4A3	Homo sapiens	101-106
19522538-5	2009	In addition, we have generated functional TL1A mutants with altered disulfide bonding capability that exhibit enhanced solution properties, which will facilitate the production of materials for future cell-based and whole animal studies.	Disulfides	68-77	TNF superfamily member 15	Homo sapiens	42-46
19369250-3	2009	Here, we elucidate the conformational properties of a disulfide-reduced fragment of human PrP spanning residues 91-231 under acidic conditions, using a combination of heteronuclear NMR, analytical ultracentrifugation, and circular dichroism.	Disulfides	54-63	prion protein	Homo sapiens	90-93
19361272-6	2009	Mutating Tyr13, Thr58, and/or Asp74 to alanine in E. coli Grx1 results in the glutaredoxin-peptide mixed disulfide being thermodynamically favored over the glutaredoxin-glutathione mixed disulfide in the first step of the reaction.	Disulfides	187-196	dithiol glutaredoxin GRX1	Saccharomyces cerevisiae S288C	58-62
19393216-0	2009	Elucidation of the disulfide bridge pattern of the recombinant human growth and differentiation factor 5 dimer and the interchain Cys/Ala mutant monomer.	Disulfides	19-28	growth differentiation factor 5	Homo sapiens	69-104
19353641-0	2009	Glycerol-induced folding of unstructured disulfide-deficient lysozyme into a native-like conformation.	Disulfides	41-50	lysozyme	Homo sapiens	61-69
19353641-1	2009	2SS[6-127,64-80] variant of lysozyme which has two disulfide bridges, Cys6-Cys127 and Cys64-Cys80, and lacks the other two disulfide bridges, Cys30-Cys115 and Cys76-Cys94, was quite unstructured in water, but a part of the polypeptide chain was gradually frozen into a native-like conformation with increasing glycerol concentration.	Disulfides	51-60	lysozyme	Homo sapiens	28-36
19353641-1	2009	2SS[6-127,64-80] variant of lysozyme which has two disulfide bridges, Cys6-Cys127 and Cys64-Cys80, and lacks the other two disulfide bridges, Cys30-Cys115 and Cys76-Cys94, was quite unstructured in water, but a part of the polypeptide chain was gradually frozen into a native-like conformation with increasing glycerol concentration.	Disulfides	123-132	lysozyme	Homo sapiens	28-36
19571676-8	2009	The inactivation is mediated by oxidation of Cys277, which leads to Src homodimers linked by a disulfide bond between the Cys277 residues of two Src monomers.	Disulfides	95-104	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	68-71
19571676-8	2009	The inactivation is mediated by oxidation of Cys277, which leads to Src homodimers linked by a disulfide bond between the Cys277 residues of two Src monomers.	Disulfides	95-104	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	145-148
19477928-4	2009	During oxidation, four electrons were transferred from Tim13 with the insertion of two disulfide bonds in succession.	Disulfides	87-96	translocase of inner mitochondrial membrane 13	Homo sapiens	55-60
19397273-5	2009	Their Raman spectra show major modifications of the PIN-a structure as compared to the solid form, such as the formation of beta-sheets or unordered structures, the modification of the environment of the Trp domain and, the conformation of disulfide bridges.	Disulfides	240-249	puroindoline	Triticum aestivum	52-57
19393216-3	2009	Native homodimeric GDF5 belongs to the transforming growth factor beta (TGF-beta) superfamily; each monomer contains a cystine knot formed by three intrachain disulfide bridges, and the monomers are connected via an interchain disulfide bridge.	Disulfides	159-168	growth differentiation factor 5	Homo sapiens	19-23
19393216-3	2009	Native homodimeric GDF5 belongs to the transforming growth factor beta (TGF-beta) superfamily; each monomer contains a cystine knot formed by three intrachain disulfide bridges, and the monomers are connected via an interchain disulfide bridge.	Disulfides	227-236	growth differentiation factor 5	Homo sapiens	19-23
19449893-6	2009	LC-ESI-MS/MS and Western blotting analysis showed that lysozyme fragments were incorporated into the aggregates of ghost membrane proteins, which suggested that thio-disulfide exchange among lysozyme and membrane proteins was triggered when the fibrils interacted with erythrocyte membranes.	Disulfides	166-175	lysozyme	Homo sapiens	55-63
19630761-2	2009	VWF subunits dimerize in the ER and assemble into disulfide-linked multimers in the trans-Golgi, which lacks known chaperones and has an acidic pH that inhibits disulfide rearrangement.	Disulfides	50-59	von Willebrand factor	Homo sapiens	0-3
19630761-2	2009	VWF subunits dimerize in the ER and assemble into disulfide-linked multimers in the trans-Golgi, which lacks known chaperones and has an acidic pH that inhibits disulfide rearrangement.	Disulfides	161-170	von Willebrand factor	Homo sapiens	0-3
19534505-1	2009	This Letter reports the use of disulfide linkages to stabilize a beta-sheet dimer with a well-defined structure in aqueous and dimethyl sulfoxide solutions.	Disulfides	31-40	amyloid beta precursor protein	Homo sapiens	63-69
19552405-0	2009	Use of a temporary "solubilizing" peptide tag for the Fmoc solid-phase synthesis of human insulin glargine via use of regioselective disulfide bond formation.	Disulfides	133-142	insulin	Homo sapiens	90-97
19552405-7	2009	The applicability of the method was demonstrated by the novel preparation of insulin glargine via solid-phase synthesis of each of the two chains--including the notoriously poorly soluble A-chain--followed by their combination in solution via regioselective disulfide bond formation.	Disulfides	258-267	insulin	Homo sapiens	77-84
19432394-7	2009	When guanidinium chloride insoluble Muc2 units were analyzed, N-terminal parts of the Fc-gamma binding protein (Fcgbp) was found to be covalently attached in mouse and human colon, whereas its C-terminus was lost by reducing the disulfide bonds.	Disulfides	229-238	Fc fragment of IgG binding protein	Mus musculus	86-110
19432394-7	2009	When guanidinium chloride insoluble Muc2 units were analyzed, N-terminal parts of the Fc-gamma binding protein (Fcgbp) was found to be covalently attached in mouse and human colon, whereas its C-terminus was lost by reducing the disulfide bonds.	Disulfides	229-238	Fc fragment of IgG binding protein	Mus musculus	112-117
19477919-3	2009	We now show that protein disulfide isomerase (PDI) controls MHC class I disassembly by regulating dissociation of the tapasin-ERp57 disulfide conjugate.	Disulfides	25-34	TAP binding protein	Homo sapiens	118-125
19477919-3	2009	We now show that protein disulfide isomerase (PDI) controls MHC class I disassembly by regulating dissociation of the tapasin-ERp57 disulfide conjugate.	Disulfides	25-34	protein disulfide isomerase family A member 3	Homo sapiens	126-131
19449893-6	2009	LC-ESI-MS/MS and Western blotting analysis showed that lysozyme fragments were incorporated into the aggregates of ghost membrane proteins, which suggested that thio-disulfide exchange among lysozyme and membrane proteins was triggered when the fibrils interacted with erythrocyte membranes.	Disulfides	166-175	lysozyme	Homo sapiens	191-199
19449893-8	2009	The exposure of interior hydrophobic residues and the increased level of solvent-accessible disulfides in the lysozyme fibrils are thought to be involved in membrane disruption.	Disulfides	92-102	lysozyme	Homo sapiens	110-118
19456123-0	2009	A new function of GAPDH from Chlamydomonas reinhardtii: a thiol-disulfide exchange reaction with CP12.	Disulfides	64-73	uncharacterized protein	Chlamydomonas reinhardtii	97-101
19456123-5	2009	Algal CP12 contains four cysteine residues involved in two disulfide bridges in its oxidized state and has some alpha-helical secondary structural elements.	Disulfides	59-68	uncharacterized protein	Chlamydomonas reinhardtii	6-10
19456123-8	2009	Surprisingly, the partner protein GAPDH induced the cleavage of the disulfide bridge between the cysteine residues of CP12 and the spin-label, resulting in the full release of the label.	Disulfides	68-77	uncharacterized protein	Chlamydomonas reinhardtii	118-122
19366703-4	2009	However, the mature form of VEGF-D (VEGF-D(DeltaNDeltaC)) is predominantly a non-covalent dimer even though the cysteine residues (Cys-44 and Cys-53) forming the intersubunit disulfide bridges in the other members of the VEGF family are also conserved in VEGF-D.	Disulfides	175-184	vascular endothelial growth factor A	Homo sapiens	28-32
19533034-5	2009	Recently, we demonstrated that the putative transmembrane domain (TMD; residues 111-135) of Syrian hamster PrP penetrates into the membrane upon the reduction of the conserved disulfide bond of PrP.	Disulfides	176-185	major prion protein	Mesocricetus auratus	107-110
19533034-5	2009	Recently, we demonstrated that the putative transmembrane domain (TMD; residues 111-135) of Syrian hamster PrP penetrates into the membrane upon the reduction of the conserved disulfide bond of PrP.	Disulfides	176-185	major prion protein	Mesocricetus auratus	194-197
19533034-7	2009	We show that the reduction of the disulfide bond of PrP removes motional restriction of the TMD, which might, in turn, expose the TMD into solvent.	Disulfides	34-43	major prion protein	Mesocricetus auratus	52-55
19533034-9	2009	We suggest that the disulfide bond regulates the membrane binding mode of PrP by controlling the motional freedom of the TMD.	Disulfides	20-29	major prion protein	Mesocricetus auratus	74-77
19549303-1	2009	BACKGROUND: AVE9633 is a new immunoconjugate comprising a humanized monoclonal antibody, anti-CD33 antigen, linked through a disulfide bond to the maytansine derivative DM4, a cytotoxic agent and potent tubulin inhibitor.	Disulfides	125-134	CD33 molecule	Homo sapiens	94-98
19284778-3	2009	For one such hit class, defined by a central aminobenzylpiperidine (ABP) moiety, X-ray crystal structures of BACE mutant-disulfide conjugates revealed that the fragment bound by engaging both catalytic aspartates with hydrogen bonds.	Disulfides	121-130	beta-secretase 1	Homo sapiens	109-113
19361226-7	2009	These observations support a putative role for ERp18 within the cell as an oxidase, introducing disulfide bonds to substrate proteins, providing structural confirmation of ERp18"s role as a thiol-disulfide oxidoreductase.	Disulfides	96-105	thioredoxin domain containing 12	Homo sapiens	47-52
19099209-3	2009	The scFv-Fc fusion protein, showing spontaneous Fc fragment-mediated homodimerization via disulfide bridges, was affinity-purified on protein A Sepharose from culture supernatant.	Disulfides	90-99	immunglobulin heavy chain variable region	Homo sapiens	4-8
19038358-5	2009	We show that Grx1 efficiently catalyzes gp120, and CD4 disulfide reduction in vitro, even at low plasma levels of glutathione.	Disulfides	55-64	CD4 molecule	Homo sapiens	51-54
19038358-0	2009	Human glutaredoxin-1 catalyzes the reduction of HIV-1 gp120 and CD4 disulfides and its inhibition reduces HIV-1 replication.	Disulfides	68-78	CD4 molecule	Homo sapiens	64-67
19038358-1	2009	Reduction of intramolecular disulfides in the HIV-1 envelope protein gp120 occurs after its binding to the CD4 receptor.	Disulfides	28-38	CD4 molecule	Homo sapiens	107-110
19385064-5	2009	Cysteine assignments in a Rspo2 derivative containing only the two furin-like domains (Rspo2-2F) provided the first information about the disulfide bonding pattern of this motif, which was characterized by multiple short loops and unpaired cysteine residues, and established that the loss-of-function cysteine mutants disrupted disulfide bond formation.	Disulfides	138-147	R-spondin 2	Homo sapiens	26-31
19385064-5	2009	Cysteine assignments in a Rspo2 derivative containing only the two furin-like domains (Rspo2-2F) provided the first information about the disulfide bonding pattern of this motif, which was characterized by multiple short loops and unpaired cysteine residues, and established that the loss-of-function cysteine mutants disrupted disulfide bond formation.	Disulfides	138-147	R-spondin 2	Homo sapiens	87-92
19385064-5	2009	Cysteine assignments in a Rspo2 derivative containing only the two furin-like domains (Rspo2-2F) provided the first information about the disulfide bonding pattern of this motif, which was characterized by multiple short loops and unpaired cysteine residues, and established that the loss-of-function cysteine mutants disrupted disulfide bond formation.	Disulfides	328-337	R-spondin 2	Homo sapiens	26-31
19462475-1	2009	Interferon-alpha2b (IFN-alpha2b) and human serum albumin (HSA) fusion protein (IFN-alpha2b-HSA) is a promising long acting formulation of IFN-alpha2b for the treatment of hepatitis C. However, accelerated mechanical and thermal stress tests revealed that IFN-alpha2b-HSA was prone to disulfide-linked aggregation.	Disulfides	284-293	albumin	Homo sapiens	43-56
19178384-5	2009	The structure reveals an insulin/relaxin-like fold with three helical segments that are braced by three disulfide bonds and enclose a hydrophobic core.	Disulfides	104-113	insulin	Homo sapiens	25-32
19282281-9	2009	Modeling studies indicate that residue Cys-239 of beta1-tubulin is close to a highly conserved Cys-354 residue suggesting the possibility that disulfide formation could play a significant role in the stability of microtubules formed with beta1- but not with beta5-tubulin.	Disulfides	143-152	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	50-55
19282281-9	2009	Modeling studies indicate that residue Cys-239 of beta1-tubulin is close to a highly conserved Cys-354 residue suggesting the possibility that disulfide formation could play a significant role in the stability of microtubules formed with beta1- but not with beta5-tubulin.	Disulfides	143-152	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	238-243
19329427-0	2009	Domain interplay mediated by an essential disulfide linkage is critical for the activity and secretion of the metastasis-promoting enzyme autotaxin.	Disulfides	42-51	ectonucleotide pyrophosphatase/phosphodiesterase 2	Homo sapiens	138-147
19386499-4	2009	The drug linkers were conjugated to mAbs cAC10 (anti-CD30) and h1F6 (anti-CD70) via alkylation of reduced interchain disulfides to give ADCs loaded with 4 drugs/mAb.	Disulfides	117-127	CD70 molecule	Homo sapiens	74-78
19416874-0	2009	Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS.	Disulfides	20-29	superoxide dismutase 1, soluble	Mus musculus	15-19
19416874-2	2009	Using a highly sensitive detergent extraction assay, we traced the appearance and abundance of detergent-insoluble and disulfide cross-linked aggregates of SOD1 throughout the disease course of SOD1-fALS mice (G93A, G37R, and H46R/H48Q).	Disulfides	119-128	superoxide dismutase 1, soluble	Mus musculus	156-160
19416874-3	2009	We demonstrate that the accumulation of disulfide cross-linked, detergent-insoluble, aggregates of mutant SOD1 occurs primarily in the later stages of the disease, concurrent with the appearance of rapidly progressing symptoms.	Disulfides	40-49	superoxide dismutase 1, soluble	Mus musculus	106-110
19416874-5	2009	Also, using both cell culture and mouse models, we find that mutant protein lacking the normal intramolecular disulfide bond is a major component of the insoluble SOD1 aggregates.	Disulfides	110-119	superoxide dismutase 1, soluble	Mus musculus	163-167
19416874-7	2009	Within the final stages of disease, abnormalities in the oxidation of a normal intramolecular disulfide bond in mutant SOD1 facilitate the aggregation of mutant protein.	Disulfides	94-103	superoxide dismutase 1, soluble	Mus musculus	119-123
19564937-3	2009	Furthermore, use of HP-beta-CD could also increase the stability of disulfide bonds which are important to the conformation of insulin.	Disulfides	68-77	insulin	Homo sapiens	127-134
19150607-0	2009	Human pancreas-specific protein disulfide isomerase homolog (PDIp) is redox-regulated through formation of an inter-subunit disulfide bond.	Disulfides	32-41	protein disulfide isomerase family A member 2	Homo sapiens	61-65
19150607-3	2009	We found that formation of an inter-subunit disulfide bond in the recombinant human PDIp can alter not only its structure, but also its functions.	Disulfides	44-53	protein disulfide isomerase family A member 2	Homo sapiens	84-88
19150607-4	2009	PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond.	Disulfides	198-207	protein disulfide isomerase family A member 2	Homo sapiens	0-4
19150607-5	2009	The oxidized PDIp (with an inter-subunit disulfide bond) appears to expose more hydrophobic patches and is more sensitive to protease digestion compared to the reduced form.	Disulfides	41-50	protein disulfide isomerase family A member 2	Homo sapiens	13-17
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Disulfides	35-44	protein disulfide isomerase family A member 2	Homo sapiens	53-57
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Disulfides	35-44	protein disulfide isomerase family A member 2	Homo sapiens	172-176
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Disulfides	35-44	protein disulfide isomerase family A member 2	Homo sapiens	172-176
19150607-8	2009	In addition, we observed that the formation of the inter-subunit disulfide bond in PDIp is redox-dependent and is favored under oxidizing conditions, and that PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions.	Disulfides	65-74	protein disulfide isomerase family A member 2	Homo sapiens	83-87
19150607-8	2009	In addition, we observed that the formation of the inter-subunit disulfide bond in PDIp is redox-dependent and is favored under oxidizing conditions, and that PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions.	Disulfides	65-74	protein disulfide isomerase family A member 2	Homo sapiens	159-163
19150607-9	2009	In light of these observations, it is concluded that the structures and functions of human PDIp are redox-regulated through formation of an inter-subunit disulfide bond between two cysteine-4 residues.	Disulfides	154-163	protein disulfide isomerase family A member 2	Homo sapiens	91-95
19332105-6	2009	Interestingly, approximately 70 kDa fragments released upon reduction contained peptides from both the N and C terminal regions, which most likely represent fragments of a sparsely glycosylated PRG4 population that are disulfide-linked to extensively glycosylated, intact monomers.	Disulfides	219-228	proteoglycan 4	Bos taurus	194-198
19332105-7	2009	CONCLUSIONS: The analyses described here have demonstrated the presence of native disulfide-bonded multimers of PRG4 in normal bovine synovial fluids.	Disulfides	82-91	proteoglycan 4	Bos taurus	112-116
19332105-0	2009	Disulfide-bonded multimers of proteoglycan 4 PRG4 are present in normal synovial fluids.	Disulfides	0-9	proteoglycan 4	Bos taurus	30-44
19332105-0	2009	Disulfide-bonded multimers of proteoglycan 4 PRG4 are present in normal synovial fluids.	Disulfides	0-9	proteoglycan 4	Bos taurus	45-49
19337691-0	2009	Structure/function analysis of a critical disulfide bond in the active site of L-xylulose reductase.	Disulfides	42-51	dicarbonyl and L-xylulose reductase	Homo sapiens	79-99
19337691-2	2009	The crystal structure of human XR complemented with site-directed mutagenesis (Cys138Ala) indicated that the disulfide bond in the active site between Cys138 and Cys150 is unstable and may affect the reactivity of the enzyme.	Disulfides	109-118	dicarbonyl and L-xylulose reductase	Homo sapiens	31-33
19337691-6	2009	Thus, the action of human XR may be regulated by cellular redox conditions through reversible disulfide-bond formation and by S-cysteinylation.	Disulfides	94-103	dicarbonyl and L-xylulose reductase	Homo sapiens	26-28
19233858-7	2009	The spinal cord insoluble fraction from G85R/WTSOD1 mice had evidence of G85R-WTSOD1 heterodimers and WTSOD1 homodimers (in addition to G85R homodimers) with intermolecular disulfide bond cross-linking.	Disulfides	173-182	superoxide dismutase 1, soluble	Mus musculus	45-51
19233858-8	2009	These studies suggest that WTSOD1 can be recruited into disease-associated aggregates by redox processes, providing an explanation for the accelerated disease seen in G85R mice following WTSOD1 overexpression, and suggesting the importance of incorrect disulfide-linked protein as key to MTSOD1 toxicity.	Disulfides	253-262	superoxide dismutase 1, soluble	Mus musculus	27-33
19258317-0	2009	Formation of two intramolecular disulfide bonds is necessary for ApoA-I-dependent cholesterol efflux mediated by ABCA1.	Disulfides	32-41	apolipoprotein A1	Homo sapiens	65-71
19063682-2	2009	Using an engineered disulfide bond formation strategy, we characterized the relative conformational changes taking place within the PTH type 1 receptor (PTHR1) at the interface of transmembrane (TM)5 and TM6 on binding the PTH agonist, PTH(1-34), compared with the antagonist PTH(7-34).	Disulfides	20-29	parathyroid hormone	Homo sapiens	153-156
19063682-2	2009	Using an engineered disulfide bond formation strategy, we characterized the relative conformational changes taking place within the PTH type 1 receptor (PTHR1) at the interface of transmembrane (TM)5 and TM6 on binding the PTH agonist, PTH(1-34), compared with the antagonist PTH(7-34).	Disulfides	20-29	parathyroid hormone	Homo sapiens	153-156
19063682-2	2009	Using an engineered disulfide bond formation strategy, we characterized the relative conformational changes taking place within the PTH type 1 receptor (PTHR1) at the interface of transmembrane (TM)5 and TM6 on binding the PTH agonist, PTH(1-34), compared with the antagonist PTH(7-34).	Disulfides	20-29	parathyroid hormone	Homo sapiens	153-156
19063682-2	2009	Using an engineered disulfide bond formation strategy, we characterized the relative conformational changes taking place within the PTH type 1 receptor (PTHR1) at the interface of transmembrane (TM)5 and TM6 on binding the PTH agonist, PTH(1-34), compared with the antagonist PTH(7-34).	Disulfides	20-29	parathyroid hormone	Homo sapiens	132-135
19063682-2	2009	Using an engineered disulfide bond formation strategy, we characterized the relative conformational changes taking place within the PTH type 1 receptor (PTHR1) at the interface of transmembrane (TM)5 and TM6 on binding the PTH agonist, PTH(1-34), compared with the antagonist PTH(7-34).	Disulfides	20-29	parathyroid hormone 1 receptor	Homo sapiens	153-158
19454248-2	2009	This report describes a process that rapidly and reproducibly precipitates high-abundance disulfide-rich proteins, including albumin and transferrin, from serum and plasma.	Disulfides	90-99	transferrin	Homo sapiens	137-148
19227972-5	2009	These properties include the following: (1) an ablated copper-binding site, (2) a substantially weakened affinity for zinc, (3) a binding site for a calcium ion, (4) the ability to form stable heterocomplexes with the copper chaperone for SOD1 (CCS), and (5) compromised CCS-mediated oxidation of the intrasubunit disulfide bond in vivo.	Disulfides	314-323	superoxide dismutase 1	Homo sapiens	239-243
19281255-1	2009	Novel phenylazomethine dendrimers with a disulfide core (SS-DPA G1-4) were synthesized in nearly quantitative yields.	Disulfides	41-50	palmitoyl-protein thioesterase 2	Homo sapiens	64-68
19359471-5	2009	A cysteine residue within the AGR2 thioredoxin-like domain forms mixed disulfide bonds with MUC2, indicating a direct role for AGR2 in mucin processing.	Disulfides	71-80	anterior gradient 2	Mus musculus	30-34
19359471-5	2009	A cysteine residue within the AGR2 thioredoxin-like domain forms mixed disulfide bonds with MUC2, indicating a direct role for AGR2 in mucin processing.	Disulfides	71-80	anterior gradient 2	Mus musculus	127-131
19167089-6	2009	Exposing Sp1-3 to micromolar amounts of ebselen resulted in Zn(2+) release from this peptide and the formation of a disulfide bond by oxidation of zinc finger SH groups, the likely mechanism for DNA binding inhibition.	Disulfides	116-125	Sp1 transcription factor	Homo sapiens	9-14
19196713-1	2009	ERp57 is a thiol oxidoreductase that catalyzes disulfide formation in heavy chains of class I histocompatibility molecules.	Disulfides	47-56	protein disulfide isomerase family A member 3	Homo sapiens	0-5
19196713-6	2009	Moreover, ERp57 formed a mixed disulfide with tapasin and promoted efficient peptide loading in the absence of interactions with calnexin and calreticulin.	Disulfides	31-40	protein disulfide isomerase family A member 3	Homo sapiens	10-15
19416153-1	2009	The relaxin peptide hormones are members of the insulin superfamily and share a structural fold that is characterized by two peptide chains which are cross-braced by three disulfide bonds.	Disulfides	172-181	insulin	Homo sapiens	48-55
19238172-0	2009	Oxidative modification of caspase-9 facilitates its activation via disulfide-mediated interaction with Apaf-1.	Disulfides	67-76	apoptotic peptidase activating factor 1	Homo sapiens	103-109
19238172-5	2009	Hydrogen peroxide treatment causes the activation of caspase-9 and apoptosis, and promotes an interaction between caspase-9 and apoptotic protease-activating factor 1 (Apaf-1) via disulfide formation.	Disulfides	180-189	apoptotic peptidase activating factor 1	Homo sapiens	128-166
19238172-5	2009	Hydrogen peroxide treatment causes the activation of caspase-9 and apoptosis, and promotes an interaction between caspase-9 and apoptotic protease-activating factor 1 (Apaf-1) via disulfide formation.	Disulfides	180-189	apoptotic peptidase activating factor 1	Homo sapiens	168-174
19238172-6	2009	In addition, in an in vitro mitochondria-free system, the thiol-oxidant diamide promotes auto-cleavage of caspase-9 and the caspase-9/Apaf-1 interaction by facilitating the formation of disulfide-linked complexes.	Disulfides	186-195	apoptotic peptidase activating factor 1	Homo sapiens	134-140
19238172-7	2009	Finally, a point mutation at C403 of caspase-9 impairs both H(2)O(2)-promoted caspase-9 activation and interaction with Apaf-1 through the abolition of disulfide formation.	Disulfides	152-161	apoptotic peptidase activating factor 1	Homo sapiens	120-126
19059469-2	2009	Disulfide and thioether linked conjugates were prepared by coupling Cyt c to cysteinyl-nonaarginine, C(R)(9), through SPDP and SMPB cross-linkers, respectively.	Disulfides	0-9	cytochrome c, somatic	Homo sapiens	68-73
19059469-5	2009	However, the biological activity of the internalized Cyt c, indicated by apoptosis in HeLa cells, was expressed only in the thioether (SMPB) conjugate, but not the disulfide (SPDP) conjugate or free Cyt c.	Disulfides	164-173	cytochrome c, somatic	Homo sapiens	53-58
19152385-0	2009	Protein instability during HIC: evidence of unfolding reversibility, and apparent adsorption strength of disulfide bond-reduced alpha-lactalbumin variants.	Disulfides	105-114	lactalbumin alpha	Homo sapiens	128-145
19152385-4	2009	Additionally, variants of alpha-lactalbumin in which one of the disulfide bonds is reduced were synthesized to examine the effects of conformational stability on apparent retention.	Disulfides	64-73	lactalbumin alpha	Homo sapiens	26-43
19223469-5	2009	Oxidative stress induced by cellular glucose deprivation reduces the RNA-binding activity of IRP2 but not IRP2-C512S or IRP2-C516S, consistent with the formation of a disulfide bond between IRP2 C512 and C516 during oxidative stress.	Disulfides	167-176	iron responsive element binding protein 2	Homo sapiens	93-97
19273857-5	2009	This inactivation is caused by oxidation of a specific cysteine residue (Cys-277), which results in homodimerization of Src linked by a disulfide bridge.	Disulfides	136-145	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	120-123
19050038-2	2009	Cysteine-150 (C150) in Rds has been implicated in intermolecular disulfide bonding essential for functional Rds complexes.	Disulfides	65-74	peripherin 2	Mus musculus	23-26
19050038-2	2009	Cysteine-150 (C150) in Rds has been implicated in intermolecular disulfide bonding essential for functional Rds complexes.	Disulfides	65-74	peripherin 2	Mus musculus	108-111
19204593-0	2009	Effects of acute and chronic exercise on disulfide-linked growth hormone variants.	Disulfides	41-50	growth hormone 1	Homo sapiens	58-72
19204593-1	2009	PURPOSE: To test the hypothesis that the appearance of disulfide-linked growth hormone (GH) aggregates during and after an acute resistance exercise test (ARET) in men could be influenced by chronic physical training.	Disulfides	55-64	growth hormone 1	Homo sapiens	72-86
19204593-1	2009	PURPOSE: To test the hypothesis that the appearance of disulfide-linked growth hormone (GH) aggregates during and after an acute resistance exercise test (ARET) in men could be influenced by chronic physical training.	Disulfides	55-64	growth hormone 1	Homo sapiens	88-90
19204593-4	2009	To determine whether GH molecules were disulfide-linked, serum samples were chemically reduced via glutathione (GSH).	Disulfides	39-48	growth hormone 1	Homo sapiens	21-23
19204593-9	2009	Post hoc testing indicated that serum contained IRGH disulfide-linked GH aggregates at the mid, 0-, 15-, and 30-min posttime points of the ARET (P &lt; 0.01), whereas GSH reduction did not affect IFGH concentrations.	Disulfides	53-62	growth hormone 1	Homo sapiens	50-52
19204593-12	2009	The physiological significance of increased proportions of disulfide-linked GH aggregates postexercise remains uncertain; however, structural alterations in GH moieties after acute exercise may represent important regulatory steps in mediating GH biological activity at selected target tissues.	Disulfides	59-68	growth hormone 1	Homo sapiens	76-78
19098004-1	2009	alpha-Conotoxins are small disulfide-rich peptides from the venom of the Conus species that target the nicotinic acetylcholine receptor (nAChR).	Disulfides	27-36	cholinergic receptor nicotinic alpha 4 subunit	Homo sapiens	103-135
19230722-3	2009	Here we report that cell-permeable chemical probes, which are selective for sulfenic acid, inhibit peroxide-dependent nuclear accumulation of Yap1, trap the Gpx3 sulfenic acid intermediate, and block formation of the Yap1-Gpx3 intermolecular disulfide directly in cells.	Disulfides	242-251	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	142-146
19230722-3	2009	Here we report that cell-permeable chemical probes, which are selective for sulfenic acid, inhibit peroxide-dependent nuclear accumulation of Yap1, trap the Gpx3 sulfenic acid intermediate, and block formation of the Yap1-Gpx3 intermolecular disulfide directly in cells.	Disulfides	242-251	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	217-221
19230722-4	2009	In addition, we present electrostatic calculations that show cysteine oxidation is accompanied by significant changes in charge distribution, which might facilitate essential conformational rearrangements in Gpx3 during catalysis and intermolecular disulfide formation with Yap1.	Disulfides	249-258	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	274-278
19098004-1	2009	alpha-Conotoxins are small disulfide-rich peptides from the venom of the Conus species that target the nicotinic acetylcholine receptor (nAChR).	Disulfides	27-36	cholinergic receptor nicotinic alpha 4 subunit	Homo sapiens	137-142
19106090-0	2009	A major peroxiredoxin-induced activation of Yap1 transcription factor is mediated by reduction-sensitive disulfide bonds and reveals a low level of transcriptional activation.	Disulfides	105-114	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	44-48
19106090-5	2009	In the present study, we show that Tsa1 can interact with Yap1 via disulfide linkages and induce the formation of intramolecular disulfide bonds in Yap1 in ybp1-1 cells.	Disulfides	129-138	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	148-152
19106090-2	2009	Yap1, the master transcription factor for the oxidative stress response in budding yeast, is activated by the formation of disulfide bonds in response to H(2)O(2).	Disulfides	123-132	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	0-4
19106090-8	2009	These data support our hypothesis that changes in the redox status of Yap1 to reduction-resistant forms by multiple disulfide bond formation are important for determining the level and duration of Yap1 activity in the dynamic equilibrium of redox reactions in cells exposed to H(2)O(2).	Disulfides	116-125	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	70-74
19106090-8	2009	These data support our hypothesis that changes in the redox status of Yap1 to reduction-resistant forms by multiple disulfide bond formation are important for determining the level and duration of Yap1 activity in the dynamic equilibrium of redox reactions in cells exposed to H(2)O(2).	Disulfides	116-125	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	197-201
19106090-3	2009	Gpx3 (glutathione peroxidase-like protein 3) acts as a receptor for H(2)O(2), and Ybp1 (Yap1-binding protein 1) is crucial for Gpx3-dependent disulfide bond formation in Yap1.	Disulfides	142-151	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	88-92
19106090-3	2009	Gpx3 (glutathione peroxidase-like protein 3) acts as a receptor for H(2)O(2), and Ybp1 (Yap1-binding protein 1) is crucial for Gpx3-dependent disulfide bond formation in Yap1.	Disulfides	142-151	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	170-174
19106090-5	2009	In the present study, we show that Tsa1 can interact with Yap1 via disulfide linkages and induce the formation of intramolecular disulfide bonds in Yap1 in ybp1-1 cells.	Disulfides	67-76	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	58-62
19274343-9	2009	These results suggest that ERp18 has a reduction role on disulfide bonds in wild-type hGnRHR folding.	Disulfides	57-66	thioredoxin domain containing 12	Homo sapiens	27-32
19039312-4	2009	RESULTS: Preincubation of cells with DTT, a maneuver designed to target receptor disulfides, resulted in concentration-dependent decreases in specific (125)I-AngII binding to AT1Rs and acute angiotensin-stimulated intracellular calcium mobilization but no decreases in specific (125)I-AVP binding to V1Rs or AVP-stimulated intracellular calcium mobilization.	Disulfides	81-91	angiotensinogen	Rattus norvegicus	158-163
19039312-5	2009	In contrast, preincubation of the ligands with DTT followed by acute exposure to the cells, a maneuver designed to target ligand disulfides, blunted calcium mobilization to AVP robustly but to AngII only minimally.	Disulfides	129-139	angiotensinogen	Rattus norvegicus	193-198
19038292-2	2009	This study investigates whether S-glutathionylation of mitochondrial proteins plays a role in DOX-induced myocardial injury using a line of transgenic mice expressing the human mitochondrial glutaredoxin 2 (Glrx2), a thiotransferase catalyzing the reduction as well as formation of protein-glutathione mixed disulfides, in cardiomyocytes.	Disulfides	308-318	glutaredoxin 2	Homo sapiens	191-205
19038292-2	2009	This study investigates whether S-glutathionylation of mitochondrial proteins plays a role in DOX-induced myocardial injury using a line of transgenic mice expressing the human mitochondrial glutaredoxin 2 (Glrx2), a thiotransferase catalyzing the reduction as well as formation of protein-glutathione mixed disulfides, in cardiomyocytes.	Disulfides	308-318	glutaredoxin 2	Homo sapiens	207-212
19179285-7	2009	The crystal structure of the complex of ACI with human carboxypeptidase A1, one of its potential targets in vivo, revealed a protein with a fold consisting of two tandem homologous domains, each containing a beta-ribbon and two disulfide bonds.	Disulfides	228-237	carboxypeptidase A1	Homo sapiens	55-74
19037098-4	2009	Like the human counterparts, each Tim9 and Tim10 subunit contains a central loop flanked by disulfide bonds that separate two extended N- and C-terminal tentacle-like helices.	Disulfides	92-101	translocase of inner mitochondrial membrane 9	Homo sapiens	34-38
18992757-10	2009	We hypothesize that the substitutions of Ser23 and Gln52 in yGrx1 by Ala23 and Glu52 in yGrx2 modify the capability of the active-site C-terminal cysteine to attack the mixed disulfide between the N-terminal active-site cysteine and the glutathione molecule.	Disulfides	175-184	dithiol glutaredoxin GRX1	Saccharomyces cerevisiae S288C	60-65
19091820-6	2009	Similar to other BSP proteins, BSPH1 contains two fibronectin type-II (Fn2) domains, each consisting of two disulfide bonds.	Disulfides	108-117	binder of sperm protein homolog 1	Homo sapiens	31-36
19111842-1	2009	Human ATP-binding cassette (ABC) transporter ABCG2 (BCRP/MXR/ABCP) is a plasma membrane protein carrying intra- and inter-molecular disulfide bonds and an N-linked glycan.	Disulfides	132-141	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	45-50
19111842-1	2009	Human ATP-binding cassette (ABC) transporter ABCG2 (BCRP/MXR/ABCP) is a plasma membrane protein carrying intra- and inter-molecular disulfide bonds and an N-linked glycan.	Disulfides	132-141	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	52-56
19111842-1	2009	Human ATP-binding cassette (ABC) transporter ABCG2 (BCRP/MXR/ABCP) is a plasma membrane protein carrying intra- and inter-molecular disulfide bonds and an N-linked glycan.	Disulfides	132-141	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	57-60
19111842-1	2009	Human ATP-binding cassette (ABC) transporter ABCG2 (BCRP/MXR/ABCP) is a plasma membrane protein carrying intra- and inter-molecular disulfide bonds and an N-linked glycan.	Disulfides	132-141	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	61-65
19111842-2	2009	Both disulfide bond formation and N-glycosylation are critical check points determining the stability and degradation fate of ABCG2 protein in the endoplasmic reticulum (ER).	Disulfides	5-14	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	126-131
18842679-6	2009	We focused on whey acidic protein four-disulfide core domain 1 (WFDC1), a known secreted protease inhibitor, and found it to be downregulated in the CAFs.	Disulfides	39-48	WAP four-disulfide core domain 1	Homo sapiens	64-69
19578238-1	2009	BACKGROUND: This study was conducted to construct a basis for a therapeutic strategy against human T-lymphotropic virus type-I (HTLV-I)-associated myelopathy/tropical spastic paraparesis (HAM/TSP) using a compound that contained a disulfide moiety, prosultiamine, which is a homologue of allithiamine originally synthesized by allicin and thiamine-thiol, for the targeting of HTLV-I-infected cells.	Disulfides	231-240	thrombospondin 1	Homo sapiens	192-195
19224592-1	2009	We have performed a detailed characterization of recombinant human growth hormone that included the identification of the entire sequence with disulfide linkages as well as subtle modifications by a sensitive liquid chromatography coupled online with tandem mass spectrometry (LC-MS) approach using the accurate peptide mass (FTICR MS) and sequence assignment (MS/MS measurement).	Disulfides	143-152	growth hormone 1	Homo sapiens	67-81
19054761-2	2009	One such enzyme, ERp57, is thought to catalyze the isomerization of non-native disulfide bonds formed in glycoproteins with unstructured disulfide-rich domains.	Disulfides	79-88	protein disulfide isomerase family A member 3	Homo sapiens	17-22
19054761-2	2009	One such enzyme, ERp57, is thought to catalyze the isomerization of non-native disulfide bonds formed in glycoproteins with unstructured disulfide-rich domains.	Disulfides	137-146	protein disulfide isomerase family A member 3	Homo sapiens	17-22
19054761-5	2009	In addition, some glycoproteins only require ERp57 for correct disulfide formation if they enter the calnexin cycle.	Disulfides	63-72	protein disulfide isomerase family A member 3	Homo sapiens	45-50
19119025-2	2009	It functions within the multimeric peptide-loading complex (PLC) as a disulfide-linked, stable heterodimer with the thiol oxidoreductase ERp57, and this covalent interaction is required to support optimal PLC activity.	Disulfides	70-79	protein disulfide isomerase family A member 3	Homo sapiens	137-142
19117448-6	2009	The online LC-MS approach is successfully demonstrated in the characterization of disulfide linkages of recombinant human growth hormone (Nutropin), a therapeutic monoclonal antibody, and tissue plasminogen activator (Activase).	Disulfides	82-91	growth hormone 1	Homo sapiens	122-136
18796561-0	2009	Oxidative, multistep activation of the noncanonical NF-kappaB pathway via disulfide Bcl-3/p50 complex.	Disulfides	74-83	nuclear factor kappa B subunit 1	Homo sapiens	90-93
20028322-5	2009	The sequence of the human A(3)AR contains only one cysteine residue (Cys166) in the second extracellular loop (EL2), which putatively forms a conserved disulfide bridge with the respective cysteine residues of TM3 (Cys83).	Disulfides	152-161	adenosine A3 receptor	Homo sapiens	26-32
19225211-1	2009	Disulfide-bond-A oxidoreductase-like protein (DsbA-L) has been suggested to take part in the disulfide bond formation progress of proteins, including insulin and adiponectin.	Disulfides	93-102	insulin	Homo sapiens	150-157
19225211-1	2009	Disulfide-bond-A oxidoreductase-like protein (DsbA-L) has been suggested to take part in the disulfide bond formation progress of proteins, including insulin and adiponectin.	Disulfides	93-102	adiponectin, C1Q and collagen domain containing	Homo sapiens	162-173
18796561-4	2009	The early phase, coinciding with substantial thiol depletion, produces a cytosolic preparative complex, consisting of p50 and its interactor Bcl-3 linked by interprotein disulfide bridges.	Disulfides	170-179	nuclear factor kappa B subunit 1	Homo sapiens	118-121
18990587-0	2009	Mapping disulfide bonds in insulin with the Route 66 Method: selective cleavage of S-C bonds using alkali and alkaline earth metal enolate complexes.	Disulfides	8-17	insulin	Homo sapiens	27-34
18990587-1	2009	Simple and fast identification of disulfide linkages in insulin is demonstrated with a peptic digest using the Route 66 method.	Disulfides	34-43	insulin	Homo sapiens	56-63
19031361-0	2009	Antigenotoxic effects of the disulfide compound persicasulfide A (PSA) on rat lymphocytes exposed to oxidative stress.	Disulfides	29-38	aminopeptidase puromycin sensitive	Rattus norvegicus	66-69
18428798-0	2009	Evaluation of the physical stability of the EC5 domain of E-cadherin: effects of pH, temperature, ionic strength, and disulfide bonds.	Disulfides	118-127	cadherin 1	Homo sapiens	58-68
19059647-2	2009	The N-terminal portion of serglycin contains a conserved disulfide motif that is similar to motifs found in secretory granule compounds of neuroendocrine cells.	Disulfides	57-66	serglycin	Homo sapiens	26-35
19059647-11	2009	These findings are thus in accordance with a role for the N-terminal disulfide motif in serglycin for regulation of mast cell secretory granule integrity.	Disulfides	69-78	serglycin	Homo sapiens	88-97
19033368-3	2009	To examine whether such changes take place, we have constructed a phi29 DNA polymerase mutant able to form a disulfide bond between the apexes of TPR2 and thumb to limit the mobility of TPR2.	Disulfides	109-118	DnaJ heat shock protein family (Hsp40) member C7	Homo sapiens	146-150
19033368-3	2009	To examine whether such changes take place, we have constructed a phi29 DNA polymerase mutant able to form a disulfide bond between the apexes of TPR2 and thumb to limit the mobility of TPR2.	Disulfides	109-118	DnaJ heat shock protein family (Hsp40) member C7	Homo sapiens	186-190
19033368-5	2009	Despite the fact that no TPR2 motion is needed to allow the polymerase to use the terminal protein (TP) as primer during the initiation of phi29 TP-DNA replication, the disulfide bond prevents the DNA polymerase from entering the elongation phase, suggesting that TPR2 movements are necessary to allow the TP priming domain to move out from the polymerase during transition from initiation to elongation.	Disulfides	169-178	DnaJ heat shock protein family (Hsp40) member C7	Homo sapiens	264-268
19251032-1	2009	The identification in the 1950s of insulin, an essential carbohydrate regulatory hormone, as consisting of not one but two peptide chains linked by three disulfide bonds in a distinctive pattern was a milestone in peptide chemistry.	Disulfides	154-163	insulin	Homo sapiens	35-42
19325915-7	2009	ALS mutations enhanced the ability of disulfide-reduced SOD1 to form amyloid-like aggregates, and apo-AS-SOD1 formed amyloid-like aggregates at pH 7 only when an ALS mutation was also present.	Disulfides	38-47	superoxide dismutase 1	Homo sapiens	56-60
19325915-8	2009	These results indicate that some mutations related to ALS promote formation of amyloid-like aggregates by facilitating the loss of metals and/or by making the intramolecular disulfide bond more susceptible to reduction, thus allowing the conversion of SOD1 to a form that aggregates to form resembling amyloid.	Disulfides	174-183	superoxide dismutase 1	Homo sapiens	252-256
19251032-7	2009	The six cysteine residues that form the three insulin disulfide cross-links - one intramolecular within the A-chain and two intermolecular between that A- and B-chains - are absolutely conserved across all members of the superfamily.	Disulfides	54-63	insulin	Homo sapiens	46-53
18849342-7	2008	These interactions were required for the efficient maturation of NA as it prematurely formed intramolecular disulfides and aggregated when calnexin and calreticulin interactions were abolished.	Disulfides	108-118	calreticulin	Homo sapiens	152-164
19052230-2	2008	Each SOD1 monomer binds to 1 copper and 1 zinc ion and maintains its disulfide bond (Cys-57-Cys-146) in the reducing cytoplasm of cell.	Disulfides	69-78	superoxide dismutase 1	Homo sapiens	5-9
19052230-3	2008	Mounting experimental evidence suggests that metal loss and/or disulfide reduction are important for initiating misfolding and aggregation of SOD1.	Disulfides	63-72	superoxide dismutase 1	Homo sapiens	142-146
19052230-4	2008	To uncover the role of metals and the disulfide bond in the SOD1 folding, we systemically study the folding thermodynamics and structural dynamics of SOD1 monomer and dimer with and without metal binding and under disulfide-intact or disulfide-reduced environments in computational simulations.	Disulfides	38-47	superoxide dismutase 1	Homo sapiens	60-64
19052230-8	2008	The reduction of the disulfide bond in SOD1 with metal ions depleted results in a flexible Glu-49-Asn-53 loop, which, in turn, disrupts dimer formation.	Disulfides	21-30	superoxide dismutase 1	Homo sapiens	39-43
19052230-12	2008	Our simulation study sheds light on the critical role of metals and disulfide bond in SOD1 folding and aggregation.	Disulfides	68-77	superoxide dismutase 1	Homo sapiens	86-90
19035371-1	2008	Insulin is a peptide hormone consisting of 51 amino acids in two chains with three disulfide bridges.	Disulfides	83-92	insulin	Homo sapiens	0-7
19035371-3	2008	Herein, we report the chemical synthesis of insulin by the step-wise, Fmoc-based, solid-phase synthesis of single-chain precursors with solubilising extensions, which under redox conditions, spontaneously fold with the correct pairing of the three disulfide bridges.	Disulfides	248-257	insulin	Homo sapiens	44-51
19055324-1	2008	ENOX (ECTO-NOX) proteins are growth-related cell surface proteins that catalyze both hydroquinone or NADH oxidation and protein disulfide-thiol interchange and exhibit both prion-like and time-keeping (clock) properties.	Disulfides	128-137	ecto-NOX disulfide-thiol exchanger 2	Homo sapiens	0-4
18930922-7	2008	We determined the structure of ROAD-1 using NMR spectroscopy and find that the synthetic peptide adopts the canonical disulfide pairing and alpha-defensin fold.	Disulfides	118-127	oral alpha defensin 1	Macaca mulatta	31-37
19091013-3	2008	PDI is capable of mediating thio-disulfide interchange reactions and could enable the reduction of gp120 disulfide bonds, which triggers the major conformational changes in gp120 and gp41 required for virus entry.	Disulfides	33-42	protein disulfide isomerase family A member 2	Homo sapiens	0-3
18991392-3	2008	Like other members of the pyridine nucleotide-disulfide oxidoreductase family, TrxR is a homodimer; in the enzyme from D. melanogaster (DmTrxR), each catalytically active unit consists of three redox centers: FAD and an N-terminal Cys-57-Cys-62 redox-active disulfide from one monomer and a Cys-489"-Cys-490" C-terminal redox-active disulfide from the second monomer.	Disulfides	46-55	Thioredoxin reductase-1	Drosophila melanogaster	79-83
19022905-3	2008	Metal-free apo-SOD1 is a relatively stable protein and has been shown to form amyloid fibers in vitro only when it has been subjected to severely destabilizing conditions, such as low pH or reduction of its disulfide bonds.	Disulfides	207-216	superoxide dismutase 1, soluble	Mus musculus	15-19
19022905-4	2008	Here, by contrast, we show that a small amount of disulfide-reduced apo-SOD1 can rapidly initiate fibrillation of this exceptionally stable and highly structured protein under mild, physiologically accessible conditions, thus providing an unusual demonstration of a specific, physiologically relevant form of a protein acting as an initiating agent for the fibrillation of another form of the same protein.	Disulfides	50-59	superoxide dismutase 1, soluble	Mus musculus	72-76
19022905-5	2008	We also show that, once initiated, elongation can proceed via recruitment of either apo- or partially metallated disulfide-intact SOD1 and that the presence of copper, but not zinc, ions inhibits fibrillation.	Disulfides	113-122	superoxide dismutase 1, soluble	Mus musculus	130-134
19061645-6	2008	The binary complex structure and results of engineered disulfide linkage experiments reveal that the plug and motif B loop, which block the access of template DNA to the active site in the apo-form mini-vRNAP, undergo a large-scale conformational change upon promoter binding, explaining the restricted promoter specificity that is critical for N4 phage early transcription.	Disulfides	55-64	virion RNA polymerase	Escherichia phage N4	203-208
18991392-3	2008	Like other members of the pyridine nucleotide-disulfide oxidoreductase family, TrxR is a homodimer; in the enzyme from D. melanogaster (DmTrxR), each catalytically active unit consists of three redox centers: FAD and an N-terminal Cys-57-Cys-62 redox-active disulfide from one monomer and a Cys-489"-Cys-490" C-terminal redox-active disulfide from the second monomer.	Disulfides	258-267	Thioredoxin reductase-1	Drosophila melanogaster	79-83
19018669-8	2008	This shows that the Cys228-Cys239 disulfide bond of gp120 is required for high-affinity binding to CD4.	Disulfides	34-43	CD4 molecule	Homo sapiens	99-102
18991392-4	2008	A dyad of His-464" and Glu-469" in TrxR acts as the acid-base catalyst of the dithiol-disulfide interchange reactions required in catalysis [Huang, H.-H., et al.	Disulfides	86-95	Thioredoxin reductase-1	Drosophila melanogaster	35-39
18937031-3	2008	In addition, we successfully expressed bovine pancreatic trypsin inhibitor (BPTI), which contains three pairs of disulfide bonds, as the soluble form.	Disulfides	113-122	trophoblast Kunitz domain protein 1	Bos taurus	57-74
18783346-11	2008	CTRP3, CTRP5, CTRP6 and CTRP10 trimers are further assembled into higher-order oligomeric complexes via disulfide bonding mediated by their N-terminal cysteine residues.	Disulfides	104-113	complement component 1, q subcomponent-like 2	Mus musculus	24-30
19020013-10	2008	Through molecular modeling and site-directed mutagenesis, we predict that Cys 31 disrupts the disulfide bond between Cys 744 and Cys 798 on the NR1 subunit of the NMDA receptor by directly interacting with Cys 744 leading to a free thiol group on Cys 798 and subsequent persistent activation of the NMDA receptor.	Disulfides	94-103	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	144-147
18817872-5	2008	The levels of disulfide-reduced SOD1 peaked at the end stage of the disease, whereas protein disulfide isomerase (PDI), a chaperone capable of rearranging disulfide bonds between cysteine residues of SOD1, was increased prior to the end stage.	Disulfides	14-23	superoxide dismutase 1	Rattus norvegicus	32-36
18817872-5	2008	The levels of disulfide-reduced SOD1 peaked at the end stage of the disease, whereas protein disulfide isomerase (PDI), a chaperone capable of rearranging disulfide bonds between cysteine residues of SOD1, was increased prior to the end stage.	Disulfides	14-23	superoxide dismutase 1	Rattus norvegicus	200-204
18817872-5	2008	The levels of disulfide-reduced SOD1 peaked at the end stage of the disease, whereas protein disulfide isomerase (PDI), a chaperone capable of rearranging disulfide bonds between cysteine residues of SOD1, was increased prior to the end stage.	Disulfides	93-102	superoxide dismutase 1	Rattus norvegicus	200-204
19011089-0	2008	A disulfide-bond A oxidoreductase-like protein (DsbA-L) regulates adiponectin multimerization.	Disulfides	2-11	adiponectin, C1Q and collagen domain containing	Homo sapiens	66-77
19036713-4	2008	A recent report now proposes that DYNLL/LC8-driven interactions are also regulated by changes in cellular redox state, which lead to intermonomer disulfide bond formation and ultimately activation of the transcription factor NF-kappaB.	Disulfides	146-155	dynein light chain LC8-type 1	Homo sapiens	40-43
19036713-4	2008	A recent report now proposes that DYNLL/LC8-driven interactions are also regulated by changes in cellular redox state, which lead to intermonomer disulfide bond formation and ultimately activation of the transcription factor NF-kappaB.	Disulfides	146-155	nuclear factor kappa B subunit 1	Homo sapiens	225-234
18795288-2	2008	High expression of active single-chain antibody fragment (scFv) in Escherichia coli has not been successful, as the protein contains three intramolecular disulfide bonds that are difficult to form correctly in the bacterial intracellular environment.	Disulfides	154-163	immunglobulin heavy chain variable region	Homo sapiens	58-62
18692070-1	2008	The disulfide bond between Cys14 and Cys38 of bovine pancreatic trypsin inhibitor lies on the surface of the inhibitor and forms part of the protease-binding region.	Disulfides	4-13	trophoblast Kunitz domain protein 1	Bos taurus	64-81
18703498-8	2008	Fourth, all of the cysteine residues in human SOD1 are critical for its retention in mitochondria due to their involvement in intramolecular disulfide bonds and in the interaction with CCS.	Disulfides	141-150	superoxide dismutase 1	Homo sapiens	46-50
18712897-2	2008	This study demonstrated that copper induced the disulfide-linkage between Tus, such as alpha-naphthylthiourea (ANTU) and fluorescein-5-isothiocyanate cadaverine (FTC), with albumin (Alb), a major carrier protein in plasma with multiple functions.	Disulfides	48-57	albumin	Homo sapiens	173-180
18729328-11	2008	Under somewhat more oxidizing, but still physiologically relevant, conditions, GSH/GSSG = 1 ( E h = -231.1 mV), a Cys319-Cys319 disulfide is detected far from the dimerization domain of the Keap1 homodimer.	Disulfides	128-137	kelch like ECH associated protein 1	Homo sapiens	190-195
18846282-6	2008	We confirmed the thioredoxin-dependent reduction of a disulfide bond in CHLI2 and thiol-modulation of its ATPase activity.	Disulfides	54-63	magnesium chelatase i2	Arabidopsis thaliana	72-77
18722437-1	2008	In the presence of a catalytic amount of RhH(PPh3)4 and 1,2-bis(diphenylphosphino)benzene, an aromatic fluoride, an organic disulfide (0.5 equiv), and triphenylphosphine (0.5 equiv) reacted in refluxing chlorobenzene to give an aryl sulfide in high yield.	Disulfides	124-133	caveolin 1	Homo sapiens	45-49
18628206-6	2008	The observations that the redox potential of ERp16 (-165 mV) was within the range of that of the ER (-135 to -185 mV) and that ERp16 catalyzed disulfide isomerization of scrambled ribonuclease A suggest a role for ERp16 in protein disulfide isomerization in the ER.	Disulfides	143-152	thioredoxin domain containing 12	Homo sapiens	127-132
18628206-6	2008	The observations that the redox potential of ERp16 (-165 mV) was within the range of that of the ER (-135 to -185 mV) and that ERp16 catalyzed disulfide isomerization of scrambled ribonuclease A suggest a role for ERp16 in protein disulfide isomerization in the ER.	Disulfides	143-152	thioredoxin domain containing 12	Homo sapiens	127-132
18628206-6	2008	The observations that the redox potential of ERp16 (-165 mV) was within the range of that of the ER (-135 to -185 mV) and that ERp16 catalyzed disulfide isomerization of scrambled ribonuclease A suggest a role for ERp16 in protein disulfide isomerization in the ER.	Disulfides	231-240	thioredoxin domain containing 12	Homo sapiens	45-50
18628206-6	2008	The observations that the redox potential of ERp16 (-165 mV) was within the range of that of the ER (-135 to -185 mV) and that ERp16 catalyzed disulfide isomerization of scrambled ribonuclease A suggest a role for ERp16 in protein disulfide isomerization in the ER.	Disulfides	231-240	thioredoxin domain containing 12	Homo sapiens	127-132
18628206-6	2008	The observations that the redox potential of ERp16 (-165 mV) was within the range of that of the ER (-135 to -185 mV) and that ERp16 catalyzed disulfide isomerization of scrambled ribonuclease A suggest a role for ERp16 in protein disulfide isomerization in the ER.	Disulfides	231-240	thioredoxin domain containing 12	Homo sapiens	127-132
18628206-9	2008	Our results suggest that ERp16 mediates disulfide bond formation in the ER and plays an important role in cellular defense against prolonged ER stress.	Disulfides	40-49	thioredoxin domain containing 12	Homo sapiens	25-30
18729328-0	2008	Prospective type 1 and type 2 disulfides of Keap1 protein.	Disulfides	30-40	kelch like ECH associated protein 1	Homo sapiens	44-49
18634816-4	2008	When rats were treated with galactosamine/lipopolysaccharide (GalN/LPS), mtMGST1 activity was significantly increased, and the increased activity was reduced by the disulfide reducing agent dithiothreitol.	Disulfides	165-174	galanin and GMAP prepropeptide	Rattus norvegicus	62-66
18634816-5	2008	In mitochondria from GalN/LPS-treated rats, disulfide-linked mtMGST1 dimer and mixed protein glutathione disulfides (glutathionylation) were detected.	Disulfides	44-53	galanin and GMAP prepropeptide	Rattus norvegicus	21-25
18804034-5	2008	These agents used in part a thiol-dependent mechanism to inhibit TGM2, consistent with the activation of TGM2 by reduction of an intramolecular disulfide bond.	Disulfides	144-153	transglutaminase 2	Homo sapiens	105-109
18710266-6	2008	The degree of cross-linking between lysozyme molecules was controlled by manipulating both the extent of chemical reduction of the intramolecular disulfide bonds and sonication time.	Disulfides	146-155	lysozyme	Homo sapiens	36-44
18779421-9	2008	The novel identified N352S mutation is predicted to increase TDP-43 phosphorylation, while the G348C mutation might interfere with normal TDP-43 function by forming intermolecular disulfide bridges.	Disulfides	180-189	TAR DNA binding protein	Homo sapiens	138-144
18712897-2	2008	This study demonstrated that copper induced the disulfide-linkage between Tus, such as alpha-naphthylthiourea (ANTU) and fluorescein-5-isothiocyanate cadaverine (FTC), with albumin (Alb), a major carrier protein in plasma with multiple functions.	Disulfides	48-57	albumin	Homo sapiens	182-185
18713008-3	2008	The peptides of the cleaved SLPI (cSLPI) remain coupled due to the disulfide bonds in the molecule but under reducing conditions the cleavage can be observed as peptide products.	Disulfides	67-76	secretory leukocyte peptidase inhibitor	Homo sapiens	28-32
18627133-7	2008	By synthesizing a panel of variants to Defb14 (the murine orthologue of HBD3), we exploit ion mobility to distinguish conformational differences which arise due to disulfide formation and to the hydrophobicity of the peptide sequence.	Disulfides	164-173	defensin beta 14	Mus musculus	39-45
18803177-2	2008	The method includes reduction of CASH disulfides to thiol with tri-n-butylphosphine, derivatization of the thiol with 2-chloro-1-methylquinolinium tetrafluoroborate, separation of CASH 2-S-quinolinium derivate from those of plasma endo- and exogenous thiol derivatives by capillary zone electrophoresis based on acetonitrile stacking and quantitation with the use of ultraviolet detection.	Disulfides	38-48	CASP8 and FADD like apoptosis regulator	Homo sapiens	33-37
18579519-5	2008	TNFalpha induced the production of reactive oxygen species, which oxidized LC8 to a homodimer linked by the reversible formation of a disulfide bond between the Cys(2) residues of each subunit and thereby resulted in its dissociation from IkappaBalpha.	Disulfides	134-143	tumor necrosis factor	Homo sapiens	0-8
18579519-5	2008	TNFalpha induced the production of reactive oxygen species, which oxidized LC8 to a homodimer linked by the reversible formation of a disulfide bond between the Cys(2) residues of each subunit and thereby resulted in its dissociation from IkappaBalpha.	Disulfides	134-143	dynein light chain LC8-type 1	Homo sapiens	75-78
18552350-3	2008	SOD1 becomes stabilized and enzymatically active after copper and zinc binding and intramolecular disulfide formation, but it remains unknown which step(s) in the SOD1 maturation process is important in the pathological aggregation.	Disulfides	98-107	superoxide dismutase 1	Homo sapiens	0-4
18552350-5	2008	fALS mutations impair either zinc binding, disulfide formation, or both, leading to accumulation of the aggregation-prone, apo, and disulfide-reduced SOD1.	Disulfides	43-52	superoxide dismutase 1	Homo sapiens	150-154
18552350-5	2008	fALS mutations impair either zinc binding, disulfide formation, or both, leading to accumulation of the aggregation-prone, apo, and disulfide-reduced SOD1.	Disulfides	132-141	superoxide dismutase 1	Homo sapiens	150-154
18515409-5	2008	Chemical cross-linking of DSG to HSA via a disulfide-based cross-linker and its administration to cells carrying DeltaF508-CFTR resulted in a greater enhancement of DeltaF508-CFTR function than when free DSG was used.	Disulfides	43-52	CF transmembrane conductance regulator	Homo sapiens	175-179
18635760-3	2008	NPR1 is sequestered in the cytoplasm as an oligomer through intermolecular disulfide bonds.	Disulfides	75-84	natriuretic peptide receptor 1	Homo sapiens	0-4
18642256-0	2008	Hydrophobic interactions as substitutes for a conserved disulfide linkage in the type IIa bacteriocins, leucocin A and pediocin PA-1.	Disulfides	56-65	PAXIP1 associated glutamate rich protein 1	Homo sapiens	128-132
18669652-4	2008	We explored the contacts between alpha and beta1 by determining the extent of endogenous disulfide bond formation between cysteines substituted just extracellular to the two beta1 transmembrane (TM) helices, TM1 and TM2, and to the seven alpha TM helices, consisting of S1-S6, conserved in all voltage-dependent potassium channels, and the unique S0 helix, which we previously concluded was partly surrounded by S1-S4.	Disulfides	89-98	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	174-179
18646836-7	2008	Soluble inhibitor blocked the binding of CETP to the immobilized drug, as did preincubation with a disulfide-containing covalent inhibitor.	Disulfides	99-108	cholesteryl ester transfer protein	Homo sapiens	41-45
18646836-8	2008	To provide a first estimate of the binding site for torcetrapib-like inhibitors, CETP was modified with a disulfide-containing agent that modifies Cys-13 of CETP.	Disulfides	106-115	cholesteryl ester transfer protein	Homo sapiens	81-85
18646836-8	2008	To provide a first estimate of the binding site for torcetrapib-like inhibitors, CETP was modified with a disulfide-containing agent that modifies Cys-13 of CETP.	Disulfides	106-115	cholesteryl ester transfer protein	Homo sapiens	157-161
18646836-9	2008	Mass spectrometry of the modified protein indicated that a single half-molecule of the disulfide was covalently bound to CETP, and peptide mapping after digestion with pepsin confirmed previous reports based on mutagenesis that Cys-13 was the site of modification.	Disulfides	87-96	cholesteryl ester transfer protein	Homo sapiens	121-125
18650385-1	2008	ERp57 is an oxidoreductase that, in conjunction with calnexin and calreticulin, assists disulfide bond formation in folding glycoproteins.	Disulfides	88-97	protein disulfide isomerase family A member 3	Homo sapiens	0-5
18450751-6	2008	Interestingly, whereas the NR2 KN disulfide was found to potentiate channel gating and M3 accessibility, NR1 EI exhibited the opposite phenotype, suggesting that the EI disulfide may trap the NR1 ligand-binding domain in a lower efficacy conformation.	Disulfides	169-178	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	105-108
18450751-6	2008	Interestingly, whereas the NR2 KN disulfide was found to potentiate channel gating and M3 accessibility, NR1 EI exhibited the opposite phenotype, suggesting that the EI disulfide may trap the NR1 ligand-binding domain in a lower efficacy conformation.	Disulfides	169-178	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	192-195
18616463-1	2008	The cathelicidin antimicrobial peptide bactenecin is a beta-hairpin molecule with a single disulfide bond and broad antimicrobial activity.	Disulfides	91-100	cathelicidin antimicrobial peptide	Homo sapiens	4-38
18550799-0	2008	The torsin-family AAA+ protein OOC-5 contains a critical disulfide adjacent to Sensor-II that couples redox state to nucleotide binding.	Disulfides	57-66	Torsin-like protein	Caenorhabditis elegans	31-36
18550799-4	2008	In vitro experiments with OOC-5, a torsinA homolog from Caenorhabditis elegans, demonstrate that redox changes that reduce this disulfide bond affect the binding of ATP and ADP and cause an attendant local conformational change detected by limited proteolysis.	Disulfides	128-137	Torsin-like protein	Caenorhabditis elegans	26-31
18550799-5	2008	Transgenic worms expressing an ooc-5 gene with cysteine-to-serine mutations that disrupt the disulfide bond have a very low embryo hatch rate compared with wild-type controls, indicating these two cysteines are essential for OOC-5 function.	Disulfides	93-102	Torsin-like protein	Caenorhabditis elegans	31-36
18650385-1	2008	ERp57 is an oxidoreductase that, in conjunction with calnexin and calreticulin, assists disulfide bond formation in folding glycoproteins.	Disulfides	88-97	calreticulin	Homo sapiens	66-78
18650385-2	2008	ERp57 also forms a mixed disulfide with the MHC class I-specific chaperone tapasin, and this dimeric conjugate edits the peptide repertoire bound by MHC class I molecules.	Disulfides	25-34	protein disulfide isomerase family A member 3	Homo sapiens	0-5
20641767-3	2004	In addition, insulin from these mammals is known to have an invariant location of three disulfide bonds (6).	Disulfides	88-97	insulin	Homo sapiens	13-20
18511416-9	2008	Complexes with PQ or with PRiMA contained heavy components, which migrated abnormally in SDS-PAGE but probably resulted from disulfide bonding of four AChE(T) subunits with the four upstream cysteines of the associated protein.	Disulfides	125-134	acetylcholinesterase (Cartwright blood group)	Homo sapiens	151-155
18657506-4	2008	ROS-generating compounds, e.g., the environmental toxins menadione and beta-lapachone (in vivo IC(50) = 0.45 muM) also cause intermolecular disulfide crosslinking of SMN.	Disulfides	140-149	latexin	Homo sapiens	109-112
18576448-5	2008	A combination of solid-phase peptide synthesis methods together with regioselective disulfide bond formation were used to obtain INSL5.	Disulfides	84-93	insulin like 5	Homo sapiens	129-134
18576448-8	2008	Following sequential disulfide bond formation and chain combination, the resulting synthetic INSL5, which was obtained in good overall yield, was shown to possess a similar secondary structure to human relaxin-3 (H3 relaxin).	Disulfides	21-30	insulin like 5	Homo sapiens	93-98
18653895-4	2008	Here, we found that an ER-resident protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins, and accelerated ERAD through its physical and functional associations with EDEM (ER degradation-enhancing alpha-mannosidase-like protein) and an ER-resident chaperone BiP.	Disulfides	87-96	ER degradation enhancing alpha-mannosidase like protein 1	Homo sapiens	201-205
18653895-4	2008	Here, we found that an ER-resident protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins, and accelerated ERAD through its physical and functional associations with EDEM (ER degradation-enhancing alpha-mannosidase-like protein) and an ER-resident chaperone BiP.	Disulfides	87-96	ER degradation enhancing alpha-mannosidase like protein 1	Homo sapiens	207-262
18445468-5	2008	The described refolding strategy can be used to prepare other Co(II)-substituted Zn(II)-metalloenzymes, particularly those that contain a solvent-exposable disulfide, which often causes oxidation of Co(II) to Co(III).	Disulfides	156-165	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	62-68
18445468-5	2008	The described refolding strategy can be used to prepare other Co(II)-substituted Zn(II)-metalloenzymes, particularly those that contain a solvent-exposable disulfide, which often causes oxidation of Co(II) to Co(III).	Disulfides	156-165	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	199-205
18445468-5	2008	The described refolding strategy can be used to prepare other Co(II)-substituted Zn(II)-metalloenzymes, particularly those that contain a solvent-exposable disulfide, which often causes oxidation of Co(II) to Co(III).	Disulfides	156-165	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	209-216
18337307-1	2008	The CCS copper chaperone is critical for maturation of Cu, Zn-superoxide dismutase (SOD1) through insertion of the copper co-factor and oxidization of an intra-subunit disulfide.	Disulfides	168-177	superoxide dismutase 1, soluble	Mus musculus	84-88
18448186-1	2008	Human interferon-alpha (IFN-alpha), a 19.2 KD protein containing two disulfide bonds (cys1-cys98; cys29-cys138), was reduced and modified with a reversible lipidization agent.	Disulfides	69-78	interferon alpha 1	Homo sapiens	24-33
18448186-2	2008	The product of the lipidization, PAL-IFN, was homogenous, with four palmitoyl moieties linked to the four Cys residues in the protein molecule via reversible disulfide linkages.	Disulfides	158-167	interferon alpha 1	Homo sapiens	37-40
18448186-5	2008	Evidence suggested that IFN was slowly released from PAL-IFN into blood circulation upon reduction of the disulfide bonds in vivo.	Disulfides	106-115	interferon alpha 1	Homo sapiens	24-27
18448186-5	2008	Evidence suggested that IFN was slowly released from PAL-IFN into blood circulation upon reduction of the disulfide bonds in vivo.	Disulfides	106-115	interferon alpha 1	Homo sapiens	57-60
18430864-0	2008	Effect of cysteine mutagenesis on the function and disulfide bond formation of human ABCG2.	Disulfides	51-60	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	85-90
18430864-3	2008	Based on its apparent half size in sequence when compared with other traditional ABC transporters, ABCG2 has been thought to exist and function as a homodimer linked by intermolecular disulfide bonds.	Disulfides	184-193	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	99-104
18430864-7	2008	Mapping of the cysteine residues showed that three cysteine residues (Cys284, Cys374, and Cys438) are required concurrently for the function of ABCG2 and potentially for intramolecular disulfide bond formation.	Disulfides	185-194	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	144-149
18430864-9	2008	Thus, we conclude that Cys284, Cys374, and Cys438, which may be involved in intramolecular disulfide bond formation, are concurrently required for ABCG2 function, whereas Cys592, Cys603, and Cys608, potentially involved in intermolecular disulfide bond formation, are not required.	Disulfides	91-100	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	147-152
18430864-9	2008	Thus, we conclude that Cys284, Cys374, and Cys438, which may be involved in intramolecular disulfide bond formation, are concurrently required for ABCG2 function, whereas Cys592, Cys603, and Cys608, potentially involved in intermolecular disulfide bond formation, are not required.	Disulfides	238-247	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	147-152
18668433-4	2008	This review paper will address the new aspects of ABCG2 in terms of post-translational modifications (i.e., disulfide bond formation, ubiquitination, and endoplasmic reticulum-associated degradation) of ABCG2 protein, high-speed screening, and quantitative structure-activity relationship (QSAR) analysis to evaluate ABCG2-drug interactions, and genetic polymorphisms potentially associated with photosensitivity.	Disulfides	108-117	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	50-55
18668433-4	2008	This review paper will address the new aspects of ABCG2 in terms of post-translational modifications (i.e., disulfide bond formation, ubiquitination, and endoplasmic reticulum-associated degradation) of ABCG2 protein, high-speed screening, and quantitative structure-activity relationship (QSAR) analysis to evaluate ABCG2-drug interactions, and genetic polymorphisms potentially associated with photosensitivity.	Disulfides	108-117	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	203-208
18668433-4	2008	This review paper will address the new aspects of ABCG2 in terms of post-translational modifications (i.e., disulfide bond formation, ubiquitination, and endoplasmic reticulum-associated degradation) of ABCG2 protein, high-speed screening, and quantitative structure-activity relationship (QSAR) analysis to evaluate ABCG2-drug interactions, and genetic polymorphisms potentially associated with photosensitivity.	Disulfides	108-117	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	203-208
18468997-4	2008	To obtain a better understanding of the structure and function of the Cys-box-containing subfamily, we identified the disulfide bonds in Gas2p from Saccharomyces cerevisiae by an improved mass spectrometric methodology.	Disulfides	118-127	1,3-beta-glucanosyltransferase	Saccharomyces cerevisiae S288C	137-142
18502910-7	2008	Hydrogen peroxide induced an array of changes in the myocardium, including formation of disulfide bonds that were intermolecular for Prdx1, Prdx2, and Prdx3 but intramolecular within Prdx5.	Disulfides	88-97	peroxiredoxin 5	Rattus norvegicus	183-188
18502910-8	2008	For Prdx1, Prdx2, and Prdx5, disulfide bond formation can be approximated to an EC(50) of 10-100, 1-10, and 100-1,000 microM peroxide, respectively.	Disulfides	29-38	peroxiredoxin 5	Rattus norvegicus	22-27
18549960-3	2008	The Tribolium receptor for the AVPL, the first such receptor identified in any insect, was expressed in a reporter system, and showed a strong response (EC(50)=1.5 nM) to AVPL F1, the monomeric form having an intramolecular disulfide bond.	Disulfides	224-233	oxytocin/vasopressin-like peptide	Tribolium castaneum	31-35
18549960-3	2008	The Tribolium receptor for the AVPL, the first such receptor identified in any insect, was expressed in a reporter system, and showed a strong response (EC(50)=1.5 nM) to AVPL F1, the monomeric form having an intramolecular disulfide bond.	Disulfides	224-233	oxytocin/vasopressin-like peptide	Tribolium castaneum	171-175
18631007-6	2008	In vitro and in vivo analysis indicated ligand-independent activation of the Ret-Cys515Ser mutant due to aberrant disulfide homodimerization, increased mitogenic activity, and ability to induce anchorage-independent growth in NIH-3T3 cells in comparison to wild-type Ret, suggesting a possible role of Cys515Ser in tumor development.	Disulfides	114-123	ret proto-oncogene	Mus musculus	77-80
18424440-3	2008	We previously characterized an engineered variant of factor VIII which contains a disulfide bond between the A2 and the A3 subunits that prevents the spontaneous dissociation of the A2 subunit following thrombin activation.	Disulfides	82-91	coagulation factor II, thrombin	Homo sapiens	203-211
18337307-2	2008	The disulfide helps stabilize the SOD1 polypeptide, which can be particularly important in cases of amyotrophic lateral sclerosis (ALS) linked to misfolding of mutant SOD1.	Disulfides	4-13	superoxide dismutase 1, soluble	Mus musculus	34-38
18337307-2	2008	The disulfide helps stabilize the SOD1 polypeptide, which can be particularly important in cases of amyotrophic lateral sclerosis (ALS) linked to misfolding of mutant SOD1.	Disulfides	4-13	superoxide dismutase 1, soluble	Mus musculus	167-171
18337307-4	2008	Herein we show that disease in these G93A/CCS mice correlates with incomplete oxidation of the SOD1 disulfide.	Disulfides	100-109	superoxide dismutase 1, soluble	Mus musculus	95-99
18337307-5	2008	In the brain and spinal cord, CCS over-expression failed to enhance oxidation of the G93A SOD1 disulfide and if anything, effected some accumulation of disulfide-reduced SOD1.	Disulfides	152-161	superoxide dismutase 1, soluble	Mus musculus	170-174
18459800-0	2008	Mapping peptide hormone-receptor interactions using a disulfide-trapping approach.	Disulfides	54-63	nuclear receptor subfamily 4 group A member 1	Homo sapiens	16-32
18378676-6	2008	These findings support the notion that metal-deficient and/or disulfide-reduced mutant SOD1 species contribute to toxicity in SOD1-linked amyotrophic lateral sclerosis.	Disulfides	62-71	superoxide dismutase 1, soluble	Mus musculus	87-91
18459800-6	2008	Since the geometry governing disulfide bond formation is more constrained than Bpa cross-linking, this novel approach can be employed to generate a more refined molecular model of the PTH-PTHR1 complex.	Disulfides	29-38	parathyroid hormone 1 receptor	Homo sapiens	188-193
18465877-4	2008	At 37 degrees C in the absence of extracellular Na (+), copper phenanthroline catalyzes disulfide bond formation between cysteines at position 122 in adjacent NCX1 proteins.	Disulfides	88-97	solute carrier family 8 member A1	Homo sapiens	159-163
18459800-9	2008	The new sites identified by the disulfide-trapping procedure were used as constraints in molecular dynamics simulations to generate an updated model of the PTH-PTHR1 complex.	Disulfides	32-41	parathyroid hormone 1 receptor	Homo sapiens	160-165
18537677-4	2008	Unlike previously described protein structures with SH3 domain folds, MIA is a secreted single-domain protein of 12 kDa that contains an additional antiparallel beta-sheet and two disulfide bonds.	Disulfides	180-189	MIA SH3 domain containing	Homo sapiens	70-73
18533692-3	2008	Using the phage surface display technique, we previously identified a disulfide-bond-constrained peptide (-CHKKPSKSC-, STB1) cognitive of TiO2.	Disulfides	70-79	VANGL planar cell polarity protein 2	Homo sapiens	119-123
18385137-2	2008	Two different folding variants of EC-SOD exist based on the disulfide bridge connectivity, resulting in enzymatically active (aEC-SOD) and inactive (iEC-SOD) subunits.	Disulfides	60-69	superoxide dismutase 3	Homo sapiens	34-40
18385137-2	2008	Two different folding variants of EC-SOD exist based on the disulfide bridge connectivity, resulting in enzymatically active (aEC-SOD) and inactive (iEC-SOD) subunits.	Disulfides	60-69	superoxide dismutase 1	Homo sapiens	37-40
18385137-2	2008	Two different folding variants of EC-SOD exist based on the disulfide bridge connectivity, resulting in enzymatically active (aEC-SOD) and inactive (iEC-SOD) subunits.	Disulfides	60-69	superoxide dismutase 1	Homo sapiens	130-133
18385137-9	2008	This study shows that generation of the EC-SOD folding variants is an intracellular event that depends on a free cysteine residue not involved in disulfide bonding.	Disulfides	146-155	superoxide dismutase 3	Homo sapiens	40-46
18458339-4	2008	We show here that Cu(I)HCox17(2S-S), i.e., the copper-loaded form of the protein, can transfer simultaneously copper(I) and two electrons to the human cochaperone Sco1 (HSco1) in the oxidized state, i.e., with its metal-binding cysteines forming a disulfide bond.	Disulfides	248-257	synthesis of cytochrome C oxidase 1	Homo sapiens	163-167
18316367-0	2008	A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis.	Disulfides	19-28	superoxide dismutase 1	Homo sapiens	72-76
18316367-1	2008	One of the mechanisms by which mutations in superoxide dismutase 1 (SOD1) cause familial amyotrophic lateral sclerosis (fALS) is proposed to involve the accumulation of detergent-insoluble, disulfide-cross-linked, mutant protein.	Disulfides	190-199	superoxide dismutase 1	Homo sapiens	44-66
18316367-1	2008	One of the mechanisms by which mutations in superoxide dismutase 1 (SOD1) cause familial amyotrophic lateral sclerosis (fALS) is proposed to involve the accumulation of detergent-insoluble, disulfide-cross-linked, mutant protein.	Disulfides	190-199	superoxide dismutase 1	Homo sapiens	68-72
18316367-3	2008	In the present study, we used a panel of experimental and disease-linked mutations at cysteine residues of SOD1 (positions 6, 57, 111, and 146) in cell culture assays for aggregation to demonstrate that extensive disulfide cross-linking is not required for the formation of mutant SOD1 aggregates.	Disulfides	213-222	superoxide dismutase 1	Homo sapiens	107-111
18316367-5	2008	Furthermore we demonstrate that aggregate structures in symptomatic SOD1-G93A mice can be dissociated such that they no longer sediment upon ultracentrifugation (i.e. appear soluble) under relatively mild conditions that leave disulfide bonds intact.	Disulfides	227-236	superoxide dismutase 1, soluble	Mus musculus	68-72
18211964-1	2008	RNase A (bovine pancreatic RNase) is the founding member an extensive family of divergent proteins that share specific elements of sequence homology, a unique disulfide-bonded tertiary structure, and the ability to hydrolyze polymeric RNA.	Disulfides	159-168	ribonuclease pancreatic	Bos taurus	0-7
17926344-0	2008	Disulfide linkage patterns of pig zona pellucida glycoproteins ZP3 and ZP4.	Disulfides	0-9	zona pellucida glycoprotein 4	Sus scrofa	71-74
17926344-3	2008	In this study, we analyzed the disulfide linkages of pig ZP3 and ZP4 purified from ovaries.	Disulfides	31-40	zona pellucida glycoprotein 4	Sus scrofa	65-68
18179776-6	2008	To recycle Erv1 into its oxidized form, electrons are transferred to cytochrome c connecting the disulfide relay system to the electron transport chain of mitochondria.	Disulfides	97-106	cytochrome c, somatic	Homo sapiens	69-81
18262489-5	2008	Thiol modification experiments indicate that a disulfide bond is formed between two of the three zinc-binding ligands when BHMT is inactive in a reducing agent-free buffer, and that this disulfide can be readily reduced with the concomitant restoration of activity by re-establishing reducing conditions.	Disulfides	47-56	betaine-homocysteine methyltransferase	Mus musculus	123-127
18262489-5	2008	Thiol modification experiments indicate that a disulfide bond is formed between two of the three zinc-binding ligands when BHMT is inactive in a reducing agent-free buffer, and that this disulfide can be readily reduced with the concomitant restoration of activity by re-establishing reducing conditions.	Disulfides	187-196	betaine-homocysteine methyltransferase	Mus musculus	123-127
18258686-7	2008	PTH enhanced formation of disulfide bonds in the K240C/F447C and A242C/F447C mutants.	Disulfides	26-35	parathyroid hormone	Homo sapiens	0-3
18258686-8	2008	For the F238C/F447C mutant, a disulfide bond is formed in the basal state, but is disrupted by interaction with PTH.	Disulfides	30-39	parathyroid hormone	Homo sapiens	112-115
18546891-3	2008	Using LC-ESITOFMS and FTMS analysis, we determined that the major structural change in oxidized HSA in healthy human plasma is a disulfide-bonded cysteine at the thiol of Cys34 of reduced HSA.	Disulfides	129-138	albumin	Homo sapiens	96-99
18546891-3	2008	Using LC-ESITOFMS and FTMS analysis, we determined that the major structural change in oxidized HSA in healthy human plasma is a disulfide-bonded cysteine at the thiol of Cys34 of reduced HSA.	Disulfides	129-138	albumin	Homo sapiens	188-191
18358490-5	2008	Z(A beta 3) is a dimer of affibody subunits linked via a disulfide bridge involving a selected cysteine mutation at position 28.	Disulfides	57-66	amyloid beta precursor protein	Homo sapiens	2-8
18223257-0	2008	Structural characterization of PTX3 disulfide bond network and its multimeric status in cumulus matrix organization.	Disulfides	36-45	pentraxin related gene	Mus musculus	31-35
18223257-2	2008	PTX3 exerts its functions by interacting with a number of structurally unrelated molecules, a capacity that is likely to rely on its complex multimeric structure stabilized by interchain disulfide bonds.	Disulfides	187-196	pentraxin related gene	Mus musculus	0-4
18223257-6	2008	Additional interchain disulfide bonds formed by the C-terminal domain cysteines Cys(317) and Cys(318) are responsible for linking the PTX3 tetramers into octamers.	Disulfides	22-31	pentraxin related gene	Mus musculus	134-138
18331357-1	2008	Eppin has two potential protease inhibitory domains: a whey acid protein or four disulfide core domain and a Kunitz domain.	Disulfides	81-90	epididymal peptidase inhibitor	Homo sapiens	0-5
18322014-0	2008	Txnip balances metabolic and growth signaling via PTEN disulfide reduction.	Disulfides	55-64	thioredoxin interacting protein	Mus musculus	0-5
18258262-8	2008	The cross-linking of the N-terminal region of recombinant yeast cofilin to actin residues 346 and 374 with dithio-bis-maleimidoethane (12.4 A) and via disulfide bond formation was also documented.	Disulfides	151-160	actin	Saccharomyces cerevisiae S288C	75-80
18178549-3	2008	Here we show that ERp44 interacts with FGE forming heterodimeric and, to a lesser extent, also heterotetrameric and octameric complexes, which are stabilized through disulfide bonding between cysteine 29 of ERp44 and cysteines 50 and 52 in the N-terminal region of FGE.	Disulfides	166-175	endoplasmic reticulum protein 44	Homo sapiens	18-23
18178549-3	2008	Here we show that ERp44 interacts with FGE forming heterodimeric and, to a lesser extent, also heterotetrameric and octameric complexes, which are stabilized through disulfide bonding between cysteine 29 of ERp44 and cysteines 50 and 52 in the N-terminal region of FGE.	Disulfides	166-175	endoplasmic reticulum protein 44	Homo sapiens	207-212
18212083-3	2008	Many secreted proteins require addition of disulfide bonds by the DsbA disulfide oxidoreductase for activity or stability.	Disulfides	43-52	thiol:disulfide interchange protein DsbA/DsbL	Haemophilus influenzae Rd KW20	66-70
18212083-8	2008	The presence of a dsbA-dependent disulfide bond in HbpA was verified by an alkylation protection assay, and HbpA was less abundant in a dsbA mutant.	Disulfides	33-42	thiol:disulfide interchange protein DsbA/DsbL	Haemophilus influenzae Rd KW20	18-22
18245105-7	2008	This indicates that the lack of a disulfide bond in ONC, analogous to the (65-72) disulfide bond in RNase A which plays an important role in its oxidative regeneration, does not adversely affect the oxidative folding of ONC.	Disulfides	82-91	ribonuclease pancreatic	Bos taurus	100-107
18322014-1	2008	Thioredoxin-interacting protein (Txnip) inhibits thioredoxin NADPH-dependent reduction of protein disulfides.	Disulfides	98-108	thioredoxin interacting protein	Mus musculus	0-31
18322014-1	2008	Thioredoxin-interacting protein (Txnip) inhibits thioredoxin NADPH-dependent reduction of protein disulfides.	Disulfides	98-108	thioredoxin interacting protein	Mus musculus	33-38
18322016-6	2008	Based on our data, we propose a model for thioredoxin f-mediated activation of PRK and GAPDH by two mechanisms: directly through reduction of disulfide bonds within these enzymes and indirectly by mediating the breakdown of the complex in response to changes in light intensity.	Disulfides	142-151	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	87-92
18158302-8	2008	These data indicate that AtRTL2 may use a dimeric mechanism to cleave double-stranded RNA, but unlike bacterial or yeast RNase III proteins, AtRTL2 forms homodimers through formation of disulfide bonds, suggesting that redox conditions may operate to regulate the activity of RNaseIII.	Disulfides	186-195	RNAse THREE-like protein 2	Arabidopsis thaliana	25-31
18274674-9	2008	Mixed disulfide formation contributed to maintaining TF in a state of low functionality.	Disulfides	6-15	coagulation factor III	Mus musculus	53-55
18274674-10	2008	We propose that reduced PDI activates TF by isomerization of a mixed disulfide and a free thiol to an intramolecular disulfide.	Disulfides	69-78	coagulation factor III	Mus musculus	38-40
18274674-10	2008	We propose that reduced PDI activates TF by isomerization of a mixed disulfide and a free thiol to an intramolecular disulfide.	Disulfides	117-126	coagulation factor III	Mus musculus	38-40
18036150-4	2008	We tested whether disulfide bonds could form between A288C in TM3 paired with M227C, Y228C, I229C, or S231C in TM1.	Disulfides	18-27	tropomyosin 3 L homeolog	Xenopus laevis	62-65
18158302-8	2008	These data indicate that AtRTL2 may use a dimeric mechanism to cleave double-stranded RNA, but unlike bacterial or yeast RNase III proteins, AtRTL2 forms homodimers through formation of disulfide bonds, suggesting that redox conditions may operate to regulate the activity of RNaseIII.	Disulfides	186-195	RNAse THREE-like protein 2	Arabidopsis thaliana	141-147
18302793-4	2008	RESULTS: A CB1 receptor model was constructed to include the extracellular loops, particularly extracellular loop 2 which possesses an internal disulfide linkage.	Disulfides	144-153	cannabinoid receptor 1	Homo sapiens	11-14
18195363-8	2008	The disulfide group (oxidized form) is necessary to lower the platelet response to activation by thrombin and collagen.	Disulfides	4-13	coagulation factor II, thrombin	Homo sapiens	97-105
18298375-8	2008	Residue C21 can be involved in the formation of the disulfide bond between the N-terminal domain of GAPDs and fibrous sheath proteins.	Disulfides	52-61	TBL1X/Y related 1	Homo sapiens	8-11
18298375-8	2008	Residue C21 can be involved in the formation of the disulfide bond between the N-terminal domain of GAPDs and fibrous sheath proteins.	Disulfides	52-61	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	100-105
18171083-3	2008	Rds forms a mixture of disulfide-linked homomeric dimers, octamers, and higher-order oligomers, with Cys150 playing a crucial role in its oligomerization.	Disulfides	23-32	peripherin 2	Mus musculus	0-3
18067335-0	2008	Molecular aspects of boundary lubrication by human lubricin: effect of disulfide bonds and enzymatic digestion.	Disulfides	71-80	proteoglycan 4	Homo sapiens	51-59
18067335-4	2008	LUB molecules aggregate in oligomers where the protein extremities are linked by disulfide bonds.	Disulfides	81-90	proteoglycan 4	Homo sapiens	0-3
17964057-2	2008	Elafin and SLPI are structurally related in that both have a fold with a four-disulfide core or whey acidic protein (WAP) domain responsible for inhibiting proteases.	Disulfides	78-87	secretory leukocyte peptidase inhibitor	Homo sapiens	11-15
17692480-8	2008	The IL-2 mutein aggregates are linked by both disulfide and non-disulfide bonds and their relative contribution is temperature-dependent.	Disulfides	46-55	interleukin 2	Homo sapiens	4-8
18039656-2	2008	The formation of a mixed disulfide between the heavy chain of Class I and components of the loading complex (ERp57, protein disulfide isomerase, and tapasin) suggests that these molecules are involved in the redox regulation of components during assembly and peptide loading.	Disulfides	25-34	protein disulfide isomerase family A member 3	Homo sapiens	109-114
18039656-2	2008	The formation of a mixed disulfide between the heavy chain of Class I and components of the loading complex (ERp57, protein disulfide isomerase, and tapasin) suggests that these molecules are involved in the redox regulation of components during assembly and peptide loading.	Disulfides	25-34	TAP binding protein	Homo sapiens	149-156
18039656-3	2008	We demonstrate here that a disulfide formed between heavy chain and tapasin can occur between cysteine residues located in the cytosolic regions of these proteins following translation of heavy chain in an in vitro translation system.	Disulfides	27-36	TAP binding protein	Homo sapiens	68-75
18039656-5	2008	A ternary complex between heavy chain, ERp57, and tapasin was observed and shown to be stabilized by a disulfide between both tapasinheavy chain and tapasin-ERp57.	Disulfides	103-112	protein disulfide isomerase family A member 3	Homo sapiens	39-44
18039656-5	2008	A ternary complex between heavy chain, ERp57, and tapasin was observed and shown to be stabilized by a disulfide between both tapasinheavy chain and tapasin-ERp57.	Disulfides	103-112	TAP binding protein	Homo sapiens	50-57
18039656-5	2008	A ternary complex between heavy chain, ERp57, and tapasin was observed and shown to be stabilized by a disulfide between both tapasinheavy chain and tapasin-ERp57.	Disulfides	103-112	TAP binding protein	Homo sapiens	126-133
18039656-5	2008	A ternary complex between heavy chain, ERp57, and tapasin was observed and shown to be stabilized by a disulfide between both tapasinheavy chain and tapasin-ERp57.	Disulfides	103-112	protein disulfide isomerase family A member 3	Homo sapiens	157-162
18171083-7	2008	Velocity sedimentation under reducing- and nonreducing conditions and co-immunoprecipitation experiments showed the presence of Rds mainly as homo- and hetero-tetramers with Rom-1 in the photoreceptor inner segment (IS), while higher-order, disulfide-linked intermediate complexes and oligomers were exclusively present in the photoreceptor OS.	Disulfides	241-250	peripherin 2	Mus musculus	128-131
17692480-8	2008	The IL-2 mutein aggregates are linked by both disulfide and non-disulfide bonds and their relative contribution is temperature-dependent.	Disulfides	64-73	interleukin 2	Homo sapiens	4-8
18088104-0	2008	Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol.	Disulfides	69-78	S100 calcium binding protein A1	Homo sapiens	47-53
18037437-1	2008	The importance of actin hydrophobic loop 262-274 dynamics to actin polymerization and filament stability has been shown recently with the use of the yeast mutant actin L180C/L269C/C374A, in which the hydrophobic loop could be locked in a "parked" conformation by a disulfide bond between C180 and C269.	Disulfides	265-274	actin	Saccharomyces cerevisiae S288C	18-23
18088104-3	2008	272, 2557-2565) that the chemical modification of Cys 85 residue of S100A1 protein by disulfide bond formation with small thiols such as glutathione, cysteine, or beta-mercaptoethanol (betaME) leads to a dramatic increase of the protein affinity for calcium.	Disulfides	86-95	S100 calcium binding protein A1	Homo sapiens	68-74
18088104-5	2008	Systematic, structural studies of various mixed disulfides of S100A1 in the apo and holo states are necessary to elucidate the mechanism of this phenomenon.	Disulfides	48-58	S100 calcium binding protein A1	Homo sapiens	62-68
18004974-4	2008	The insulin superfamily provides a series of disulfide-containing proteins for the studies of in vitro oxidative folding.	Disulfides	45-54	insulin	Homo sapiens	4-11
18182488-5	2008	The symmetry and location of interdomain contacts suggest that decreasing pH along the secretory pathway coordinates the disulfide-linked assembly of VWF multimers with their tubular packaging.	Disulfides	121-130	von Willebrand factor	Homo sapiens	150-153
18006498-2	2008	MutSOD1 forms high molecular weight oligomers, which disappear under reducing conditions, both in neural tissues of FALS transgenic mice and in transfected cultured cells, indicating a role for aberrant intermolecular disulfide cross-linking in the oligomerization and aggregation process.	Disulfides	218-227	superoxide dismutase 1, soluble	Mus musculus	0-7
18006498-4	2008	Our results suggest that the formation of mutSOD1 aggregates are the consequence of covalent disulfide cross-linking and non-covalent interactions.	Disulfides	93-102	superoxide dismutase 1, soluble	Mus musculus	42-49
18006498-7	2008	Treatments that deplete the cellular pool of GSH exacerbate mutSOD1s insolubility, whereas an overload of intracellular GSH or overexpression of glutaredoxin-1, which specifically catalyzes the reduction of protein-SSG-mixed disulfides, significantly rescues mutSOD1s solubility.	Disulfides	225-235	glutaredoxin	Mus musculus	145-159
18095866-6	2008	Upon oxidation, 1-C-Grx1 forms an intramolecular disulfide bridge and, to a minor degree, covalent dimers.	Disulfides	49-58	dithiol glutaredoxin GRX1	Saccharomyces cerevisiae S288C	20-24
19734126-7	2008	Inclusion of reduced serum albumin as a source of free thiols for the protein disulfide interchange activity catalyzed by ENOX2 failed to result in insulin reduction in the presence of ENOX2.	Disulfides	78-87	ecto-NOX disulfide-thiol exchanger 2	Homo sapiens	122-127
18209575-5	2008	These data suggest that thiol-disulfide exchange permits reduction of disulfide groups in thrombin and fibrinogen, altering their tertiary structure and physiological function.	Disulfides	30-39	coagulation factor II, thrombin	Homo sapiens	90-98
18638502-6	2008	TSR domains of the three trout properdin isoforms seem to adopt the folding pattern of human thrombospondin 1 TSP-1 domains, where each TSP-1 domain forms an antiparallel three-stranded structure that consists of alternative stacked layers of Trp and Arg residues from respective strands capped by disulfide bonds on each end.	Disulfides	298-307	thrombospondin 1	Homo sapiens	93-109
18638502-6	2008	TSR domains of the three trout properdin isoforms seem to adopt the folding pattern of human thrombospondin 1 TSP-1 domains, where each TSP-1 domain forms an antiparallel three-stranded structure that consists of alternative stacked layers of Trp and Arg residues from respective strands capped by disulfide bonds on each end.	Disulfides	298-307	thrombospondin 1	Homo sapiens	110-115
18199549-6	2008	The epitope of the antibody was mapped to region on the coiled-coil structure formed between Ln-gamma 2 and its partner chains Ln-alpha 3 and Ln-beta 3 in Ln-5, whose structure is further stabilized by disulfide bonds.	Disulfides	202-211	laminin subunit gamma 2	Homo sapiens	93-103
18199549-6	2008	The epitope of the antibody was mapped to region on the coiled-coil structure formed between Ln-gamma 2 and its partner chains Ln-alpha 3 and Ln-beta 3 in Ln-5, whose structure is further stabilized by disulfide bonds.	Disulfides	202-211	laminin subunit beta 3	Homo sapiens	142-151
17704192-3	2008	We show herein that H2O2 induces formation of an intermolecular disulfide linkage of human SUMO protease SENP1 via the active-site Cys 603 and a unique residue Cys 613.	Disulfides	64-73	SUMO specific peptidase 1	Homo sapiens	105-110
17704192-5	2008	In vivo formation of a disulfide-linked dimer of SENP1 is also detected in cultured cells in response to oxidative stress.	Disulfides	23-32	SUMO specific peptidase 1	Homo sapiens	49-54
18224541-1	2008	We have studied the modulation and differential sensitivity of the estrogen receptor (ER) in breast cancer in the presence of protecting or modifying agents of disulfide bonds and sulfhydryl groups present in the ER steroid-binding domain.	Disulfides	160-169	estrogen receptor 1	Homo sapiens	67-84
18224541-1	2008	We have studied the modulation and differential sensitivity of the estrogen receptor (ER) in breast cancer in the presence of protecting or modifying agents of disulfide bonds and sulfhydryl groups present in the ER steroid-binding domain.	Disulfides	160-169	estrogen receptor 1	Homo sapiens	86-88
18209575-5	2008	These data suggest that thiol-disulfide exchange permits reduction of disulfide groups in thrombin and fibrinogen, altering their tertiary structure and physiological function.	Disulfides	30-39	fibrinogen beta chain	Homo sapiens	103-113
18209575-5	2008	These data suggest that thiol-disulfide exchange permits reduction of disulfide groups in thrombin and fibrinogen, altering their tertiary structure and physiological function.	Disulfides	70-79	coagulation factor II, thrombin	Homo sapiens	90-98
18209575-5	2008	These data suggest that thiol-disulfide exchange permits reduction of disulfide groups in thrombin and fibrinogen, altering their tertiary structure and physiological function.	Disulfides	70-79	fibrinogen beta chain	Homo sapiens	103-113
17906223-4	2008	Because PON1 has one disulfide and one free cysteine residue, the samples were reduced with dithiothreitol before electrophoresis.	Disulfides	21-30	paraoxonase 1	Homo sapiens	8-12
18211349-5	2008	Gelation was prevented upon treatment of SPI with iodoacetamide, which carbaminomethylated the cysteine residues, establishing the role of disulfide bonds in network formation.	Disulfides	139-148	chromogranin A	Homo sapiens	41-44
18386550-2	2008	It is composed of apolipoprotein B (Apo B)-100 and apolipoprotein(a) which are linked by a disulfide bond.	Disulfides	91-100	apolipoprotein B	Homo sapiens	18-46
18072732-8	2008	The 4 native disulfide bonds in RNaseA were detected by MassMatrix with multiple validated peptide matches for each disulfide bond with high statistical scores.	Disulfides	13-22	ribonuclease pancreatic	Bos taurus	32-38
18072732-8	2008	The 4 native disulfide bonds in RNaseA were detected by MassMatrix with multiple validated peptide matches for each disulfide bond with high statistical scores.	Disulfides	116-125	ribonuclease pancreatic	Bos taurus	32-38
18991774-1	2008	We use the procedure established for "disulfide stability analysis in redox system" to investigate the unfolding process of porcine insulin precursor (PIP).	Disulfides	38-47	prolactin induced protein	Homo sapiens	151-154
18991774-4	2008	Besides, the comparison of the intermediates captured in PIP unfolding process with those intermediates captured in its refolding process revealed that some intermediates captured during both unfolding/refolding processes of PIP have identical disulfide pairing pattern, from which we suggest that the unfolding/refolding processes of PIP share some common intermediates but flow in the opposite direction.	Disulfides	244-253	prolactin induced protein	Homo sapiens	225-228
18991774-4	2008	Besides, the comparison of the intermediates captured in PIP unfolding process with those intermediates captured in its refolding process revealed that some intermediates captured during both unfolding/refolding processes of PIP have identical disulfide pairing pattern, from which we suggest that the unfolding/refolding processes of PIP share some common intermediates but flow in the opposite direction.	Disulfides	244-253	prolactin induced protein	Homo sapiens	225-228
17959149-2	2007	We have examined the oxidative folding of the model four-disulfide-bond-containing protein bovine pancreatic ribonuclease A (RNase A) in its presence; results indicate that RNase A regeneration rate increases in a curcumin-dependent manner.	Disulfides	57-66	ribonuclease pancreatic	Bos taurus	125-132
18088070-8	2008	Bovine SP-B exists as dimers and all cysteines are oxidized to form disulfide bonds in physiological conditions, which is in agreement with the observed mass shift upon reduction of the SP-B dimer.	Disulfides	68-77	surfactant protein B	Bos taurus	7-11
17963731-5	2007	We demonstrate that the avidity of full-length RAP for LRP1 in vitro can be partially reconstituted by assembly of truncated, disulfide-linked RAP peptides on tetravalent streptavidin or bivalent immunoglobulin scaffolds.	Disulfides	126-135	LDL receptor related protein 1	Homo sapiens	55-59
18691493-5	2008	It has been proposed that PDI activates TF by changing the disulfide status of the membrane-proximal Cys186-Cys209 pair of TF.	Disulfides	59-68	coagulation factor III	Mus musculus	40-42
18691493-5	2008	It has been proposed that PDI activates TF by changing the disulfide status of the membrane-proximal Cys186-Cys209 pair of TF.	Disulfides	59-68	coagulation factor III	Mus musculus	123-125
18691493-6	2008	Indeed, PDI was shown to cleave mixed disulfide bonds of TF with glutathione.	Disulfides	38-47	coagulation factor III	Mus musculus	57-59
18691493-7	2008	This might enable the formation of an intrachain disulfide bond which is associated with an increased procoagulant efficiency of TF.	Disulfides	49-58	coagulation factor III	Mus musculus	129-131
18052040-0	2007	Carboxyl-terminal disulfide bond of acid sphingomyelinase is critical for its secretion and enzymatic function.	Disulfides	18-27	sphingomyelin phosphodiesterase 1	Homo sapiens	36-57
18052043-7	2007	We therefore conclude the higher affinity of Cyc.ext.Pep.1 for mAb198 reflects the fact that incorporation of additional residues producing a single disulfide bond endows Pep.1 with a conformational rigidity that mimics the structure of mAb198-bound Pep.1.	Disulfides	149-158	cytochrome c, somatic	Homo sapiens	45-48
17959149-2	2007	We have examined the oxidative folding of the model four-disulfide-bond-containing protein bovine pancreatic ribonuclease A (RNase A) in its presence; results indicate that RNase A regeneration rate increases in a curcumin-dependent manner.	Disulfides	57-66	ribonuclease pancreatic	Bos taurus	173-180
17981053-1	2007	In mammals, interferon-gamma-inducible-lysosomal thiol reductase (GILT) has been demonstrated to play a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction, thus unfolding native protein Ag and facilitating subsequent cleavage by proteases.	Disulfides	202-211	IFI30 lysosomal thiol reductase	Homo sapiens	66-70
18020457-4	2007	In response to H2O2, the Yap1 probe forms mixed disulfide bonds with a variety of proteins.	Disulfides	48-57	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	25-29
17964869-0	2007	Effect of a disulfide bond on mevalonate kinase.	Disulfides	12-21	mevalonate kinase	Rattus norvegicus	30-47
17964869-3	2007	Crystal structure and sequence alignment show that a unique disulfide bond exists in mevalonate kinase of thermostable species Methanococcus jannaschii, but not in rat mevalonate kinase.	Disulfides	60-69	mevalonate kinase	Rattus norvegicus	85-102
17964869-4	2007	In the present study, we investigated the effect of the disulfide bond in M. jannaschii mevalonate kinase and an engineered disulfide bond in rat mevalonate kinase mutant A141C on the properties of enzymes through characterization of their wild-type and variant enzymes.	Disulfides	56-65	mevalonate kinase	Rattus norvegicus	88-105
17964869-4	2007	In the present study, we investigated the effect of the disulfide bond in M. jannaschii mevalonate kinase and an engineered disulfide bond in rat mevalonate kinase mutant A141C on the properties of enzymes through characterization of their wild-type and variant enzymes.	Disulfides	124-133	mevalonate kinase	Rattus norvegicus	146-163
17964869-5	2007	Our result suggests that the Cys107-Cys281 disulfide bond is important for maintaining the conformation and the thermal activity of M. jannaschii mevalonate kinase.	Disulfides	43-52	mevalonate kinase	Rattus norvegicus	146-163
17964869-7	2007	The thiol-titration and fluorescence experiment further indicate that rat mevalonate kinase A141C variant enzyme has a new disulfide bond, which makes the variant protein enhance its thermal activity and resist to urea denaturation.	Disulfides	123-132	mevalonate kinase	Rattus norvegicus	74-91
17988684-1	2007	The structure in the extracellular, intradiscal domain of rhodopsin surrounding the Cys110-Cys187 disulfide bond has been shown to be important for correct folding of this receptor in vivo.	Disulfides	98-107	rhodopsin	Homo sapiens	58-67
17925407-0	2007	Shear-induced disulfide bond formation regulates adhesion activity of von Willebrand factor.	Disulfides	14-23	von Willebrand factor	Homo sapiens	70-91
17925407-7	2007	The shear-induced thiol-disulfide exchange increases VWF binding to platelets.	Disulfides	24-33	von Willebrand factor	Homo sapiens	53-56
17925407-8	2007	The thiol-disulfide exchange involves some or all of nine cysteine residues (Cys(889), Cys(898), Cys(2448), Cys(2451), Cys(2490), Cys(2491), Cys(2453), Cys(2528), and Cys(2533)) in the D3 and C domains as determined by mass spectrometry of the tryptic VWF peptides.	Disulfides	10-19	von Willebrand factor	Homo sapiens	252-255
17925407-9	2007	These results suggest that the thiol-disulfide state may serve as an important structural determinant of VWF adhesion activity and can be modified by fluid shear stress.	Disulfides	37-46	von Willebrand factor	Homo sapiens	105-108
18071269-1	2007	The conditional ero1-1 mutant, deficient in the ER-localized PDI oxidase Ero1p, is blocked in disulfide bond formation under restrictive conditions, such as high temperature, lack of oxygen, or high concentrations of membrane-permeant thiols.	Disulfides	94-103	ER oxidoreductin	Saccharomyces cerevisiae S288C	16-22
18071269-1	2007	The conditional ero1-1 mutant, deficient in the ER-localized PDI oxidase Ero1p, is blocked in disulfide bond formation under restrictive conditions, such as high temperature, lack of oxygen, or high concentrations of membrane-permeant thiols.	Disulfides	94-103	ER oxidoreductin	Saccharomyces cerevisiae S288C	73-78
18072203-0	2007	Expression of proteins containing disulfide bonds in an insect cell-free system and confirmation of their arrangements by MALDI-TOF MS. Escherichia coli alkaline phosphatase (AP) and human lysozyme (h-LYZ), which contain two and four disulfide bonds, respectively, were expressed in a cell-free protein synthesis system constructed from Spodoptera frugiperda 21 (Sf21) cells.	Disulfides	34-43	lysozyme	Homo sapiens	189-204
17947644-5	2007	complex contains MHC-I and disulfide-linked tapasin/ER60 conjugates.	Disulfides	27-36	TAP binding protein	Homo sapiens	44-51
18025460-6	2007	Mass spectrometry results are consistent with disulfide bond formation in p53 upon DNA-mediated oxidation.	Disulfides	46-55	tumor protein p53	Homo sapiens	74-77
17726014-8	2007	Loss of the N-terminal amino group and disulfide structure are crucial for preventing TIMP-1 from inhibiting MMPs.	Disulfides	39-48	TIMP metallopeptidase inhibitor 1	Homo sapiens	86-92
17956144-3	2007	Unfolding of lysozyme structure was induced by PEF, accompanied by the cleavage of disulfide bonds and self-association aggregation when the applied PEF dosage was higher than a critical level.	Disulfides	83-92	lysozyme	Homo sapiens	13-21
17982101-5	2007	CD200R3 existed as a disulfide-linked dimer, unlike other CD200Rs, and was expressed on mast cells and basophils primarily in association with an ITAM-bearing adaptor DAP12.	Disulfides	21-30	CD200 receptor 3	Mus musculus	0-7
17948058-4	2007	Tethering a presequence peptide to Tom20 through a disulfide bond was essential for crystallization.	Disulfides	51-60	translocase of outer mitochondrial membrane 20	Homo sapiens	35-40
17711389-5	2007	Here the authors demonstrate that PDI-1, PDI-2, and PDI-3 show comparable kinetic properties in catalyzing thiol:disulfide exchange reactions in two simple peptide-based assays.	Disulfides	113-122	Protein disulfide-isomerase	Caenorhabditis elegans	52-57
17916323-2	2007	As kaliocin-1 is a cysteine-stabilized peptide, it was of interest to determine whether it contained a multidimensional gamma-core signature recently identified as common to virtually all classes of disulfide-stabilized antimicrobial peptides.	Disulfides	199-208	lactotransferrin	Homo sapiens	3-13
17922544-0	2007	Insulin receptor substrate 1 knockdown in human MCF7 ER+ breast cancer cells by nuclease-resistant IRS1 siRNA conjugated to a disulfide-bridged D-peptide analogue of insulin-like growth factor 1.	Disulfides	126-135	insulin like growth factor 1	Homo sapiens	166-194
17922505-0	2007	Preparative alkaline urea gradient PAGE: application to purification of extraordinarily-stable disulfide-linked homodimer of human growth hormone.	Disulfides	95-104	growth hormone 1	Homo sapiens	131-145
17893039-6	2007	As exemplified for thioredoxin 1, the Tnk-1 kinase SH3 domain, and the hSH3(N) domain of the T cell protein ADAP, the conformational changes associated with disulfide bond formation can be followed directly upon titration with different ratios of reduced to oxidized glutathione.	Disulfides	157-166	tyrosine kinase non receptor 1	Homo sapiens	38-43
17893043-1	2007	To understand the physiological function of glutaredoxin, a thiotransferase catalyzing the reduction of mixed disulfides of protein and glutathione, we generated a line of knockout mice deficient in the cytosolic glutaredoxin 1 (Grx1).	Disulfides	110-120	glutaredoxin	Mus musculus	44-56
17947644-5	2007	complex contains MHC-I and disulfide-linked tapasin/ER60 conjugates.	Disulfides	27-36	protein disulfide isomerase family A member 3	Homo sapiens	52-56
17720812-2	2007	Upon exposure to H(2)O(2) Orp1(Cys36) forms a disulfide-bonded complex with the C-terminal domain of the Yap1 protein (Yap1-cCRD).	Disulfides	46-55	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	105-109
17607746-5	2007	In turn, Alb-SS-X were dethiolated by the excess nonprotein SH groups because of the lower pK(a) value in mixed disulfide with respect to that of other thiols.	Disulfides	112-121	albumin	Homo sapiens	9-12
17822402-2	2007	ERp57 and tapasin form a stable disulfide-linked heterodimer within the peptide-loading complex.	Disulfides	32-41	protein disulfide isomerase family A member 3	Homo sapiens	0-5
17822402-2	2007	ERp57 and tapasin form a stable disulfide-linked heterodimer within the peptide-loading complex.	Disulfides	32-41	TAP binding protein	Homo sapiens	10-17
17822402-3	2007	We demonstrate that ERp57-deficient loading complexes, obtained by expression in a tapasin-negative cell line of a tapasin mutant (C95A) that is not able to form a disulfide bond with ERp57, are prone to aggregation.	Disulfides	164-173	protein disulfide isomerase family A member 3	Homo sapiens	20-25
17924659-1	2007	A novel hydroquinone and NADH oxidase with protein disulfide-thiol interchange activity (designated ENOX2 or tNOX), associated exclusively with the outer leaflet of the plasma membrane at the surface of cancer cells and in sera of cancer patients, is absent from the surface of noncancer cells and from sera of healthy individuals.	Disulfides	51-60	ecto-NOX disulfide-thiol exchanger 2	Homo sapiens	100-105
17924659-1	2007	A novel hydroquinone and NADH oxidase with protein disulfide-thiol interchange activity (designated ENOX2 or tNOX), associated exclusively with the outer leaflet of the plasma membrane at the surface of cancer cells and in sera of cancer patients, is absent from the surface of noncancer cells and from sera of healthy individuals.	Disulfides	51-60	ecto-NOX disulfide-thiol exchanger 2	Homo sapiens	109-113
17728248-3	2007	Interactions between nAChR subunits and ERp57 occur via transient intermolecular disulfide bonds and do not require subunit N-linked glycosylation.	Disulfides	81-90	cholinergic receptor nicotinic alpha 4 subunit	Homo sapiens	21-26
17720812-2	2007	Upon exposure to H(2)O(2) Orp1(Cys36) forms a disulfide-bonded complex with the C-terminal domain of the Yap1 protein (Yap1-cCRD).	Disulfides	46-55	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	119-123
17728248-3	2007	Interactions between nAChR subunits and ERp57 occur via transient intermolecular disulfide bonds and do not require subunit N-linked glycosylation.	Disulfides	81-90	protein disulfide isomerase family A member 3	Homo sapiens	40-45
17652454-0	2007	Disulfide Bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis.	Disulfides	0-9	mitogen-activated protein kinase 8	Homo sapiens	111-136
17914842-0	2007	Mechanism of SN2 disulfide bond cleavage by phosphorus nucleophiles.	Disulfides	17-26	solute carrier family 38 member 5	Homo sapiens	13-16
17914842-9	2007	These data indicate that the gas-phase addition of a phosphine to the disulfide moiety will most likely form a phosphonium cation-thiolate anion salt, in the presence of four or more water molecules, that provide sufficient H-bonding stabilization to allow displacement of the thiolate anion, a normal uncomplicated SN2 transition state is to be expected.	Disulfides	70-79	solute carrier family 38 member 5	Homo sapiens	316-319
17937792-2	2007	We have previously shown that the EC-SOD subunit exists in two distinct folding variants based on differences in the disulfide bridge pattern (Petersen SV, Oury TD, Valnickova Z, Thogersen IB, Hojrup P, Crapo JD, Enghild JJ.	Disulfides	117-126	superoxide dismutase 3	Homo sapiens	34-40
17937792-6	2007	The EC-SOD subunits are associated into covalently linked dimers through an inter-subunit disulfide bridge creating the theoretical possibility of 3 dimers (aa, ai or ii) with different antioxidant potentials.	Disulfides	90-99	superoxide dismutase 3	Homo sapiens	4-10
17937792-7	2007	We have analyzed the quaternary structure of the endogenous EC-SOD disulfide-linked dimer to investigate if these dimers in fact exist.	Disulfides	67-76	superoxide dismutase 3	Homo sapiens	60-66
17923089-2	2007	Here we show that one of the INAD PDZ domains (PDZ5) exists in a redox-dependent equilibrium between two conformations--a reduced form that is similar to the structure of other PDZ domains, and an oxidized form in which the ligand-binding site is distorted through formation of a strong intramolecular disulfide bond.	Disulfides	302-311	inactivation no afterpotential D	Drosophila melanogaster	29-33
17923089-3	2007	We demonstrate transient light-dependent formation of this disulfide bond in vivo and find that transgenic flies expressing a mutant INAD in which PDZ5 is locked in the reduced state display severe defects in termination of visual responses and visually mediated reflex behavior.	Disulfides	59-68	inactivation no afterpotential D	Drosophila melanogaster	133-137
17895385-1	2007	Von Willebrand factor (VWF) dimerizes through C-terminal CK domains, and VWF dimers assemble into multimers in the Golgi by forming intersubunit disulfide bonds between D3 domains.	Disulfides	145-154	von Willebrand factor	Homo sapiens	0-21
17895385-1	2007	Von Willebrand factor (VWF) dimerizes through C-terminal CK domains, and VWF dimers assemble into multimers in the Golgi by forming intersubunit disulfide bonds between D3 domains.	Disulfides	145-154	von Willebrand factor	Homo sapiens	23-26
17895385-1	2007	Von Willebrand factor (VWF) dimerizes through C-terminal CK domains, and VWF dimers assemble into multimers in the Golgi by forming intersubunit disulfide bonds between D3 domains.	Disulfides	145-154	von Willebrand factor	Homo sapiens	73-76
17895385-11	2007	This arrangement of intersubunit disulfide bonds implies that the dimeric N-terminal D"D3 domains of VWF subunits align in a parallel orientation within VWF multimers.	Disulfides	33-42	von Willebrand factor	Homo sapiens	101-104
17895385-11	2007	This arrangement of intersubunit disulfide bonds implies that the dimeric N-terminal D"D3 domains of VWF subunits align in a parallel orientation within VWF multimers.	Disulfides	33-42	von Willebrand factor	Homo sapiens	153-156
17825322-2	2007	The mutant was designed to form a disulfide bond between the N terminus and loop E3, which allows handling of opsin in detergent solution and increases thermal stability of rhodopsin by 10 deg.C.	Disulfides	34-43	rhodopsin	Homo sapiens	173-182
17686774-0	2007	Intramolecular disulfide bond is a critical check point determining degradative fates of ATP-binding cassette (ABC) transporter ABCG2 protein.	Disulfides	15-24	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	128-133
17686774-2	2007	We previously reported that ABCG2 exists in the plasma membrane as a homodimer bound via a disulfide bond at Cys-603.	Disulfides	91-100	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	28-33
17666395-0	2007	Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1.	Disulfides	0-9	superoxide dismutase 1, soluble	Mus musculus	122-126
17666395-3	2007	Recent studies suggest that mutant SOD1 readily forms an incorrect disulfide bond upon mild oxidative stress in vitro, and the insoluble SOD1 aggregates in spinal cord of ALS model mice contain multimers cross-linked via intermolecular disulfide bonds.	Disulfides	67-76	superoxide dismutase 1, soluble	Mus musculus	35-39
17666395-3	2007	Recent studies suggest that mutant SOD1 readily forms an incorrect disulfide bond upon mild oxidative stress in vitro, and the insoluble SOD1 aggregates in spinal cord of ALS model mice contain multimers cross-linked via intermolecular disulfide bonds.	Disulfides	236-245	superoxide dismutase 1, soluble	Mus musculus	35-39
17666395-3	2007	Recent studies suggest that mutant SOD1 readily forms an incorrect disulfide bond upon mild oxidative stress in vitro, and the insoluble SOD1 aggregates in spinal cord of ALS model mice contain multimers cross-linked via intermolecular disulfide bonds.	Disulfides	236-245	superoxide dismutase 1, soluble	Mus musculus	137-141
17666395-4	2007	Here we show that a non-physiological intermolecular disulfide bond between cysteines at positions 6 and 111 of mutant SOD1 is important for high molecular weight aggregate formation, ubiquitylation, and neurotoxicity, all of which were dramatically reduced when the pertinent cysteines were replaced in mutant SOD1 expressed in Neuro-2a cells.	Disulfides	53-62	superoxide dismutase 1, soluble	Mus musculus	119-123
17666395-4	2007	Here we show that a non-physiological intermolecular disulfide bond between cysteines at positions 6 and 111 of mutant SOD1 is important for high molecular weight aggregate formation, ubiquitylation, and neurotoxicity, all of which were dramatically reduced when the pertinent cysteines were replaced in mutant SOD1 expressed in Neuro-2a cells.	Disulfides	53-62	superoxide dismutase 1, soluble	Mus musculus	311-315
17666395-6	2007	We found that Dorfin ubiquitylated mutant SOD1 by recognizing the Cys(6)- and Cys(111)-disulfide cross-linked form and targeted it for proteasomal degradation.	Disulfides	87-96	superoxide dismutase 1, soluble	Mus musculus	42-46
17686774-3	2007	In the present study, we examined the importance of an intramolecular disulfide bond for stability of the ABCG2 protein.	Disulfides	70-79	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	106-111
17686774-8	2007	Ubiquitin-mediated protein degradation is suggested to be involved in degradation of misfolded ABCG2 proteins lacking the intramolecular disulfide bond.	Disulfides	137-146	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	95-100
17686774-10	2007	These results strongly suggest that two distinct pathways exist for protein degradation of ABCG2 WT and mutants lacking the intramolecular disulfide bond.	Disulfides	139-148	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	91-96
17686774-11	2007	Namely, the WT ABCG2 is degraded in lysosomes, and the misfolded ABCG2 lacking intramolecular disulfide bond undergoes ubiquitin-mediated protein degradation in proteasomes.	Disulfides	94-103	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	65-70
17613523-2	2007	GAPDH is locally deposited in disulfide-bonded aggregates at lesion sites in certain neurodegenerative diseases.	Disulfides	30-39	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	0-5
17513351-1	2007	The importance of intramolecular disulfides in a noncovalent dimeric protein interleukin-8 (IL-8) has been studied by replacing cysteines in each of the two disulfide pairs with alpha-aminobutyric acid (CH(2)-SH --&gt; CH(2)-CH(3)).	Disulfides	33-43	C-X-C motif chemokine ligand 8	Homo sapiens	77-90
17513351-1	2007	The importance of intramolecular disulfides in a noncovalent dimeric protein interleukin-8 (IL-8) has been studied by replacing cysteines in each of the two disulfide pairs with alpha-aminobutyric acid (CH(2)-SH --&gt; CH(2)-CH(3)).	Disulfides	33-43	C-X-C motif chemokine ligand 8	Homo sapiens	92-96
17513351-1	2007	The importance of intramolecular disulfides in a noncovalent dimeric protein interleukin-8 (IL-8) has been studied by replacing cysteines in each of the two disulfide pairs with alpha-aminobutyric acid (CH(2)-SH --&gt; CH(2)-CH(3)).	Disulfides	33-42	C-X-C motif chemokine ligand 8	Homo sapiens	77-90
17513351-1	2007	The importance of intramolecular disulfides in a noncovalent dimeric protein interleukin-8 (IL-8) has been studied by replacing cysteines in each of the two disulfide pairs with alpha-aminobutyric acid (CH(2)-SH --&gt; CH(2)-CH(3)).	Disulfides	33-42	C-X-C motif chemokine ligand 8	Homo sapiens	92-96
17513351-6	2007	Deleting either disulfide in IL-8 results in substantial loss in receptor activity, indicating that both disulfides are critical for function in the folded protein.	Disulfides	16-25	C-X-C motif chemokine ligand 8	Homo sapiens	29-33
17513351-6	2007	Deleting either disulfide in IL-8 results in substantial loss in receptor activity, indicating that both disulfides are critical for function in the folded protein.	Disulfides	105-115	C-X-C motif chemokine ligand 8	Homo sapiens	29-33
17636263-0	2007	Important role of the cys-191 cys-220 disulfide bond in thrombin function and allostery.	Disulfides	38-47	coagulation factor II, thrombin	Homo sapiens	56-64
17613523-4	2007	Under nonreducing in vitro conditions, oxidants induced oligomerization and insoluble aggregation of GAPDH via the formation of intermolecular disulfide bonds.	Disulfides	143-152	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	101-106
17613523-7	2007	Oxidants also caused conformational changes in GAPDH concomitant with an increase in beta-sheet content; these abnormal conformations specifically led to amyloid-like fibril formation via disulfide bonds, including Cys(149).	Disulfides	188-197	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	47-52
17613523-8	2007	Additionally, continuous exposure of GAPDH-overexpressing HeLa cells to oxidants produced disulfide bonds in GAPDH leading to both detergent-insoluble and thioflavin-S-positive aggregates, which were associated with oxidative stress-induced cell death.	Disulfides	90-99	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	37-42
17613523-8	2007	Additionally, continuous exposure of GAPDH-overexpressing HeLa cells to oxidants produced disulfide bonds in GAPDH leading to both detergent-insoluble and thioflavin-S-positive aggregates, which were associated with oxidative stress-induced cell death.	Disulfides	90-99	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	109-114
17613523-9	2007	Thus, oxidative stresses induce amyloid-like aggregation of GAPDH via aberrant disulfide bonds of the active site cysteine, and the formation of such abnormal aggregates promotes cell death.	Disulfides	79-88	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	60-65
17546662-3	2007	In addition, a nonactive site disulfide was identified between Cys28 and Cys113 in hGrx2 using redox buffers and chemical digestion.	Disulfides	30-39	glutaredoxin 2	Homo sapiens	83-88
17681017-1	2007	Four mAbs of the IgG(1) class to the thrombin-treated N-terminal disulfide knot of fibrin, secreted by various hybridomas, have been selected.	Disulfides	65-74	coagulation factor II, thrombin	Homo sapiens	37-45
17509894-3	2007	In the present study, human proinsulin was produced in the periplasm of E. coli as a fusion to ecotin, which is a small periplasmic protein of 16 kDa encoded by the host, containing one disulfide bond.	Disulfides	186-195	insulin	Homo sapiens	28-38
17433716-2	2007	The sea bass TNF-alpha (sbTNF-alpha) putative protein conserves the TNF-alpha family signature, as well as the two cysteines usually involved in the formation of a disulfide bond.	Disulfides	164-173	tumor necrosis factor	Mus musculus	13-22
17433716-2	2007	The sea bass TNF-alpha (sbTNF-alpha) putative protein conserves the TNF-alpha family signature, as well as the two cysteines usually involved in the formation of a disulfide bond.	Disulfides	164-173	tumor necrosis factor	Mus musculus	26-35
17660256-4	2007	To probe the mechanistic role of hF and thFs3A during protease inhibition, a disulfide bond was engineered in alpha(1)-antitrypsin, which would lock the displacement of thFs3A from beta-sheet A.	Disulfides	77-86	serpin family A member 1	Homo sapiens	110-130
17546662-9	2007	The highly stabilizing nonactive site disulfide observed in hGrx2 is found to be a conserved feature within the deuterostomes and appears to be the only additional conserved intramolecular disulfide within the glutaredoxins.	Disulfides	38-47	glutaredoxin 2	Homo sapiens	60-65
17546662-9	2007	The highly stabilizing nonactive site disulfide observed in hGrx2 is found to be a conserved feature within the deuterostomes and appears to be the only additional conserved intramolecular disulfide within the glutaredoxins.	Disulfides	189-198	glutaredoxin 2	Homo sapiens	60-65
17715066-8	2007	The HIC-binding SOD1 was composed of disulfide-reduced subunits lacking metal ions and also subunits that apparently carried nonnative intrasubunit disulfide bonds.	Disulfides	37-46	superoxide dismutase 1, soluble	Mus musculus	16-20
17715066-8	2007	The HIC-binding SOD1 was composed of disulfide-reduced subunits lacking metal ions and also subunits that apparently carried nonnative intrasubunit disulfide bonds.	Disulfides	148-157	superoxide dismutase 1, soluble	Mus musculus	16-20
17593322-6	2007	The intramolecular disulfide bridge of CHO cell endomannosidase formed with the additional Cys188 was not solely responsible for the reduced enzyme activity since endomannosidase with engineered Cys188Ala or Ser substitutions did not restore enzyme activity and was ER mislocalized.	Disulfides	19-28	glycoprotein endo-alpha-1,2-mannosidase	Cricetulus griseus	48-63
17591771-6	2007	This is the first example of a cyclophilin containing this disulfide bridge.	Disulfides	59-68	cyclophilin	Schistosoma mansoni	31-42
17580849-4	2007	CHCA spots are more convenient for obtaining a precise mass fingerprint of a large number of peptides; however, the analysis of 1,5-DAN spots allows the number of disulfide bridges to be counted owing to their partial in-plume reduction by this particular matrix.	Disulfides	163-172	NBL1, DAN family BMP antagonist	Homo sapiens	132-135
17603487-3	2007	Tapasin and ERp57 have been shown to exist in the peptide-loading complex as a disulfide-linked heterodimer.	Disulfides	79-88	TAP binding protein	Homo sapiens	0-7
17603487-3	2007	Tapasin and ERp57 have been shown to exist in the peptide-loading complex as a disulfide-linked heterodimer.	Disulfides	79-88	protein disulfide isomerase family A member 3	Homo sapiens	12-17
17603488-2	2007	Here we show that in the absence of tapasin, the alpha2 disulfide bond in the MHC class I peptide-binding groove was rapidly reduced.	Disulfides	56-65	TAP binding protein	Homo sapiens	36-43
17443712-6	2007	The S1P(4) loop mimetic peptide interacted specifically with an S1P headgroup analog, O-phosphoethanolamine (PEA), as evidenced by PEA-induced perturbation of disulfide cross-linked coiled-coil first extracellular loop mimetic (CCE1a) (1)H and (15)N backbone amide chemical shifts.	Disulfides	159-168	sphingosine-1-phosphate receptor 4	Homo sapiens	4-10
17655306-4	2007	Alkyl secondary and tertiary allylic disulfides, formed by sulfide transfer from allylic heteroaryl disulfides to thiols, undergo desulfurative allylic rearrangement on treatment with PPh3 in methanolic acetonitrile at room temperature.	Disulfides	37-47	caveolin 1	Homo sapiens	184-188
17707237-0	2007	Multistep disulfide bond formation in Yap1 is required for sensing and transduction of H2O2 stress signal.	Disulfides	10-19	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	38-42
17707237-3	2007	The yeast transcription factor Yap1 is activated by disulfide-induced structural changes in the nuclear export signal in a carboxy-terminal domain.	Disulfides	52-61	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	31-35
17707237-4	2007	We show herein that the activation of Yap1 by H(2)O(2) requires multistep formation of disulfide bonds.	Disulfides	87-96	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	38-42
17707237-6	2007	The multiple interdomain disulfide bonds, which result in reduction-resistant Yap1, are required for transduction of the H(2)O(2) stress signal to induce the appropriate level and duration of specific transcription.	Disulfides	25-34	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	78-82
17675462-2	2007	We recently identified a patient with a homozygous amino acid substitution in Igbeta, a glycine to serine at codon 137, adjacent to the cysteine required for the disulfide bond between Igalpha and Igbeta.	Disulfides	162-171	CD79a molecule	Homo sapiens	185-192
17651362-1	2007	Whey acidic protein (WAP), a major whey protein present in milk of a number of mammalian species has characteristic cysteine-rich domains known as four-disulfide cores (4-DSC).	Disulfides	152-161	whey acidic protein	Ornithorhynchus anatinus	21-24
17531319-4	2007	The deduced LycCD59 protein shared the structural feature of mammalian CD59, including a conserved cysteine skeleton responsible for the formation of disulfide bonds, and a similar pattern of hydrophobic termini.	Disulfides	150-159	CD59 molecule (CD59 blood group)	Homo sapiens	15-19
17561102-4	2007	Yap1 activation involved oxidation to the intramolecular disulfide bond, a signature of activation by peroxide, and was dependent on the Yap1 peroxide sensor Orp1/Gpx3.	Disulfides	57-66	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	0-4
17459881-3	2007	Within the peptide-loading complex ERp57 is normally found disulfide-linked to tapasin, through one of its two thioredoxin-like redox motifs.	Disulfides	59-68	protein disulfide isomerase family A member 3	Homo sapiens	35-40
17442443-7	2007	Polyacrylamide gel electrophoresis under reducing or non-reducing conditions suggested that P10 subunits were oligomerized not through intermolecular disulfide bonds, but perhaps through some other type of association, such as hydrophobic or charge interactions.	Disulfides	150-159	S100 calcium binding protein A10	Homo sapiens	92-95
17610997-2	2007	Among the three known TFF peptides, TFF1 is characterized by three disulfide bonds producing a compact globular structure and an extended and disordered tail formed by amino- and carboxy-termini.	Disulfides	67-76	trefoil factor 1	Homo sapiens	36-40
17459881-3	2007	Within the peptide-loading complex ERp57 is normally found disulfide-linked to tapasin, through one of its two thioredoxin-like redox motifs.	Disulfides	59-68	TAP binding protein	Homo sapiens	79-86
17459881-4	2007	We describe here a novel trimeric complex that disulfide links together MHC class I heavy chain, ERp57 and tapasin, and that is found in association with the transporter associated with antigen processing peptide transporter.	Disulfides	47-56	protein disulfide isomerase family A member 3	Homo sapiens	97-102
17459881-4	2007	We describe here a novel trimeric complex that disulfide links together MHC class I heavy chain, ERp57 and tapasin, and that is found in association with the transporter associated with antigen processing peptide transporter.	Disulfides	47-56	TAP binding protein	Homo sapiens	107-114
17558445-2	2007	It was found that hTFPI-2/KD1 contained approximately 17% alpha-helices, 24% beta-strands, 46% random coils, 13% beta-turns, and two kinds of disulfide bonds(ggg and tgt) at 25 degrees C. The detailed conformational changes of the heated protein observed by fourier transform infrared spectroscopy, circular dichroism and Raman spectroscopy revealed that hTFPI-2/KD1 was thermally stable.	Disulfides	142-151	tissue factor pathway inhibitor 2	Homo sapiens	18-25
17391648-5	2007	Alanine substitutions of Cys124 and Cys152, residues indicated by homology modeling to be in close proximity and in the proper orientation for disulfide bonding, yielded reduced ASPA protein and activity levels.	Disulfides	143-152	aspartoacylase	Homo sapiens	178-182
17513761-5	2007	The three-dimensional structure of human HER-2 in complex with trastuzumab reveals that the Ag-binding region of HER-2 spans residues 563-626 that comprises an extensive disulfide-bonding pattern.	Disulfides	170-179	erb-b2 receptor tyrosine kinase 2	Homo sapiens	41-46
17513761-5	2007	The three-dimensional structure of human HER-2 in complex with trastuzumab reveals that the Ag-binding region of HER-2 spans residues 563-626 that comprises an extensive disulfide-bonding pattern.	Disulfides	170-179	erb-b2 receptor tyrosine kinase 2	Homo sapiens	113-118
17425334-3	2007	To clarify the role of another pair of fibrin-binding regions, Fib-2, located at the disulfide-linked COOH-terminal ends of fibronectin, we prepared by limited proteolysis a dimeric 140 kDa (Fib-2)2 fragment containing both Fib-2 regions and tested its interaction with recombinant fragments corresponding to the alphaC regions of fibrin(ogen).	Disulfides	85-94	protocadherin gamma subfamily B, 4	Homo sapiens	63-68
17425334-3	2007	To clarify the role of another pair of fibrin-binding regions, Fib-2, located at the disulfide-linked COOH-terminal ends of fibronectin, we prepared by limited proteolysis a dimeric 140 kDa (Fib-2)2 fragment containing both Fib-2 regions and tested its interaction with recombinant fragments corresponding to the alphaC regions of fibrin(ogen).	Disulfides	85-94	fibronectin 1	Homo sapiens	124-135
17428749-4	2007	The MS study also showed that an intramolecular disulfide bond was formed between C13 and C18 at the active site, and was reduced by the TTase/GSH system.	Disulfides	48-57	glutaredoxin	Mus musculus	137-142
17310324-6	2007	Hence, the renaturation of disulfide-containing lysozyme was highly affected by the extent of denaturation.	Disulfides	27-36	lysozyme	Homo sapiens	48-56
20641230-0	2004	[(18)F]SB209670 Endothelin (ET)-1 is a polypeptide of 21 amino acids and contains two disulfide bonds located close to the N-terminus.	Disulfides	86-95	endothelin 1	Homo sapiens	16-33
17488621-7	2007	AFF-1 and EFF-1 differ in their fusogenic activity and expression patterns but share eight conserved predicted disulfide bonds in their ectodomains, including a putative TGF-beta-type-I-Receptor domain.	Disulfides	111-120	Cell fusion protein aff-1	Caenorhabditis elegans	0-5
17397191-3	2007	Our results suggested a new 3D model of the rhodopsin-transducin complex that fully satisfied all available experimental data on site-directed mutagenesis of rhodopsin and Gtalphabetagamma as well as data from disulfide-linking experiments.	Disulfides	210-219	rhodopsin	Homo sapiens	44-53
20641513-0	2004	4-[(18)F]Fluorobenzoyl-endothelin-1 Endothelin-1 (ET-1) is a 21 amino acid polypeptide that contains two disulfide bonds located closer to the N-terminus.	Disulfides	105-114	endothelin 1	Homo sapiens	36-48
20641513-0	2004	4-[(18)F]Fluorobenzoyl-endothelin-1 Endothelin-1 (ET-1) is a 21 amino acid polypeptide that contains two disulfide bonds located closer to the N-terminus.	Disulfides	105-114	endothelin 1	Homo sapiens	50-54
17208964-1	2007	We recently identified a functionally important disulfide bridge between C255 and C511 of the human Na+/glucose cotransporter SGLT1.	Disulfides	48-57	solute carrier family 5 member 1	Homo sapiens	126-131
17316609-9	2007	Our study confirms the redox regulation of PTEN through disulfide bond formation with the hTrx-1 in Drosophila and suggests conserved mechanisms for thioredoxins and their interactions with the phosphatidylinositol-3-kinase signaling pathway in humans and fruit flies.	Disulfides	56-65	Phosphatase and tensin homolog	Drosophila melanogaster	43-47
17287397-5	2007	The oye2Delta phenotype can be completely suppressed by removing the potential for formation of the actin C285-C374 disulfide bond, the likely substrate of the Oye2p enzyme or by treating the cells with the clinically important reductant N-acetylcysteine.	Disulfides	116-125	actin	Saccharomyces cerevisiae S288C	100-105
17395713-6	2007	RESULTS: Two different antibody formats for each IgG1, IgG4, and IgE antibody were produced in mammalian cells as disulfide-linked and glycosylated Ig, which were usable in allergen-specific ELISA assays and immunoblots.	Disulfides	114-123	immunoglobulin heavy constant epsilon	Homo sapiens	65-68
17395017-2	2007	In this study reduced Trx increased the solubility and decreased the size of MUC5B glycoprotein while reducing disulfide bonds in sputum.	Disulfides	111-120	thioredoxin 1	Rattus norvegicus	22-25
17385893-1	2007	Thioredoxin reductase (TR) from Drosophila melanogaster (DmTR) is a member of the glutathione reductase (GR) family of pyridine nucleotide disulfide oxidoreductases and catalyzes the reduction of the redox-active disulfide bond of thioredoxin.	Disulfides	139-148	Thioredoxin reductase-1	Drosophila melanogaster	82-103
17385893-1	2007	Thioredoxin reductase (TR) from Drosophila melanogaster (DmTR) is a member of the glutathione reductase (GR) family of pyridine nucleotide disulfide oxidoreductases and catalyzes the reduction of the redox-active disulfide bond of thioredoxin.	Disulfides	139-148	Thioredoxin reductase-1	Drosophila melanogaster	105-107
17329258-3	2007	Human erythrocyte peroxiredoxin 2 was oxidized stoichiometrically to its disulfide-bonded homodimer by hydrogen peroxide, as monitored electrophoretically under nonreducing conditions.	Disulfides	73-82	peroxiredoxin 2	Homo sapiens	18-33
17270303-3	2007	Topical iodine protects the dermally applied insulin presumably by inactivation of endogenous sulfhydryls such as glutathione and gamma glutamylcysteine which can reduce the disulfide bonds of the hormone.	Disulfides	174-183	insulin	Homo sapiens	45-52
17392029-10	2007	In summary, computer modeling visualized possible modes of binding for those weak toxins which interact with the nAChR, provided no solutions for those weak toxins whose targets are not the nAChRs, and demonstrated that the additional disulfide in loop I cannot be a sound criteria for joining all weak toxins into one group; the conclusion about the diversity of weak toxins made from computer modeling is in accord with the earlier phylogenetic analysis.	Disulfides	235-244	cholinergic receptor nicotinic alpha 4 subunit	Homo sapiens	113-118
17121419-4	2007	Following reduction of insulin disulfide bridges, Native-PAGE indicated that A-chain was preferentially nitrated.	Disulfides	31-40	insulin	Homo sapiens	23-30
17302442-0	2007	An engineered second disulfide bond restricts lymphotactin/XCL1 to a chemokine-like conformation with XCR1 agonist activity.	Disulfides	21-30	X-C motif chemokine receptor 1	Homo sapiens	102-106
17106881-7	2007	Disulfide bond disruption significantly attenuated recombinant lubricin and LUB-C binding to cartilage surfaces, demonstrating a requirement for protein secondary structure in facilitating the appropriate localization of lubricin at relevant tissue interfaces.	Disulfides	0-9	proteoglycan 4	Homo sapiens	63-71
17106881-7	2007	Disulfide bond disruption significantly attenuated recombinant lubricin and LUB-C binding to cartilage surfaces, demonstrating a requirement for protein secondary structure in facilitating the appropriate localization of lubricin at relevant tissue interfaces.	Disulfides	0-9	proteoglycan 4	Homo sapiens	221-229
17110014-3	2007	Recently we have shown that native bovine plasma fetuin-A partially exists as a disulfide-bridged two-chain protein with a heavy N-terminal and a lighter C-terminal chain similar to the structure of human fetuin-A homologue (alpha2HS glycoprotein), and also is partially phosphorylated at residues Ser120, Ser302, Ser305 and Ser306 (Wind et al., Anal.	Disulfides	80-89	alpha 2-HS glycoprotein	Homo sapiens	205-213
17110014-3	2007	Recently we have shown that native bovine plasma fetuin-A partially exists as a disulfide-bridged two-chain protein with a heavy N-terminal and a lighter C-terminal chain similar to the structure of human fetuin-A homologue (alpha2HS glycoprotein), and also is partially phosphorylated at residues Ser120, Ser302, Ser305 and Ser306 (Wind et al., Anal.	Disulfides	80-89	alpha 2-HS glycoprotein	Homo sapiens	225-246
17110014-7	2007	In this study we show that authentic bovine fetuin-A disulfide-bridged two-chain forms, which include the original C-terminus, were liberated from the single-chain precursor by metalloproteinases MMP-3 (stromelysin-1) and MMP-7 (matrilysin), but not by elastase, cathepsin E and cathepsin G.	Disulfides	53-62	CTSE	Bos taurus	263-290
17269660-2	2007	Recent structural data demonstrated the way in which disulfide bonds in the ligand-binding core of the NR1 subunit are arranged.	Disulfides	53-62	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	103-106
17116644-2	2007	A classic example is RNase A (also known as bovine pancreatic ribonuclease), which contains 4 conserved disulfide bonds among 8 cysteines.	Disulfides	104-113	ribonuclease pancreatic	Bos taurus	21-28
17490558-2	2007	Hirudin possesses three disulfide bridges forming the structure of core cyclic peptides, which binds to the catalytic site of thrombin so as to inhibit the catalysis of thrombin.	Disulfides	24-33	coagulation factor II, thrombin	Homo sapiens	126-134
17490558-2	2007	Hirudin possesses three disulfide bridges forming the structure of core cyclic peptides, which binds to the catalytic site of thrombin so as to inhibit the catalysis of thrombin.	Disulfides	24-33	coagulation factor II, thrombin	Homo sapiens	169-177
17046249-2	2007	It was shown from the analysis of the components that the hetero disulfide Ht-SS-G increased by binding with the DNA (CA14) with an A(3)T(3) binding motif for the structure of Hoechst33258, and that the different equilibrium shift was observed in the presence of CT14 with no A(3)T(3) binding motif.	Disulfides	65-74	sarcoma antigen 1	Homo sapiens	263-267
17130129-6	2007	Escherichia coli reduced thioredoxin (Trx) cleaved the intersubunit disulfide bond to activate MST to 2.3- and 4.9-fold the levels of activation of dithiothreitol (DTT)-treated and DTT-untreated MST, respectively.	Disulfides	68-77	thioredoxin 1	Rattus norvegicus	38-41
17130129-10	2007	Thus, Cys(32) of E. coli Trx reacted with the redox-active cysteines, Cys(154) and Cys(263), by forming an intersubunit disulfide bond and a sulfenyl Cys(247).	Disulfides	120-129	thioredoxin 1	Rattus norvegicus	25-28
17130129-11	2007	A consecutively formed disulfide bond between Trx and MST must be cleaved for the activation.	Disulfides	23-32	thioredoxin 1	Rattus norvegicus	46-49
18064354-3	2007	A hemolytic toxin isolated from the sea anemone Stichodactyla helianthus, which is active at the cell membrane level, was linked through a disulfide bond to the anti-epidermal growth factor receptor monoclonal antibody ior egf/r3.	Disulfides	139-148	epidermal growth factor receptor	Homo sapiens	166-198
17142455-8	2007	Unlike APOBEC3F, APOBEC3G strongly interacted with cellular proteins via disulfide bonds.	Disulfides	73-82	apolipoprotein B mRNA editing enzyme catalytic subunit 3G	Homo sapiens	17-25
17196530-4	2007	The crystal structure of the ligand-binding domain of NR1 reveals a flexible disulfide bond (C744-C798), which may account for its susceptibility to reduction and subsequent reaction with NO that is observed with biochemical techniques.	Disulfides	77-86	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	54-57
17122395-6	2007	The formation of intramolecular disulfide bonds has been proposed to be crucial for the H(2)O(2)-induced nuclear localization of Yap1, and we verified the importance of cysteine residues of Yap1 in response to EGCG and GTE.	Disulfides	32-41	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	129-133
17122395-6	2007	The formation of intramolecular disulfide bonds has been proposed to be crucial for the H(2)O(2)-induced nuclear localization of Yap1, and we verified the importance of cysteine residues of Yap1 in response to EGCG and GTE.	Disulfides	32-41	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	190-194
17226937-6	2007	In the proposed reaction mechanism, the active-site cysteine residue of GSTO1-1 reacts with the S-(phenacyl)glutathione substrate to give an acetophenone and a mixed disulfide with the active-site cysteine; a second thiol substrate (e.g., glutathione or 2-mercaptoethanol) reacts with the active-site disulfide to regenerate the catalytically active enzyme and to form a mixed disulfide.	Disulfides	166-175	glutathione S-transferase omega 1	Rattus norvegicus	72-79
17982272-2	2007	It forms disulfide-linked heterodimers with the trefoil factor family (TFF) peptide TFF1.	Disulfides	9-18	trefoil factor 1	Homo sapiens	84-88
17226937-6	2007	In the proposed reaction mechanism, the active-site cysteine residue of GSTO1-1 reacts with the S-(phenacyl)glutathione substrate to give an acetophenone and a mixed disulfide with the active-site cysteine; a second thiol substrate (e.g., glutathione or 2-mercaptoethanol) reacts with the active-site disulfide to regenerate the catalytically active enzyme and to form a mixed disulfide.	Disulfides	301-310	glutathione S-transferase omega 1	Rattus norvegicus	72-79
17226937-6	2007	In the proposed reaction mechanism, the active-site cysteine residue of GSTO1-1 reacts with the S-(phenacyl)glutathione substrate to give an acetophenone and a mixed disulfide with the active-site cysteine; a second thiol substrate (e.g., glutathione or 2-mercaptoethanol) reacts with the active-site disulfide to regenerate the catalytically active enzyme and to form a mixed disulfide.	Disulfides	301-310	glutathione S-transferase omega 1	Rattus norvegicus	72-79
17518268-1	2007	Phenoxodiol, a synthetic isoflavene with clinical efficacy in the management of ovarian and other forms of human cancer, blocked the activity of a cancer-specific and growth-related cell surface ECTO-NOX protein with both oxidative (hydroquinone) and protein disulfide-thiol interchange activity designated tNOX.	Disulfides	259-268	ecto-NOX disulfide-thiol exchanger 2	Homo sapiens	307-311
17135761-19	2007	The dimers of Can f 1 and of Can f 2 were not built with a disulfide bridge but by non-covalent association.	Disulfides	59-68	minor allergen Can f 2	Canis lupus familiaris	29-36
17903313-8	2007	P1 and P2 are phosphorylated soon after their synthesis, but after binding to DNA most of the phosphate groups are removed and cysteine residues are oxidized, forming disulfide bridges that link the protamines together.	Disulfides	167-176	protamine 1	Homo sapiens	0-9
17059431-9	2007	Measurement of the endogenous thrombin potential in FVIII-deficient plasma supplemented with these FVIII variants confirmed that the disulfide bond-stabilized variants supported high levels of thrombin generation at lower concentrations than did WT FVIII.	Disulfides	133-142	coagulation factor II, thrombin	Homo sapiens	30-38
17059431-9	2007	Measurement of the endogenous thrombin potential in FVIII-deficient plasma supplemented with these FVIII variants confirmed that the disulfide bond-stabilized variants supported high levels of thrombin generation at lower concentrations than did WT FVIII.	Disulfides	133-142	coagulation factor II, thrombin	Homo sapiens	193-201
18604945-7	2007	A disulfide-stabilized structure incorporating a sarafotoxin (SRT) 6b model was examined as a matrix metalloproteinase (MMP)-3 inhibitor.	Disulfides	2-11	matrix metallopeptidase 3	Homo sapiens	94-126
18351130-1	2007	A novel hydroquinone and NADH oxidase with protein disulfide-thiol interchange activity (designated ENOX2 or tNOX), associated exclusively with the outer leaflet of the plasma membrane at the surface of cancer cells and in sera of cancer patients, is absent from the surface of noncancer cells and from sera from healthy individuals.	Disulfides	51-60	ecto-NOX disulfide-thiol exchanger 2	Homo sapiens	100-105
18351130-1	2007	A novel hydroquinone and NADH oxidase with protein disulfide-thiol interchange activity (designated ENOX2 or tNOX), associated exclusively with the outer leaflet of the plasma membrane at the surface of cancer cells and in sera of cancer patients, is absent from the surface of noncancer cells and from sera from healthy individuals.	Disulfides	51-60	ecto-NOX disulfide-thiol exchanger 2	Homo sapiens	109-113
17141371-0	2007	Recombinant production and structural studies of the Aplysia water-borne protein pheromone enticin indicates it has a novel disulfide stabilized fold.	Disulfides	124-133	enticin	Aplysia californica	91-98
17141371-7	2007	The three disulfide bonds in enticin were characterized by endoproteinase Glu-C proteolysis followed by mass spectrometric characterization of the fragments.	Disulfides	10-19	enticin	Aplysia californica	29-36
17141371-11	2007	A model for enticin was prepared based on its helical structure and these disulfide constraints.	Disulfides	74-83	enticin	Aplysia californica	12-19
17071618-0	2006	Identification of cysteines involved in S-nitrosylation, S-glutathionylation, and oxidation to disulfides in ryanodine receptor type 1.	Disulfides	95-105	ryanodine receptor 1	Homo sapiens	109-134
17071618-1	2006	The skeletal muscle Ca(2+)-release channel (ryanodine receptor type 1 (RyR1)) is a redox sensor, susceptible to reversible S-nitrosylation, S-glutathionylation, and disulfide oxidation.	Disulfides	165-174	ryanodine receptor 1	Homo sapiens	44-69
17071618-1	2006	The skeletal muscle Ca(2+)-release channel (ryanodine receptor type 1 (RyR1)) is a redox sensor, susceptible to reversible S-nitrosylation, S-glutathionylation, and disulfide oxidation.	Disulfides	165-174	ryanodine receptor 1	Homo sapiens	71-75
17071618-5	2006	Using a combination of Western blotting and sulfhydryl-directed fluorescent labeling, we found that two large regions of RyR1 (amino acids 1-2401 and 3120-4475), previously shown to be involved in disulfide bond formation, are also major sites of both S-nitrosylation and S-glutathionylation.	Disulfides	197-206	ryanodine receptor 1	Homo sapiens	121-125
17071618-8	2006	In summary, we have identified a discrete subset of cysteines that are likely to be involved in the functional response of RyR1 to different redox modifications (S-nitrosylation, S-glutathionylation, and oxidation to disulfides).	Disulfides	217-227	ryanodine receptor 1	Homo sapiens	123-127
16927250-5	2006	We identified nine proteins that sensitively reacted to LAA treatment by using two-dimensional (2-D) gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight-MS. A subunit of protein-disulfide isomerase (a thiol/disulfide exchange catalyst) and immunoglobulin-heavy-chain binding protein (BiP, identical to Hsp70 chaperone) showed quantitative expression profile differences.	Disulfides	209-218	heat shock protein family A (Hsp70) member 5	Homo sapiens	271-313
17070779-6	2006	This PON1 inactivation was associated with the formation of a mixed disulfide bond between GSSG and PON1"s cysteine residue(s), as detected by immunoblotting with anti-glutathione IgG.	Disulfides	68-77	paraoxonase 1	Homo sapiens	5-9
17070779-6	2006	This PON1 inactivation was associated with the formation of a mixed disulfide bond between GSSG and PON1"s cysteine residue(s), as detected by immunoblotting with anti-glutathione IgG.	Disulfides	68-77	paraoxonase 1	Homo sapiens	100-104
16927250-5	2006	We identified nine proteins that sensitively reacted to LAA treatment by using two-dimensional (2-D) gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight-MS. A subunit of protein-disulfide isomerase (a thiol/disulfide exchange catalyst) and immunoglobulin-heavy-chain binding protein (BiP, identical to Hsp70 chaperone) showed quantitative expression profile differences.	Disulfides	209-218	heat shock protein family A (Hsp70) member 5	Homo sapiens	315-318
16927250-5	2006	We identified nine proteins that sensitively reacted to LAA treatment by using two-dimensional (2-D) gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight-MS. A subunit of protein-disulfide isomerase (a thiol/disulfide exchange catalyst) and immunoglobulin-heavy-chain binding protein (BiP, identical to Hsp70 chaperone) showed quantitative expression profile differences.	Disulfides	209-218	heat shock protein family A (Hsp70) member 5	Homo sapiens	333-338
17128987-3	2006	While reaction of redox agents with RhoA stimulates guanine nucleotide dissociation, RhoA is subsequently inactivated through formation of an intramolecular disulfide that prevents guanine nucleotide binding thereby causing RhoA inactivation.	Disulfides	157-166	ras homolog family member A	Homo sapiens	85-89
17128987-3	2006	While reaction of redox agents with RhoA stimulates guanine nucleotide dissociation, RhoA is subsequently inactivated through formation of an intramolecular disulfide that prevents guanine nucleotide binding thereby causing RhoA inactivation.	Disulfides	157-166	ras homolog family member A	Homo sapiens	36-40
17109834-8	2006	Both glutathione reductase and glutaredoxin that reduce oxidized glutathione and protein glutathione mixed disulfides, respectively, were constitutively expressed at higher levels in females.	Disulfides	107-117	glutaredoxin	Mus musculus	31-43
17128987-3	2006	While reaction of redox agents with RhoA stimulates guanine nucleotide dissociation, RhoA is subsequently inactivated through formation of an intramolecular disulfide that prevents guanine nucleotide binding thereby causing RhoA inactivation.	Disulfides	157-166	ras homolog family member A	Homo sapiens	85-89
17110238-2	2006	It has many properties in common with low-density lipoprotein, but contains a unique protein moiety designated apo(a), which is linked to apolipoprotein B-100 by a single disulfide bond.	Disulfides	171-180	apolipoprotein B	Homo sapiens	138-158
17023413-3	2006	In a library of N-terminal mutant C5aR molecules screened for activation by C5a, residues 24-30 of the C5aR showed a marked propensity to mutate to cysteine, most likely indicating that sulfhydryl groups at these positions are appropriately situated to form disulfide interactions with the unpaired Cys(27) of human C5a.	Disulfides	258-267	complement C5a receptor 1	Homo sapiens	103-107
17029235-1	2006	AtFKBP13, an immunophilin in the chloroplast thylakoid lumen, participates in redox-regulatory processes via a pair of conserved disulfide bonds that are present at the N- and C-termini of the protein.	Disulfides	129-138	FK506-binding protein 13	Arabidopsis thaliana	0-8
17002656-8	2006	Plasmin(ogen), vitronectin, glycoprotein 1balpha, integrin beta(3) and thrombomodulin also contain -RHStaple disulfides, and there is circumstantial evidence that the function of these proteins may involve cleavage/formation of these disulfide bonds.	Disulfides	109-119	integrin subunit beta 3	Homo sapiens	50-85
17002656-8	2006	Plasmin(ogen), vitronectin, glycoprotein 1balpha, integrin beta(3) and thrombomodulin also contain -RHStaple disulfides, and there is circumstantial evidence that the function of these proteins may involve cleavage/formation of these disulfide bonds.	Disulfides	109-118	integrin subunit beta 3	Homo sapiens	50-85
17088012-8	2006	Disulfide bridge formation may be an interesting mechanism that prevents proteolysis of [Abu(86,94)]CART (85-102)(red) and terminates its ability to reverse amphetamine-induced hyperlocomotion.	Disulfides	0-9	CART prepropeptide	Homo sapiens	100-104
17115050-3	2006	Success was achieved for GluR5, GluR6 and GluR7 with intermolecular disulfide cross-links but not by engineering the dimer interface.	Disulfides	68-77	glutamate ionotropic receptor kainate type subunit 1	Homo sapiens	25-30
17139364-0	2006	Differential effects of the loss of intrachain- versus interchain-disulfide bonds in the cystine-knot domain of von Willebrand factor on the clinical phenotype of von Willebrand disease.	Disulfides	66-75	von Willebrand factor	Homo sapiens	112-133
17139364-1	2006	Von Willebrand factor (VWF) contains a large number of cysteine residues, which all form disulfide bonds.	Disulfides	89-98	von Willebrand factor	Homo sapiens	0-21
17139364-1	2006	Von Willebrand factor (VWF) contains a large number of cysteine residues, which all form disulfide bonds.	Disulfides	89-98	von Willebrand factor	Homo sapiens	23-26
17139364-8	2006	Our data suggest that loss of a single disulfide bond in the CK-domain of VWF leads to a recessive, quantitative VWF deficiency if an intrachain-disulfide bond is involved, and to a dominant-negative, qualitative defect of VWF if an interchain-disulfide bond is involved.	Disulfides	39-48	von Willebrand factor	Homo sapiens	74-77
16831481-2	2006	Vascular endothelial growth factor (VEGF) siRNA was conjugated to poly(ethylene glycol) (PEG) via a disulfide linkage (siRNA-PEG).	Disulfides	100-109	vascular endothelial growth factor A	Homo sapiens	0-34
16831481-2	2006	Vascular endothelial growth factor (VEGF) siRNA was conjugated to poly(ethylene glycol) (PEG) via a disulfide linkage (siRNA-PEG).	Disulfides	100-109	vascular endothelial growth factor A	Homo sapiens	36-40
17139364-8	2006	Our data suggest that loss of a single disulfide bond in the CK-domain of VWF leads to a recessive, quantitative VWF deficiency if an intrachain-disulfide bond is involved, and to a dominant-negative, qualitative defect of VWF if an interchain-disulfide bond is involved.	Disulfides	39-48	von Willebrand factor	Homo sapiens	113-116
17139364-8	2006	Our data suggest that loss of a single disulfide bond in the CK-domain of VWF leads to a recessive, quantitative VWF deficiency if an intrachain-disulfide bond is involved, and to a dominant-negative, qualitative defect of VWF if an interchain-disulfide bond is involved.	Disulfides	145-154	von Willebrand factor	Homo sapiens	74-77
17139364-8	2006	Our data suggest that loss of a single disulfide bond in the CK-domain of VWF leads to a recessive, quantitative VWF deficiency if an intrachain-disulfide bond is involved, and to a dominant-negative, qualitative defect of VWF if an interchain-disulfide bond is involved.	Disulfides	145-154	von Willebrand factor	Homo sapiens	113-116
17139364-8	2006	Our data suggest that loss of a single disulfide bond in the CK-domain of VWF leads to a recessive, quantitative VWF deficiency if an intrachain-disulfide bond is involved, and to a dominant-negative, qualitative defect of VWF if an interchain-disulfide bond is involved.	Disulfides	145-154	von Willebrand factor	Homo sapiens	74-77
17139364-8	2006	Our data suggest that loss of a single disulfide bond in the CK-domain of VWF leads to a recessive, quantitative VWF deficiency if an intrachain-disulfide bond is involved, and to a dominant-negative, qualitative defect of VWF if an interchain-disulfide bond is involved.	Disulfides	145-154	von Willebrand factor	Homo sapiens	113-116
16930550-3	2006	Four of the proteins were found to belong to the Kazal protease inhibitor family and were named SPINK8, SPINK10, SPINK11, and SPINK12, whereas one of the proteins, WFDC10, contained the WAP four-disulfide core domain structure.	Disulfides	195-204	serine peptidase inhibitor, Kazal type 12	Mus musculus	126-133
17087494-3	2006	The oxidized form of the Yap1 redox domain (Yap1-RD) fragment, derived from the Yap1 transcription factor, contains two disulfide bonds, one between Cys303 and Cys598 and one between Cys310 and Cys629.	Disulfides	120-129	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	25-29
17087494-3	2006	The oxidized form of the Yap1 redox domain (Yap1-RD) fragment, derived from the Yap1 transcription factor, contains two disulfide bonds, one between Cys303 and Cys598 and one between Cys310 and Cys629.	Disulfides	120-129	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	44-48
17087494-3	2006	The oxidized form of the Yap1 redox domain (Yap1-RD) fragment, derived from the Yap1 transcription factor, contains two disulfide bonds, one between Cys303 and Cys598 and one between Cys310 and Cys629.	Disulfides	120-129	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	44-48
16956893-4	2006	The constitutive activity of oncogenic STAT3C was reported to depend on spontaneous dimerization directed by disulfide bonds in the absence of tyrosine phosphorylation.	Disulfides	109-118	signal transducer and activator of transcription 3	Homo sapiens	39-45
16998480-4	2006	Labeling and functional assays using cysteine mutants, together with membrane sidedness in activating reactive disulfides, show that cytoplasmically accessible Cys553 and nearby Cys558 are nitrosylation sites mediating NO sensitivity in TRPC5.	Disulfides	111-121	transient receptor potential cation channel subfamily C member 5	Homo sapiens	237-242
17105214-2	2006	Insulin conjugated to transferrin by forming disulfide bonds has been shown to improve insulin oral bioavailability in diabetic rats.	Disulfides	45-54	transferrin	Rattus norvegicus	22-33
16967438-6	2006	It is demonstrated that disulfide cyclizations of angiotensin IV can deliver ligands with high IRAP/AT4 receptor affinity.	Disulfides	24-33	leucyl and cystinyl aminopeptidase	Homo sapiens	95-99
16967438-6	2006	It is demonstrated that disulfide cyclizations of angiotensin IV can deliver ligands with high IRAP/AT4 receptor affinity.	Disulfides	24-33	leucyl and cystinyl aminopeptidase	Homo sapiens	100-112
16808898-6	2006	Gpx3 can interact with Mxr1 through the formation of an intermolecular disulfide bond.	Disulfides	71-80	peptide-methionine-S-sulfoxide reductase	Saccharomyces cerevisiae S288C	23-27
16880213-2	2006	By using yeast and mammalian expression systems, we demonstrate here that SOD1 stability is governed by post-translational modification factors that target the SOD1 disulfide.	Disulfides	165-174	superoxide dismutase 1	Homo sapiens	74-78
16880213-2	2006	By using yeast and mammalian expression systems, we demonstrate here that SOD1 stability is governed by post-translational modification factors that target the SOD1 disulfide.	Disulfides	165-174	superoxide dismutase 1	Homo sapiens	160-164
16880213-3	2006	Oxidation of the human SOD1 disulfide in vivo was found to involve both the copper chaperone for SOD1 (CCS) and the CCS-independent pathway for copper activation.	Disulfides	28-37	superoxide dismutase 1	Homo sapiens	23-27
16880213-3	2006	Oxidation of the human SOD1 disulfide in vivo was found to involve both the copper chaperone for SOD1 (CCS) and the CCS-independent pathway for copper activation.	Disulfides	28-37	superoxide dismutase 1	Homo sapiens	97-101
16705086-9	2006	We conclude that rituximab binds a discontinuous epitope in CD20, comprised of (170)ANPS(173) and (182)YCYSI(185), with both strings brought in steric proximity by a disulfide bridge between C(167) and C(183).	Disulfides	166-175	keratin 20	Homo sapiens	60-64
16952188-4	2006	The amino acid sequence of TIME-EA4 showed 46-55 % homology with the reported proteins of the Cu,Zn-SOD (superoxide dismutase) family; in particular, the SOD active site (core domain) includes metal-binding amino acid ligands and a disulfide bond, and these structures are completely identical in Bombyx SOD, bovine SOD, and TIME-EA4 proteins.	Disulfides	232-241	time interval measuring enzyme-esterase A4	Bombyx mori	32-35
16864583-1	2006	Oxidative folding of insulin-like growth factor I (IGF-I) and single-chain insulin analogs proceeds via one- and two-disulfide intermediates.	Disulfides	117-126	insulin like growth factor 1	Homo sapiens	21-49
16864583-1	2006	Oxidative folding of insulin-like growth factor I (IGF-I) and single-chain insulin analogs proceeds via one- and two-disulfide intermediates.	Disulfides	117-126	insulin like growth factor 1	Homo sapiens	51-56
16864583-1	2006	Oxidative folding of insulin-like growth factor I (IGF-I) and single-chain insulin analogs proceeds via one- and two-disulfide intermediates.	Disulfides	117-126	insulin	Homo sapiens	21-28
16864583-2	2006	A predominant one-disulfide intermediate in each case contains the canonical A20-B19 disulfide bridge (cystines 18-61 in IGF-I and 19-85 in human proinsulin).	Disulfides	18-27	insulin like growth factor 1	Homo sapiens	121-126
16864583-2	2006	A predominant one-disulfide intermediate in each case contains the canonical A20-B19 disulfide bridge (cystines 18-61 in IGF-I and 19-85 in human proinsulin).	Disulfides	18-27	insulin	Homo sapiens	146-156
16864583-2	2006	A predominant one-disulfide intermediate in each case contains the canonical A20-B19 disulfide bridge (cystines 18-61 in IGF-I and 19-85 in human proinsulin).	Disulfides	85-94	insulin like growth factor 1	Homo sapiens	121-126
16864583-2	2006	A predominant one-disulfide intermediate in each case contains the canonical A20-B19 disulfide bridge (cystines 18-61 in IGF-I and 19-85 in human proinsulin).	Disulfides	85-94	insulin	Homo sapiens	146-156
16844690-3	2006	Previous studies indicated that the CD59 binding site in C9 was located within a 25-residue disulfide-bonded loop, and in C8alpha was located within a 51-residue sequence that overlaps the CD59 binding region of C9.	Disulfides	92-101	CD59 molecule (CD59 blood group)	Homo sapiens	36-40
16894147-7	2006	This module, which governs IGF1-binding specificity, shows negligible sequence identity, significantly more alpha-helix, an additional disulfide bond, and opposite electrostatic potential compared to that of the IGF1R.	Disulfides	135-144	insulin like growth factor 1	Homo sapiens	27-31
16922503-4	2006	A model is provided by insulin, a two-chain protein containing three disulfide bridges.	Disulfides	69-78	insulin	Homo sapiens	23-30
16978024-5	2006	Meanwhile, upon in vitro incubation with a redox-active sulfhydryl protein (thioredoxin), ebselen showed a strong electrophilic potential of mediating the formation of selenenylsulfide and intra- and intermolecular disulfide linkages within the protein.	Disulfides	215-224	thioredoxin 1	Rattus norvegicus	76-87
16877534-2	2006	We have used the Drosophila S2 cell reconstitution system for identification of disulfide bonds within and between CD79a (Ig-alpha) and CD79b (Ig-beta), the heterodimeric signal transducing element of the B cell antigen receptor (BCR).	Disulfides	80-89	Rho GTPase activating protein at 1A	Drosophila melanogaster	205-234
16916842-2	2006	The structure of pig C1-INH contains a two disulfide bridge pattern identical to the human C1-INH.	Disulfides	43-52	serpin family G member 1	Sus scrofa	21-27
16882993-7	2006	Contrary to previous reports that the denaturation of cord serum AFP is an irreversible process, these results clearly show the reversibility of AFP denaturation when refolded under a redox-controlled environment, which promotes correct oxidative disulfide shuffling.	Disulfides	247-256	alpha fetoprotein	Homo sapiens	145-148
16760476-2	2006	TCI consists of two domains that are structurally very similar, each containing three disulfide bonds arranged in an almost identical fashion.	Disulfides	86-95	latexin	Homo sapiens	0-3
16766796-5	2006	We explored the mechanism of the Txnip-thioredoxin interaction and present evidence that Txnip and thioredoxin form a stable disulfide-linked complex.	Disulfides	125-134	thioredoxin interacting protein	Homo sapiens	33-38
16760476-6	2006	This study demonstrates that IIIa and IIIb are 3-disulfide species containing the native disulfide pairings of the N- and C-terminal domains of TCI, respectively, and explains why the two domains of TCI fold sequentially and independently.	Disulfides	49-58	latexin	Homo sapiens	144-147
16760476-6	2006	This study demonstrates that IIIa and IIIb are 3-disulfide species containing the native disulfide pairings of the N- and C-terminal domains of TCI, respectively, and explains why the two domains of TCI fold sequentially and independently.	Disulfides	49-58	latexin	Homo sapiens	199-202
16766796-5	2006	We explored the mechanism of the Txnip-thioredoxin interaction and present evidence that Txnip and thioredoxin form a stable disulfide-linked complex.	Disulfides	125-134	thioredoxin interacting protein	Homo sapiens	89-94
16766796-6	2006	We identified two Txnip cysteines that are important for thioredoxin binding and showed that this interaction is consistent with a disulfide exchange reaction between oxidized Txnip and reduced thioredoxin.	Disulfides	131-140	thioredoxin interacting protein	Homo sapiens	18-23
16766796-6	2006	We identified two Txnip cysteines that are important for thioredoxin binding and showed that this interaction is consistent with a disulfide exchange reaction between oxidized Txnip and reduced thioredoxin.	Disulfides	131-140	thioredoxin interacting protein	Homo sapiens	176-181
16866381-1	2006	Human insulin, which consists of disulfide cross-linked A and B polypeptide chains, readily forms amyloid fibrils under slightly destabilizing conditions.	Disulfides	33-42	insulin	Homo sapiens	6-13
16507315-1	2006	Cell-surface protein disulfide isomerase (PDI) has been proposed to promote disulfide bond rearrangements in HIV-1 envelope protein (Env) that accompany Env-mediated fusion.	Disulfides	21-30	protein disulfide isomerase family A member 2	Homo sapiens	42-45
16920040-8	2006	From the comparison of pressure effects on ESA in native and reducing conditions of disulfide bridges, we demonstrate that the restriction of structural flexibility by disulfide bridges is an important factor for the reversibility of the pressure-induced aggregation.	Disulfides	84-93	paraoxonase 1	Homo sapiens	43-46
16920040-8	2006	From the comparison of pressure effects on ESA in native and reducing conditions of disulfide bridges, we demonstrate that the restriction of structural flexibility by disulfide bridges is an important factor for the reversibility of the pressure-induced aggregation.	Disulfides	168-177	paraoxonase 1	Homo sapiens	43-46
17037070-2	2006	After transient transfection, Western blot analysis under nonreducing condition demonstrated that co-expressed GP5 and M proteins could form disulfide-linked heterodimers (GP5-M) in transiently transfected BHK-21 cells.	Disulfides	141-150	platelet glycoprotein V	Mesocricetus auratus	111-114
17037070-2	2006	After transient transfection, Western blot analysis under nonreducing condition demonstrated that co-expressed GP5 and M proteins could form disulfide-linked heterodimers (GP5-M) in transiently transfected BHK-21 cells.	Disulfides	141-150	platelet glycoprotein V	Mesocricetus auratus	172-175
16129553-1	2006	Grapes and grape extracts were compared for inhibition of a growth-related and cancer-specific form of cell surface NADH oxidase with protein disulfide-thiol interchange activity designated tNOX from human cervical carcinoma (HeLa) cells and growth of HeLa and mouse mammary 4T1 cells in culture and transplanted tumors in mice.	Disulfides	142-151	ecto-NOX disulfide-thiol exchanger 2	Homo sapiens	190-194
16803874-3	2006	Using the oxidant pervanadate to mimic B cell receptor activation and thiol antioxidants such as N-acetylcysteine (NAC) and glutathione (GSH) we show that CD21 shedding is a redox-regulated process inducible by oxidation presumably through activation of a tyrosine kinase-mediated signal pathway involving protein kinase C (PKC), and by reducing agents that either directly activate the metalloprotease and/or modify intramolecular disulfide bridges within CD21 and thereby facilitate access to the cleavage site.	Disulfides	432-441	complement C3d receptor 2	Homo sapiens	155-159
16803874-4	2006	Lack of short consensus repeat 16 (SCR16) abolishes CD21 shedding, and opening of the disulfide bridge between cys-2 (Cys941) and cys-4 (Cys968) of SCR16 is a prerequisite for CD21 shedding.	Disulfides	86-95	complement C3d receptor 2	Homo sapiens	176-180
16507315-6	2006	We found that the ability of thioredoxin to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 Env gp120 and that thioredoxin also reduces disulfide bonds in gp120 directly in the absence of CD4.	Disulfides	158-167	CD4 molecule	Homo sapiens	73-76
16507315-7	2006	We discuss the implications of these observations for identification of molecules involved in disulfide rearrangements in Env during fusion.	Disulfides	94-103	endogenous retrovirus group W member 1, envelope	Homo sapiens	122-125
16507315-5	2006	We evaluated one such candidate, thioredoxin, a PDI family member reported to reduce a labile disulfide bond in CD4.	Disulfides	94-103	protein disulfide isomerase family A member 2	Homo sapiens	48-51
16507315-5	2006	We evaluated one such candidate, thioredoxin, a PDI family member reported to reduce a labile disulfide bond in CD4.	Disulfides	94-103	CD4 molecule	Homo sapiens	112-115
16507315-6	2006	We found that the ability of thioredoxin to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 Env gp120 and that thioredoxin also reduces disulfide bonds in gp120 directly in the absence of CD4.	Disulfides	55-64	CD4 molecule	Homo sapiens	73-76
16886636-2	2006	This peptide, known as the growth-inhibitory peptide (GIP), has two cysteine residues and demonstrates reduced antigrowth activity after long-term storage, presumably due to disulfide bond formation.	Disulfides	174-183	gastric inhibitory polypeptide	Homo sapiens	27-52
16886636-2	2006	This peptide, known as the growth-inhibitory peptide (GIP), has two cysteine residues and demonstrates reduced antigrowth activity after long-term storage, presumably due to disulfide bond formation.	Disulfides	174-183	gastric inhibitory polypeptide	Homo sapiens	54-57
16828895-6	2006	CCS also oxidizes an intrasubunit disulfide in SOD1.	Disulfides	34-43	superoxide dismutase 1	Homo sapiens	47-51
16807147-3	2006	Secretory Leucocyte Protease Inhibitor (SLPI) is a 107 amino acids protein with a high density of disulfide pairing (eight).	Disulfides	98-107	secretory leukocyte peptidase inhibitor	Homo sapiens	40-44
16807147-7	2006	In this study, conformational stability of SLPI has been investigated by the method of disulfide scrambling, which permits quantification of the native and denatured (scrambled) proteins by HPLC.	Disulfides	87-96	secretory leukocyte peptidase inhibitor	Homo sapiens	43-47
16828895-7	2006	Adventitious oxidation of the disulfide can lead to gross misfolding of immature forms of SOD1, particularly with SOD1 mutants linked to amyotrophic lateral sclerosis.	Disulfides	30-39	superoxide dismutase 1	Homo sapiens	90-94
16807147-9	2006	This impediment was further overcome by the development of a novel method which distinguishes the native and scrambled isomers of SLPI by exploiting the relative stability of their disulfide bonds.	Disulfides	181-190	secretory leukocyte peptidase inhibitor	Homo sapiens	130-134
16828895-7	2006	Adventitious oxidation of the disulfide can lead to gross misfolding of immature forms of SOD1, particularly with SOD1 mutants linked to amyotrophic lateral sclerosis.	Disulfides	30-39	superoxide dismutase 1	Homo sapiens	114-118
16857017-5	2006	Using LC-ESI-TOFMS and FTMS analysis, we determined that the major structural change in oxidized HSA in healthy human plasma is a disulfide-bonded cysteine at the thiol of Cys34 of reduced HSA.	Disulfides	130-139	albumin	Homo sapiens	97-100
16781456-3	2006	Here, we show that, in the rat alveolar macrophage NR8383 cell line, H(2)O(2) produced through the ADP-stimulated respiratory burst induces the formation of a disulfide bond between PTP1B and GSH that was detectable with an antibody to glutathione-protein complexes and was reversed by DTT addition.	Disulfides	159-168	protein tyrosine phosphatase, non-receptor type 1	Rattus norvegicus	182-187
16857017-5	2006	Using LC-ESI-TOFMS and FTMS analysis, we determined that the major structural change in oxidized HSA in healthy human plasma is a disulfide-bonded cysteine at the thiol of Cys34 of reduced HSA.	Disulfides	130-139	albumin	Homo sapiens	189-192
16784240-0	2006	Probing receptor binding activity of interleukin-8 dimer using a disulfide trap.	Disulfides	65-74	C-X-C motif chemokine ligand 8	Homo sapiens	37-50
16563642-8	2006	This band was sensitive to reducing agents (50 mM dithiothreitol) and showed sodium dodecylsulphate stability, suggesting the existence of disulfide-linked CB1 dimers in the membrane preparations.	Disulfides	139-148	cannabinoid receptor 1	Homo sapiens	156-159
16947075-1	2006	In milk, kappa-casein, a mixture of disulfide-bonded polymers, stabilizes and regulates the size of the unique colloidal complex of protein, Ca2+ and inorganic phosphate (Pi) termed the casein (CN) micelle.	Disulfides	36-45	casein kappa	Bos taurus	9-21
16644738-4	2006	In the disulfide-reduced form, A4V apoSOD1 exchanged like a "random coil" polypeptide at 20 degrees C and began to populate folded states at 4 degrees C. These local and global unfolding events could facilitate intermolecular protein-protein interactions that cause the aggregation or neurotoxicity of A4V SOD1.	Disulfides	7-16	superoxide dismutase 1	Homo sapiens	38-42
16633351-2	2006	We show that native disulfides in human interferon alpha-2b and in a fragment of an antibody to CD4(+) can be modified by site-specific bisalkylation of the two cysteine sulfur atoms to form a three-carbon PEGylated bridge.	Disulfides	20-30	CD4 molecule	Homo sapiens	96-99
16480776-6	2006	In addition, bat CD4 lacked cystein, which suggested that the disulfide bond could not be formed.	Disulfides	62-71	CD4 molecule	Homo sapiens	17-20
16566923-3	2006	Using hGC-1 purified from baculovirus Sf9 cells we demonstrated that hGC-1 is a secreted glycoprotein containing N-linked carbohydrate chains and forms disulfide-bonded multimers.	Disulfides	152-161	olfactomedin 4	Homo sapiens	69-74
16289048-6	2006	Comparison of cat myocilin to human myocilin shows a 87% similarity, including conservation of the N-terminal leucine zipper, N-linked glycosylation site, C-terminal olfactomedin domain, and all five cysteine residues thought to be involved in disulfide bond formation.	Disulfides	244-253	myocilin	Homo sapiens	18-26
16706977-6	2006	RESULTS: Both disulfide bond-stabilized variants had improved affinity for von Willebrand factor (VWF).	Disulfides	14-23	von Willebrand factor	Homo sapiens	75-96
16642033-4	2006	A mutant Bcl-2 with two cysteines introduced at positions predicted to result in a disulfide bond that would inhibit the mobility of alpha5-alpha6 helices (Bcl-2-S105C/E152C) was only active in a reducing environment.	Disulfides	83-92	BCL2 apoptosis regulator	Homo sapiens	9-14
16642033-4	2006	A mutant Bcl-2 with two cysteines introduced at positions predicted to result in a disulfide bond that would inhibit the mobility of alpha5-alpha6 helices (Bcl-2-S105C/E152C) was only active in a reducing environment.	Disulfides	83-92	BCL2 apoptosis regulator	Homo sapiens	156-161
16709847-2	2006	The disulfide bond in the second extracellular domain (D2) of CD4 is reduced on the cell surface, which leads to formation of disulfide-linked homodimers.	Disulfides	4-13	CD4 molecule	Homo sapiens	62-65
16709847-2	2006	The disulfide bond in the second extracellular domain (D2) of CD4 is reduced on the cell surface, which leads to formation of disulfide-linked homodimers.	Disulfides	126-135	CD4 molecule	Homo sapiens	62-65
16709847-5	2006	Mild reduction of the extracellular part of CD4 resulted in formation of disulfide-linked dimers, which supports the domain-swapped model.	Disulfides	73-82	CD4 molecule	Homo sapiens	44-47
16709847-6	2006	The functional significance of dimer formation for coreceptor function was tested using cells expressing wild-type or disulfide-bond mutant CD4.	Disulfides	118-127	CD4 molecule	Homo sapiens	140-143
16709847-7	2006	Eliminating the D2 disulfide bond markedly impaired CD4"s coreceptor function.	Disulfides	19-28	CD4 molecule	Homo sapiens	52-55
16709847-10	2006	These findings imply that disulfide-linked dimeric CD4 is the preferred coreceptor for binding to APC.	Disulfides	26-35	CD4 molecule	Homo sapiens	51-54
16706977-6	2006	RESULTS: Both disulfide bond-stabilized variants had improved affinity for von Willebrand factor (VWF).	Disulfides	14-23	von Willebrand factor	Homo sapiens	98-101
16706977-10	2006	In summary, introduction of engineered interdomain disulfides results in FVIIIa variants that resist spontaneous loss of activity while retaining susceptibility to APC proteolytic inactivation and maintaining VWF binding.	Disulfides	51-61	von Willebrand factor	Homo sapiens	209-212
16386761-3	2006	MGST1 activity was increased by ONOO(-) in the presence of high amounts of reducing agents including glutathione (GSH) and the activities increased by ONOO(-) or ONOO(-) plus GSH treatment were decreased by 30-40% by further incubation with dithiothreitol (DTT, reducing disulfide) or by sodium arsenite (reducing sulfenic acid).	Disulfides	271-280	microsomal glutathione S-transferase 1	Rattus norvegicus	0-5
16567808-4	2006	This implicates ERp57 in heavy chain disulfide formation, isomerization, or reduction as well as in the loading of peptides onto class I molecules.	Disulfides	37-46	protein disulfide isomerase family A member 3	Homo sapiens	16-21
16567808-6	2006	Depletion of ERp57 by RNA interference delayed heavy chain disulfide bond formation, slowed folding of the heavy chain alpha(3) domain, and caused slight delays in the transport of class I molecules from the endoplasmic reticulum to the Golgi apparatus.	Disulfides	59-68	protein disulfide isomerase family A member 3	Homo sapiens	13-18
16567808-9	2006	These studies demonstrate that ERp57 is involved in disulfide formation in vivo but do not support a role for ERp57 in peptide loading of class I molecules.	Disulfides	52-61	protein disulfide isomerase family A member 3	Homo sapiens	31-36
16700550-5	2006	Oxidant-treated iPLA(2)beta modifications were studied by LC-MS/MS analyses of tryptic digests and included DTT-reversible events, e.g., formation of disulfide bonds and sulfenic acids, and others not so reversed, e.g., formation of sulfonic acids, Trp oxides, and Met sulfoxides.	Disulfides	150-159	phospholipase A2 group VI	Homo sapiens	16-27
16622833-4	2006	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.	Disulfides	45-54	serpin family A member 1	Homo sapiens	31-35
16700550-8	2006	Intermolecular disulfide bond formation might also cause reversible inactivation because oxidant-treated iPLA(2)beta contains DTT-reducible oligomers, and oligomerization occurs with time- and temperature-dependent iPLA(2)beta inactivation that is attenuated by DTT or ATP.	Disulfides	15-24	phospholipase A2 group VI	Homo sapiens	105-116
16700550-8	2006	Intermolecular disulfide bond formation might also cause reversible inactivation because oxidant-treated iPLA(2)beta contains DTT-reducible oligomers, and oligomerization occurs with time- and temperature-dependent iPLA(2)beta inactivation that is attenuated by DTT or ATP.	Disulfides	15-24	phospholipase A2 group VI	Homo sapiens	215-226
16386761-6	2006	Since DTT can reduce S-nitrosothiol and disulfide bond to thiol, S-nitrosylation and a mixed disulfide bond formation of MGST1 were suggested.	Disulfides	93-102	microsomal glutathione S-transferase 1	Rattus norvegicus	121-126
16386761-7	2006	Thus, it was demonstrated that MGST1 is activated by reactive nitrogen species through a forming dimeric protein, mixed disulfide bond, nitrosylation and sulfenic acid.	Disulfides	120-129	microsomal glutathione S-transferase 1	Rattus norvegicus	31-36
16681396-1	2006	Secretory leucocyte protease inhibitor (SLPI) is a 107-amino acid protein with a high density of disulfide pairing (eight).	Disulfides	97-106	secretory leukocyte peptidase inhibitor	Homo sapiens	0-38
16581025-5	2006	The structure shows an oligomeric mode with a unique assembly mechanism by which the oligomerization of CLIC4 can be performed without any intramolecular disulfide bond formation.	Disulfides	154-163	chloride intracellular channel 4	Homo sapiens	104-109
16681385-6	2006	Treatment of p53-null Saos-2 cells with reversibly cationized p53 revealed that all events examined as indications of the activation of p53 in cells, such as reduction of disulfide bonds followed by tetramer formation, localization into the nucleus, induction of p53 target genes, and induction of apoptosis of cells, occurred.	Disulfides	171-180	tumor protein p53	Homo sapiens	13-16
16681385-6	2006	Treatment of p53-null Saos-2 cells with reversibly cationized p53 revealed that all events examined as indications of the activation of p53 in cells, such as reduction of disulfide bonds followed by tetramer formation, localization into the nucleus, induction of p53 target genes, and induction of apoptosis of cells, occurred.	Disulfides	171-180	tumor protein p53	Homo sapiens	62-65
16681396-1	2006	Secretory leucocyte protease inhibitor (SLPI) is a 107-amino acid protein with a high density of disulfide pairing (eight).	Disulfides	97-106	secretory leukocyte peptidase inhibitor	Homo sapiens	40-44
16681385-6	2006	Treatment of p53-null Saos-2 cells with reversibly cationized p53 revealed that all events examined as indications of the activation of p53 in cells, such as reduction of disulfide bonds followed by tetramer formation, localization into the nucleus, induction of p53 target genes, and induction of apoptosis of cells, occurred.	Disulfides	171-180	tumor protein p53	Homo sapiens	62-65
16681385-6	2006	Treatment of p53-null Saos-2 cells with reversibly cationized p53 revealed that all events examined as indications of the activation of p53 in cells, such as reduction of disulfide bonds followed by tetramer formation, localization into the nucleus, induction of p53 target genes, and induction of apoptosis of cells, occurred.	Disulfides	171-180	tumor protein p53	Homo sapiens	62-65
16681396-3	2006	Despite an exceedingly large number of possible folding intermediates ( approximately 46 million disulfide isomers) and their potential to complicate the refolding process, oxidative folding of SLPI turns out to be surprisingly simple and efficient.	Disulfides	97-106	secretory leukocyte peptidase inhibitor	Homo sapiens	194-198
16681396-4	2006	Complete oxidative folding and a near-quantitative recovery of the native SLPI can be achieved in a simple buffer solution using air oxidation without any supplementing thiol catalyst or redox agent, a phenomenon that has not yet been observed with other disulfide proteins.	Disulfides	255-264	secretory leukocyte peptidase inhibitor	Homo sapiens	74-78
16681396-6	2006	Nonetheless, studies of reductive unfolding of native SLPI and oxidative folding of a six-disulfide variant of SLPI enable us to propose an underlying mechanism accounting for the unique folding efficiency of SLPI in the absence of a redox agent.	Disulfides	90-99	secretory leukocyte peptidase inhibitor	Homo sapiens	111-115
16681396-6	2006	Nonetheless, studies of reductive unfolding of native SLPI and oxidative folding of a six-disulfide variant of SLPI enable us to propose an underlying mechanism accounting for the unique folding efficiency of SLPI in the absence of a redox agent.	Disulfides	90-99	secretory leukocyte peptidase inhibitor	Homo sapiens	111-115
16681396-7	2006	Our studies indicate that oxidative folding of SLPI undergoes heterogeneous populations of one-, two-, three-, four-, five-, six-, and seven-disulfide isomers, including two nativelike isomers, SLPI-6A and SLPI-7A, as transient intermediates.	Disulfides	141-150	secretory leukocyte peptidase inhibitor	Homo sapiens	47-51
16681396-8	2006	Formation of the last two native disulfide bonds leading to the conversion of SLPI-6A --&gt; SLPI-7A --&gt; N-SLPI is relatively slow and represents the final stage of oxidative folding.	Disulfides	33-42	secretory leukocyte peptidase inhibitor	Homo sapiens	78-82
16681396-8	2006	Formation of the last two native disulfide bonds leading to the conversion of SLPI-6A --&gt; SLPI-7A --&gt; N-SLPI is relatively slow and represents the final stage of oxidative folding.	Disulfides	33-42	secretory leukocyte peptidase inhibitor	Homo sapiens	93-97
16681396-8	2006	Formation of the last two native disulfide bonds leading to the conversion of SLPI-6A --&gt; SLPI-7A --&gt; N-SLPI is relatively slow and represents the final stage of oxidative folding.	Disulfides	33-42	secretory leukocyte peptidase inhibitor	Homo sapiens	93-97
16423450-1	2006	Eppin (epididymal protease inhibitor) is a member of the whey acidic protein (WAP)-type four-disulfide core (WFDC) gene family.	Disulfides	93-102	epididymal peptidase inhibitor	Homo sapiens	0-5
16423450-1	2006	Eppin (epididymal protease inhibitor) is a member of the whey acidic protein (WAP)-type four-disulfide core (WFDC) gene family.	Disulfides	93-102	epididymal peptidase inhibitor	Homo sapiens	7-36
16681396-9	2006	Most importantly, free cysteines of SLPI-6A and SLPI-7A also act as a thiol catalyst in promoting the disulfide shuffling of diverse non-native intermediates accumulated along the folding pathway.	Disulfides	102-111	secretory leukocyte peptidase inhibitor	Homo sapiens	36-40
16681396-9	2006	Most importantly, free cysteines of SLPI-6A and SLPI-7A also act as a thiol catalyst in promoting the disulfide shuffling of diverse non-native intermediates accumulated along the folding pathway.	Disulfides	102-111	secretory leukocyte peptidase inhibitor	Homo sapiens	48-52
16626818-1	2006	An insertion of residues in the third extracellular loop and a disulfide bond linking this loop to the N-terminal domain were identified in a structural model of a G-protein coupled receptor specific to angiotensin II (AT1 receptor), built in homology to the seven-transmembrane-helix bundle of rhodopsin.	Disulfides	63-72	angiotensinogen	Homo sapiens	203-217
16682620-2	2006	Highly specific thiol-containing inhibitors of the human inflammatory caspase-1 were identified by using disulfide trapping, a method for site-directed small-molecule discovery.	Disulfides	105-114	caspase 1	Homo sapiens	70-79
16682620-6	2006	Recently, disulfide trapping identified a similar small-molecule site and allosteric transition in the apoptotic caspase-7 that shares only a 23% sequence identity with caspase-1.	Disulfides	10-19	caspase 1	Homo sapiens	169-178
16547006-1	2006	Biglycan and decorin are two closely related proteoglycans whose protein cores contain leucine-rich repeats flanked by disulfides.	Disulfides	119-129	biglycan	Homo sapiens	0-8
16626818-1	2006	An insertion of residues in the third extracellular loop and a disulfide bond linking this loop to the N-terminal domain were identified in a structural model of a G-protein coupled receptor specific to angiotensin II (AT1 receptor), built in homology to the seven-transmembrane-helix bundle of rhodopsin.	Disulfides	63-72	rhodopsin	Homo sapiens	295-304
16626818-2	2006	Both the insertion and the disulfide bond were located close to an extracellular locus, flanked by the second extracellular loop (EC-2), the third extracellular loop (EC-3) and the N-terminal domain of the receptor; they contained residues identified by mutagenesis studies to bind the angiotensin II N-terminal segment (residues D1 and R2).	Disulfides	27-36	angiotensinogen	Homo sapiens	286-300
16626818-3	2006	It was postulated that the insertion and the disulfide bond, also found in other receptors such as those for bradykinin, endothelin, purine and other ligands, might play a role in regulating the function of the AT1 receptor.	Disulfides	45-54	kininogen 1	Homo sapiens	109-119
16771675-1	2006	Activation of the enzyme Cu,Zn-superoxide dismutase (SOD1) involves several posttranslational modifications including copper and zinc binding, as well as formation of the intramolecular disulfide bond.	Disulfides	186-195	superoxide dismutase 1	Homo sapiens	53-57
16636274-3	2006	Recent biochemical studies suggest that it is the immature disulfide-reduced forms of the familial ALS mutant SOD1 proteins that play a critical role; these forms tend to misfold, oligomerize, and readily undergo incorrect disulfide formation upon mild oxidative stress in vitro.	Disulfides	59-68	superoxide dismutase 1, soluble	Mus musculus	110-114
16636274-3	2006	Recent biochemical studies suggest that it is the immature disulfide-reduced forms of the familial ALS mutant SOD1 proteins that play a critical role; these forms tend to misfold, oligomerize, and readily undergo incorrect disulfide formation upon mild oxidative stress in vitro.	Disulfides	223-232	superoxide dismutase 1, soluble	Mus musculus	110-114
16636274-4	2006	Here we provide physiological support for this mechanism of aggregate formation and show that a significant fraction of the insoluble SOD1 aggregates in spinal cord of the ALS-model transgenic mice contain multimers cross-linked via intermolecular disulfide bonds.	Disulfides	248-257	superoxide dismutase 1, soluble	Mus musculus	134-138
16636274-5	2006	These insoluble disulfide-linked SOD1 multimers are found only in the spinal cord of symptomatic transgenic animals, are not observed in unafflicted tissue such as brain cortex and liver, and can incorporate WT SOD1 protein.	Disulfides	16-25	superoxide dismutase 1, soluble	Mus musculus	33-37
16636274-5	2006	These insoluble disulfide-linked SOD1 multimers are found only in the spinal cord of symptomatic transgenic animals, are not observed in unafflicted tissue such as brain cortex and liver, and can incorporate WT SOD1 protein.	Disulfides	16-25	superoxide dismutase 1, soluble	Mus musculus	211-215
16636275-6	2006	This conversion, observed in the mitochondrial fraction of the spinal cord, involved formation of insoluble SOD1 dimers and multimers that are crosslinked through intermolecular disulfide bonds via oxidation of cysteine residues in SOD1.	Disulfides	178-187	superoxide dismutase 1, soluble	Mus musculus	108-112
16636275-6	2006	This conversion, observed in the mitochondrial fraction of the spinal cord, involved formation of insoluble SOD1 dimers and multimers that are crosslinked through intermolecular disulfide bonds via oxidation of cysteine residues in SOD1.	Disulfides	178-187	superoxide dismutase 1, soluble	Mus musculus	232-236
16771675-3	2006	Recent in vitro and in vivo assays reveal that CCS not only delivers copper to SOD1 under stringent copper limitation, but it also facilitates the stepwise conversion of the disulfide-reduced immature SOD1 to the active disulfide-containing enzyme.	Disulfides	174-183	superoxide dismutase 1	Homo sapiens	79-83
16771675-3	2006	Recent in vitro and in vivo assays reveal that CCS not only delivers copper to SOD1 under stringent copper limitation, but it also facilitates the stepwise conversion of the disulfide-reduced immature SOD1 to the active disulfide-containing enzyme.	Disulfides	174-183	superoxide dismutase 1	Homo sapiens	201-205
16771675-3	2006	Recent in vitro and in vivo assays reveal that CCS not only delivers copper to SOD1 under stringent copper limitation, but it also facilitates the stepwise conversion of the disulfide-reduced immature SOD1 to the active disulfide-containing enzyme.	Disulfides	220-229	superoxide dismutase 1	Homo sapiens	79-83
16771675-3	2006	Recent in vitro and in vivo assays reveal that CCS not only delivers copper to SOD1 under stringent copper limitation, but it also facilitates the stepwise conversion of the disulfide-reduced immature SOD1 to the active disulfide-containing enzyme.	Disulfides	220-229	superoxide dismutase 1	Homo sapiens	201-205
16467570-3	2006	In addition, calnexin and calreticulin possess binding sites for ATP, Ca2+, non-native polypeptides and ERp57, an enzyme that catalyzes disulfide bond formation, reduction and isomerization.	Disulfides	136-145	calreticulin	Homo sapiens	26-38
16607115-5	2006	The activities of nuclear factor kappaB and activator protein 1 are stimulated not only by hydrogen peroxide, which is produced in tissues by regulated enzymatic processes, but also by an oxidative shift in thiol-disulfide redox status.	Disulfides	213-222	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	44-63
16677073-1	2006	Disulfide bonds are formed in the endoplasmic reticulum (ER) by sequential interchange reactions: Ero1alpha and Ero1beta transfer oxidative equivalents to protein disulfide isomerase (PDI), which in turn oxidizes cargo proteins.	Disulfides	0-9	endoplasmic reticulum oxidoreductase 1 beta	Homo sapiens	112-120
16677077-4	2006	The formation and rearrangement of disulfide bonds is modulated by a family of enzymes known as the thiol isomerases, which include protein disulfide isomerase (PDI), ERp5, ERp57, and ERp72.	Disulfides	35-44	protein disulfide isomerase family A member 3	Homo sapiens	173-178
16677077-4	2006	The formation and rearrangement of disulfide bonds is modulated by a family of enzymes known as the thiol isomerases, which include protein disulfide isomerase (PDI), ERp5, ERp57, and ERp72.	Disulfides	35-44	protein disulfide isomerase family A member 4	Homo sapiens	184-189
16441516-0	2006	Mapping superoxide dismutase 1 domains of non-native interaction: roles of intra- and intermolecular disulfide bonding in aggregation.	Disulfides	101-110	superoxide dismutase 1, soluble	Mus musculus	8-30
16441516-5	2006	By a cell-free aggregation assay, analysis of transgenic mouse tissues, and mutagenesis approaches, we found evidence that redox conditions may modulate SOD1 aggregation; reduction of the native intramolecular disulfide bonds may predispose SOD1 to unfolding and aggregation, whereas non-native intermolecular disulfide linkages may help stabilize aggregates in vivo.	Disulfides	210-219	superoxide dismutase 1, soluble	Mus musculus	153-157
16441516-5	2006	By a cell-free aggregation assay, analysis of transgenic mouse tissues, and mutagenesis approaches, we found evidence that redox conditions may modulate SOD1 aggregation; reduction of the native intramolecular disulfide bonds may predispose SOD1 to unfolding and aggregation, whereas non-native intermolecular disulfide linkages may help stabilize aggregates in vivo.	Disulfides	310-319	superoxide dismutase 1, soluble	Mus musculus	153-157
16481623-2	2006	This mechanism is particularly widespread in plants, where almost 200 proteins have been linked to thioredoxin (Trx), a widely distributed small regulatory disulfide protein.	Disulfides	156-165	thioredoxin H4-2	Triticum aestivum	99-110
16481623-2	2006	This mechanism is particularly widespread in plants, where almost 200 proteins have been linked to thioredoxin (Trx), a widely distributed small regulatory disulfide protein.	Disulfides	156-165	thioredoxin H4-2	Triticum aestivum	112-115
16455044-8	2006	The binding and uptake of [35S]L-homocystine, the disulfide homodimer of L-homocysteine, was mediated by systems X(AG), L, and ASC but not by system A.	Disulfides	50-59	PYD and CARD domain containing	Homo sapiens	127-130
16478632-1	2006	In mammals, interferon-gamma-inducible-lysosomal thiol reductase (GILT) has been demonstrated to play a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction, thus unfolding native protein Ag and facilitating subsequent cleavage by proteases.	Disulfides	202-211	interferon gamma	Homo sapiens	12-28
16478632-1	2006	In mammals, interferon-gamma-inducible-lysosomal thiol reductase (GILT) has been demonstrated to play a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction, thus unfolding native protein Ag and facilitating subsequent cleavage by proteases.	Disulfides	202-211	IFI30 lysosomal thiol reductase	Homo sapiens	66-70
16478632-5	2006	The deduced LycGILT possesses the typical structural feature of mammalian GILT, including an active-site CXXC motif, a GILT signature sequence CQHGX2ECX2NX4C, and other six cysteines responsible for the formation of disulfide bonds in the C-terminus.	Disulfides	216-225	IFI30 lysosomal thiol reductase	Homo sapiens	15-19
16755874-6	2006	A disulfide linkage occurs between Sg and Eppin, indicating the specificity of binding.	Disulfides	2-11	epididymal peptidase inhibitor	Homo sapiens	42-47
16624935-3	2006	The endogenous murine SOD1 (mSOD1) also lacks Cu and is disulfide reduced but is active and oxidized in mice expressing the low-level unstable mutants G85R and G127insTGGG.	Disulfides	56-65	superoxide dismutase 1, soluble	Mus musculus	22-26
16624935-3	2006	The endogenous murine SOD1 (mSOD1) also lacks Cu and is disulfide reduced but is active and oxidized in mice expressing the low-level unstable mutants G85R and G127insTGGG.	Disulfides	56-65	superoxide dismutase 1, soluble	Mus musculus	28-33
16624935-7	2006	mSOD1 was increased fourfold in mitochondria from high-level hSOD1 mice but was normal in those with low levels, suggesting that the Cu deficiency and disulfide reduction cause mitochondrial overloading.	Disulfides	151-160	superoxide dismutase 1, soluble	Mus musculus	0-5
16624935-7	2006	mSOD1 was increased fourfold in mitochondria from high-level hSOD1 mice but was normal in those with low levels, suggesting that the Cu deficiency and disulfide reduction cause mitochondrial overloading.	Disulfides	151-160	superoxide dismutase 1	Homo sapiens	61-66
16606344-1	2006	Growth and differentiation factor 5 (GDF-5) is a homodimeric protein stabilized by a single disulfide bridge between cysteine 465 in the respective monomers, as well as by three intramolecular cysteine bridges within each subunit.	Disulfides	92-101	growth differentiation factor 5	Homo sapiens	0-35
16606344-1	2006	Growth and differentiation factor 5 (GDF-5) is a homodimeric protein stabilized by a single disulfide bridge between cysteine 465 in the respective monomers, as well as by three intramolecular cysteine bridges within each subunit.	Disulfides	92-101	growth differentiation factor 5	Homo sapiens	37-42
16519733-9	2006	All of these modifications promote CD4 distension on SDS-PAGE analysis and indicate that, when CD4 inter-beta-sheet disulfides in the D1 and D4 Ig folds are disrupted, there is an unravelling of the oxidized form to an extended 59 kDa unfolded state.	Disulfides	116-126	CD4 molecule	Homo sapiens	35-38
16519733-9	2006	All of these modifications promote CD4 distension on SDS-PAGE analysis and indicate that, when CD4 inter-beta-sheet disulfides in the D1 and D4 Ig folds are disrupted, there is an unravelling of the oxidized form to an extended 59 kDa unfolded state.	Disulfides	116-126	CD4 molecule	Homo sapiens	95-98
16497834-0	2006	The chloroplast protein disulfide isomerase RB60 reacts with a regulatory disulfide of the RNA-binding protein RB47.	Disulfides	24-33	uncharacterized protein	Chlamydomonas reinhardtii	44-48
16497834-4	2006	We found that RB60 reacts with high selectivity with the disulfide of RB47, suggesting that the redox states of these two redox partners are coupled.	Disulfides	57-66	uncharacterized protein	Chlamydomonas reinhardtii	14-18
16516209-1	2006	The oxidoreductase ERp57 is involved in the formation and breaking of disulfide bonds in assembling proteins within the environment of the endoplasmic reticulum.	Disulfides	70-79	protein disulfide isomerase family A member 3	Homo sapiens	19-24
16516209-4	2006	Alkylation studies indicated that the central residue mutants retained the normal disulfide bond in the motif, whereas this disulfide bond became more resistant to reduction following addition of a third residue into the redox motif, demonstrating an optimum spacing within the redox-active motif of ERp57.	Disulfides	124-133	protein disulfide isomerase family A member 3	Homo sapiens	300-305
16519457-8	2006	The remaining S 2p component (approximately one-third of the sulfur layer), intermediate in binding energy between the other two components, is attributed to a chemisorbed species with a S binding configuration distinct from the majority alkylthiolate: for example, S bound to Pt bound to O, S with a different Pt coordination number, or S in an adsorbed disulfide.	Disulfides	355-364	ribosomal protein S2	Homo sapiens	14-18
16395663-0	2006	Influence of the disulfide bond configuration on the dynamics of the spin label attached to cytochrome c.	Disulfides	17-26	cytochrome c, somatic	Homo sapiens	92-104
16520549-0	2006	Structure-activity relationships of anti-HIV-1 peptides with disulfide linkage between D- and L-cysteine at positions i and i+3, respectively, derived from HIV-1 gp41 C-peptide.	Disulfides	61-70	insulin	Homo sapiens	167-176
16467570-3	2006	In addition, calnexin and calreticulin possess binding sites for ATP, Ca2+, non-native polypeptides and ERp57, an enzyme that catalyzes disulfide bond formation, reduction and isomerization.	Disulfides	136-145	protein disulfide isomerase family A member 3	Homo sapiens	104-109
16291754-3	2006	We have focused on two cysteine residues (Cys(88) and Cys(120)), which form a disulfide bridge in the N-terminal domain of calreticulin, on a tryptophan residue located in the carbohydrate binding site (Trp(302)), and on certain residues located at the tip of the "hairpin-like" P-domain of the protein (Glu(238), Glu(239), Asp(241), Glu(243), and Trp(244)).	Disulfides	78-87	calreticulin	Homo sapiens	123-135
16274992-1	2006	Disulfide Tethering was applied to the active site of human caspase-1, resulting in the discovery of a novel, tricyclic molecular fragment that selectively binds in S4.	Disulfides	0-9	caspase 1	Homo sapiens	60-69
16382486-3	2006	We have applied the reducing properties of 1,5-diaminonaphthalene (1,5-DAN) as a MALDI matrix to amino acid sequencing and disulfide bond mapping of human urotensin II possessing one disulfide bond, and human guanylin possessing two disulfide bonds.	Disulfides	183-192	NBL1, DAN family BMP antagonist	Homo sapiens	71-74
16382486-3	2006	We have applied the reducing properties of 1,5-diaminonaphthalene (1,5-DAN) as a MALDI matrix to amino acid sequencing and disulfide bond mapping of human urotensin II possessing one disulfide bond, and human guanylin possessing two disulfide bonds.	Disulfides	183-192	NBL1, DAN family BMP antagonist	Homo sapiens	71-74
16382486-7	2006	In addition, comparison of the theoretical and measured values of the mass differences between corresponding MS/MS product ions using 1,5-DAN and DHB narrowed down the possible disulfide bond arrangement candidates.	Disulfides	177-186	NBL1, DAN family BMP antagonist	Homo sapiens	138-141
16382486-8	2006	Consequently, 1,5-DAN as a reductive matrix facilitates rapid amino acid sequencing and disulfide mapping for peptides containing disulfide bonds.	Disulfides	88-97	NBL1, DAN family BMP antagonist	Homo sapiens	18-21
16382486-8	2006	Consequently, 1,5-DAN as a reductive matrix facilitates rapid amino acid sequencing and disulfide mapping for peptides containing disulfide bonds.	Disulfides	130-139	NBL1, DAN family BMP antagonist	Homo sapiens	18-21
16303754-8	2006	Our initial studies focused on disulfide bond formation between the SNARE motifs of Bet1p and Sec22p.	Disulfides	31-40	SNAP receptor SEC22	Saccharomyces cerevisiae S288C	94-100
16303754-11	2006	Using this disulfide cross-linking assay, we show that inhibition of transport with anti-Sly1p antibodies blocked formation of the Bet1p-Sec22p heterodimer.	Disulfides	11-20	syntaxin-binding protein	Saccharomyces cerevisiae S288C	89-94
16420479-6	2006	Wild-type and HT apoE3-NT form dimers in solution via an intermolecular disulfide bond.	Disulfides	72-81	apolipoprotein E	Homo sapiens	17-22
16446504-10	2006	These results strongly support the hypothesis that C255 and C511 form a disulfide bridge in human SGLT1 and that this disulfide bridge is involved in the conformational change of the free carrier.	Disulfides	72-81	solute carrier family 5 member 1	Homo sapiens	98-103
16446504-10	2006	These results strongly support the hypothesis that C255 and C511 form a disulfide bridge in human SGLT1 and that this disulfide bridge is involved in the conformational change of the free carrier.	Disulfides	118-127	solute carrier family 5 member 1	Homo sapiens	98-103
16444599-1	2006	Our work has identified a cancer-specific, cell surface and growth-related quinol oxidase with both NADH oxidase and protein disulfide-thiol interchange activities, a member of the ECTO-NOX protein family designated tNOX.	Disulfides	125-134	ecto-NOX disulfide-thiol exchanger 2	Homo sapiens	216-220
16291742-0	2006	Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form.	Disulfides	88-97	superoxide dismutase 1	Homo sapiens	6-10
16303754-11	2006	Using this disulfide cross-linking assay, we show that inhibition of transport with anti-Sly1p antibodies blocked formation of the Bet1p-Sec22p heterodimer.	Disulfides	11-20	SNAP receptor SEC22	Saccharomyces cerevisiae S288C	137-143
16240315-3	2006	Thiol to disulfide linkage generated a small dynamic library of bifunctional ligands in the presence of calmodulin, a protein with two independently mobile domains.	Disulfides	9-18	calmodulin 1	Homo sapiens	104-114
16387300-4	2006	TRX-1 is active at reducing protein disulfides in the presence of a heterologous thioredoxin reductase.	Disulfides	36-46	Thioredoxin-1	Caenorhabditis elegans	0-5
16240315-4	2006	The binding constant of the bifunctional ligand (disulfide) most amplified by the presence of calmodulin is nearly two orders of magnitude higher than that of the corresponding monofunctional ligand (thiol).	Disulfides	49-58	calmodulin 1	Homo sapiens	94-104
16183032-3	2006	After exiting the Golgi the propeptide is removed prior to final proteolytic processing in azurophil granules, resulting in formation of a symmetric MPO homodimer linked by a disulfide bond.	Disulfides	175-184	myeloperoxidase	Homo sapiens	149-152
16303761-3	2006	Stimulation of c-met requires two-chain, disulfide-linked HGF.	Disulfides	41-50	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	15-20
16388576-4	2006	Disulfide interchange, involving Cys184 on ThiF, then generates the ThiS-ThiF acyl disulfide, which functions as the sulfur donor for thiazole formation.	Disulfides	0-9	thioredoxin interacting protein	Homo sapiens	43-47
16257968-8	2006	Phage display of a C214A mutation of FGF-BP1 reduced binding to FGF-2, indicating the functional significance of this disulfide bond.	Disulfides	118-127	fibroblast growth factor 2	Homo sapiens	64-69
16388576-4	2006	Disulfide interchange, involving Cys184 on ThiF, then generates the ThiS-ThiF acyl disulfide, which functions as the sulfur donor for thiazole formation.	Disulfides	0-9	thioredoxin interacting protein	Homo sapiens	73-77
16387659-6	2006	In each TIM9.10 subunit, a signature "twin CX3C" motif forms two intramolecular disulfides.	Disulfides	80-90	translocase of inner mitochondrial membrane 9	Homo sapiens	8-12
16407158-0	2006	Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p.	Disulfides	11-21	ER oxidoreductin	Saccharomyces cerevisiae S288C	121-126
16407158-1	2006	Ero1p is a key enzyme in the disulfide bond formation pathway in eukaryotic cells in both aerobic and anaerobic environments.	Disulfides	29-38	ER oxidoreductin	Saccharomyces cerevisiae S288C	0-5
16388676-2	2006	[reaction: see text] Diphenyl diselenide (and disulfide) undergo facile reaction with indium(I) iodide and the corresponding intermediate complex condenses in situ with a variety of substituted vinyl bromides in the presence of a catalytic amount of tetrakis(triphenylphosphine)palladium(0) [Pd(PPh3)4] in THF at room temperature to produce vinylic selenides and sulfides in good yields.	Disulfides	46-55	caveolin 1	Homo sapiens	295-299
16343416-0	2006	Disulfide between Cys392 and Cys438 of human serum albumin is redox-active, which is responsible for the thioredoxin-supported lipid peroxidase activity.	Disulfides	0-9	albumin	Homo sapiens	45-58
17019437-1	2006	A phage-displayed random 7-mer disulfide bridge-constrained peptide library was used to map the surface of the RhoA GTPase and to find peptides able to recognize RhoA switch regions.	Disulfides	31-40	ras homolog family member A	Homo sapiens	111-115
17019437-1	2006	A phage-displayed random 7-mer disulfide bridge-constrained peptide library was used to map the surface of the RhoA GTPase and to find peptides able to recognize RhoA switch regions.	Disulfides	31-40	ras homolog family member A	Homo sapiens	162-166
16391466-7	2006	As alpha-lipoic acid contains a disulfide bond, it may react with the SH group of CPR.	Disulfides	32-41	cytochrome p450 oxidoreductase	Homo sapiens	82-85
16877258-3	2006	The aim of this review article is to address new aspects of ABCG2 related to redox biology, namely the posttranslational modification (intra- and intermolecular disulfide bond formation) of ABCG2 protein and the transport of porphyrin and chlorophyll metabolites, as well as the high-speed screening and QSAR analysis method to evaluate ABCG2-drug interactions.	Disulfides	161-170	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	60-65
15985360-4	2006	RP-HPLC and mass spectrometric analysis indicated that the proinsulin contained the correct disulfide bridging pattern.	Disulfides	92-101	insulin	Homo sapiens	59-69
16782456-6	2006	CaR is a member of Family C GPCRs, having a large extracellular agonist binding domain, and functioning as a disulfide-linked dimer.	Disulfides	109-118	calcium sensing receptor	Homo sapiens	0-3
16877258-3	2006	The aim of this review article is to address new aspects of ABCG2 related to redox biology, namely the posttranslational modification (intra- and intermolecular disulfide bond formation) of ABCG2 protein and the transport of porphyrin and chlorophyll metabolites, as well as the high-speed screening and QSAR analysis method to evaluate ABCG2-drug interactions.	Disulfides	161-170	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	190-195
16877258-3	2006	The aim of this review article is to address new aspects of ABCG2 related to redox biology, namely the posttranslational modification (intra- and intermolecular disulfide bond formation) of ABCG2 protein and the transport of porphyrin and chlorophyll metabolites, as well as the high-speed screening and QSAR analysis method to evaluate ABCG2-drug interactions.	Disulfides	161-170	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	190-195
17003517-3	2006	These include the molecular chaperones calnexin and calreticulin, which enhance the proper folding and subunit assembly of class I molecules and also retain assembly intermediates within the ER; ERp57, a thiol oxidoreductase that promotes heavy chain disulfide formation and proper assembly of the peptide loading complex; tapasin, which recruits class I molecules to the TAP peptide transporter and enhances the loading of high affinity peptide ligands; and Bap31, which is involved in clustering assembled class I molecules at ER exit sites for export along the secretory pathway.	Disulfides	251-260	calreticulin	Homo sapiens	52-64
17003517-3	2006	These include the molecular chaperones calnexin and calreticulin, which enhance the proper folding and subunit assembly of class I molecules and also retain assembly intermediates within the ER; ERp57, a thiol oxidoreductase that promotes heavy chain disulfide formation and proper assembly of the peptide loading complex; tapasin, which recruits class I molecules to the TAP peptide transporter and enhances the loading of high affinity peptide ligands; and Bap31, which is involved in clustering assembled class I molecules at ER exit sites for export along the secretory pathway.	Disulfides	251-260	protein disulfide isomerase family A member 3	Homo sapiens	195-200
16531095-2	2006	Cells secrete TGF-beta as a latent protein complex, consisting of disulfide-bonded homodimers of growth factor and latency-associated propeptide.	Disulfides	66-75	transforming growth factor beta 1	Homo sapiens	14-22
16528971-6	2006	These results strongly suggest that Cys603 is prerequisite for homodimer formation of ABCG2 via a disulfide bond.	Disulfides	98-107	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	86-91
16409464-1	2006	The D3 domain of von Willebrand factor (VWF) is involved in the multimerization process of the protein through the formation of disulfide bridges.	Disulfides	128-137	von Willebrand factor	Homo sapiens	17-38
17192673-4	2006	ColQ characterizes the collagen-tailed forms (Aforms) of AChE and butyrylcholinesterase (BChE), which are localized in the basal lamina at neuromuscular junctions (NMJs) of vertebrates (Krejci et al., 1999); in these molecules (A4, A8, A12), one, two, or three tetramers of catalytic subunits are disulfide-linked to the strands of a triple helix of ColQ collagen.	Disulfides	297-306	acetylcholinesterase (Cartwright blood group)	Homo sapiens	57-61
16409464-1	2006	The D3 domain of von Willebrand factor (VWF) is involved in the multimerization process of the protein through the formation of disulfide bridges.	Disulfides	128-137	von Willebrand factor	Homo sapiens	40-43
17072021-3	2006	In addition, they interact with non-native conformers of glycoprotein polypeptide chains to prevent aggregation and recruit the thiol oxidoreductase ERp57 to catalyze glycoprotein disulfide formation/isomerization.	Disulfides	180-189	protein disulfide isomerase family A member 3	Homo sapiens	149-154
16243379-0	2006	Growth hormone administration to aged animals reduces disulfide glutathione levels in hippocampus.	Disulfides	54-63	growth hormone 1	Homo sapiens	0-14
16373475-0	2006	Enthalpic and entropic contributions mediate the role of disulfide bonds on the conformational stability of interleukin-4.	Disulfides	57-66	interleukin 4	Homo sapiens	108-121
16292667-3	2006	Endoplasmic reticulum (ER) oxidoreductin encoded by the ERO1 gene of the yeast Saccharomyces cerevisiae is essential for the formation of protein disulfide bonds in the ER and for cell viability.	Disulfides	146-155	ER oxidoreductin	Saccharomyces cerevisiae S288C	56-60
16877880-3	2006	In addition, Lp(a) contains a unique hydrophilic, carbohydrate-rich protein, apo(a), linked to apoB through a single disulfide bond connecting the C-terminal regions of the two proteins.	Disulfides	117-126	apolipoprotein B	Homo sapiens	95-99
16373475-3	2006	Here, we perform a detailed analysis of the role of disulfides in the conformational stability of human Interleukin-4 (IL4), a four-helix bundle protein.	Disulfides	52-62	interleukin 4	Homo sapiens	104-117
16373475-3	2006	Here, we perform a detailed analysis of the role of disulfides in the conformational stability of human Interleukin-4 (IL4), a four-helix bundle protein.	Disulfides	52-62	interleukin 4	Homo sapiens	119-122
16800793-1	2006	Insulin is a double-chain (designated A and B chain respectively) protein hormone containing three disulfides, while insulin is synthesized in vivo as a single-chain precursor and folded well before being released from B-cells.	Disulfides	99-109	insulin	Homo sapiens	0-7
16373475-4	2006	In order to evaluate the contribution of two out of the three disulfides to the structure and stability of IL4, two IL4 mutants, C3T-IL4 and C24T-IL4, were used.	Disulfides	62-72	interleukin 4	Homo sapiens	107-110
16800793-2	2006	Although the structure and function of insulin have been well characterized, the progress in oxidative folding pathway studies of insulin has been very slow, mainly due to the difficulties brought about by its disulfide-linked double-chain structure.	Disulfides	210-219	insulin	Homo sapiens	130-137
16373475-10	2006	Thus, disulfide bridges in IL4 play a critical role in maintaining the thermodynamic stability and core packing of the helix bundle.	Disulfides	6-15	interleukin 4	Homo sapiens	27-30
16204238-7	2005	We demonstrate that the single extracellular cysteine residue in the tail (Cys-51) could form a disulfide bond, both in our recombinant protein and in physiologically expressed 4-1BBL.	Disulfides	96-105	TNF superfamily member 9	Homo sapiens	177-183
17220939-1	2006	Orexin A (OxA), a recently discovered neuropeptide, is synthesized mainly by neurons located in the posterolateral hypothalamus and is a 33 amino acid peptide with N-terminal pyroglutamyl residue and two inter-chain disulfide bonds.	Disulfides	216-225	hypocretin neuropeptide precursor	Rattus norvegicus	0-8
16407063-3	2006	Unique structural features of the N- and C-terminal regions, and the disulfide bond location, distinguish TSPN-1 from the laminin G domain and other concanavalin A-like lectins/glucanases superfamily members.	Disulfides	69-78	thrombospondin 1	Homo sapiens	106-112
16219769-4	2005	Yap1p localization to the nucleus requires the oxidant-specific formation of disulfide bonds in the N-terminal cysteine-rich domain (N-CRD) and/or the C-terminal cysteine-rich domain (C-CRD).	Disulfides	77-86	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	0-5
16357186-4	2005	This event is most likely due to a peculiar surviving pathway of these cells involving: (a) the formation of mixed disulfides between reduced glutathione (GSH) and protein thiols, (b) a higher and inducible glutathione peroxidase activity, and/or (c) an efficient modulation of the phospho-active levels of the extracellular signal-regulated kinases 1 and 2 (ERK 1/2).	Disulfides	115-125	mitogen-activated protein kinase 1	Homo sapiens	311-357
16357186-4	2005	This event is most likely due to a peculiar surviving pathway of these cells involving: (a) the formation of mixed disulfides between reduced glutathione (GSH) and protein thiols, (b) a higher and inducible glutathione peroxidase activity, and/or (c) an efficient modulation of the phospho-active levels of the extracellular signal-regulated kinases 1 and 2 (ERK 1/2).	Disulfides	115-125	mitogen-activated protein kinase 3	Homo sapiens	359-366
16219769-6	2005	This dually disulfide-bonded structure has been argued to mask the nuclear export signal in the C-CRD that would otherwise prevent Yap1p nuclear accumulation.	Disulfides	12-21	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	131-136
16219769-10	2005	These data demonstrate that the dually disulfide-bonded Yap1p N- and C-CRDs form a bifunctional protein domain controlling both nuclear localization and transcriptional activation.	Disulfides	39-48	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	56-61
16367905-1	2005	Breast cancer resistance protein (BCRP/ABCG2) is a half-molecule ATP-binding cassette transporter that we have previously suggested might function as a homodimer, bridged by disulfide bonds.	Disulfides	174-183	ATP-binding cassette, sub-family A (ABC1), member 13	Mus musculus	65-97
16261627-0	2005	A novel DFNA9 mutation in the vWFA2 domain of COCH alters a conserved cysteine residue and intrachain disulfide bond formation resulting in progressive hearing loss and site-specific vestibular and central oculomotor dysfunction.	Disulfides	102-111	cochlin	Homo sapiens	8-13
16261627-0	2005	A novel DFNA9 mutation in the vWFA2 domain of COCH alters a conserved cysteine residue and intrachain disulfide bond formation resulting in progressive hearing loss and site-specific vestibular and central oculomotor dysfunction.	Disulfides	102-111	cochlin	Homo sapiens	46-50
16199504-8	2005	Results of these calculations are in good agreement with the x-ray data available for the dark-adapted rhodopsin as well as with the available experimental biophysical data on the disulfide-linked mutants of rhodopsin.	Disulfides	180-189	rhodopsin	Homo sapiens	103-112
16199504-8	2005	Results of these calculations are in good agreement with the x-ray data available for the dark-adapted rhodopsin as well as with the available experimental biophysical data on the disulfide-linked mutants of rhodopsin.	Disulfides	180-189	rhodopsin	Homo sapiens	208-217
16336686-5	2005	However, it was not clear what role, if any, the disulfide bonds play in the membrane topology of the L1R protein.	Disulfides	49-58	IMV membrane protein	Vaccinia virus	102-105
16336686-8	2005	These results suggest that protein disulphide isomerases may be involved in reorganization of disulfide bonds within the L1R protein.	Disulfides	94-103	IMV membrane protein	Vaccinia virus	121-124
16287128-7	2005	Co-immunoprecipitation experiments demonstrated that the mutant A-domains were specifically associated with ERp72, a chaperone protein known to be involved in mediating disulfide bond formation.	Disulfides	169-178	protein disulfide isomerase family A member 4	Homo sapiens	108-113
16186172-4	2005	Here we show that increased GAPDH disulfide bonding is observed in detergent-insoluble extracts from AD patient and transgenic AD mouse brain tissue compared with age-matched controls.	Disulfides	34-43	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	28-33
16125204-3	2005	The MGST1 activity increased by gallic acid was decreased by further incubation with sodium arsenite, a sulfenic acid reducing agent, but was not with dithiothreitol, a disulfide bond reducing agent.	Disulfides	169-178	microsomal glutathione S-transferase 1	Rattus norvegicus	4-9
16285718-7	2005	Rituximab binding is abolished by reduction and alkylation of CD20, with data consistent with the proposed antibody epitope being within the disulfide-bonded loop formed between cysteine residues 167 and 183.	Disulfides	141-150	keratin 20	Homo sapiens	62-66
16285718-8	2005	Disulfide-bond-dependent antibody binding is partially recovered following reoxidation of reduced CD20.	Disulfides	0-9	keratin 20	Homo sapiens	98-102
16247791-8	2005	In contrast, a similar removal of the fourth disulfide bridge of Pi1, another scorpion toxin from the same structural family, has no impact on its 3D structure, pharmacology, or channel interaction.	Disulfides	45-54	serpin family A member 1	Homo sapiens	65-68
16302782-5	2005	It seemed likely that, at 800 MPa, the formation of a beta-LG disulfide-bonded network preceded the formation of disulfide bonds between alpha-LA or BSA and beta-LG to form multiprotein aggregates, possibly because the disulfide bonds of alpha-LA and BSA are less exposed than those of beta-LG either during or after pressure treatment.	Disulfides	62-71	lactalbumin alpha	Homo sapiens	137-145
16302782-5	2005	It seemed likely that, at 800 MPa, the formation of a beta-LG disulfide-bonded network preceded the formation of disulfide bonds between alpha-LA or BSA and beta-LG to form multiprotein aggregates, possibly because the disulfide bonds of alpha-LA and BSA are less exposed than those of beta-LG either during or after pressure treatment.	Disulfides	113-122	lactalbumin alpha	Homo sapiens	137-145
16302782-5	2005	It seemed likely that, at 800 MPa, the formation of a beta-LG disulfide-bonded network preceded the formation of disulfide bonds between alpha-LA or BSA and beta-LG to form multiprotein aggregates, possibly because the disulfide bonds of alpha-LA and BSA are less exposed than those of beta-LG either during or after pressure treatment.	Disulfides	113-122	lactalbumin alpha	Homo sapiens	137-145
16107343-6	2005	Because the transporter migrated as a dimer in SDS-PAGE, when only Cys-603 was present (C592A-C608A), the data suggest that Cys-603 forms a symmetrical intermolecular disulfide bridge in the ABCG2 homodimer that is not essential for protein expression and function.	Disulfides	167-176	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	191-196
16107343-10	2005	This supports the conclusion that Cys-592 and Cys-608 form an intramolecular disulfide bridge in ABCG2 that is critical for substrate specificity.	Disulfides	77-86	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	97-102
16107343-0	2005	Identification of intra- and intermolecular disulfide bridges in the multidrug resistance transporter ABCG2.	Disulfides	44-53	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	102-107
16107343-12	2005	Altogether, our data are consistent with a scenario in which an inter- and an intramolecular disulfide bridge together are of fundamental importance for the structural and functional integrity of ABCG2.	Disulfides	93-102	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	196-201
16107343-2	2005	ABCG2 is believed to be a functional homodimer that has been proposed to be linked by disulfide bridges.	Disulfides	86-95	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	0-5
16131495-8	2005	We documented the assembly properties of a Ure2p variant in which a disulfide bond was established between the N- and C-terminal domains and showed that it possesses assembly properties indistinguishable from those of wild-type Ure2p.	Disulfides	68-77	glutathione peroxidase	Saccharomyces cerevisiae S288C	43-48
16131495-8	2005	We documented the assembly properties of a Ure2p variant in which a disulfide bond was established between the N- and C-terminal domains and showed that it possesses assembly properties indistinguishable from those of wild-type Ure2p.	Disulfides	68-77	glutathione peroxidase	Saccharomyces cerevisiae S288C	228-233
16254321-1	2005	The surface (SU) and transmembrane (TM) subunits of Moloney murine leukemia virus (Mo-MLV) Env are disulfide linked.	Disulfides	99-108	endogenous retrovirus group W member 1, envelope	Homo sapiens	91-94
16307478-6	2005	For the catalytic cycle of TPx1, we conclude that oxidation of the peroxidatic Cys50 by the oxidising substrate is followed by the formation of an intermolecular disulfide bond between Cys50 and Cys170" of the second subunit, which is then attacked by an external electron donor such as thioredoxin or plasmoredoxin.	Disulfides	162-171	peroxiredoxin 2	Homo sapiens	27-31
16229492-9	2005	Cys149 and Cys153 formed an intramolecular disulfide in the AS/GAPDH incubates.	Disulfides	43-52	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	63-68
16260597-0	2005	Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.	Disulfides	6-15	protein disulfide isomerase family A member 3	Homo sapiens	111-116
16272376-8	2005	TraN appears to require both intra- and intermolecular disulfide bond formation for its stability and structure as demonstrated by its instability in a dsbA mutant and its aberrant migration on SDS-polyacrylamide gels under non-reducing conditions or by cross-linking with bis(sulfosuccinimidyl)suberate (BS3).	Disulfides	55-64	tRNA-Ala (anticodon TGC) 7-1	Homo sapiens	0-4
16081415-0	2005	SIRPbeta1 is expressed as a disulfide-linked homodimer in leukocytes and positively regulates neutrophil transepithelial migration.	Disulfides	28-37	superoxide dismutase 1	Homo sapiens	45-54
16081415-5	2005	Furthermore, although SIRPalpha (Bit/PTPNS-1) is expressed as a monomer, we showed that SIRPbeta1 is expressed on the cell surface as a disulfide-linked homodimer with bond formation mediated by Cys-320 in the membrane-proximal Ig loop.	Disulfides	136-145	superoxide dismutase 1	Homo sapiens	153-162
16115607-5	2005	However, minicollagen XXI was secreted as disulfide-bonded homotrimers by coexpression with prolyl 4-hydroxylase in the stably transfected Drosophila S2 cells.	Disulfides	42-51	HIF prolyl hydroxylase	Drosophila melanogaster	92-112
16115607-6	2005	Minicollagen XXI coexpressed with prolyl 4-hydroxylase contained sufficient amounts of hydroxyproline to form thermal stable pepsin-resistant triple helices consisting of both interchain and non-interchain disulfide-bonded trimers.	Disulfides	206-215	HIF prolyl hydroxylase	Drosophila melanogaster	34-54
16217027-8	2005	The addition of NADPH to the TrxR2 crystals resulted in a color change, indicating reduction of the active-site disulfide and formation of a species presumed to be the flavin-thiolate charge transfer complex.	Disulfides	112-121	thioredoxin reductase 2	Homo sapiens	29-34
16193070-0	2005	Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex.	Disulfides	32-41	TAP binding protein	Homo sapiens	0-7
16193070-0	2005	Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex.	Disulfides	32-41	protein disulfide isomerase family A member 3	Homo sapiens	12-17
16193070-1	2005	We previously showed that the major histocompatibility complex (MHC) class I chaperone tapasin can be detected as a mixed disulfide with the thiol-oxidoreductase ERp57.	Disulfides	122-131	TAP binding protein	Homo sapiens	87-94
16215634-6	2005	In general, replacement of B8Gly by other amino acids causes significant detriment to the foldability of single-chain insulin: the conformations of the three B8 mutants are essentially different from that of wild-type molecules as revealed by circular dichroism; their disulfide stabilities in redox buffer are significantly decreased; their in vitro refolding efficiencies are decreased approximately two folds; the structural stabilities of the mutants with Ser or Thr substitution are decreased significantly, while Leu substitution has little effect as measured by equilibrium guanidine denaturation.	Disulfides	269-278	insulin	Homo sapiens	118-125
16193070-2	2005	Here we show that tapasin is a unique and preferred substrate, a substantial majority of which is disulfide-linked to ERp57 within the cell.	Disulfides	98-107	TAP binding protein	Homo sapiens	18-25
16193070-2	2005	Here we show that tapasin is a unique and preferred substrate, a substantial majority of which is disulfide-linked to ERp57 within the cell.	Disulfides	98-107	protein disulfide isomerase family A member 3	Homo sapiens	118-123
16193070-8	2005	Thus, tapasin association specifically inhibits the escape pathway required for disulfide-bond isomerization within conventional protein substrates, suggesting a specific structural role for ERp57 within the MHC class I peptide-loading complex.	Disulfides	80-89	TAP binding protein	Homo sapiens	6-13
16193070-8	2005	Thus, tapasin association specifically inhibits the escape pathway required for disulfide-bond isomerization within conventional protein substrates, suggesting a specific structural role for ERp57 within the MHC class I peptide-loading complex.	Disulfides	80-89	protein disulfide isomerase family A member 3	Homo sapiens	191-196
16221844-9	2005	Disulfide bonds formed in 5-HT3A/K81C/A304C and 5-HT3A/K81C/I305C when coexpressed with 5-HT3B.	Disulfides	0-9	5-hydroxytryptamine receptor 3A	Homo sapiens	26-32
16221844-9	2005	Disulfide bonds formed in 5-HT3A/K81C/A304C and 5-HT3A/K81C/I305C when coexpressed with 5-HT3B.	Disulfides	0-9	5-hydroxytryptamine receptor 3A	Homo sapiens	48-54
16188974-3	2005	We demonstrate here that the cellular protease cathepsin L is involved in converting the Hendra virus precursor F protein (F(0)) to the active F(1) + F(2) disulfide-linked heterodimer.	Disulfides	155-164	cathepsin L	Homo sapiens	47-58
16115028-4	2005	The catalytic thiol-protein oxidoreductase (TPOR) activity of MIF is mediated by a Cys-Ala-Leu-Cys active site between residues 57 and 60 that can undergo reversible intramolecular disulfide formation.	Disulfides	181-190	MPL proto-oncogene, thrombopoietin receptor	Homo sapiens	14-42
16115028-4	2005	The catalytic thiol-protein oxidoreductase (TPOR) activity of MIF is mediated by a Cys-Ala-Leu-Cys active site between residues 57 and 60 that can undergo reversible intramolecular disulfide formation.	Disulfides	181-190	MPL proto-oncogene, thrombopoietin receptor	Homo sapiens	44-48
16138305-0	2005	Characterisation of disulfide-bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR.	Disulfides	20-29	lysozyme	Homo sapiens	68-76
16138305-0	2005	Characterisation of disulfide-bond dynamics in non-native states of lysozyme and its disulfide deletion mutants by NMR.	Disulfides	85-94	lysozyme	Homo sapiens	68-76
16138305-1	2005	This report describes NMR-spectroscopic investigations of the conformational dynamics of disulfide bonds in hen-egg-white lysozyme substitution mutants.	Disulfides	89-98	lysozyme	Homo sapiens	122-130
16138305-3	2005	The NMR analysis of heteronuclear 15N-relaxation rates shows that the barrier to disulfide-bond isomerisation can vary substantially in different lysozyme mutants and depends on the residual structure present in these states.	Disulfides	81-90	lysozyme	Homo sapiens	146-154
16138305-4	2005	The investigations reveal cooperativity in the modulation of micro- to millisecond dynamics that is due to the presence of multiple disulfide bridges in lysozyme.	Disulfides	132-141	lysozyme	Homo sapiens	153-161
16172913-5	2005	Although expression of B. mori calreticulin was affected by disturbances in intracellular calcium levels, other ER stress conditions such as inhibition of intracellular protein transport, reduction of disulfide formation, glycosylation inhibition, heat shock and oxidative stress did not disrupt induction of B. mori calreticulin.	Disulfides	201-210	calreticulin	Bombyx mori	31-43
15972297-3	2005	We show by computer simulation that the two cysteine residues of Bax may form disulfide bridges, producing conformational changes that favor Bax translocation.	Disulfides	78-87	BCL2 associated X, apoptosis regulator	Homo sapiens	65-68
15972297-3	2005	We show by computer simulation that the two cysteine residues of Bax may form disulfide bridges, producing conformational changes that favor Bax translocation.	Disulfides	78-87	BCL2 associated X, apoptosis regulator	Homo sapiens	141-144
15958382-3	2005	Influences that may destabilize SOD1 in vivo include impaired metal ion binding, reduction of the intrasubunit disulfide bond, or oxidative modification.	Disulfides	111-120	superoxide dismutase 1, soluble	Mus musculus	32-36
16043170-10	2005	beta1-, beta2- and beta3-adrenoceptors contain extracellular cysteine residues susceptible to oxidation (i.e., disulfide-bridge formation) whereas only the beta1- and beta2-adrenoceptors contain extracellular tyrosine residues susceptible to nitration.	Disulfides	111-120	adrenoceptor beta 1	Rattus norvegicus	0-38
15958382-7	2005	These findings suggest that a susceptibility to the cellular disulfide reducing environment and zinc loss may convert otherwise stable SOD1 mutants into metal-deficient forms with locally destabilized electrostatic and zinc-binding loops.	Disulfides	61-70	superoxide dismutase 1, soluble	Mus musculus	135-139
15971207-3	2005	For this purpose, we focused on two scorpion peptides, the well-characterized maurotoxin with its variant Pi1-like disulfide bridging (MTX(Pi1)), used as a molecular template, and butantoxin (BuTX), used as an N-terminal domain provider.	Disulfides	115-124	serpin family A member 1	Homo sapiens	106-109
15971207-6	2005	Transfer of the BuTX N-terminal domain to MTX(Pi1) results in a chimera with five disulfide bridges (BuTX-MTX(Pi1)) that exhibits 22-fold greater affinity for Kv1.2 than MTX(Pi1) itself, in spite of the lower affinity of BuTX as compared to MTX(Pi1).	Disulfides	82-91	serpin family A member 1	Homo sapiens	46-49
15971207-6	2005	Transfer of the BuTX N-terminal domain to MTX(Pi1) results in a chimera with five disulfide bridges (BuTX-MTX(Pi1)) that exhibits 22-fold greater affinity for Kv1.2 than MTX(Pi1) itself, in spite of the lower affinity of BuTX as compared to MTX(Pi1).	Disulfides	82-91	serpin family A member 1	Homo sapiens	110-113
15971207-6	2005	Transfer of the BuTX N-terminal domain to MTX(Pi1) results in a chimera with five disulfide bridges (BuTX-MTX(Pi1)) that exhibits 22-fold greater affinity for Kv1.2 than MTX(Pi1) itself, in spite of the lower affinity of BuTX as compared to MTX(Pi1).	Disulfides	82-91	potassium voltage-gated channel subfamily A member 2	Homo sapiens	159-164
15971207-6	2005	Transfer of the BuTX N-terminal domain to MTX(Pi1) results in a chimera with five disulfide bridges (BuTX-MTX(Pi1)) that exhibits 22-fold greater affinity for Kv1.2 than MTX(Pi1) itself, in spite of the lower affinity of BuTX as compared to MTX(Pi1).	Disulfides	82-91	serpin family A member 1	Homo sapiens	110-113
15971207-6	2005	Transfer of the BuTX N-terminal domain to MTX(Pi1) results in a chimera with five disulfide bridges (BuTX-MTX(Pi1)) that exhibits 22-fold greater affinity for Kv1.2 than MTX(Pi1) itself, in spite of the lower affinity of BuTX as compared to MTX(Pi1).	Disulfides	82-91	serpin family A member 1	Homo sapiens	110-113
15944340-2	2005	An alternative hypothesis was investigated: Antioxidants that are also strong reducers of disulfide bonds inhibit the binding of Ang II to its surface receptors with consequent attenuation of signal transduction and cell action.	Disulfides	90-99	angiotensinogen	Homo sapiens	129-135
16147889-1	2005	Human THROMBOSPONDIN-1 play versatile roles in platelet aggregation, angiogenesis, and tumorigenesis, which forms a disulfide-linked homotrimeric complex.	Disulfides	116-125	thrombospondin 1	Homo sapiens	6-22
16182193-3	2005	This could enable PDI to reduce gp120 disulfide bonds, which triggers the major conformational changes in gp120 and gp41 required for virus entry.	Disulfides	38-47	protein disulfide isomerase family A member 2	Homo sapiens	18-21
16102036-3	2005	von Willebrand factor multimer assembly depends on the ability of the propeptide to promote disulfide bond formation in the Golgi, possibly by acting as a pH-sensitive oxidoreductase.	Disulfides	92-101	von Willebrand factor	Homo sapiens	0-21
16102057-1	2005	Fibrinogen molecules are comprised of two sets of disulfide-bridged Aalpha-, Bbeta-, and gamma-chains.	Disulfides	50-59	fibrinogen beta chain	Homo sapiens	0-10
15880782-5	2005	Insulin is a protein hormone consisting of two peptide chains linked by three disulfide bonds.	Disulfides	78-87	insulin	Homo sapiens	0-7
15917240-7	2005	Site-directed mutagenesis of CD147 implicated the disulfide bridge in the Ig-like C2 domain of CD147 as the target of pCMBS attack.	Disulfides	50-59	basigin	Oryctolagus cuniculus	29-34
15917240-7	2005	Site-directed mutagenesis of CD147 implicated the disulfide bridge in the Ig-like C2 domain of CD147 as the target of pCMBS attack.	Disulfides	50-59	basigin	Oryctolagus cuniculus	95-100
15990096-1	2005	Native insulin denatures and unfolds in the presence of thiol catalyst via disulfide scrambling (isomerization).	Disulfides	75-84	insulin	Homo sapiens	7-14
15990096-7	2005	These results demonstrate that stability and unfolding pathway of insulin in the presence of endogenous thiol differ fundamentally from its reversible denaturation observed in the absence of thiol, in which native disulfide bonds of insulin were kept intact during the process of denaturation.	Disulfides	214-223	insulin	Homo sapiens	66-73
15990096-7	2005	These results demonstrate that stability and unfolding pathway of insulin in the presence of endogenous thiol differ fundamentally from its reversible denaturation observed in the absence of thiol, in which native disulfide bonds of insulin were kept intact during the process of denaturation.	Disulfides	214-223	insulin	Homo sapiens	233-240
16284729-3	2005	Furthermore, a three-dimensional structural model of the ECD was constructed by homology modeling, using the structure of the ECD of GC-A as a template (van den Akker et al., 2000, Nature, 406: 101-104) and the information of the disulfide linkages.	Disulfides	230-239	grancalcin	Homo sapiens	133-137
15980323-6	2005	The amino acid sequence of kaliocin-1 includes the "multidimensional antimicrobial signature" conserved in disulfide-containing antimicrobial peptides and a striking similarity to brevinin-1Sa, an antimicrobial peptide from frog skin secretions, exhibiting a "Rana box"-like sequence.	Disulfides	107-116	lactotransferrin	Homo sapiens	27-37
16080717-3	2005	The resultant homology model reveals that carp ovum cystatin shares similar folds as chicken egg white cystatin, particularly in the conserved regions of Q48-V49-G52 and P98-W99 and the locations of two disulfide bonds, C67-C76 and C90-C110.	Disulfides	203-212	cystatin C	Gallus gallus	52-60
15879598-2	2005	TrxRs are the only enzymes catalyzing the NADPH-dependent reduction of the active site disulfide in thioredoxins (Trxs), which play essential roles in substrate reductions, defense against oxidative stress, and redox regulation by thiol redox control.	Disulfides	87-96	thioredoxin 1	Rattus norvegicus	100-112
15879598-6	2005	In this study we report that rat TrxR1 activity in Trx-dependent disulfide reduction was inhibited by curcumin.	Disulfides	65-74	thioredoxin 1	Rattus norvegicus	33-36
16008366-4	2005	The folding pathways of RNase B were determined to be similar to those of RNase A in that two structured intermediates, each lacking one native disulfide bond, were found to populate the regeneration pathways at 25 degrees C and pH 8.3.	Disulfides	144-153	ribonuclease pancreatic	Bos taurus	74-81
16002696-8	2005	Furthermore, the thiol oxidoreductase ERp57 was detected in FcRn-CNX complexes, suggesting its role in disulfide bond formation of the FcRn H chain.	Disulfides	103-112	protein disulfide isomerase family A member 3	Homo sapiens	38-43
16002696-8	2005	Furthermore, the thiol oxidoreductase ERp57 was detected in FcRn-CNX complexes, suggesting its role in disulfide bond formation of the FcRn H chain.	Disulfides	103-112	Fc gamma receptor and transporter	Homo sapiens	60-64
16002696-8	2005	Furthermore, the thiol oxidoreductase ERp57 was detected in FcRn-CNX complexes, suggesting its role in disulfide bond formation of the FcRn H chain.	Disulfides	103-112	Fc gamma receptor and transporter	Homo sapiens	135-139
15998262-3	2005	However, insulin receptor kinase (IRK) autophosphorylation and/or kinase activity were found to be markedly enhanced by a more limited exposure to hydrogen peroxide or by an oxidative shift in the thiol/disulfide redox status.	Disulfides	203-212	insulin	Homo sapiens	9-16
15976011-2	2005	The available commercial yeast display vector pYD1 (Invitrogen) displays the protein of interest flanked on the N-terminus by Aga2, the disulfide of which binds the myristylated surface membrane protein Aga1.	Disulfides	136-145	Aga2p	Saccharomyces cerevisiae S288C	126-130
16113787-5	2005	We demonstrate by immunochemical, ligand-binding and plasminogen activation studies, that homocysteine modifies the structure and function of lipoprotein(a) in human plasma; it reduces the apo(a)/apoB disulfide bond causing the appearance of free apo(a) with high affinity for fibrin that inhibits plasminogen binding and plasmin formation (r= -0.995, p =0.002).	Disulfides	201-210	apolipoprotein B	Homo sapiens	196-200
15834133-6	2005	In contrast, PCPE-1 enhanced C-terminal processing of human fibrillar procollagen III but only when this substrate was in its native, disulfide-bonded conformation.	Disulfides	134-143	procollagen C-endopeptidase enhancer	Homo sapiens	13-19
15989776-7	2005	CONCLUSION: The CGT52TGT point mutation of MBL gene does not affect the secretion of its product, but a Cys introduced by the mutation could form another disulfide bond which may disrupt the structure of MBL molecule as well as its function.	Disulfides	154-163	mannose-binding lectin family member 3, pseudogene	Homo sapiens	43-46
15989776-7	2005	CONCLUSION: The CGT52TGT point mutation of MBL gene does not affect the secretion of its product, but a Cys introduced by the mutation could form another disulfide bond which may disrupt the structure of MBL molecule as well as its function.	Disulfides	154-163	mannose-binding lectin family member 3, pseudogene	Homo sapiens	204-207
15907935-7	2005	The disulfide-deficient hen lysozyme offers a particularly simple model system for thermodynamic and kinetic studies of protofibril formation as well as for screening drugs for amyloidosis.	Disulfides	4-13	lysozyme	Homo sapiens	28-36
15896311-6	2005	A new signaling model is proposed where in its natural state the disulfide structural motif represses the ARM domain activity, which, in turn, represses the catalytic module activity of ANF-RGC.	Disulfides	65-74	natriuretic peptide A	Homo sapiens	186-189
15797870-4	2005	The N-terminal extension of SK2-L is cysteine-rich and mediates disulfide bond formation between SK2-L subunits or with heterologous proteins.	Disulfides	64-73	skin antigen 2	Mus musculus	28-31
15896311-7	2005	ANF signaling relieves the disulfide structural motif restraint on the ARM inhibition and stimulates the catalytic module of the cyclase.	Disulfides	27-36	natriuretic peptide A	Homo sapiens	0-3
15924415-3	2005	The TFF1 complex was immunopurified from human gastric mucosa and shown to comprise two proteins joined by a disulfide bond.	Disulfides	109-118	trefoil factor 1	Homo sapiens	4-8
15924415-11	2005	In conclusion, the heterodimer comprises one molecule each of TFF1 and TFIZ1, and the disulfide bond between TFF1 and TFIZ1 is the most important factor stabilizing the heterodimer.	Disulfides	86-95	trefoil factor 1	Homo sapiens	62-66
15924415-11	2005	In conclusion, the heterodimer comprises one molecule each of TFF1 and TFIZ1, and the disulfide bond between TFF1 and TFIZ1 is the most important factor stabilizing the heterodimer.	Disulfides	86-95	trefoil factor 1	Homo sapiens	109-113
15896311-2	2005	Juxtaposed to each side of the transmembrane module is a Cys423-Cys432 disulfide ANF signaling module motif and the ATP-regulated transduction module (ARM) motif.	Disulfides	71-80	natriuretic peptide A	Homo sapiens	81-84
15814611-2	2005	Glutaredoxin (Grx) and protein-disulfide isomerase (PDI) are members of the thioredoxin superfamily of thiol/disulfide exchange catalysts.	Disulfides	31-40	thioredoxin 1	Rattus norvegicus	76-87
15797870-4	2005	The N-terminal extension of SK2-L is cysteine-rich and mediates disulfide bond formation between SK2-L subunits or with heterologous proteins.	Disulfides	64-73	skin antigen 2	Mus musculus	97-100
15862712-0	2005	Extracellular superoxide dismutase: structural and functional considerations of a protein shaped by two different disulfide bridge patterns.	Disulfides	114-123	superoxide dismutase 3	Homo sapiens	0-34
15885653-6	2005	Thus, the C351A and C361A mutations might cause a global reorganization of the disulfide bonds of SGLT1.	Disulfides	79-88	solute carrier family 5 member 1	Homo sapiens	98-103
15854654-5	2005	The cyclic nature due to a disulfide bridge between Cys1 and Cys6 of vasopressin provides structural rigidity to the peptide hormone.	Disulfides	27-36	arginine vasopressin	Homo sapiens	69-80
15857110-1	2005	A series of novel, disulfide-constrained human beta-melanocyte stimulating hormone (beta-MSH)-derived peptides were optimized for in vitro melanocortin-4 receptor (MC-4R) binding affinity, agonist efficacy, and selectivity.	Disulfides	19-28	proopiomelanocortin	Homo sapiens	47-82
15857110-1	2005	A series of novel, disulfide-constrained human beta-melanocyte stimulating hormone (beta-MSH)-derived peptides were optimized for in vitro melanocortin-4 receptor (MC-4R) binding affinity, agonist efficacy, and selectivity.	Disulfides	19-28	proopiomelanocortin	Homo sapiens	84-92
15590901-1	2005	Eppin (SPINLW1; GeneID, 57119) is a single-copy gene encoding a cysteine-rich protein found only in the testis and epididymis, which contains both Kunitz-type and WAP-type four disulfide core protease inhibitor consensus sequences.	Disulfides	177-186	epididymal peptidase inhibitor	Homo sapiens	0-5
15590901-1	2005	Eppin (SPINLW1; GeneID, 57119) is a single-copy gene encoding a cysteine-rich protein found only in the testis and epididymis, which contains both Kunitz-type and WAP-type four disulfide core protease inhibitor consensus sequences.	Disulfides	177-186	epididymal peptidase inhibitor	Homo sapiens	7-14
15590901-5	2005	Reduction and carboxymethylation of Cys239 blocks binding of 125I-rEppin, indicating that a disulfide bond may be necessary for Eppin binding.	Disulfides	92-101	epididymal peptidase inhibitor	Homo sapiens	67-72
15867268-1	2005	Secretory proteins such as apolipoprotein B-100 (apoB) undergo oxidative folding (formation of disulfide bonds) in the endoplasmic reticulum (ER) before secretion.	Disulfides	95-104	apolipoprotein B	Homo sapiens	27-47
15867268-1	2005	Secretory proteins such as apolipoprotein B-100 (apoB) undergo oxidative folding (formation of disulfide bonds) in the endoplasmic reticulum (ER) before secretion.	Disulfides	95-104	apolipoprotein B	Homo sapiens	49-53
15807524-0	2005	Structural mechanism of oxidative regulation of the phosphatase Cdc25B via an intramolecular disulfide bond.	Disulfides	93-102	cell division cycle 25B	Homo sapiens	64-70
15691826-5	2005	Recently the intramolecular disulfide has been shown to be required for SOD1 activity, leading us to examine these states of several disease-causing SOD1 mutants.	Disulfides	28-37	superoxide dismutase 1	Homo sapiens	72-76
15691826-5	2005	Recently the intramolecular disulfide has been shown to be required for SOD1 activity, leading us to examine these states of several disease-causing SOD1 mutants.	Disulfides	28-37	superoxide dismutase 1	Homo sapiens	149-153
15691826-6	2005	We find that ALS mutations have the greatest effect on the most immature form of SOD1, destabilizing the metal-free and disulfide-reduced polypeptide to the point that it is unfolded at physiological temperatures (Tm<37 degrees C).	Disulfides	120-129	superoxide dismutase 1	Homo sapiens	13-16
15691826-6	2005	We find that ALS mutations have the greatest effect on the most immature form of SOD1, destabilizing the metal-free and disulfide-reduced polypeptide to the point that it is unfolded at physiological temperatures (Tm<37 degrees C).	Disulfides	120-129	superoxide dismutase 1	Homo sapiens	81-85
15691826-9	2005	Thus it is the earliest disulfide-reduced polypeptides in the SOD1 assembly pathway that are most destabilized with respect to unfolding and oxidative aggregation by ALS-causing mutations.	Disulfides	24-33	superoxide dismutase 1	Homo sapiens	62-66
15691826-9	2005	Thus it is the earliest disulfide-reduced polypeptides in the SOD1 assembly pathway that are most destabilized with respect to unfolding and oxidative aggregation by ALS-causing mutations.	Disulfides	24-33	superoxide dismutase 1	Homo sapiens	166-169
15823038-1	2005	The low-density lipoprotein receptor-related protein (LRP) is a large receptor that contains extensive glycosylation sites and disulfide bonds.	Disulfides	127-136	LDL receptor related protein 1	Homo sapiens	54-57
15823038-7	2005	Since previous studies have shown that N-glycan-bound calnexin/calreticulin are also capable of recruiting ERp57, our results suggest that N-linked glycosylation and RAP can independently and cooperatively recruit oxidoreductases to facilitate protein folding and proper disulfide bond formation.	Disulfides	271-280	calreticulin	Homo sapiens	63-75
15823038-7	2005	Since previous studies have shown that N-glycan-bound calnexin/calreticulin are also capable of recruiting ERp57, our results suggest that N-linked glycosylation and RAP can independently and cooperatively recruit oxidoreductases to facilitate protein folding and proper disulfide bond formation.	Disulfides	271-280	protein disulfide isomerase family A member 3	Homo sapiens	107-112
15705573-6	2005	Substituting Cys-195 prevents formation not only of the intradomain disulfide, but also of the interchain disulfide bond with light chain, BiP displacement, and secretion.	Disulfides	106-115	growth differentiation factor 10	Homo sapiens	139-142
15829265-7	2005	Abolishment of disulfide-linked CD40/CD40 dimers in these transfected cells was sufficient to inhibit CD40-induced mRNA expression and secretion of IL-8.	Disulfides	15-24	C-X-C motif chemokine ligand 8	Homo sapiens	148-152
15807524-1	2005	Cdc25B phosphatase, an important regulator of the cell cycle, forms an intramolecular disulfide bond in response to oxidation leading to reversible inactivation of phosphatase activity.	Disulfides	86-95	cell division cycle 25B	Homo sapiens	0-6
15761664-1	2005	Purple acid phosphatase (PAP), also known as tartrate-resistant acid phosphatase (TRAP), uteroferrin or type 5 acid phosphatase (Acp5) is synthesized as an N-glycosylated monomeric latent precursor, which can be processed by limited proteolysis to a disulfide-linked two-subunit form with increased enzyme activity.	Disulfides	250-259	acid phosphatase 3	Rattus norvegicus	25-28
15794637-6	2005	Respective B chain libraries containing mixtures of d or l substitutions at B8 exhibit a stereospecific perturbation of insulin chain combination: l amino acids impede native disulfide pairing, whereas diverse d substitutions are well-tolerated.	Disulfides	175-184	insulin	Homo sapiens	120-127
16511049-1	2005	Thioredoxin reductase 1 (Trr1) from Saccharomyces cerevisiae is a member of the family of pyridine nucleotide-disulfide oxidoreductases capable of reducing the redox-active disulfide bond of the cytosolic thioredoxin 1 (Trx1) and thioredoxin 2 (Trx2).	Disulfides	110-119	thioredoxin TRX2	Saccharomyces cerevisiae S288C	245-249
16511049-2	2005	NADPH, Trr1 and Trx1 (or Trx2) comprise the thioredoxin system, which is involved in several biological processes, including the reduction of disulfide bonds and response to oxidative stress.	Disulfides	142-151	thioredoxin TRX2	Saccharomyces cerevisiae S288C	25-29
15653747-3	2005	The validity of the apoB model was supported by conservation of disulfide bonds, location of all proline residues in turns and loops, and conservation of the hydrophobic faces of the two C-terminal amphipathic beta-sheets, betaA (residues 600-763) and betaB (residues 780-1000).	Disulfides	64-73	apolipoprotein B	Homo sapiens	20-24
15769853-5	2005	We also obtained evidence that both ABCG2-wt and ABCG2-K86M exist in the cells as disulfide-linked dimers.	Disulfides	82-91	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	36-41
15769853-5	2005	We also obtained evidence that both ABCG2-wt and ABCG2-K86M exist in the cells as disulfide-linked dimers.	Disulfides	82-91	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	49-54
15741328-0	2005	Extraordinarily stable disulfide-linked homodimer of human growth hormone.	Disulfides	23-32	growth hormone 1	Homo sapiens	59-73
15644496-2	2005	The triggering of fusion requires cleavage of two of the nine disulfide bonds of gp120 by a cell-surface protein disulfide-isomerase (PDI).	Disulfides	62-71	protein disulfide isomerase family A member 2	Homo sapiens	134-137
15723073-4	2005	This peptide competes with the fibrin fragment N-terminal disulfide knot-II (an analog of the fibrin E1 fragment) for binding to vascular endothelial (VE)-cadherin, thereby preventing transmigration of leukocytes across endothelial cell monolayers.	Disulfides	58-67	cadherin 5	Homo sapiens	129-163
15736947-0	2005	Kinetic and structural properties of disulfide engineered phospholipase A2: insight into the role of disulfide bonding patterns.	Disulfides	37-46	phospholipase A2 group IB	Homo sapiens	58-74
15736947-0	2005	Kinetic and structural properties of disulfide engineered phospholipase A2: insight into the role of disulfide bonding patterns.	Disulfides	101-110	phospholipase A2 group IB	Homo sapiens	58-74
15736947-1	2005	The family of secreted 14 kDa phospholipase A(2) (PLA2) enzymes have a common motif for the catalytic site but differ in their disulfide architecture.	Disulfides	127-136	phospholipase A2 group IB	Homo sapiens	50-54
15736947-2	2005	The functional significance of such structural changes has been analyzed by comparing the kinetic and spectroscopic properties of a series of disulfide mutants engineered into the sequence of pig pancreatic IB PLA2 to resemble the mammalian paralogues of the PLA2 family [Janssen et al.	Disulfides	142-151	phospholipase A2, major isoenzyme	Sus scrofa	210-214
15736947-6	2005	We report a detailed comparison of the functional parameters of pig iso-PLA2, as well as several of the human homologues, with these disulfide engineered mutants of pig IB PLA2.	Disulfides	133-142	phospholipase A2, major isoenzyme	Sus scrofa	172-176
15736947-7	2005	The crystal structure of the ligand free and the active site inhibitor-MJ33 bound forms of PLA2 engineered to have the disulfide bonding pattern of group-X (eng-X) are also reported and compared with the structure of group-IB and human group-X PLA2.	Disulfides	119-128	phospholipase A2 group IB	Homo sapiens	91-95
15736947-10	2005	We suggest that the disulfide architecture of the PLA2 paralogues has a marginal influence on interface binding.	Disulfides	20-29	phospholipase A2 group IB	Homo sapiens	50-54
15706081-2	2005	The yeast transcription factor Yap1 is activated by formation of a disulfide bond, which inhibits nuclear export in response to peroxide stress, with resultant enhancement of the nuclear localization of Yap1.	Disulfides	67-76	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	31-35
15706081-2	2005	The yeast transcription factor Yap1 is activated by formation of a disulfide bond, which inhibits nuclear export in response to peroxide stress, with resultant enhancement of the nuclear localization of Yap1.	Disulfides	67-76	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	203-207
15706081-3	2005	A glutathione peroxidase-like protein, Gpx3, which has peroxiredoxin activity, is required for formation of the disulfide bond in Yap1.	Disulfides	112-121	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	130-134
15653693-3	2005	Oxidized glutathione led to enzyme inactivation with simultaneous formation of a mixed disulfide between glutathione and the cysteine residue(s) in IDPm, which was detected by immunoblotting with anti-GSH IgG.	Disulfides	87-96	isocitrate dehydrogenase (NADP(+)) 2	Homo sapiens	148-152
15653693-4	2005	The inactivated IDPm was reactivated enzymatically by glutaredoxin2 in the presence of GSH, indicating that the inactivated form of IDPm is a glutathionyl mixed disulfide.	Disulfides	161-170	isocitrate dehydrogenase (NADP(+)) 2	Homo sapiens	16-20
15653693-4	2005	The inactivated IDPm was reactivated enzymatically by glutaredoxin2 in the presence of GSH, indicating that the inactivated form of IDPm is a glutathionyl mixed disulfide.	Disulfides	161-170	glutaredoxin 2	Homo sapiens	54-67
15653693-4	2005	The inactivated IDPm was reactivated enzymatically by glutaredoxin2 in the presence of GSH, indicating that the inactivated form of IDPm is a glutathionyl mixed disulfide.	Disulfides	161-170	isocitrate dehydrogenase (NADP(+)) 2	Homo sapiens	132-136
15550394-0	2005	Site-specific disulfide capture of agonist and antagonist peptides on the C5a receptor.	Disulfides	14-23	complement C5a receptor 1	Homo sapiens	74-86
15835752-8	2005	CONCLUSIONS: These results suggest that, although the presence of N-glycan does not affect the localization of BCRP, disulfide bonds and some peptide sequences in both the N- and C-terminals are necessary for the apical expression of BCRP.	Disulfides	117-126	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	234-238
15649413-1	2005	Human mitochondrial glutaredoxin 2 (Grx2) catalyzes glutathione-dependent dithiol reaction mechanisms, reducing protein disulfides, and monothiol reactions, reducing mixed disulfides between proteins and GSH (de-/glutathionylation).	Disulfides	120-130	glutaredoxin 2	Homo sapiens	20-34
15649413-1	2005	Human mitochondrial glutaredoxin 2 (Grx2) catalyzes glutathione-dependent dithiol reaction mechanisms, reducing protein disulfides, and monothiol reactions, reducing mixed disulfides between proteins and GSH (de-/glutathionylation).	Disulfides	120-130	glutaredoxin 2	Homo sapiens	36-40
15649413-1	2005	Human mitochondrial glutaredoxin 2 (Grx2) catalyzes glutathione-dependent dithiol reaction mechanisms, reducing protein disulfides, and monothiol reactions, reducing mixed disulfides between proteins and GSH (de-/glutathionylation).	Disulfides	172-182	glutaredoxin 2	Homo sapiens	20-34
15649413-1	2005	Human mitochondrial glutaredoxin 2 (Grx2) catalyzes glutathione-dependent dithiol reaction mechanisms, reducing protein disulfides, and monothiol reactions, reducing mixed disulfides between proteins and GSH (de-/glutathionylation).	Disulfides	172-182	glutaredoxin 2	Homo sapiens	36-40
15466936-1	2005	Formation and rearrangement of disulfide bonds during the correct folding of nascent proteins is modulated by a family of enzymes known as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERP5), and ERP57.	Disulfides	31-40	protein disulfide isomerase family A member 3	Homo sapiens	250-255
15585673-5	2005	On the basis of simulated mutation analyses, we hypothesized that this protease resistance is due to disulfide bond-related tertiary folding in IL-8/CXCL8.	Disulfides	101-110	C-X-C motif chemokine ligand 8	Homo sapiens	144-148
15585673-5	2005	On the basis of simulated mutation analyses, we hypothesized that this protease resistance is due to disulfide bond-related tertiary folding in IL-8/CXCL8.	Disulfides	101-110	C-X-C motif chemokine ligand 8	Homo sapiens	149-154
15820978-3	2005	We describe here modified human Epo [Epo(NDS)] with mutations His32Gly, Cys33Pro, Trp88Cys and Pro90Ala that result in the rearrangement of the disulfide bonding pattern from Cys29-Cys33 to Cys29-Cys88 and that, in the context of an Fc-Epo(NDS) fusion protein, lead to significantly improved properties.	Disulfides	144-153	erythropoietin	Homo sapiens	32-35
15820978-3	2005	We describe here modified human Epo [Epo(NDS)] with mutations His32Gly, Cys33Pro, Trp88Cys and Pro90Ala that result in the rearrangement of the disulfide bonding pattern from Cys29-Cys33 to Cys29-Cys88 and that, in the context of an Fc-Epo(NDS) fusion protein, lead to significantly improved properties.	Disulfides	144-153	erythropoietin	Homo sapiens	37-45
15820978-3	2005	We describe here modified human Epo [Epo(NDS)] with mutations His32Gly, Cys33Pro, Trp88Cys and Pro90Ala that result in the rearrangement of the disulfide bonding pattern from Cys29-Cys33 to Cys29-Cys88 and that, in the context of an Fc-Epo(NDS) fusion protein, lead to significantly improved properties.	Disulfides	144-153	erythropoietin	Homo sapiens	236-244
15550394-8	2005	However, when a cysteine residue is placed on their N terminus they can be trapped by disulfide interchange to specific cysteines in helix III and VI and not to other cysteines, engineered into the C5aR.	Disulfides	86-95	complement C5a receptor 1	Homo sapiens	198-202
15592500-0	2005	Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond formation and VEGF secretion under hypoxia: implication for cancer.	Disulfides	69-78	hypoxia inducible factor 1 subunit alpha	Homo sapiens	35-40
15592500-2	2005	We show that secretion of vascular endothelial growth factor (VEGF), a protein with multiple disulfide bonds, was indeed impeded under hypoxia and was partially restored by artificial increase of oxidizing equivalents with diamide.	Disulfides	93-102	vascular endothelial growth factor A	Homo sapiens	26-60
15592500-2	2005	We show that secretion of vascular endothelial growth factor (VEGF), a protein with multiple disulfide bonds, was indeed impeded under hypoxia and was partially restored by artificial increase of oxidizing equivalents with diamide.	Disulfides	93-102	vascular endothelial growth factor A	Homo sapiens	62-66
15567151-0	2005	1.42A crystal structure of mini-IGF-1(2): an analysis of the disulfide isomerization property and receptor binding property of IGF-1 based on the three-dimensional structure.	Disulfides	61-70	insulin like growth factor 1	Homo sapiens	32-37
15664856-1	2005	PDI is an enzyme that acts as a chaperone, shufflase, and oxidase during the folding of disulfide-containing proteins.	Disulfides	88-97	protein disulfide isomerase family A member 2	Homo sapiens	0-3
15579663-5	2005	The regulation is of an all-or-nothing type, lacking the fine-tuning provided by the second N-terminal disulfide found only in NADP-MDH from higher plants.	Disulfides	103-112	uncharacterized protein	Chlamydomonas reinhardtii	127-135
15537649-7	2005	Endoglin, a disulfide-linked homodimer, is an accessory component of the TGF-beta receptor complex and mainly expressed on endothelial cells.	Disulfides	12-21	transforming growth factor, beta 1	Rattus norvegicus	73-81
15466247-1	2005	Group I metabotropic glutamate receptors (mGluRs) form stable, disulfide-linked homodimers.	Disulfides	63-72	glutamate metabotropic receptor 1	Rattus norvegicus	42-48
15680231-3	2005	The mechanism includes three steps with (1) formation of a sulfenic acid intermediate with a concomitant release of 1 mol of methionine per mol of enzyme; (2) formation of an intramonomeric disulfide Msr bond followed by; (3) reduction of the oxidized Msr by thioredoxin (Trx).	Disulfides	190-199	5-methyltetrahydrofolate-homocysteine methyltransferase reductase	Homo sapiens	200-203
15680231-3	2005	The mechanism includes three steps with (1) formation of a sulfenic acid intermediate with a concomitant release of 1 mol of methionine per mol of enzyme; (2) formation of an intramonomeric disulfide Msr bond followed by; (3) reduction of the oxidized Msr by thioredoxin (Trx).	Disulfides	190-199	5-methyltetrahydrofolate-homocysteine methyltransferase reductase	Homo sapiens	252-255
15475357-0	2005	PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum.	Disulfides	43-52	protein disulfide isomerase like, testis expressed	Homo sapiens	0-5
15475357-7	2005	We show that PDILT is an ER resident glycoprotein that liaises with partner proteins in disulfide-dependent complexes within the testis.	Disulfides	88-97	protein disulfide isomerase like, testis expressed	Homo sapiens	13-18
15507452-0	2005	Conformational HER-2/neu B-cell epitope peptide vaccine designed to incorporate two native disulfide bonds enhances tumor cell binding and antitumor activities.	Disulfides	91-100	erb-b2 receptor tyrosine kinase 2	Homo sapiens	15-24
15507452-5	2005	The disulfide-paired specific antibodies exhibited enhanced cross-reactivity to HER-2/neu expressed on BT-474 cell line as determined by flow cytometry.	Disulfides	4-13	erb-b2 receptor tyrosine kinase 2	Homo sapiens	80-89
15567151-1	2005	Insulin and insulin-like growth factor 1 (IGF-1) share a homologous sequence, a similar three-dimensional structure and weakly overlapping biological activity, but IGF-1 folds into two thermodynamically stable disulfide isomers, while insulin folds into one unique stable tertiary structure.	Disulfides	210-219	insulin	Homo sapiens	0-7
15567151-1	2005	Insulin and insulin-like growth factor 1 (IGF-1) share a homologous sequence, a similar three-dimensional structure and weakly overlapping biological activity, but IGF-1 folds into two thermodynamically stable disulfide isomers, while insulin folds into one unique stable tertiary structure.	Disulfides	210-219	insulin like growth factor 1	Homo sapiens	12-40
15567151-1	2005	Insulin and insulin-like growth factor 1 (IGF-1) share a homologous sequence, a similar three-dimensional structure and weakly overlapping biological activity, but IGF-1 folds into two thermodynamically stable disulfide isomers, while insulin folds into one unique stable tertiary structure.	Disulfides	210-219	insulin like growth factor 1	Homo sapiens	42-47
15567151-1	2005	Insulin and insulin-like growth factor 1 (IGF-1) share a homologous sequence, a similar three-dimensional structure and weakly overlapping biological activity, but IGF-1 folds into two thermodynamically stable disulfide isomers, while insulin folds into one unique stable tertiary structure.	Disulfides	210-219	insulin like growth factor 1	Homo sapiens	164-169
15567151-1	2005	Insulin and insulin-like growth factor 1 (IGF-1) share a homologous sequence, a similar three-dimensional structure and weakly overlapping biological activity, but IGF-1 folds into two thermodynamically stable disulfide isomers, while insulin folds into one unique stable tertiary structure.	Disulfides	210-219	insulin	Homo sapiens	12-19
15567151-3	2005	In this study, the crystal structure of mini-IGF-1(2), a disulfide isomer of an artificial analog of IGF-1, was solved by the SAD/SIRAS method using our in-house X-ray source.	Disulfides	57-66	insulin like growth factor 1	Homo sapiens	45-50
15567151-3	2005	In this study, the crystal structure of mini-IGF-1(2), a disulfide isomer of an artificial analog of IGF-1, was solved by the SAD/SIRAS method using our in-house X-ray source.	Disulfides	57-66	insulin like growth factor 1	Homo sapiens	101-106
15567151-5	2005	Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds.	Disulfides	213-222	insulin like growth factor 1	Homo sapiens	51-56
15567151-5	2005	Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds.	Disulfides	213-222	insulin	Homo sapiens	61-68
15567151-5	2005	Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds.	Disulfides	213-222	insulin	Homo sapiens	104-111
15567151-5	2005	Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds.	Disulfides	304-313	insulin like growth factor 1	Homo sapiens	51-56
15567151-5	2005	Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds.	Disulfides	304-313	insulin	Homo sapiens	61-68
15567151-5	2005	Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds.	Disulfides	304-313	insulin	Homo sapiens	104-111
15567151-5	2005	Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds.	Disulfides	304-313	insulin like growth factor 1	Homo sapiens	51-56
15567151-5	2005	Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds.	Disulfides	304-313	insulin	Homo sapiens	61-68
15837518-1	2005	Fibrinogen is a large, complex, fibrous glycoprotein with three pairs of polypeptide chains linked together by 29 disulfide bonds.	Disulfides	114-123	fibrinogen beta chain	Homo sapiens	0-10
15567151-5	2005	Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds.	Disulfides	304-313	insulin	Homo sapiens	104-111
15686534-4	2005	Our studies reveal that the susceptibility of the (40-95) disulfide bond of Y92G bovine pancreatic ribonuclease A (RNase A) to reduction results in a reduced rate of oxidative regeneration, compared with wild-type RNase A.	Disulfides	58-67	ribonuclease pancreatic	Bos taurus	99-113
15625724-0	2005	Engineering disulfide bonds of the novel human beta-defensins hBD-27 and hBD-28: differences in disulfide formation and biological activity among human beta-defensins.	Disulfides	12-21	defensin beta 127	Homo sapiens	62-68
15625724-0	2005	Engineering disulfide bonds of the novel human beta-defensins hBD-27 and hBD-28: differences in disulfide formation and biological activity among human beta-defensins.	Disulfides	96-105	defensin beta 127	Homo sapiens	62-68
15625724-4	2005	Here we report for the first time the chemical synthesis of the new fully disulfide-bonded beta-defensins hBD-27 and hBD-28, and compare the results with synthetic procedures to obtain the known hBD-2 and hBD-3.	Disulfides	74-83	defensin beta 127	Homo sapiens	106-112
15625724-4	2005	Here we report for the first time the chemical synthesis of the new fully disulfide-bonded beta-defensins hBD-27 and hBD-28, and compare the results with synthetic procedures to obtain the known hBD-2 and hBD-3.	Disulfides	74-83	defensin beta 4A	Homo sapiens	106-111
15625724-5	2005	While hBD-27 was readily converted into a product with the desired disulfide pattern by oxidative folding, hBD-28 required a selective protective group strategy to introduce the three disulfide bonds.	Disulfides	67-76	defensin beta 127	Homo sapiens	6-12
15610969-1	2005	The thioredoxin h system has the specific capability to reduce intramolecular disulfide bonds of proteins, thereby modifying their tertiary structure.	Disulfides	78-87	thioredoxin H4-2	Triticum aestivum	4-15
16333982-2	2005	ERp72, a protein disulfide isomerase (PDI) family member, possesses 3 thioredoxin homology domains, but the participation of each domain in disulfide-bond formation and isomerization remains to be determined.	Disulfides	17-26	protein disulfide isomerase family A member 4	Homo sapiens	0-5
15686534-4	2005	Our studies reveal that the susceptibility of the (40-95) disulfide bond of Y92G bovine pancreatic ribonuclease A (RNase A) to reduction results in a reduced rate of oxidative regeneration, compared with wild-type RNase A.	Disulfides	58-67	ribonuclease pancreatic	Bos taurus	115-122
15686534-4	2005	Our studies reveal that the susceptibility of the (40-95) disulfide bond of Y92G bovine pancreatic ribonuclease A (RNase A) to reduction results in a reduced rate of oxidative regeneration, compared with wild-type RNase A.	Disulfides	58-67	ribonuclease pancreatic	Bos taurus	214-221
15686534-5	2005	In the native state of RNase A, Tyr 92 lies atop its (40-95) disulfide bond, effectively shielding this bond from the reducing agent, thereby promoting protein oxidative regeneration.	Disulfides	61-70	ribonuclease pancreatic	Bos taurus	23-30
15694701-11	2005	These thiol groups can, in turn, initiate a disulfide exchange reaction with plasma proteins, predominantly with fibrinogen, to form an insoluble and protease-resistant fibrin-like polymer.	Disulfides	44-53	fibrinogen beta chain	Homo sapiens	113-123
15533639-1	2005	Exposure of concentrated and purified monomeric insulin solutions to inorganic oxidants as iodine and chlorine lead to the appearance of a minor peak on gel chromatography that was disulfide cross-linked.	Disulfides	181-190	insulin	Homo sapiens	48-55
15700231-4	2005	Disulfide bond cleavage was also observed using RP-HPLC and MS after incubation of the intramolecular homodimer of mouse S100A8 (mass 20614 Da).	Disulfides	0-9	S100 calcium binding protein A8 (calgranulin A)	Mus musculus	121-127
15533639-6	2005	Since the conformation of proinsulin is similar to that of insulin, involving the exposure of the anterior A7-B7 disulfide bridge, the authors hypothesize that proinsulin dimers rather than insulin dimers might be formed in Type 1 diabetes (TD1), leading to the autoimmune destruction of pancreatic B-cells.	Disulfides	113-122	insulin	Homo sapiens	26-36
15533639-6	2005	Since the conformation of proinsulin is similar to that of insulin, involving the exposure of the anterior A7-B7 disulfide bridge, the authors hypothesize that proinsulin dimers rather than insulin dimers might be formed in Type 1 diabetes (TD1), leading to the autoimmune destruction of pancreatic B-cells.	Disulfides	113-122	insulin	Homo sapiens	29-36
15533639-6	2005	Since the conformation of proinsulin is similar to that of insulin, involving the exposure of the anterior A7-B7 disulfide bridge, the authors hypothesize that proinsulin dimers rather than insulin dimers might be formed in Type 1 diabetes (TD1), leading to the autoimmune destruction of pancreatic B-cells.	Disulfides	113-122	insulin	Homo sapiens	160-170
15533639-6	2005	Since the conformation of proinsulin is similar to that of insulin, involving the exposure of the anterior A7-B7 disulfide bridge, the authors hypothesize that proinsulin dimers rather than insulin dimers might be formed in Type 1 diabetes (TD1), leading to the autoimmune destruction of pancreatic B-cells.	Disulfides	113-122	insulin	Homo sapiens	59-66
15533639-7	2005	Proinsulin is present in a soluble aggregate state in the coated granule and may further accumulate allowing disulfide exchange due to abnormalities of the processing enzymes.	Disulfides	109-118	insulin	Homo sapiens	0-10
16173397-3	2005	In despite of three disulfide bonds, the recombinant protein was correctly folded which was conformed by TNFalpha ligand binding assay in ELISA variant.	Disulfides	20-29	tumor necrosis factor	Homo sapiens	105-113
16909016-9	2005	For example, WTL SOD1 mutants are more susceptible than wild-type SOD1 to reduction of the intrasubunit disulfide bond between Cys-57 and Cys-146 at physiological pH and temperature.	Disulfides	104-113	superoxide dismutase 1	Homo sapiens	17-21
16909016-9	2005	For example, WTL SOD1 mutants are more susceptible than wild-type SOD1 to reduction of the intrasubunit disulfide bond between Cys-57 and Cys-146 at physiological pH and temperature.	Disulfides	104-113	superoxide dismutase 1	Homo sapiens	66-70
15485869-7	2004	The Cys-57 --&gt; Ser mutant of SOD1, a protein incapable of forming the intrasubunit disulfide bond, sediments as a monomer in the absence of metal ions and as a dimer when metals are bound.	Disulfides	86-95	superoxide dismutase 1	Homo sapiens	32-36
15485869-8	2004	Taken together, these data indicate that the stability imparted to the human SOD1 dimer by metal binding and the formation of the intrasubunit disulfide bond are mediated by independent molecular mechanisms.	Disulfides	143-152	superoxide dismutase 1	Homo sapiens	77-81
15485869-6	2004	Reduction of the intrasubunit disulfide bond within each SOD1 subunit by 5-10 mM TCEP promotes dissociation of apo-SOD1 dimers, whereas the metal-bound enzyme remains a stable dimer under these conditions.	Disulfides	30-39	superoxide dismutase 1	Homo sapiens	57-61
15485869-6	2004	Reduction of the intrasubunit disulfide bond within each SOD1 subunit by 5-10 mM TCEP promotes dissociation of apo-SOD1 dimers, whereas the metal-bound enzyme remains a stable dimer under these conditions.	Disulfides	30-39	superoxide dismutase 1	Homo sapiens	115-119
15486973-4	2004	These PARP-1-protein interactions resisted salt extraction, disulfide reduction, RNase and DNase digestion.	Disulfides	60-69	poly(ADP-ribose) polymerase 1	Homo sapiens	6-12
15466413-3	2004	Here we describe the intramolecular disulfide bonding, solution structure, and dynamics of a prototypical chordin-like CR repeat from procollagen IIA (CR(ColIIA)), which has been previously shown to bind TGF-beta1 and bone morphogenetic protein-2.	Disulfides	36-45	transforming growth factor beta 1	Homo sapiens	204-213
15675819-2	2004	Disulfide bonding patterns between bovine beta-lactoglobulin and kappa-casein.	Disulfides	0-9	casein kappa	Bos taurus	65-77
15485893-2	2004	DBP is a member of the albumin gene family and has a triple domain modular structure with extensive disulfide bonding that is characteristic of this protein family.	Disulfides	100-109	D-box binding PAR bZIP transcription factor	Homo sapiens	0-3
15675819-3	2004	Heat treatment of milk causes the heat-denaturable whey proteins to aggregate with kappa-casein (kappa-CN) via thiol-disulfide bond interchange reactions.	Disulfides	117-126	casein kappa	Bos taurus	83-95
15675819-3	2004	Heat treatment of milk causes the heat-denaturable whey proteins to aggregate with kappa-casein (kappa-CN) via thiol-disulfide bond interchange reactions.	Disulfides	117-126	casein kappa	Bos taurus	97-105
15675819-5	2004	The reaction at 60 degrees C between beta-LG A and an activated kappa-CN formed small disulfide-bonded aggregates.	Disulfides	86-95	casein kappa	Bos taurus	64-72
15486973-5	2004	An inherent ability of PARP-1 to reassemble with the lamins became evident after a cycle of solubilization/dialysis using either urea or Triton X-100 and disulfide reduction, indicating that these interactions were dominated by hydrophobic forces.	Disulfides	154-163	poly(ADP-ribose) polymerase 1	Homo sapiens	23-29
15581343-0	2004	An intersheet packing interaction in A beta fibrils mapped by disulfide cross-linking.	Disulfides	62-71	amyloid beta precursor protein	Homo sapiens	37-43
15653430-0	2004	Replacement of the interchain disulfide bridge-forming amino acids A7 and B7 by glutamate impairs the structure and activity of insulin.	Disulfides	30-39	insulin	Homo sapiens	128-135
15544802-0	2004	Ligand-induced conformational changes in the Bacillus subtilis chemoreceptor McpB determined by disulfide crosslinking in vivo.	Disulfides	96-105	hlyB-like ABC transporter-like protein	Escherichia coli	77-81
15544802-1	2004	Previously, we characterized the organization of the transmembrane (TM) domain of the Bacillus subtilis chemoreceptor McpB using disulfide crosslinking.	Disulfides	129-138	hlyB-like ABC transporter-like protein	Escherichia coli	118-122
15544811-3	2004	Here Abeta oligomers are studied by non-covalent complexes mass spectrometry and disulfide rearrangement.	Disulfides	81-90	amyloid beta precursor protein	Homo sapiens	5-10
15653430-2	2004	Site-directed mutagenesis results (the two cysteine residues of disulfide A7-B7 were replaced by serine) showed that disulfide A7-B7 is crucial to both the structure and activity of insulin.	Disulfides	64-73	insulin	Homo sapiens	182-189
15653430-2	2004	Site-directed mutagenesis results (the two cysteine residues of disulfide A7-B7 were replaced by serine) showed that disulfide A7-B7 is crucial to both the structure and activity of insulin.	Disulfides	117-126	insulin	Homo sapiens	182-189
15653430-1	2004	Insulin contains three disulfide bonds, one intrachain bond, A6-A11, and two interchain bonds, A7-B7 and A20-B19.	Disulfides	23-32	insulin	Homo sapiens	0-7
15653430-4	2004	Did the negative charge of the modification groups restore the loss of activity and/or the disturbance of structure of these insulin analogs caused by deletion of disulfide A7-B7?	Disulfides	163-172	insulin	Homo sapiens	125-132
15375179-1	2004	Lipoprotein(a) [Lp(a)] is assembled via an initial noncovalent interaction between apolipoprotein B100 (apoB) and apolipoprotein(a) [apo(a)] that facilitates the formation of a disulfide bond between the two proteins.	Disulfides	177-186	apolipoprotein B	Homo sapiens	83-102
15653430-7	2004	The present results suggest that removal of disulfide A7-B7 will result in serious loss of biological activity and the native conformation of insulin, even if the disulfide is replaced by residues with a negative charge.	Disulfides	44-53	insulin	Homo sapiens	142-149
15653430-7	2004	The present results suggest that removal of disulfide A7-B7 will result in serious loss of biological activity and the native conformation of insulin, even if the disulfide is replaced by residues with a negative charge.	Disulfides	163-172	insulin	Homo sapiens	142-149
15545361-4	2004	These results indicate that beta-LG and alpha-LA associated with MFGM proteins via disulfide bonds during the high-pressure treatment of whole milk.	Disulfides	83-92	lactalbumin alpha	Homo sapiens	40-48
15375179-1	2004	Lipoprotein(a) [Lp(a)] is assembled via an initial noncovalent interaction between apolipoprotein B100 (apoB) and apolipoprotein(a) [apo(a)] that facilitates the formation of a disulfide bond between the two proteins.	Disulfides	177-186	apolipoprotein B	Homo sapiens	104-108
15364921-4	2004	AAT-1 and AAT-3 contain a cysteine residue in the second putative extracellular loop through which a disulfide bridge can form with a heavy chain.	Disulfides	101-110	Amino Acid Transporter	Caenorhabditis elegans	10-15
15364913-6	2004	The 10CC segment constitutes an exchangeable module containing five conserved disulfide bridges, and using module-shuffling and truncations, we have shown that the 10CC segment is a major ligand-binding region in Sortilin.	Disulfides	78-87	sortilin 1	Homo sapiens	213-221
15583744-9	2004	The disulfide-linked complexes of multimerin and factor V in platelets, which are cleaved by thrombin to liberate factor Va, could be important for modulating the function of platelet factor V and its delivery onto activated platelets.	Disulfides	4-13	coagulation factor II, thrombin	Homo sapiens	93-101
15474476-5	2004	The N-terminal peptide fragment of ZPA remained disulfide bond linked to the ZPA glycoprotein moiety following proteolysis.	Disulfides	48-57	zzona pellucida glycoprotein 2 L homeolog	Xenopus laevis	35-38
15326189-2	2004	The structural interplay of conserved disulfide bond and metal-site occupancy in human copper,zinc superoxide dismutase (hSOD1) is of increasing interest as these post-translational modifications are known to dramatically alter the catalytic chemistry, the subcellular localization, and the susceptibility of the protein to aggregation.	Disulfides	38-47	superoxide dismutase 1	Homo sapiens	121-126
15347644-8	2004	Both protein disulfide formation and glutathionylation were catalyzed by the mitochondrial thiol transferase glutaredoxin 2 (Grx2), as were protein deglutathionylation and the reduction of protein disulfides by GSH.	Disulfides	13-22	glutaredoxin 2	Homo sapiens	109-123
15347644-8	2004	Both protein disulfide formation and glutathionylation were catalyzed by the mitochondrial thiol transferase glutaredoxin 2 (Grx2), as were protein deglutathionylation and the reduction of protein disulfides by GSH.	Disulfides	13-22	glutaredoxin 2	Homo sapiens	125-129
15347644-8	2004	Both protein disulfide formation and glutathionylation were catalyzed by the mitochondrial thiol transferase glutaredoxin 2 (Grx2), as were protein deglutathionylation and the reduction of protein disulfides by GSH.	Disulfides	197-207	glutaredoxin 2	Homo sapiens	109-123
15347644-8	2004	Both protein disulfide formation and glutathionylation were catalyzed by the mitochondrial thiol transferase glutaredoxin 2 (Grx2), as were protein deglutathionylation and the reduction of protein disulfides by GSH.	Disulfides	197-207	glutaredoxin 2	Homo sapiens	125-129
15474476-5	2004	The N-terminal peptide fragment of ZPA remained disulfide bond linked to the ZPA glycoprotein moiety following proteolysis.	Disulfides	48-57	zzona pellucida glycoprotein 2 L homeolog	Xenopus laevis	77-80
15518578-2	2004	Human EC-SOD contains an additional cysteine residue and folds into two forms with distinct disulfide bridge patterns.	Disulfides	92-101	superoxide dismutase 3	Homo sapiens	6-12
15518578-7	2004	The results revealed that the disulfide bridges are homogeneous and identical to human aEC-SOD.	Disulfides	30-39	superoxide dismutase 1	Homo sapiens	91-94
15229136-6	2004	However, EPPIN lost its antibacterial activity completely on reduction and alkylation of its cysteines, indicating the importance of disulfide bonds for its activity.	Disulfides	133-142	epididymal peptidase inhibitor	Homo sapiens	9-14
15522970-0	2004	Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers.	Disulfides	39-48	superoxide dismutase 1	Homo sapiens	17-37
15522970-2	2004	A striking, as well as an unusual, feature of SOD is that it maintains intrasubunit disulfide bonds in the reducing environment of the cytosol.	Disulfides	84-93	superoxide dismutase 1	Homo sapiens	46-49
15522970-3	2004	Here, we investigate the role of these disulfide bonds in folding and assembly of the SOD apo protein (apoSOD) homodimer through extensive protein engineering.	Disulfides	39-48	superoxide dismutase 1	Homo sapiens	86-89
15526038-5	2004	Each WAT makes similar but unique interactions, consistent with an asymmetric pattern of disulfide linkages between the AChE tetramer subunits and ColQ.	Disulfides	89-98	acetylcholinesterase (Cartwright blood group)	Homo sapiens	120-124
15538939-0	2004	Identification of a novel mutation in the arginine vasopressin-neurophysin II gene affecting the sixth intrachain disulfide bridge of the neurophysin II moiety.	Disulfides	114-123	arginine vasopressin	Homo sapiens	42-77
15538939-11	2004	Genetic analysis revealed a novel mutation (1665T>A) in exon 2 of the AVP-NPII gene, disrupting one of the disulfide bonds present in the NPII moiety which play a fundamental role in determining the proper folding of the molecule.	Disulfides	107-116	arginine vasopressin	Homo sapiens	70-78
15477076-6	2004	Studies on (His)(6)-tagged CI-b1 revealed that three disulfide bonds were formed in the recombinant CI-b1 and the inhibitory properties of recombinant CI-b1 against alpha-chymotrypsin were similar to those of native CI-b1.	Disulfides	53-62	chymotrypsin inhibitor SCI-II	Bombyx mori	27-32
15477076-6	2004	Studies on (His)(6)-tagged CI-b1 revealed that three disulfide bonds were formed in the recombinant CI-b1 and the inhibitory properties of recombinant CI-b1 against alpha-chymotrypsin were similar to those of native CI-b1.	Disulfides	53-62	chymotrypsin inhibitor SCI-II	Bombyx mori	100-105
15477076-6	2004	Studies on (His)(6)-tagged CI-b1 revealed that three disulfide bonds were formed in the recombinant CI-b1 and the inhibitory properties of recombinant CI-b1 against alpha-chymotrypsin were similar to those of native CI-b1.	Disulfides	53-62	chymotrypsin inhibitor SCI-II	Bombyx mori	100-105
15477076-6	2004	Studies on (His)(6)-tagged CI-b1 revealed that three disulfide bonds were formed in the recombinant CI-b1 and the inhibitory properties of recombinant CI-b1 against alpha-chymotrypsin were similar to those of native CI-b1.	Disulfides	53-62	chymotrypsin inhibitor SCI-II	Bombyx mori	100-105
15294898-8	2004	Intermolecular disulfide bond formation and rotational coupling were also found using a chimera of the extracellular domain of RPTPalpha fused to the transmembrane and intracellular domain of the leukocyte common antigen-related protein (LAR).	Disulfides	15-24	protein tyrosine phosphatase receptor type F	Homo sapiens	196-236
15528998-8	2004	These results suggest that the Cys321 residue is essential for the catalytic function of GABA-T, and that it is involved in the formation of a disulfide link between two monomers of human brain GABA-T.	Disulfides	143-152	4-aminobutyrate aminotransferase	Homo sapiens	194-200
15294898-8	2004	Intermolecular disulfide bond formation and rotational coupling were also found using a chimera of the extracellular domain of RPTPalpha fused to the transmembrane and intracellular domain of the leukocyte common antigen-related protein (LAR).	Disulfides	15-24	protein tyrosine phosphatase receptor type F	Homo sapiens	238-241
15305341-1	2004	BACKGROUND: WAP-type four disulfide core (WFDC1)/ps20 is a member of the whey acidic protein family, which includes several serine protease inhibitors.	Disulfides	26-35	WAP four-disulfide core domain 1	Homo sapiens	42-47
15367692-9	2004	The redox status of Yap1 is substantially unchanged, and protein(s) interaction with Yap1 through disulfide bond is hardly detected in cells treated with MG.	Disulfides	98-107	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	85-89
15358346-1	2004	Transforming growth factor-beta1 (TGF-beta1) is secreted by most cells as a high molecular weight latent complex, which consists of latent TGF-beta1 disulfide bonded to latent TGF-beta1-binding protein (LTBP).	Disulfides	149-158	transforming growth factor beta 1	Homo sapiens	139-148
15358346-1	2004	Transforming growth factor-beta1 (TGF-beta1) is secreted by most cells as a high molecular weight latent complex, which consists of latent TGF-beta1 disulfide bonded to latent TGF-beta1-binding protein (LTBP).	Disulfides	149-158	transforming growth factor beta 1	Homo sapiens	139-148
15358346-5	2004	In addition, Cys 33 of TGF-beta1, which forms a disulfide bond with LTBP, was replaced by a serine residue.	Disulfides	48-57	transforming growth factor beta 1	Homo sapiens	23-32
15471543-3	2004	Inhibin B is comprised of the inhibin alpha subunit disulfide-linked to the inhibin/activin betaB subunit.	Disulfides	52-61	inhibin subunit alpha	Macaca mulatta	30-43
15479236-4	2004	SSA-1 was obtained both as a monomer and a dimer that has an intermolecular disulfide bond.	Disulfides	76-85	tripartite motif containing 21	Homo sapiens	0-5
15305341-1	2004	BACKGROUND: WAP-type four disulfide core (WFDC1)/ps20 is a member of the whey acidic protein family, which includes several serine protease inhibitors.	Disulfides	26-35	WAP four-disulfide core domain 1	Homo sapiens	49-53
15358346-1	2004	Transforming growth factor-beta1 (TGF-beta1) is secreted by most cells as a high molecular weight latent complex, which consists of latent TGF-beta1 disulfide bonded to latent TGF-beta1-binding protein (LTBP).	Disulfides	149-158	transforming growth factor beta 1	Homo sapiens	0-32
15358346-1	2004	Transforming growth factor-beta1 (TGF-beta1) is secreted by most cells as a high molecular weight latent complex, which consists of latent TGF-beta1 disulfide bonded to latent TGF-beta1-binding protein (LTBP).	Disulfides	149-158	transforming growth factor beta 1	Homo sapiens	34-43
15379542-0	2004	Accelerated exchange of a buried water molecule in selectively disulfide-reduced bovine pancreatic trypsin inhibitor.	Disulfides	63-72	trophoblast Kunitz domain protein 1	Bos taurus	99-116
15450603-1	2004	The essential flavoenzyme Ero1p both creates de novo disulfide bonds and transfers these disulfides to the folding catalyst protein disulfide isomerase (PDI).	Disulfides	89-99	protein disulfide isomerase family A member 2	Homo sapiens	153-156
15388324-2	2004	The misfolding and association of B27 heavy chains through non-native disulfide bonds has recently been implicated.	Disulfides	70-79	melanocortin 2 receptor accessory protein	Homo sapiens	34-37
15473697-5	2004	Although the overall structural topology between BACE1 and BACE2 protease domains is quite similar, the former contains 3 disulfide bonds but the latter only two.	Disulfides	122-131	beta-secretase 1	Homo sapiens	49-54
15356344-4	2004	To help fill this gap, we have studied AtFKBP13, an FKBP-type immunophilin earlier shown to interact with a redox-active protein of the lumen, and found the enzyme to contain a pair of disulfide bonds in x-ray structural studies.	Disulfides	185-194	FK506-binding protein 13	Arabidopsis thaliana	39-47
15272010-7	2004	Disulfide cross-linking was detected in CFTR mutants M348C(TM6)/T1142C(TM12), T351C(TM6)/T1142C(TM12), and W356C(TM6)/W1145C(TM12) in a wild-type background.	Disulfides	0-9	CF transmembrane conductance regulator	Homo sapiens	40-44
15226299-0	2004	Identification of disulfide bonds among the nine core 2 N-acetylglucosaminyltransferase-M cysteines conserved in the mucin beta6-N-acetylglucosaminyltransferase family.	Disulfides	18-27	glucosaminyl (N-acetyl) transferase 2, I-branching enzyme	Mus musculus	56-87
15226299-0	2004	Identification of disulfide bonds among the nine core 2 N-acetylglucosaminyltransferase-M cysteines conserved in the mucin beta6-N-acetylglucosaminyltransferase family.	Disulfides	18-27	glucosaminyl (N-acetyl) transferase 2, I-branching enzyme	Mus musculus	129-160
15305013-1	2004	Secretory phospholipase A2 (sPLA2) is a growing family of structurally related, disulfide-rich, low molecular weight, lipolytic enzymes with a His-Asp catalytic dyad.	Disulfides	80-89	phospholipase A2 group X	Homo sapiens	0-26
15387823-5	2004	Although SDS-PAGE studies suggested that the lone cysteine residue at position 71 was involved in interprotomer disulfide-bridging in TraM, altering Cys-71 to a serine did not significantly affect dimerization or the antiactivator activity of this mutant protein when expressed at wild-type levels in vivo.	Disulfides	112-121	translocation associated membrane protein 1	Homo sapiens	134-138
15305013-1	2004	Secretory phospholipase A2 (sPLA2) is a growing family of structurally related, disulfide-rich, low molecular weight, lipolytic enzymes with a His-Asp catalytic dyad.	Disulfides	80-89	phospholipase A2 group X	Homo sapiens	28-33
15304042-8	2004	Moreover, the existence of a subsequent disulfide-linked Cys in gamma 275C fibrinogen augments the impairment caused by a His or Ala substitution.	Disulfides	40-49	fibrinogen beta chain	Homo sapiens	75-85
15322779-4	2004	Unlike avian and mammalian CD4, fugu CD4 lacks the Cys pair of the first Ig-like domain, but has a unique possible disulfide bond in the third domain.	Disulfides	115-124	CD4 molecule	Homo sapiens	37-40
15499198-0	2004	Kinetic studies of covalent binding between N-acetyl-L-cysteine and human serum albumin through a mixed-disulfide using an N-methylpyridinium polymer-based column.	Disulfides	104-113	albumin	Homo sapiens	74-87
15499198-1	2004	The binding properties of the disulfide covalent bond between N-acetyl-L-cysteine (NAC) and human serum albumin (HSA) were investigated.	Disulfides	30-39	albumin	Homo sapiens	98-111
15499198-1	2004	The binding properties of the disulfide covalent bond between N-acetyl-L-cysteine (NAC) and human serum albumin (HSA) were investigated.	Disulfides	30-39	albumin	Homo sapiens	113-116
15123809-2	2004	Rhodopsin dysfunction has been linked to misfolding, caused by chemical modifications that affect the naturally occurring disulfide bond between C110 and C187.	Disulfides	122-131	rhodopsin	Homo sapiens	0-9
15222748-14	2004	By tethering the N- and C-terminal domains of the extracellular alpha subunit, insulin is proposed to stabilize an active conformation of the disulfide-linked transmembrane tyrosine kinase.	Disulfides	142-151	insulin	Homo sapiens	79-86
15075334-7	2004	Further mutagenesis and functional analyses demonstrated that Cys(600) was absolutely essential for ectodomain shedding, suggesting that Cys(600), similar to Cys(225), participates in disulfide bonding, which is critical for both the processing and catalysis of TACE.	Disulfides	184-193	a disintegrin and metallopeptidase domain 17	Mus musculus	262-266
15235575-0	2004	In vitro and in vivo characterization of disulfide bond use in myocilin complex formation.	Disulfides	41-50	myocilin	Homo sapiens	63-71
15235575-4	2004	We investigated the role of these covalent interactions in disulfide bond formation within myocilin.	Disulfides	59-68	myocilin	Homo sapiens	91-99
15235575-9	2004	RESULTS: Human aqueous humor showed myocilin in several distinct large complexes in non-reduced SDS-PAGE gels, indicating disulfide bonds occur.	Disulfides	122-131	myocilin	Homo sapiens	36-44
15235575-15	2004	CONCLUSIONS: Myocilin complexes present in human aqueous humor are in part due to disulfide bond formation between cysteine amino acids.	Disulfides	82-91	myocilin	Homo sapiens	13-21
15181236-2	2004	Thioredoxin reduces exposed protein disulfides and couples with peroxiredoxin to scavenge reactive oxygen species.	Disulfides	36-46	thioredoxin 1	Rattus norvegicus	0-11
15147896-1	2004	Human nerve growth factor (NGF) belongs to the structural family of cystine knot proteins, characterized by a disulfide pattern in which one disulfide bond threads through a ring formed by a pair of two other disulfides connecting two adjacent beta-strands.	Disulfides	110-119	nerve growth factor	Homo sapiens	6-25
15147896-1	2004	Human nerve growth factor (NGF) belongs to the structural family of cystine knot proteins, characterized by a disulfide pattern in which one disulfide bond threads through a ring formed by a pair of two other disulfides connecting two adjacent beta-strands.	Disulfides	110-119	nerve growth factor	Homo sapiens	27-30
15147896-1	2004	Human nerve growth factor (NGF) belongs to the structural family of cystine knot proteins, characterized by a disulfide pattern in which one disulfide bond threads through a ring formed by a pair of two other disulfides connecting two adjacent beta-strands.	Disulfides	141-150	nerve growth factor	Homo sapiens	6-25
15147896-1	2004	Human nerve growth factor (NGF) belongs to the structural family of cystine knot proteins, characterized by a disulfide pattern in which one disulfide bond threads through a ring formed by a pair of two other disulfides connecting two adjacent beta-strands.	Disulfides	141-150	nerve growth factor	Homo sapiens	27-30
15147896-1	2004	Human nerve growth factor (NGF) belongs to the structural family of cystine knot proteins, characterized by a disulfide pattern in which one disulfide bond threads through a ring formed by a pair of two other disulfides connecting two adjacent beta-strands.	Disulfides	209-219	nerve growth factor	Homo sapiens	6-25
15147896-1	2004	Human nerve growth factor (NGF) belongs to the structural family of cystine knot proteins, characterized by a disulfide pattern in which one disulfide bond threads through a ring formed by a pair of two other disulfides connecting two adjacent beta-strands.	Disulfides	209-219	nerve growth factor	Homo sapiens	27-30
15210130-10	2004	Thus, the presence of redox agents interfered with the ability of the tailspike monomers to associate, demonstrating that disulfide associations play an important role during the assembly of this cytoplasmic protein.	Disulfides	122-131	basic leucine zipper nuclear factor 1	Homo sapiens	196-215
15261455-5	2004	Conserved glycosilation sites (beta19) and cysteine residues (beta15, beta79, beta117, beta173) forming disulfide bridges have been identified in the goat DQB1 molecule.	Disulfides	104-113	boLa class II histocompatibility antigen, DQB*0101 beta chain	Bos taurus	155-159
15182179-1	2004	The redox-active dithiol/disulfide C315-Xaa-Xaa-C318 center has been implicated in the regulation of the human mitochondrial branched chain aminotransferase isozyme (hBCATm) [Conway, M. E., Yennawar, N., Wallin, R., Poole, L. B., and Hutson, S. M. (2002) Biochemistry 41, 9070-9078].	Disulfides	25-34	branched chain amino acid transaminase 2	Homo sapiens	166-172
15165856-4	2004	In the crystal structure, ferric Cgb is dimerized through two intermolecular disulfide bonds between Cys38(B2) and Cys83(E9), and the dimerization interface is similar to that of lamprey Hb and Ngb.	Disulfides	77-86	cytoglobin	Homo sapiens	33-36
15163543-5	2004	On the other hand, arsenite has high affinity for sulfhydryl groups and thus can form covalent bonds with the disulfide bridges in the molecules of insulin, insulin receptors, glucose transporters (GLUTs), and enzymes involved in glucose metabolism (e.g., pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase).	Disulfides	110-119	insulin	Homo sapiens	148-155
15163543-5	2004	On the other hand, arsenite has high affinity for sulfhydryl groups and thus can form covalent bonds with the disulfide bridges in the molecules of insulin, insulin receptors, glucose transporters (GLUTs), and enzymes involved in glucose metabolism (e.g., pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase).	Disulfides	110-119	insulin	Homo sapiens	157-164
15122914-2	2004	We analyzed the extent of the formation of a disulfide bond in each lysozyme variant using a redox buffer (pH 8) containing 1.0 mM reduced and 0.1 mM oxidized glutathione in the absence or presence of 6 M guanidine hydrochloride.	Disulfides	45-54	lysozyme	Homo sapiens	68-76
15122914-3	2004	In the presence of 6 M guanidine hydrochloride, the extent of the formation of the disulfide bond in each lysozyme variant was proportional to the distance between cysteine residues, indicating that reduced hen lysozyme under a highly denaturing condition adopted a randomly coiled structure.	Disulfides	83-92	lysozyme	Homo sapiens	106-114
15122914-3	2004	In the presence of 6 M guanidine hydrochloride, the extent of the formation of the disulfide bond in each lysozyme variant was proportional to the distance between cysteine residues, indicating that reduced hen lysozyme under a highly denaturing condition adopted a randomly coiled structure.	Disulfides	83-92	lysozyme	Homo sapiens	211-219
15122914-6	2004	Moreover, the scattering data for the extents of the formation of the disulfide bonds among all lysozyme variants were observed.	Disulfides	70-79	lysozyme	Homo sapiens	96-104
15123809-8	2004	Fast mode analysis of rhodopsin using the Gaussian network model also identifies the disulfide bond and the retinal ligand binding pocket to be the most rigid region in rhodopsin.	Disulfides	85-94	rhodopsin	Homo sapiens	22-31
15123809-8	2004	Fast mode analysis of rhodopsin using the Gaussian network model also identifies the disulfide bond and the retinal ligand binding pocket to be the most rigid region in rhodopsin.	Disulfides	85-94	rhodopsin	Homo sapiens	169-178
15109247-0	2004	An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis.	Disulfides	16-25	superoxide dismutase 1	Homo sapiens	66-88
15181931-4	2004	Dimerisation and specific binding of PrPc and PrPSc seems critical in PrPSc biosynthesis and is influenced by N-glycosylation and disulfide bond formation.	Disulfides	130-139	prion protein	Homo sapiens	37-41
15081894-1	2004	The disulfide bonds of the Na(+)/glucose cotransporter (SGLT1) are believed to participate in the binding of the transport inhibitor phlorizin.	Disulfides	4-13	solute carrier family 5 member 1	Homo sapiens	56-61
15081894-2	2004	Here, we investigated the role of the [560-608] disulfide bond on the phlorizin-binding function of the C-terminal loop 13 of SGLT1 using 3-iodoacetamidophlorizin (3-IAP) as a probe.	Disulfides	48-57	solute carrier family 5 member 1	Homo sapiens	126-131
15141017-0	2004	Disulfide-constrained peptides that bind to the extracellular portion of the prostate-specific membrane antigen.	Disulfides	0-9	folate hydrolase 1	Homo sapiens	77-111
15096212-2	2004	We have investigated the in vitro refolding process of human proinsulin (HPI) and an artificial mini-C derivative of HPI (porcine insulin precursor, PIP), and found that they have significantly different disulfide-formation pathways.	Disulfides	204-213	insulin	Homo sapiens	61-71
15096212-2	2004	We have investigated the in vitro refolding process of human proinsulin (HPI) and an artificial mini-C derivative of HPI (porcine insulin precursor, PIP), and found that they have significantly different disulfide-formation pathways.	Disulfides	204-213	prolactin induced protein	Homo sapiens	149-152
15096212-6	2004	The results show that disulfide reshuffling is easier to induce in HPI than in PIP by the addition of thiol reagent.	Disulfides	22-31	prolactin induced protein	Homo sapiens	79-82
14871896-3	2004	Here we have characterized several fundamental structural and functional properties of ERp57 in vitro, such as the domain organization, shape, redox potential, and the ability to catalyze different thiol-disulfide exchange reactions.	Disulfides	204-213	protein disulfide isomerase family A member 3	Homo sapiens	87-92
14871896-7	2004	Furthermore, ERp57 was shown to efficiently catalyze disulfide reduction, disulfide isomerization, and dithiol oxidation in substrate proteins.	Disulfides	53-62	protein disulfide isomerase family A member 3	Homo sapiens	13-18
14871896-7	2004	Furthermore, ERp57 was shown to efficiently catalyze disulfide reduction, disulfide isomerization, and dithiol oxidation in substrate proteins.	Disulfides	74-83	protein disulfide isomerase family A member 3	Homo sapiens	13-18
15050830-1	2004	NMR spectroscopy has been used to follow the urea-induced unfolding of the low pH molten globule states of a single-disulfide variant of human alpha-lactalbumin ([28-111] alpha-LA) and of two mutants, each with a single proline substitution in a helix.	Disulfides	116-125	lactalbumin alpha	Homo sapiens	143-160
15050830-2	2004	[28-111] alpha-LA forms a molten globule very similar to that formed by the wild-type four-disulfide protein, and this variant has been used as a model for the alpha-lactalbumin (alpha-LA) molten globule in a number of studies.	Disulfides	91-100	lactalbumin alpha	Homo sapiens	9-17
15070359-0	2004	Structural change of the heme pocket due to disulfide bridge formation is significantly larger for neuroglobin than for cytoglobin.	Disulfides	44-53	cytoglobin	Homo sapiens	120-130
15070359-1	2004	Human neuroglobin (hNgb) and human cytoglobin (hCygb), two recently discovered members of the vertebrate globin family, are known to be able to form an intramolecular disulfide bridge.	Disulfides	167-176	cytoglobin	Homo sapiens	35-53
15123246-3	2004	The rates of reduction of bovine pancreatic ribonuclease A (RNase A) and RNase B and the formation and consumption of their reductive intermediates are identical, indicating that the unfolding events necessary to expose disulfide bonds for reduction are not affected by the oligosaccharide.	Disulfides	220-229	ribonuclease pancreatic	Bos taurus	44-58
14744871-3	2004	To examine the fate of aberrant forms of a well characterized, disulfide-bonded secreted protein, we expressed bovine pancreatic trypsin inhibitor in yeast.	Disulfides	63-72	trophoblast Kunitz domain protein 1	Bos taurus	129-146
14744871-4	2004	Bovine pancreatic trypsin inhibitor is a single domain, 58-amino acid polypeptide containing three disulfide bonds, and yeast cells secrete the wild type protein.	Disulfides	99-108	trophoblast Kunitz domain protein 1	Bos taurus	18-35
14729680-1	2004	The extracellular calcium-sensing receptor (CaR) forms a disulfide-linked dimer through cysteine residues within its N-terminal extracellular domain (ECD).	Disulfides	57-66	calcium sensing receptor	Homo sapiens	18-42
14729680-1	2004	The extracellular calcium-sensing receptor (CaR) forms a disulfide-linked dimer through cysteine residues within its N-terminal extracellular domain (ECD).	Disulfides	57-66	calcium sensing receptor	Homo sapiens	44-47
15039220-1	2004	IL-12 consists of two disulfide-linked subunits, p40 and p35, that form functionally active heterodimers for the induction of Th1 cells.	Disulfides	22-31	negative elongation factor complex member C/D, Th1l	Mus musculus	126-129
14732708-0	2004	Appropriate NR1-NR1 disulfide-linked homodimer formation is requisite for efficient expression of functional, cell surface N-methyl-D-aspartate NR1/NR2 receptors.	Disulfides	20-29	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	12-19
14732708-0	2004	Appropriate NR1-NR1 disulfide-linked homodimer formation is requisite for efficient expression of functional, cell surface N-methyl-D-aspartate NR1/NR2 receptors.	Disulfides	20-29	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	12-15
14732708-5	2004	Two-dimensional electrophoresis under non-reducing and reducing conditions revealed that the 226-kDa band contained disulfide-linked NR1-2a subunits.	Disulfides	116-125	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	133-136
14732708-7	2004	The c-Myc epitope is inserted adjacent to cysteine 79 of the NR1-2a subunit; therefore, it is possible that the tag may prevent the formation of NR1 disulfide bridges.	Disulfides	149-158	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	61-64
14732708-7	2004	The c-Myc epitope is inserted adjacent to cysteine 79 of the NR1-2a subunit; therefore, it is possible that the tag may prevent the formation of NR1 disulfide bridges.	Disulfides	149-158	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	145-148
14732708-10	2004	These results provide the first biochemical evidence for the formation of NR1-NR1 intersubunit disulfide-linked homodimers involving cysteine 79.	Disulfides	95-104	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	74-81
14732708-11	2004	They suggest that disulfide bridging and structural integrity within the NR1 N-terminal domain is requisite for cell surface N-methyl-D-aspartate receptor expression.	Disulfides	18-27	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	73-76
15002034-5	2004	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that CEA-Fc formed disulfide-linked dimers with a molecular weight of about 170 kDa and a monomer size of 85kDa.	Disulfides	95-104	CEA cell adhesion molecule 3	Homo sapiens	81-84
14574523-5	2004	We performed a series of molecular dynamics simulations of insulin in solution under equilibrium conditions, under chemical stress (imitated by reducing the disulfide bonds in the protein molecule), and under short-lived thermal stress (imitated by increasing simulation temperature for up to 2 ns).	Disulfides	157-166	insulin	Homo sapiens	59-66
15016916-2	2004	Here, we show that an intrinsically unfolded protein (U), represented by a disulfide-deficient variant of hen lysozyme with no tertiary structure, forms an amyloid-like fibril after prolonged incubation.	Disulfides	75-84	lysozyme	Homo sapiens	110-118
15111715-2	2004	Reduction of the disulfide bonds of the CM proteins with thioredoxin or dithiothreitol altered their properties so that, like the metabolic proteins, they were insoluble in methanol.	Disulfides	17-26	thioredoxin H4-2	Triticum aestivum	57-68
15023075-4	2004	The nature of des [30-75] is similar to that of des [40-95] RNase A, in that des [30-75] ONC is also a disulfide-secure species.	Disulfides	103-112	ribonuclease pancreatic	Bos taurus	60-67
14985508-9	2004	up to 48 h), a disulfide compound shown to induce Nrf2 activation in vitro and improve GSH levels in vivo.	Disulfides	15-24	NFE2 like bZIP transcription factor 2	Rattus norvegicus	50-54
14985082-3	2004	Being highly susceptible to oxidation Hsp22 forms disulfide crosslinked dimers and poorly soluble high molecular mass oligomers.	Disulfides	50-59	heat shock protein family B (small) member 8	Homo sapiens	38-43
15009465-0	2004	Recombinant fibrinogen, gamma275Arg--&gt;Cys, exhibits formation of disulfide bond with cysteine and severely impaired D:D interactions.	Disulfides	68-77	fibrinogen beta chain	Homo sapiens	12-22
15801461-2	2004	Covalent immobilization was achieved by the formation of a disulfide bond between N-succinimidyl 3-(2-pyridyldithio)propionate-(SPDP-) modified cytochrome c and SPDP-silanized ITO.	Disulfides	59-68	cytochrome c, somatic	Homo sapiens	144-156
15004694-4	2004	Most recently, specific ERp57-mediated disulfide bond rearrangements have been identified inside the loading complex.	Disulfides	39-48	protein disulfide isomerase family A member 3	Homo sapiens	24-29
14978101-8	2004	Mutagenesis of these cysteines decreases tapasin"s electrophoretic mobility, suggesting that these residues form an intramolecular disulfide bond.	Disulfides	131-140	TAP binding protein	Homo sapiens	41-48
14670948-0	2004	Disulfide cross-linking analysis shows that transmembrane segments 5 and 8 of human P-glycoprotein are close together on the cytoplasmic side of the membrane.	Disulfides	0-9	ATP binding cassette subfamily B member 1	Homo sapiens	84-98
14673134-3	2004	The wild-type human AMH protein is synthesized as a disulfide-linked dimer of two identical 70-kDa polypeptides, which undergoes proteolytic processing to generate a 110-kDa N-terminal dimer and a bioactive 25-kDa TGF-beta-like C-terminal dimer.	Disulfides	52-61	transforming growth factor beta 1	Homo sapiens	214-222
14963131-0	2004	Vaccinia virus A28L gene encodes an essential protein component of the virion membrane with intramolecular disulfide bonds formed by the viral cytoplasmic redox pathway.	Disulfides	107-116	hypothetical protein	Vaccinia virus	15-19
14990700-5	2004	Mutational and biophysical analysis suggested that the internal fusion peptide of p10 lacks alpha-helical content and exists as a disulfide-stabilized loop structure.	Disulfides	130-139	S100 calcium binding protein A10	Homo sapiens	82-85
14668347-3	2004	Three of these genes (designated AAT-1 to AAT-3) have a much higher degree of similarity to the mammalian homologues than the other six, including the presence of a cysteine residue at the position known to form a disulfide bridge to the glycoprotein partner in mammalian HATs.	Disulfides	214-223	AAT1	Homo sapiens	33-47
14676218-7	2004	Furthermore Grx2 was a substrate for NADPH and thioredoxin reductase, which efficiently reduced both the active site disulfide and the GSH-glutaredoxin intermediate formed in the reduction of glutathionylated substrates.	Disulfides	117-126	glutaredoxin 2	Homo sapiens	12-16
14670948-3	2004	We used cysteine-scanning mutagenesis and disulfide cross-linking analysis to determine which TM segment in the COOH half of P-gp was close to TMs 5 and 6 since these segments in the NH(2) half are important for drug binding.	Disulfides	42-51	ATP binding cassette subfamily B member 1	Homo sapiens	125-129
14676218-8	2004	Using this novel electron donor pathway, Grx2 reduced low molecular weight disulfides such as CoA but with particular high efficiency glutathionylated substrates including GSSG.	Disulfides	75-85	glutaredoxin 2	Homo sapiens	41-45
14755371-0	2004	C1272S: a new candidate mutation in type 2A von Willebrand disease that disrupts the disulfide loop responsible for the interaction of VWF with platelet GP Ib-IX.	Disulfides	85-94	von Willebrand factor	Homo sapiens	135-138
14975452-2	2004	Herein we report that peroxynitrite-induced disulfides in porcine brain tubulin are repaired by the thioredoxin reductase system composed of rat liver thioredoxin reductase, human or Escherichia coli thioredoxin, and NADPH.	Disulfides	44-54	peroxiredoxin 5	Rattus norvegicus	100-121
14739934-5	2004	Based on disulfide engineering and structure-guided suppressor analyses, Pre6 takes the position normally occupied by Pre9, a substitution that depends on a network of intersubunit salt bridges.	Disulfides	9-18	proteasome core particle subunit alpha 4	Saccharomyces cerevisiae S288C	73-77
14755371-5	2004	This candidate mutation would interrupt the formation of the disulfide loop 1272-1458, which is important in maintaining the adequate conformation of the VWF functional domain that interacts with platelet glycoprotein Ib-IX.	Disulfides	61-70	von Willebrand factor	Homo sapiens	154-157
14999003-0	2004	Flexibility exists in the region of [A6-A11, A7-B7] disulfide bonds during insulin precursor folding.	Disulfides	52-61	insulin	Homo sapiens	75-82
15625578-1	2004	Thioredoxin (Trx) is a multifunctional protein with a redox-active disulfide/dithiol in the active site.	Disulfides	67-76	thioredoxin 1	Rattus norvegicus	0-11
15625578-1	2004	Thioredoxin (Trx) is a multifunctional protein with a redox-active disulfide/dithiol in the active site.	Disulfides	67-76	thioredoxin 1	Rattus norvegicus	13-16
12962983-6	2004	The overall structure of IgE, i.e. four constant domains and the positions of putative disulfide-bridge formations, are conserved, as is an N-glycosylation site in the third constant domain.	Disulfides	87-96	immunoglobulin heavy constant epsilon	Homo sapiens	25-28
14607843-7	2004	In an effort to identify target proteins of TRP14, a mutant of TRP14, in which the active site cysteine (Cys(46)) was substituted with serine, was shown to form a disulfide-linked complex with LC8 cytoplasmic dynein light chain.	Disulfides	163-172	dynein light chain LC8-type 1	Homo sapiens	193-196
14741343-2	2004	Equilibrium intermediates of disulfide reduced lysozyme in TFE are known to contain considerable amounts of alpha-helical structure and resemble the early intermediate in the oxidative refolding of lysozyme.	Disulfides	29-38	lysozyme	Homo sapiens	47-55
14741343-2	2004	Equilibrium intermediates of disulfide reduced lysozyme in TFE are known to contain considerable amounts of alpha-helical structure and resemble the early intermediate in the oxidative refolding of lysozyme.	Disulfides	29-38	lysozyme	Homo sapiens	198-206
14561762-1	2004	The recently discovered cyclotides kalata B1 and kalata B2 are miniproteins containing a head-to-tail cyclized backbone and a cystine knot motif, in which disulfide bonds and the connecting backbone segments form a ring that is penetrated by the third disulfide bond.	Disulfides	155-164	immunoglobulin kappa variable 7-3 (pseudogene)	Homo sapiens	42-58
14561762-1	2004	The recently discovered cyclotides kalata B1 and kalata B2 are miniproteins containing a head-to-tail cyclized backbone and a cystine knot motif, in which disulfide bonds and the connecting backbone segments form a ring that is penetrated by the third disulfide bond.	Disulfides	252-261	immunoglobulin kappa variable 7-3 (pseudogene)	Homo sapiens	42-58
15706060-1	2004	Capsaicin and the principal green tea catechin, (-)-epigallocatechin-3-gallate (EGCg), target tNOX, a tumor (cancer)-specific surface hydroquinone (NADH) oxidase with protein disulfide-thiol interchange activity (ECTO-NOX protein).	Disulfides	175-184	ecto-NOX disulfide-thiol exchanger 2	Homo sapiens	94-98
15379675-3	2004	In this article, we will review the "classical" functions of 3 classes of antimicrobial molecules, namely defensins, cathelicidins, and the four-disulfide core proteins secretory leukocyte proteinase inhibitor (SLPI) and elafin.	Disulfides	145-154	secretory leukocyte peptidase inhibitor	Homo sapiens	169-209
15379675-3	2004	In this article, we will review the "classical" functions of 3 classes of antimicrobial molecules, namely defensins, cathelicidins, and the four-disulfide core proteins secretory leukocyte proteinase inhibitor (SLPI) and elafin.	Disulfides	145-154	secretory leukocyte peptidase inhibitor	Homo sapiens	211-215
14999003-3	2004	The results indicate that the shift mutation in the disulfide bond caused more conformational change and a greater decrease in biological activity than the deletion mutation on the proinsulin molecule.	Disulfides	52-61	insulin	Homo sapiens	181-191
14999006-0	2004	Effects of deletion and shift of the A20-B19 disulfide bond on the structure, activity, and refolding of proinsulin.	Disulfides	45-54	insulin	Homo sapiens	105-115
14985534-0	2004	Covalent disulfide-linked anti-CEA diabody allows site-specific conjugation and radiolabeling for tumor targeting applications.	Disulfides	9-18	carcinoembryonic antigen gene family	Mus musculus	31-34
14750599-2	2004	Peripherin 2 and ROM1 assemble as a mixture of core noncovalent homomeric and heteromeric tetramers that further link together through disulfide bonds to form higher order oligomers.	Disulfides	135-144	peripherin 2 (retinal degeneration, slow) S homeolog	Xenopus laevis	0-12
15507277-4	2004	The binding site for GPIbalpha on vWF resides in the conserved A1 domain, encompassing the disulfide bond at Cys509-Cys695.	Disulfides	91-100	von Willebrand factor	Homo sapiens	34-37
15115177-0	2004	Two-state folding of lysozyme versus multiple-state folding of alpha-lactalbumin illustrated by the technique of disulfide scrambling.	Disulfides	113-122	lactalbumin alpha	Homo sapiens	63-80
15115177-3	2004	We demonstrate here such divergent folding mechanisms of lysozyme and alphaLA using the technique of disulfide scrambling.	Disulfides	101-110	lysozyme	Homo sapiens	57-65
15384137-2	2004	In particular, human growth hormone (hGH) (200 fmol) was analyzed with high sequence coverage (&gt;95%), including the sites of disulfide linkages.	Disulfides	128-137	growth hormone 1	Homo sapiens	21-35
14530264-4	2003	Both cysteine residues in cytoglobin, although localized in other positions than in human neuroglobin, may form a disulfide bond as well.	Disulfides	114-123	cytoglobin	Homo sapiens	26-36
14744022-0	2003	Role of disulfide bonds in the structure and activity of human insulin.	Disulfides	8-17	insulin	Homo sapiens	63-70
14744022-1	2003	Insulin contains two inter-chain disulfide bonds between the A and B chains (A7-B7 and A20-B19), and one intra-chain linkage in the A chain (A6-A11).	Disulfides	33-42	insulin	Homo sapiens	0-7
14744022-3	2003	Structural and biological studies of the three des mutants revealed that all three disulfide bonds are essential for the receptor binding activity of insulin, whereas the different disulfide bonds make different contributions to the overall structure of insulin.	Disulfides	83-92	insulin	Homo sapiens	150-157
14744022-3	2003	Structural and biological studies of the three des mutants revealed that all three disulfide bonds are essential for the receptor binding activity of insulin, whereas the different disulfide bonds make different contributions to the overall structure of insulin.	Disulfides	181-190	insulin	Homo sapiens	254-261
14744022-6	2003	In addition, different refolding efficiencies between the three des mutants suggest that the disulfide bonds are formed sequentially in the order A20-B19, A7-B7 and A6-A11 in the folding pathway of proinsulin.	Disulfides	93-102	insulin	Homo sapiens	198-208
14690403-0	2003	Steric effects governing disulfide bond interchange during thermal aggregation in solutions of beta-lactoglobulin B and alpha-lactalbumin.	Disulfides	25-34	lactalbumin alpha	Homo sapiens	120-137
14690403-1	2003	Intermolecular disulfide bond formation in pure beta-lactoglobulin (beta-Lg) B and in its 1:1 mixture with alpha-lactalbumin (alpha-La), heated at 85 degrees C for 10 min in solutions of low and high (100 mM NaCl) ionic strength and pH 6.0, was studied by reverse-phase HPLC and MALDI-TOF mass spectrometry.	Disulfides	15-24	lactalbumin alpha	Homo sapiens	107-124
14690403-1	2003	Intermolecular disulfide bond formation in pure beta-lactoglobulin (beta-Lg) B and in its 1:1 mixture with alpha-lactalbumin (alpha-La), heated at 85 degrees C for 10 min in solutions of low and high (100 mM NaCl) ionic strength and pH 6.0, was studied by reverse-phase HPLC and MALDI-TOF mass spectrometry.	Disulfides	15-24	lactalbumin alpha	Homo sapiens	126-134
14690424-0	2003	Solution structure of the disulfide-linked dimer of human intestinal trefoil factor (TFF3): the intermolecular orientation and interactions are markedly different from those of other dimeric trefoil proteins.	Disulfides	26-35	trefoil factor 3	Homo sapiens	85-89
14690424-1	2003	The trefoil protein TFF3 forms a homodimer (via a disulfide linkage) that is thought to have increased biological activity over the monomer.	Disulfides	50-59	trefoil factor 3	Homo sapiens	20-24
14522978-2	2003	GRX functions via a disulfide exchange reaction by utilizing the active site Cys-Pro-Tyr-Cys.	Disulfides	20-29	glutaredoxin	Rattus norvegicus	0-3
14522978-5	2003	Under stress, Akt underwent disulfide bond formation between Cys-297 and Cys-311 and dephosphorylation in accordance with an increased association with protein phosphatase 2A.	Disulfides	28-37	AKT serine/threonine kinase 1	Rattus norvegicus	14-17
12954635-0	2003	Highly conserved cysteines of mouse core 2 beta1,6-N-acetylglucosaminyltransferase I form a network of disulfide bonds and include a thiol that affects enzyme activity.	Disulfides	103-112	glucosaminyl (N-acetyl) transferase 2, I-branching enzyme	Mus musculus	43-82
12947032-0	2003	Glutamine and KGF each regulate extracellular thiol/disulfide redox and enhance proliferation in Caco-2 cells.	Disulfides	52-61	fibroblast growth factor 7	Homo sapiens	14-17
14563687-0	2003	An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling.	Disulfides	98-107	ATP binding cassette subfamily B member 1	Homo sapiens	70-84
14615576-3	2003	Cu/Zn-SOD is a homodimer containing four cysteine residues within each subunit, and EC-SOD is a tetramer composed of two disulfide-bonded dimers in which each subunit contains six cysteines.	Disulfides	121-130	superoxide dismutase 3	Homo sapiens	84-90
14615576-7	2003	The results show that human EC-SOD exists in two forms, each with a unique disulfide bridge pattern.	Disulfides	75-84	superoxide dismutase 3	Homo sapiens	28-34
14615576-8	2003	One form (active EC-SOD) is enzymatically active and contains a disulfide bridge pattern similar to Cu/Zn-SOD.	Disulfides	64-73	superoxide dismutase 3	Homo sapiens	17-23
14615576-9	2003	The other form (inactive EC-SOD) has a different disulfide bridge pattern and is enzymatically inactive.	Disulfides	49-58	superoxide dismutase 3	Homo sapiens	25-31
12947032-2	2003	We determined whether Gln and KGF alter intra- and extracellular thiol/disulfide redox pools in Caco-2 cells cultured in oxidizing or reducing cell medium and whether such redox variations are a determinant of proliferative responses to these agents.	Disulfides	71-80	fibroblast growth factor 7	Homo sapiens	30-33
12947032-9	2003	The results indicate that thiol/disulfide redox state in the extracellular milieu is an important determinant of Caco-2 cell proliferation induced by Gln and KGF, that this control is independent of intracellular GSH redox status, and that both Gln and KGF enhance the capability of Caco-2 cells to modulate extremes of extracellular redox.	Disulfides	32-41	fibroblast growth factor 7	Homo sapiens	158-161
12947032-9	2003	The results indicate that thiol/disulfide redox state in the extracellular milieu is an important determinant of Caco-2 cell proliferation induced by Gln and KGF, that this control is independent of intracellular GSH redox status, and that both Gln and KGF enhance the capability of Caco-2 cells to modulate extremes of extracellular redox.	Disulfides	32-41	fibroblast growth factor 7	Homo sapiens	253-256
14628104-4	2003	A cysteine residue in the second cytoplasmic domain in mammalian C5aR, required for formation of disulfide-linked dimers, is seen in trout C5aR but not in other similar rhodopsin-like receptors.	Disulfides	97-106	complement C5a receptor 1	Homo sapiens	65-69
14623191-8	2003	To further characterize the folding of SOD1, we study the role of cysteine residues in folding and find that non-native disulfide bond formation may significantly alter SOD1 folding dynamics and aggregation propensity.	Disulfides	120-129	superoxide dismutase 1	Homo sapiens	39-43
14623191-8	2003	To further characterize the folding of SOD1, we study the role of cysteine residues in folding and find that non-native disulfide bond formation may significantly alter SOD1 folding dynamics and aggregation propensity.	Disulfides	120-129	superoxide dismutase 1	Homo sapiens	169-173
12954635-5	2003	The only non-conserved residue within the beta1,6-N-acetylglucosaminyltransferase family, Cys235, is also a free thiol in the presence of dithiothreitol; however, in the absence of reductant, Cys235 forms an intermolecular disulfide linkage.	Disulfides	223-232	glucosaminyl (N-acetyl) transferase 2, I-branching enzyme	Mus musculus	42-81
14573855-0	2003	Peptide models of four possible insulin folding intermediates with two disulfides.	Disulfides	71-81	insulin	Homo sapiens	32-39
14573855-6	2003	In redox buffer, the disulfides of the model peptides are more easily reduced than those of the wild-type PIP.	Disulfides	21-31	prolactin induced protein	Homo sapiens	106-109
12893820-2	2003	C4BP is a disulfide-linked polymer of seven alpha-chains and a unique beta-chain, the alpha- and beta-chains being composed of eight and three complement control protein (CCP) domains, respectively.	Disulfides	10-19	complement component 4 binding protein alpha	Homo sapiens	0-4
14556853-2	2003	Activation by H2O2 involves Yap1 Cys303-Cys598 intra-molecular disulfide bond formation directed by the H2O2 sensor Orp1/Gpx3.	Disulfides	63-72	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	28-32
14556629-0	2003	The redox domain of the Yap1p transcription factor contains two disulfide bonds.	Disulfides	64-73	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	24-29
14556629-5	2003	MALDI-TOF mass spectrometry analysis revealed that the oxidized form of Yap1p contains two disulfide bonds between C303-C598 and C310-C629.	Disulfides	91-100	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	72-77
13679035-5	2003	In contrast, only one of the single mutants of disulfide bonds C22-C157 and C136-C201 (missing from human trypsin 2) was expressed in E. coli.	Disulfides	47-56	serine protease 2	Homo sapiens	106-115
14516203-1	2003	To assess the role of the [65-72] disulfide bond in the oxidative folding of RNase A, use has been made of [C65S, C72S], a three-disulfide-containing mutant of RNase A which regenerates from its two-disulfide precursor in an oxidation and conformational folding-coupled rate-determining step.	Disulfides	34-43	ribonuclease pancreatic	Bos taurus	77-84
13679575-3	2003	Furthermore, as shown by x-ray analysis, the disulfide-bridged nonapeptide, nonhelical in aqueous solutions, is able to adopt a quasihelical conformer while binding to the groove created by ligand attachment to estrogen receptor alpha.	Disulfides	45-54	estrogen receptor 1	Homo sapiens	211-234
14517240-3	2003	Here we show that ERp44 mediates Ero1alpha ER localization through the formation of reversible mixed disulfides.	Disulfides	101-111	endoplasmic reticulum protein 44	Homo sapiens	18-23
14580323-0	2003	Formation of disulfide bond in p53 correlates with inhibition of DNA binding and tetramerization.	Disulfides	13-22	tumor protein p53	Homo sapiens	31-34
14580323-5	2003	Sulfite-mediated disulfide bond cleavage followed by reaction with 2-nitro-5-thiosulfobenzoate showed that oxidized p53 contains a single disulfide bond per monomer.	Disulfides	17-26	tumor protein p53	Homo sapiens	116-119
14580323-5	2003	Sulfite-mediated disulfide bond cleavage followed by reaction with 2-nitro-5-thiosulfobenzoate showed that oxidized p53 contains a single disulfide bond per monomer.	Disulfides	138-147	tumor protein p53	Homo sapiens	116-119
14499592-6	2003	Upon reduction with dithiothreitol (DTT), alpha-thrombin unfolded in a "sequential" manner with sequential reduction of Cys(168)-Cys(182) within the B-chain followed by the inter-chain disulfide, generating two distinct partially reduced intermediates, I-1 and I-2, respectively.	Disulfides	185-194	coagulation factor II, thrombin	Homo sapiens	48-56
12972292-5	2003	We conclude that the ETB receptor shows remarkable stability in lysosomes, held together by disulfide bonds, and maintaining ligand binding for long periods of time.	Disulfides	92-101	endothelin receptor type B	Homo sapiens	21-24
14499592-4	2003	alpha-Thrombin is composed of a light A-chain (36 residues) and a heavy B-chain (259 residues) linked covalently by an inter-chain disulfide bond (Cys(1)-Cys(122)).	Disulfides	131-140	coagulation factor II, thrombin	Homo sapiens	6-14
14499592-7	2003	Conformational stability of alpha-thrombin was investigated by the technique of disulfide scrambling.	Disulfides	80-89	coagulation factor II, thrombin	Homo sapiens	34-42
14499592-8	2003	alpha-Thrombin denatures by scrambling its native disulfide bonds in the presence of denaturant [urea, guanidine hydrochloride (GdmCl) or guanidine thiocyanate (GdmSCN)] and a thiol initiator.	Disulfides	50-59	coagulation factor II, thrombin	Homo sapiens	6-14
12845650-1	2003	Interleukin-12 (IL-12) is a disulfide-linked p40-p35 heterodimeric cytokine and plays a key role in linking innate cellular immunity to an adaptive Th1 response against pathogens and tumor cells and in counteracting a Th2 immune response.	Disulfides	28-37	negative elongation factor complex member C/D, Th1l	Mus musculus	148-151
14522910-6	2003	The ps20 protein contains a whey acidic protein-type four-disulfide core domain, which is a functional motif characterized by serine protease inhibition activity in a number of whey acidic protein domain-containing proteins.	Disulfides	58-67	WAP four-disulfide core domain 1	Homo sapiens	4-8
14522910-6	2003	The ps20 protein contains a whey acidic protein-type four-disulfide core domain, which is a functional motif characterized by serine protease inhibition activity in a number of whey acidic protein domain-containing proteins.	Disulfides	58-67	coagulation factor II, thrombin	Homo sapiens	126-141
12791669-3	2003	We have shown that disulfide exchange is necessary for platelet adhesion to fibrinogen, fibronectin, and collagen.	Disulfides	19-28	fibrinogen beta chain	Homo sapiens	76-86
12791669-3	2003	We have shown that disulfide exchange is necessary for platelet adhesion to fibrinogen, fibronectin, and collagen.	Disulfides	19-28	fibronectin 1	Homo sapiens	88-99
12835318-5	2003	We used disulfide-trapping experiments to show that C5a receptors, expressed in mammalian cells, reside in membranes as oligomers (Klco, J. M., Lassere, T. B., and Baranski, T. J.	Disulfides	8-17	complement C5a receptor 1	Homo sapiens	52-55
12835319-6	2003	Using a disulfide-trapping strategy to probe the intermolecular contact surfaces, we demonstrate cross-linking of C5a receptors in membranes prepared from both human neutrophils and stably transfected mammalian cells that is mediated by a cysteine in the second intracellular loop.	Disulfides	8-17	complement C5a receptor 1	Homo sapiens	114-117
12796500-12	2003	Cyclo-57,60-[Asp57,Dap60]MIF-(50-65) activated ERK1/2, indicating that CXXC-dependent disulfide and beta-turn formation is associated with an activity-inducing conformation.	Disulfides	86-95	mitogen-activated protein kinase 3	Homo sapiens	47-53
12957712-1	2003	Several cyclic disulfide alpha-melanocyte stimulating hormone (alpha-MSH) analogues containing the aromatic fluorescent amino acid beta-(2-naphthyl)-D-alanine (D-Nal) have high affinity and selectivity for the melanocortin (MC)-4 receptor.	Disulfides	15-24	proopiomelanocortin	Homo sapiens	25-61
12957712-1	2003	Several cyclic disulfide alpha-melanocyte stimulating hormone (alpha-MSH) analogues containing the aromatic fluorescent amino acid beta-(2-naphthyl)-D-alanine (D-Nal) have high affinity and selectivity for the melanocortin (MC)-4 receptor.	Disulfides	15-24	proopiomelanocortin	Homo sapiens	63-72
12967471-5	2003	Transgenic mice expressing VEGF-E(NZ-7) showed a dramatic increase in angiogenesis with very few side effects (such as edema and hemorrhagic spots), suggesting strong angiogenic signaling and a potential clinical utility of VEGF-E. VEGF family members bear three loops produced via three intramolecular disulfide bonds, and cooperation between loop-1 and loop-3 is necessary for the specific binding and activation of VEGFR-2 for angiogenesis.	Disulfides	303-312	vascular endothelial growth factor A	Homo sapiens	27-31
12815038-9	2003	We validate the prediction that this site is chymase-susceptible by showing that chymase hydrolyzes albumin uniquely at the predicted location, with the resulting fragments remaining disulfide-linked.	Disulfides	183-192	chymase 1	Homo sapiens	45-52
12815038-9	2003	We validate the prediction that this site is chymase-susceptible by showing that chymase hydrolyzes albumin uniquely at the predicted location, with the resulting fragments remaining disulfide-linked.	Disulfides	183-192	chymase 1	Homo sapiens	81-88
12815038-9	2003	We validate the prediction that this site is chymase-susceptible by showing that chymase hydrolyzes albumin uniquely at the predicted location, with the resulting fragments remaining disulfide-linked.	Disulfides	183-192	albumin	Homo sapiens	100-107
14499914-0	2003	The disulfide-rich region of platelet glycoprotein (GP) IIIa contains hydrophilic peptide sequences that bind anti-GPIIIa autoantibodies from patients with immune thrombocytopenic purpura (ITP).	Disulfides	4-13	integrin subunit beta 3	Homo sapiens	115-121
14499914-4	2003	to confirm whether the disulfide rich repeat region of GPIIIa contains target epitopes for antiplatelet antibodies in patients with ITP; (2).	Disulfides	23-32	integrin subunit beta 3	Homo sapiens	55-61
12813049-8	2003	Recombinant FGFRL1 protein was produced in a baculovirus system with intact disulfide bonds.	Disulfides	76-85	fibroblast growth factor receptor like 1	Homo sapiens	12-18
12967471-5	2003	Transgenic mice expressing VEGF-E(NZ-7) showed a dramatic increase in angiogenesis with very few side effects (such as edema and hemorrhagic spots), suggesting strong angiogenic signaling and a potential clinical utility of VEGF-E. VEGF family members bear three loops produced via three intramolecular disulfide bonds, and cooperation between loop-1 and loop-3 is necessary for the specific binding and activation of VEGFR-2 for angiogenesis.	Disulfides	303-312	vascular endothelial growth factor A	Homo sapiens	224-228
12953119-7	2003	An intramolecular disulfide bridge in TGA1 precludes interaction with NPR1, and NPR1 can only stimulate the DNA binding activity of the reduced form of TGA1.	Disulfides	18-27	bZIP transcription factor family protein	Arabidopsis thaliana	38-42
14522053-4	2003	Here we applied a chemical disulfide crosslinking method to probe the damage-searching mechanism of two O(6)-alkylguanine-DNA alkyltransferases, the Escherichia coli C-Ada and the human AGT.	Disulfides	27-36	angiotensinogen	Homo sapiens	186-189
12953119-7	2003	An intramolecular disulfide bridge in TGA1 precludes interaction with NPR1, and NPR1 can only stimulate the DNA binding activity of the reduced form of TGA1.	Disulfides	18-27	bZIP transcription factor family protein	Arabidopsis thaliana	152-156
12816954-3	2003	Thioredoxin reductase has an N-terminal redox-active disulfide (Cys57-Cys62) adjacent to the flavin and a redox-active C-terminal cysteine pair (Cys489"-Cys490" in the other subunit) that transfer electrons from Cys57-Cys62 to the substrate thioredoxin.	Disulfides	53-62	Thioredoxin reductase-1	Drosophila melanogaster	0-21
12904077-3	2003	Our peptide library consists of a novel series of cyclic alpha-MSH analogues that have disulfide bridges between Cys or Cys-like residues at positions 4 and 10, giving rise to 23-membered rings fused at the C-terminal end with the C-terminal fragment of beta-MSH (Pro-Pro-Lys-Asp).	Disulfides	87-96	proopiomelanocortin	Homo sapiens	57-66
13678524-2	2003	The oxidoreductase ERp57 is involved in the assembly of MHC class I molecules and is a component of the peptide loading complex, where it is found disulfide-bonded to tapasin.	Disulfides	147-156	protein disulfide isomerase family A member 3	Homo sapiens	19-24
13678524-2	2003	The oxidoreductase ERp57 is involved in the assembly of MHC class I molecules and is a component of the peptide loading complex, where it is found disulfide-bonded to tapasin.	Disulfides	147-156	TAP binding protein	Homo sapiens	167-174
12846565-5	2003	Sequence alignments show that it is very similar to other CP12s, with four conserved cysteine residues forming two disulfide bridges in the oxidized CP12.	Disulfides	115-124	uncharacterized protein	Chlamydomonas reinhardtii	58-62
12859988-4	2003	This conclusion is also supported by the following biochemical properties: (1) R(myt1) was proved to have interchain disulfide bonds stabilizing its dimeric structure; (2) it failed to be phosphorylated by the catalytic (C) subunit purified from mussel; (3) it has a higher pI value than that of the R(myt2) isoform; and (4) it showed cross-reactivity with mammalian anti-RIbeta antibody.	Disulfides	117-126	myelin transcription factor 1	Homo sapiens	79-85
12878230-4	2003	The comparison of conserved cysteine residues between TAM and human and Limulus alpha(2)Ms made it possible to predict the pattern of disulfide bridges and explain the atypical molecular arrangement of TAM.	Disulfides	134-143	Myeloproliferative syndrome, transient (transient abnormal myelopoiesis)	Homo sapiens	54-57
14567441-0	2003	An inter-subunit disulfide bond affects affinity of human lung extracellular superoxide dismutase to heparin.	Disulfides	17-26	superoxide dismutase 3	Homo sapiens	63-97
14567441-4	2003	Western blot analysis of the heparin affinity chromatography product indicated that the presence of the inter-subunit disulfide bond affects the affinity of EC-SOD for heparin.	Disulfides	118-127	superoxide dismutase 3	Homo sapiens	157-163
14567441-6	2003	The present study suggests that, not only the processing of the C-terminal region but inter-subunit disulfide bonds also play a role in determining the tissue distribution of EC-SOD.	Disulfides	100-109	superoxide dismutase 3	Homo sapiens	175-181
12761212-9	2003	A putative physiological role for Erp18 in native disulfide bond formation is discussed.	Disulfides	50-59	thioredoxin domain containing 12	Homo sapiens	34-39
12909348-1	2003	We have recently described a novel gene on human chromosome 20q 12-13.2 called Eppin (Epididymal protease inhibitor) that expresses three mRNAs encoding two isoforms of a cysteine-rich protein containing both Kunitz-type and WAP-type (four disulfide core) consensus sequences (Richardson et al., 2001).	Disulfides	240-249	epididymal peptidase inhibitor	Homo sapiens	79-84
12909348-1	2003	We have recently described a novel gene on human chromosome 20q 12-13.2 called Eppin (Epididymal protease inhibitor) that expresses three mRNAs encoding two isoforms of a cysteine-rich protein containing both Kunitz-type and WAP-type (four disulfide core) consensus sequences (Richardson et al., 2001).	Disulfides	240-249	epididymal peptidase inhibitor	Homo sapiens	86-115
12846574-5	2003	TFF1 and TFF3 form intermolecular disulfide bonds via an extra-trefoil domain cysteine residue and are present in vivo as monomers and homodimers and as complexes with other proteins.	Disulfides	34-43	trefoil factor 1	Homo sapiens	0-4
12846574-5	2003	TFF1 and TFF3 form intermolecular disulfide bonds via an extra-trefoil domain cysteine residue and are present in vivo as monomers and homodimers and as complexes with other proteins.	Disulfides	34-43	trefoil factor 3	Homo sapiens	9-13
12600986-0	2003	Pulmonary surfactant protein-A (SP-A) restores the surface properties of surfactant after oxidation by a mechanism that requires the Cys6 interchain disulfide bond and the phospholipid binding domain.	Disulfides	149-158	surfactant protein A1	Rattus norvegicus	32-36
12837250-3	2003	We found that in an uninduced state, NPR1 is present as an oligomer formed through intermolecular disulfide bonds.	Disulfides	98-107	natriuretic peptide receptor 1	Homo sapiens	37-41
12730244-7	2003	When Grx5 was incubated with glutathione disulfide, a transient mixed disulfide was formed between glutathione and the cystein 60 of the protein because of its low pKa.	Disulfides	41-50	monothiol glutaredoxin GRX5	Saccharomyces cerevisiae S288C	5-9
12730244-8	2003	Binding of glutathione to Cys-60 promoted a decrease in the Cys-117 pKa value that triggered the formation of a disulfide bond between both cysteine residues of the protein, indicating that Cys-117 plays an essential role in the catalytic mechanism of Grx5.	Disulfides	112-121	monothiol glutaredoxin GRX5	Saccharomyces cerevisiae S288C	252-256
12730244-9	2003	The disulfide bond in Grx5 could be reduced by GSH but at a rate at least 20 times slower than that observed for the reduction of glutaredoxin 1 from E. coli, a dithiolic glutaredoxin.	Disulfides	4-13	monothiol glutaredoxin GRX5	Saccharomyces cerevisiae S288C	22-26
12600986-8	2003	We conclude that SP-A can reverse the detrimental effects of surfactant oxidation on the biophysical properties of surfactant, by a mechanism that is dependent on interchain disulfide bond formation and the C-terminal domains of the protein.	Disulfides	174-183	surfactant protein A1	Rattus norvegicus	17-21
12769559-1	2003	A system of RhH(PPh3)4, trifluoromethanesulfonic acid, and (p-tol)3P catalyzes the disulfide exchange reaction.	Disulfides	83-92	caveolin 1	Homo sapiens	16-20
12774022-9	2003	In conclusion, these findings suggest that extramitochondrial glutathione depletion alters the thiol-disulfide redox state, leading to inhibition of NF-kappaB transactivation of survival genes and to sustained activation of JNK, both of which contribute to the sensitization to TNF-induced apoptosis.	Disulfides	101-110	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	149-158
12774022-9	2003	In conclusion, these findings suggest that extramitochondrial glutathione depletion alters the thiol-disulfide redox state, leading to inhibition of NF-kappaB transactivation of survival genes and to sustained activation of JNK, both of which contribute to the sensitization to TNF-induced apoptosis.	Disulfides	101-110	tumor necrosis factor	Mus musculus	278-281
12781465-1	2003	Mass spectrometry, proteomics, and protein chemistry methods are used to characterize the cleavage products of 79 kDa transferrin proteins induced by iron-catalyzed oxidation, including a novel C-terminal polypeptide released upon disulfide reduction.	Disulfides	231-240	transferrin	Homo sapiens	118-129
12781465-3	2003	Incubation of transferrin with reductants, such as dithiothreitol (DTT) or tris(2-carboxyethyl)-phosphine (TCEP), yields an increase in multiple charging observed by ESI-MS and an increase in molecular weight consistent with disulfide reduction.	Disulfides	225-234	transferrin	Homo sapiens	14-25
12781462-5	2003	The distinction and complementarity of the two fragmentation techniques were particularly remarkable in their effects on ANP, a disulfide bond-containing peptide.	Disulfides	128-137	natriuretic peptide A	Homo sapiens	121-124
12781462-6	2003	While the predominant fragmentation pathway in CID of ANP was the loss of CH(3)SOH (64 Da) from the molecular ion, ECD of ANP resulted in many sequence-informative products, including those from cleavages within the disulfide-bonded cyclic structure, to allow for the direct localization of Met(O) without the typical procedures for disulfide bond reduction followed by [bond]SH alkylation.	Disulfides	333-342	natriuretic peptide A	Homo sapiens	122-125
12781465-5	2003	Protein acetylation and MS/MS sequencing demonstrate that the fragment originates from the C-terminus of the protein, and that it is a separate polypeptide linked via three disulfide bonds to the main transferrin chain.	Disulfides	173-182	transferrin	Homo sapiens	201-212
12551920-4	2003	We found that BACE undergoes cleavage on a surface-exposed alpha-helix between amino acid residues Leu-228 and Ala-229, generating stable N- and C-terminal fragments that remain covalently associated via a disulfide bond.	Disulfides	206-215	beta-secretase 1	Homo sapiens	14-18
12784209-0	2003	Ultraviolet illumination-induced reduction of alpha-lactalbumin disulfide bridges.	Disulfides	64-73	lactalbumin alpha	Homo sapiens	46-63
12721369-6	2003	The ability to export proteins with disulfide bonds and the folding proofing feature of the Tat pathway are of interest for biotechnology applications.	Disulfides	36-45	twin-arginine translocation (TAT) pathway signal sequence domain protein	Escherichia coli	92-95
12784209-6	2003	Mass spectrometry data obtained for trypsin-fragmented UV-illuminated alpha-lactalbumin with acrylodan-modified free thiol groups reveal the reduction of the 61-77 and 73-91 disulfide bridges.	Disulfides	174-183	lactalbumin alpha	Homo sapiens	70-87
12791260-5	2003	NKp44 Ig domain disulfide bridge topology defines a new Ig structural subfamily.	Disulfides	16-25	natural cytotoxicity triggering receptor 2	Homo sapiens	0-5
12624089-3	2003	We have investigated the disulfide-forming pathway of a single-chain porcine insulin precursor (PIP).	Disulfides	25-34	insulin	Homo sapiens	77-84
12624089-3	2003	We have investigated the disulfide-forming pathway of a single-chain porcine insulin precursor (PIP).	Disulfides	25-34	prolactin induced protein	Homo sapiens	96-99
12695123-0	2003	Rat J chain is disulfide-linked to alpha-chains in rat polymeric (pIgA) and secretory IgA (SIgA).	Disulfides	15-24	joining chain of multimeric IgA and IgM	Rattus norvegicus	4-11
12727972-2	2003	We have synthesized the human N-terminal POMC fragment 1-28-POMC with the disulfide bridges in the correct position between cysteine residues 2-24 and 8-20 and studied the activity of these peptides in adrenocortical tumor cells in vitro.	Disulfides	74-83	proopiomelanocortin	Homo sapiens	41-45
12727972-2	2003	We have synthesized the human N-terminal POMC fragment 1-28-POMC with the disulfide bridges in the correct position between cysteine residues 2-24 and 8-20 and studied the activity of these peptides in adrenocortical tumor cells in vitro.	Disulfides	74-83	proopiomelanocortin	Homo sapiens	60-64
12614883-0	2003	A frame shifted disulfide bridged analogue of angiotensin II.	Disulfides	16-25	angiotensinogen	Homo sapiens	46-60
12682008-6	2003	Elimination of this disulfide bond causes A-beta-sheet closure and abrogates the polymerization.	Disulfides	20-29	amyloid beta precursor protein	Homo sapiens	42-48
12831531-4	2003	Molecular modeling and ligand docking simulations suggested that scFv41.4 could function as a disulfide-deficient single domain scFv.	Disulfides	94-103	immunglobulin heavy chain variable region	Homo sapiens	65-69
12590147-8	2003	Such a maneuver allows analysis of more seriously misfolded mutants with further foreshortening of the linker sequence or loss (by mutation) of the insulin interchain disulfide bonds.	Disulfides	167-176	insulin	Homo sapiens	148-155
12582175-0	2003	Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge.	Disulfides	120-129	phosphatidylinositol glycan anchor biosynthesis class T	Sus scrofa	68-73
12582175-4	2003	Here we report that two subunits of mammalian GPI transamidase, GPI8 and PIG-T, form a functionally important disulfide bond between conserved cysteine residues.	Disulfides	110-119	phosphatidylinositol glycan anchor biosynthesis class T	Sus scrofa	73-78
12582175-8	2003	Antibodies against GPI8 and PIG-T revealed that endogenous as well as exogenous proteins formed a disulfide bond.	Disulfides	98-107	phosphatidylinositol glycan anchor biosynthesis class T	Sus scrofa	28-33
12582175-9	2003	Furthermore trypanosome GPI8 forms a similar intermolecular disulfide bond via its conserved cysteine residue, suggesting that the trypanosome GPI transamidase is also a multimeric complex likely containing the orthologue of PIG-T.	Disulfides	60-69	phosphatidylinositol glycan anchor biosynthesis class T	Sus scrofa	225-230
12547834-9	2003	Permanent disulfide opening by reduction with dithiothreitol and alkylation with N-ethylmaleimide rescued ANP binding to NPRA(W74C).	Disulfides	10-19	natriuretic peptide receptor 1	Homo sapiens	121-125
12659192-11	2003	Thus, disulfide-intact gaseous lysozyme ions generated from the denatured state in water/methanol (2/8) refold into compact structures in the gas phase on a time scale of milliseconds or less.	Disulfides	6-15	lysozyme	Homo sapiens	31-39
12509414-5	2003	Cysteine 3635, within the 3614-3643 sequence of RYR1, can form a disulfide bond with a cysteine on an adjacent subunit within the RYR1 tetramer.	Disulfides	65-74	ryanodine receptor 1	Homo sapiens	48-52
12509414-5	2003	Cysteine 3635, within the 3614-3643 sequence of RYR1, can form a disulfide bond with a cysteine on an adjacent subunit within the RYR1 tetramer.	Disulfides	65-74	ryanodine receptor 1	Homo sapiens	130-134
12509414-7	2003	The close proximity of the cysteines forming the intersubunit disulfide to the two sites that bind calmodulin suggests that calmodulin is binding at a site of intersubunit contact, perhaps with one lobe bound between amino acids 3614 and 3643 on one subunit and the second lobe bound between amino acids 1975 and 1999 on an adjacent subunit.	Disulfides	62-71	calmodulin 1	Homo sapiens	99-109
12595265-7	2003	The helix alpha3 is shortened by more than two turns when compared with alpha3 of hPrP, which is enforced by the positioning of the second disulfide bond in hDpl.	Disulfides	139-148	prion protein	Homo sapiens	82-86
12509414-7	2003	The close proximity of the cysteines forming the intersubunit disulfide to the two sites that bind calmodulin suggests that calmodulin is binding at a site of intersubunit contact, perhaps with one lobe bound between amino acids 3614 and 3643 on one subunit and the second lobe bound between amino acids 1975 and 1999 on an adjacent subunit.	Disulfides	62-71	calmodulin 1	Homo sapiens	124-134
12603172-5	2003	High charge states of both cytochrome c and disulfide-reduced alpha-lactalbumin homodimers dissociate by a symmetrical charge partitioning process in which both fragment monomers carry away roughly an equal number of charges.	Disulfides	44-53	lactalbumin alpha	Homo sapiens	62-79
12612135-3	2003	Here, human lymphoid cells (Jurkat cells) were used to model effects of cellular flavin supply on secretion of IL-2 (containing one disulfide bond) and cellular stress response.	Disulfides	132-141	interleukin 2	Homo sapiens	111-115
12789612-1	2003	Endothelins (ET-1, 2 and 3) are 21-residue peptides with two disulfide bridges and a highly conserved carboxy terminal.	Disulfides	61-70	endothelin 1	Homo sapiens	0-11
12789612-1	2003	Endothelins (ET-1, 2 and 3) are 21-residue peptides with two disulfide bridges and a highly conserved carboxy terminal.	Disulfides	61-70	endothelin 1	Homo sapiens	13-26
12446709-5	2003	After dithiothreitol treatment, a portion of the molecules can reoxidize to a form more compact than the original single-chain insulin mutants formed in vivo (indicating initial disulfide mispairing).	Disulfides	178-187	insulin	Homo sapiens	127-134
12651115-2	2003	Obtaining the C-terminal lobe of human transferrin in verified native conformation has been problematic, possibly because its 11 disulfide bonds lead to misfolding when the lobe is expressed without its accompanying N-lobe.	Disulfides	129-138	transferrin	Homo sapiens	39-50
12590586-1	2003	This report describes the biochemical characterization of a double mutant of rhodopsin (N2C,D282C) in which Cys residues engineered into the protein at positions 2 (in the amino-terminal extracellular domain) and 282 (in the extracellular loop between transmembrane helices 6 and 7) are shown to form a disulfide bond and increase the thermal stability of the unliganded or opsin form of the protein.	Disulfides	303-312	rhodopsin	Homo sapiens	77-86
12592021-5	2003	Further, significant exchange contributions are observed for residues of the canonical binding site of SH3 domains including the RT-loop, the n-Src loop, for the loop comprising residues 13 to 19, which we refer to as the"disulfide loop", in part for the distal loop, and the carboxyl terminus of human MIA.	Disulfides	222-231	MIA SH3 domain containing	Homo sapiens	303-306
12458194-2	2003	Decreased metal binding site occupancy and exposure to the disulfide-reducing agents dithiothreitol, Tris(2-carboxyethyl)phosphine (TCEP), or reduced glutathione increased the fraction of anomalously migrating mutant SOD1 proteins.	Disulfides	59-68	superoxide dismutase 1, soluble	Mus musculus	217-221
12458194-5	2003	These results implicate SOD1 destabilization under cellular disulfide-reducing conditions at physiological pH and temperature as a shared property that may be relevant to amyotrophic lateral sclerosis mutant neurotoxicity.	Disulfides	60-69	superoxide dismutase 1, soluble	Mus musculus	24-28
12538769-9	2003	We conclude that c.460+1A&gt;G mutation of human SP-C results in disruption of disulfide-mediated folding encoded by Exon 4 leading to diversion of unprocessed proSP-C to aggresomes.	Disulfides	79-88	surfactant protein C	Homo sapiens	49-53
12547204-1	2003	The nuclear magnetic resonance structure of the globular domain with residues 121-230 of a variant human prion protein with two disulfide bonds, hPrP(M166C/E221C), shows the same global fold as wild-type hPrP(121-230).	Disulfides	128-137	prion protein	Homo sapiens	145-149
12547204-4	2003	High compatibility of hPrP with insertion of a second disulfide bridge in the protein X epitope was further substantiated by model calculations with additional variant structures.	Disulfides	54-63	prion protein	Homo sapiens	22-26
12547204-5	2003	The ease with which the hPrP structure can accommodate a variety of locations for a second disulfide bond within the presumed protein X-binding epitope suggests a functional role for the extensive perturbation by a natural second disulfide bond of the corresponding region in the human doppel protein.	Disulfides	91-100	prion protein	Homo sapiens	24-28
12547204-5	2003	The ease with which the hPrP structure can accommodate a variety of locations for a second disulfide bond within the presumed protein X-binding epitope suggests a functional role for the extensive perturbation by a natural second disulfide bond of the corresponding region in the human doppel protein.	Disulfides	230-239	prion protein	Homo sapiens	24-28
12446709-6	2003	Disulfide mispairing of a fraction of B9D, B10D, and B12E mutants also occurs in the context of single-chain insulin and even in authentic proinsulin expressed within the secretory pathway of mammalian cells.	Disulfides	0-9	insulin	Homo sapiens	109-116
12446709-7	2003	We conclude that analyses of the intracellular trafficking of certain oligomerization-defective insulin mutants is complicated by the formation of disulfide isomers in the secretory pathway.	Disulfides	147-156	insulin	Homo sapiens	96-103
12710518-6	2003	Cleavage of the external disulfide bond with dithiothreitol caused an inactivation of the receptor when stimulated either with Ang II or the autoantibodies in a system of cultured neonatal rat cardiomyocytes.	Disulfides	25-34	angiotensinogen	Rattus norvegicus	127-133
12545217-0	2003	Influence of A7-B7 disulfide bond deletion on the refolding and structure of proinsulin.	Disulfides	19-28	insulin	Homo sapiens	77-87
12545217-3	2003	The deletion of [ A7-B7] disulfide bond in proinsulin resulted in a significant decrease of alpha- helix content of the molecule and a great increase in sensitivity to tryptic digestion.	Disulfides	25-34	insulin	Homo sapiens	43-53
12545217-4	2003	The [A7-B7] disulfide bond deleted proinsulin showed a great loss of its receptor binding activity.	Disulfides	12-21	insulin	Homo sapiens	35-45
12629973-0	2003	Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking.	Disulfides	139-148	rhodopsin	Homo sapiens	0-9
12218052-1	2003	The human immunodeficiency virus (HIV) envelope (Env) glycoprotein (gp) 120 is a highly disulfide-bonded molecule that attaches HIV to the lymphocyte surface receptors CD4 and CXCR4.	Disulfides	88-97	CD4 molecule	Homo sapiens	168-171
12534273-2	2003	We determined the NMR solution structure and backbone (15)N relaxation rates of a disulfide cross-linked, two-chain, 37-residue polypeptide containing the 34 C-terminal residues of striated muscle alpha-tropomyosin, TM9a(251-284).	Disulfides	82-91	tropomyosin 1	Homo sapiens	197-214
12525154-7	2003	The photolabeling of these amino acids suggests that when the antagonist TDBzcholine occupies the agonist binding sites, the Cys-192-193 disulfide and Pro-194 from the alpha subunit Segment C are oriented toward the agonist site and are in proximity to gammaLeu-109/deltaLeu-111 in Segment E, a conclusion consistent with the structure of the binding site in the molluscan acetylcholine binding protein, a soluble protein that is homologous to the nAChR extracellular domain.	Disulfides	137-146	cholinergic receptor nicotinic alpha 4 subunit	Homo sapiens	448-453
16233527-1	2003	A porous wool keratin sponge was used for immobilization of lysozyme, a model bioactive substance and was demonstrated to be a unique biomaterial in terms that the activity of lysozyme linked to the sponge through disulfide bond was gradually released, while lysozyme through thioether bond was stably maintained.	Disulfides	214-223	lysozyme	Homo sapiens	60-68
15142434-3	2003	Moreover, serum thiols also reflect DNA repair capacity and the possible eventual accumulation of genetic damage, since a key DNA repair enzyme, poly ADP-ribose polymerase (PARP), is thiol/disulfide redox regulated.	Disulfides	189-198	poly(ADP-ribose) polymerase 1	Homo sapiens	145-171
15142434-3	2003	Moreover, serum thiols also reflect DNA repair capacity and the possible eventual accumulation of genetic damage, since a key DNA repair enzyme, poly ADP-ribose polymerase (PARP), is thiol/disulfide redox regulated.	Disulfides	189-198	poly(ADP-ribose) polymerase 1	Homo sapiens	173-177
12897445-0	2003	Disulfide exchange in CD4.	Disulfides	0-9	CD4 molecule	Homo sapiens	22-25
16233527-1	2003	A porous wool keratin sponge was used for immobilization of lysozyme, a model bioactive substance and was demonstrated to be a unique biomaterial in terms that the activity of lysozyme linked to the sponge through disulfide bond was gradually released, while lysozyme through thioether bond was stably maintained.	Disulfides	214-223	lysozyme	Homo sapiens	176-184
16233527-1	2003	A porous wool keratin sponge was used for immobilization of lysozyme, a model bioactive substance and was demonstrated to be a unique biomaterial in terms that the activity of lysozyme linked to the sponge through disulfide bond was gradually released, while lysozyme through thioether bond was stably maintained.	Disulfides	214-223	lysozyme	Homo sapiens	176-184
12477814-1	2003	The two major envelope proteins of arteriviruses, the membrane protein (M) and the major glycoprotein (GP(5)), associate into a disulfide-linked heterodimer that is incorporated into the virion and has been assumed to be a prerequisite for virus assembly.	Disulfides	128-137	glycoprotein V platelet	Homo sapiens	83-108
12393867-0	2002	Screening for stable mutants with amino acid pairs substituted for the disulfide bond between residues 14 and 38 of bovine pancreatic trypsin inhibitor (BPTI).	Disulfides	71-80	trophoblast Kunitz domain protein 1	Bos taurus	134-151
12218051-2	2002	PDI is present at the surface of HIV-1 target cells and reduces disulfide bonds in a model peptide attached to the cell membrane.	Disulfides	64-73	protein disulfide isomerase family A member 2	Homo sapiens	0-3
12218051-3	2002	Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors.	Disulfides	38-47	protein disulfide isomerase family A member 2	Homo sapiens	26-29
12393867-2	2002	This method was used to screen amino acid pairs substituted for the disulfide (S-S) bond between residues 14 and 38 of bovine pancreatic trypsin inhibitor.	Disulfides	68-77	trophoblast Kunitz domain protein 1	Bos taurus	137-154
12218051-3	2002	Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors.	Disulfides	158-167	protein disulfide isomerase family A member 2	Homo sapiens	26-29
12475229-0	2002	Interactions that favor the native over the non-native disulfide bond among residues 58-72 in the oxidative folding of bovine pancreatic ribonuclease A.	Disulfides	55-64	ribonuclease pancreatic	Bos taurus	137-151
12218051-3	2002	Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors.	Disulfides	158-167	CD4 molecule	Homo sapiens	142-145
12218051-3	2002	Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors.	Disulfides	158-167	protein disulfide isomerase family A member 2	Homo sapiens	199-202
12218051-8	2002	We propose that a PDI.CD4 association at the cell surface enables PDI to reach CD4-bound virus and to reduce disulfide bonds present in the domain of gp120 that binds to CD4.	Disulfides	109-118	protein disulfide isomerase family A member 2	Homo sapiens	18-21
12218051-8	2002	We propose that a PDI.CD4 association at the cell surface enables PDI to reach CD4-bound virus and to reduce disulfide bonds present in the domain of gp120 that binds to CD4.	Disulfides	109-118	CD4 molecule	Homo sapiens	22-25
12218051-8	2002	We propose that a PDI.CD4 association at the cell surface enables PDI to reach CD4-bound virus and to reduce disulfide bonds present in the domain of gp120 that binds to CD4.	Disulfides	109-118	protein disulfide isomerase family A member 2	Homo sapiens	66-69
12218051-8	2002	We propose that a PDI.CD4 association at the cell surface enables PDI to reach CD4-bound virus and to reduce disulfide bonds present in the domain of gp120 that binds to CD4.	Disulfides	109-118	CD4 molecule	Homo sapiens	79-82
12218051-8	2002	We propose that a PDI.CD4 association at the cell surface enables PDI to reach CD4-bound virus and to reduce disulfide bonds present in the domain of gp120 that binds to CD4.	Disulfides	109-118	CD4 molecule	Homo sapiens	79-82
12475219-0	2002	A protein caught in a kinetic trap: structures and stabilities of insulin disulfide isomers.	Disulfides	74-83	insulin	Homo sapiens	66-73
12475219-4	2002	Remarkably, the same two isomers are preferentially formed from native insulin or proinsulin following disulfide reassortment in guanidine hydrochloride.	Disulfides	103-112	insulin	Homo sapiens	71-78
12475219-4	2002	Remarkably, the same two isomers are preferentially formed from native insulin or proinsulin following disulfide reassortment in guanidine hydrochloride.	Disulfides	103-112	insulin	Homo sapiens	82-92
12475219-16	2002	The insulin isomers are similar in structure and stability to two-disulfide analogues whose partial folds provide models of oxidative folding intermediates.	Disulfides	66-75	insulin	Homo sapiens	4-11
12475229-1	2002	In the initial stages of the oxidative folding of both bovine pancreatic ribonuclease A (RNase A) and a 58-72 fragment thereof from the fully reduced, denatured state, the 65-72 correctly paired disulfide bond forms in preponderance over the incorrectly paired 58-65 disulfide bond.	Disulfides	195-204	ribonuclease pancreatic	Bos taurus	73-87
12434426-2	2002	The hTM409-426 peptide has a sequence of C(409)PEGYILDDGFIC(421)TDIDE (with a disulfide bond between Cys409 and Cys421) and is a selective inhibitor of thrombin.	Disulfides	78-87	coagulation factor II, thrombin	Homo sapiens	152-160
12434426-9	2002	These results indicate that the overall topology of the thrombin-bound conformation of the hTM409-426 peptide is prefolded in the free state and the primary sequence (including the disulfide bond) may be selective for an ensemble of conformations similar to that recognized by thrombin.	Disulfides	181-190	coagulation factor II, thrombin	Homo sapiens	56-64
12475229-1	2002	In the initial stages of the oxidative folding of both bovine pancreatic ribonuclease A (RNase A) and a 58-72 fragment thereof from the fully reduced, denatured state, the 65-72 correctly paired disulfide bond forms in preponderance over the incorrectly paired 58-65 disulfide bond.	Disulfides	195-204	ribonuclease pancreatic	Bos taurus	89-96
12475229-1	2002	In the initial stages of the oxidative folding of both bovine pancreatic ribonuclease A (RNase A) and a 58-72 fragment thereof from the fully reduced, denatured state, the 65-72 correctly paired disulfide bond forms in preponderance over the incorrectly paired 58-65 disulfide bond.	Disulfides	267-276	ribonuclease pancreatic	Bos taurus	73-87
12475229-1	2002	In the initial stages of the oxidative folding of both bovine pancreatic ribonuclease A (RNase A) and a 58-72 fragment thereof from the fully reduced, denatured state, the 65-72 correctly paired disulfide bond forms in preponderance over the incorrectly paired 58-65 disulfide bond.	Disulfides	267-276	ribonuclease pancreatic	Bos taurus	89-96
12239218-0	2002	Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain.	Disulfides	47-56	calreticulin	Homo sapiens	10-22
12450399-0	2002	Biophysical characterization, including disulfide bond assignments, of the anti-angiogenic type 1 domains of human thrombospondin-1.	Disulfides	40-49	thrombospondin 1	Homo sapiens	115-131
12239218-8	2002	The formation of at least one of the disulfide bonds in the CD1d heavy chain is coupled to its glucose trimming-dependent association with ERp57, calnexin, and calreticulin.	Disulfides	37-46	protein disulfide isomerase family A member 3	Homo sapiens	139-144
12372819-10	2002	This may be explained by the disulfide bond network in K4, which holds the cleaved alpha-chain together.	Disulfides	29-38	Fc gamma receptor and transporter	Homo sapiens	83-94
12239218-0	2002	Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain.	Disulfides	47-56	protein disulfide isomerase family A member 3	Homo sapiens	28-33
12239218-8	2002	The formation of at least one of the disulfide bonds in the CD1d heavy chain is coupled to its glucose trimming-dependent association with ERp57, calnexin, and calreticulin.	Disulfides	37-46	calreticulin	Homo sapiens	160-172
12437921-5	2002	When oxidized by H2O2, Gpx3 Cys36 bridges Yap1 Cys598 by a disulfide bond.	Disulfides	59-68	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	42-46
12423632-8	2002	The refolded proinsulin was correctly disulfide-bonded and native and monomeric as shown by RP-HPLC, ELISA, circular dichroism, and analytical gel filtration.	Disulfides	38-47	insulin	Homo sapiens	13-23
12437921-6	2002	This intermolecular disulfide bond is then resolved into a Yap1 intramolecular disulfide bond, the activated form of the regulator.	Disulfides	20-29	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	59-63
12437921-6	2002	This intermolecular disulfide bond is then resolved into a Yap1 intramolecular disulfide bond, the activated form of the regulator.	Disulfides	79-88	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	59-63
12207021-5	2002	When assuming that the sequential order of the disulfide bridge formation is conserved between VEGF and glycoprotein alpha-subunit, the crystal structure of the mutant C61A-C104A, which deviates by a root mean square deviation of more than 2.2 A from wild-type VEGF, identifies a true folding intermediate of VEGF.	Disulfides	47-56	vascular endothelial growth factor A	Homo sapiens	95-99
12196530-2	2002	The A and B chains of insulin combine to form native disulfide bridges without detectable isomers.	Disulfides	53-62	insulin	Homo sapiens	22-29
12408709-5	2002	First, the disulfide bridge of this lead compound was shifted and then the modified peptide was shortened from the amino and carboxy terminus to generate cyclo[21,29][Cys(21,29)]-uPA(21)(-)(30).	Disulfides	11-20	plasminogen activator, urokinase	Homo sapiens	179-182
12502529-8	2002	However, disulfide bond analysis and cysteine mutagenesis coupled with accessibility studies indicate that the structure of NCX1 diverges from a simple membrane protein consisting only of transmembrane alpha-helical segments.	Disulfides	9-18	solute carrier family 8 member A1	Homo sapiens	124-128
12183464-11	2002	Our proposal is that the generation of the Cys(298)-Cys(303) disulfide, either directly or by rearrangement of the Cys(80)-Cys(303) disulfide, may be induced by the release of the cofactor from ALR2 undergoing oxidation.	Disulfides	61-70	aldo-keto reductase family 1 member B	Homo sapiens	194-198
12220619-4	2002	Here, we demonstrate that CD157, independent of antibody crosslinking, undergoes dimerization with disulfide bond formation and localization in caveolae in CHO/CD157 and MCA/CD157 fibroblasts.	Disulfides	99-108	bone marrow stromal cell antigen 1	Homo sapiens	26-31
12220619-4	2002	Here, we demonstrate that CD157, independent of antibody crosslinking, undergoes dimerization with disulfide bond formation and localization in caveolae in CHO/CD157 and MCA/CD157 fibroblasts.	Disulfides	99-108	bone marrow stromal cell antigen 1	Homo sapiens	160-165
12220619-4	2002	Here, we demonstrate that CD157, independent of antibody crosslinking, undergoes dimerization with disulfide bond formation and localization in caveolae in CHO/CD157 and MCA/CD157 fibroblasts.	Disulfides	99-108	bone marrow stromal cell antigen 1	Homo sapiens	160-165
12183464-11	2002	Our proposal is that the generation of the Cys(298)-Cys(303) disulfide, either directly or by rearrangement of the Cys(80)-Cys(303) disulfide, may be induced by the release of the cofactor from ALR2 undergoing oxidation.	Disulfides	132-141	aldo-keto reductase family 1 member B	Homo sapiens	194-198
12403808-4	2002	We show that upon oxidation of the COOH-terminal disulfide bond in PDI by the enzyme Ero1, the A1 chain is released.	Disulfides	49-58	ER oxidoreductin	Saccharomyces cerevisiae S288C	85-89
12417021-2	2002	C4bp comprises a disulfide-linked heptamer of alpha-chains with complement (C) regulatory activity and a beta-chain.	Disulfides	17-26	complement component 4 binding protein alpha	Homo sapiens	0-4
12379854-4	2002	In contrast, mutations in WFDC1 (16q24, encoding WAP four-disulfide core domain 1) occur with low frequency in the stroma.	Disulfides	58-67	WAP four-disulfide core domain 1	Homo sapiens	26-31
12391223-3	2002	Our previous studies indicated that in IgA2 lacking Cys(133), a disulfide bond forms between the alpha-chain and the L chain when Cys(220) is followed by Arg(221), but not when Cys(220) is followed by Pro(221), suggesting that the Cys in C(H)1 might be involved in disulfide bonding to the L chain.	Disulfides	64-73	Fc gamma receptor and transporter	Homo sapiens	97-108
12391223-3	2002	Our previous studies indicated that in IgA2 lacking Cys(133), a disulfide bond forms between the alpha-chain and the L chain when Cys(220) is followed by Arg(221), but not when Cys(220) is followed by Pro(221), suggesting that the Cys in C(H)1 might be involved in disulfide bonding to the L chain.	Disulfides	265-274	Fc gamma receptor and transporter	Homo sapiens	97-108
12453408-1	2002	The endoplasmic reticulum (ER) supports disulfide formation through an essential protein relay involving Ero1p and protein disulfide isomerase (PDI).	Disulfides	40-49	ER oxidoreductin	Saccharomyces cerevisiae S288C	105-110
12453408-6	2002	Thus Ero1p directly couples disulfide formation to the consumption of molecular oxygen, but its activity is modulated by free lumenal FAD levels, potentially linking disulfide formation to a cell"s nutritional or metabolic status.	Disulfides	28-37	ER oxidoreductin	Saccharomyces cerevisiae S288C	5-10
12453408-6	2002	Thus Ero1p directly couples disulfide formation to the consumption of molecular oxygen, but its activity is modulated by free lumenal FAD levels, potentially linking disulfide formation to a cell"s nutritional or metabolic status.	Disulfides	166-175	ER oxidoreductin	Saccharomyces cerevisiae S288C	5-10
12452439-4	2002	The full-length protein and the N- and C-terminal halves of DBP remained insoluble probably because the protein did not fold to its native three-dimensional structure due to formation of accidental intra- and inter-molecular disulfide bonds during expression in bacteria or yeast.	Disulfides	225-234	D-box binding PAR bZIP transcription factor	Homo sapiens	60-63
12351392-2	2002	The multimeric size of VWF can be controlled by the glycoprotein, thrombospondin-1 (TSP-1), which facilitates reduction of the disulfide bonds that hold VWF multimers together.	Disulfides	127-136	von Willebrand factor	Homo sapiens	23-26
12351392-2	2002	The multimeric size of VWF can be controlled by the glycoprotein, thrombospondin-1 (TSP-1), which facilitates reduction of the disulfide bonds that hold VWF multimers together.	Disulfides	127-136	thrombospondin 1	Homo sapiens	66-82
12351392-2	2002	The multimeric size of VWF can be controlled by the glycoprotein, thrombospondin-1 (TSP-1), which facilitates reduction of the disulfide bonds that hold VWF multimers together.	Disulfides	127-136	thrombospondin 1	Homo sapiens	84-89
12351392-2	2002	The multimeric size of VWF can be controlled by the glycoprotein, thrombospondin-1 (TSP-1), which facilitates reduction of the disulfide bonds that hold VWF multimers together.	Disulfides	127-136	von Willebrand factor	Homo sapiens	153-156
12351392-4	2002	TSP-1 and TSP-2 are structurally similar trimeric proteins composed of disulfide-linked 150-kDa monomers.	Disulfides	71-80	thrombospondin 1	Homo sapiens	0-5
12145281-13	2002	A Drosophila MsrA gene was also cloned, and the recombinant enzyme was found to be metal-free and specific for methionine S-sulfoxide and to employ a similar sulfenic acid/disulfide mechanism.	Disulfides	172-181	Methionine sulfoxide reductase A	Drosophila melanogaster	13-17
12359323-1	2002	Apolipoprotein(a) (Apo(a)) is a glycoprotein that is linked by a disulfide bond to apolipoprotein B on low density lipoprotein particles to form lipoprotein(a) (Lp(a)).	Disulfides	65-74	apolipoprotein B	Homo sapiens	83-99
12479405-0	2002	Structural and functional properties of apolipoprotein A-I mutants containing disulfide-linked cysteines at positions 124 or 232.	Disulfides	78-87	apolipoprotein A1	Homo sapiens	40-58
12270713-4	2002	This enzyme catalyzes the formation of disulfide bonds in CNX and CRT-bound glycoprotein substrates.	Disulfides	39-48	calreticulin	Homo sapiens	66-69
12270713-9	2002	Of the 36 residues present in CRT(221-256), 32 form a well-structured core, making this fragment one of the smallest known natural sequences to form a stable non-helical fold in the absence of disulfide bonds or tightly bound metal ions.	Disulfides	193-202	calreticulin	Homo sapiens	30-33
12359097-9	2002	However, thrombin did cleave between those of prethrombin 2, but linked with disulfide bridge.	Disulfides	77-86	coagulation factor II, thrombin	Homo sapiens	9-17
12270706-10	2002	A special feature of ART2.2 is its long N-terminal extension and two disulfide bridges that are far away from the active center.	Disulfides	69-78	ADP-ribosyltransferase 2b	Rattus norvegicus	21-25
12479405-1	2002	Recombinant Cys mutants of apolipoprotein A-I (apoA-I) (A124C and A232C) have been prepared in disulfide-linked forms in order to assess the effects of unnatural covalent constraints on the folding of apoA-I in solution, its ability to bind lipids, form HDL-like particles, activate LCAT, and undergo structural adaptations to changing lipid contents.	Disulfides	95-104	apolipoprotein A1	Homo sapiens	27-45
12479405-4	2002	While the monomeric mutants produced identical rHDL to plasma apoA-I, the disulfide-linked dimers had distinct particle distributions from each other and from native apoA-I.	Disulfides	74-83	apolipoprotein A1	Homo sapiens	166-172
12479405-9	2002	From the results, it is concluded that synthetic, random disulfide-linked dimers of apoA-I have many properties analogous to those of the naturally occurring Cys mutants, apoA-I-Milano and apoA-I-Paris, which are thought to have antiatherogenic effects in vivo.	Disulfides	57-66	apolipoprotein A1	Homo sapiens	84-90
12479405-9	2002	From the results, it is concluded that synthetic, random disulfide-linked dimers of apoA-I have many properties analogous to those of the naturally occurring Cys mutants, apoA-I-Milano and apoA-I-Paris, which are thought to have antiatherogenic effects in vivo.	Disulfides	57-66	apolipoprotein A1	Homo sapiens	171-177
12479405-9	2002	From the results, it is concluded that synthetic, random disulfide-linked dimers of apoA-I have many properties analogous to those of the naturally occurring Cys mutants, apoA-I-Milano and apoA-I-Paris, which are thought to have antiatherogenic effects in vivo.	Disulfides	57-66	apolipoprotein A1	Homo sapiens	171-177
12238768-0	2002	Affinity tag for protein purification and detection based on the disulfide-linked complex of InaD and NorpA.	Disulfides	65-74	inactivation no afterpotential D	Drosophila melanogaster	93-97
12198183-2	2002	GILT facilitates unfolding of endocytosed antigens in MHC class II-containing compartments by enzymatically reducing disulfide bonds.	Disulfides	117-126	IFI30 lysosomal thiol reductase	Homo sapiens	0-4
12198183-5	2002	Both precursor and mature GILT reduce disulfide bonds with an acidic pH optimum.	Disulfides	38-47	IFI30 lysosomal thiol reductase	Homo sapiens	26-30
12198183-7	2002	Mutation of Cys-222 abolishes disulfide-linked dimerization of precursor GILT and decreases the efficiency of GILT maturation.	Disulfides	30-39	IFI30 lysosomal thiol reductase	Homo sapiens	73-77
12238768-0	2002	Affinity tag for protein purification and detection based on the disulfide-linked complex of InaD and NorpA.	Disulfides	65-74	no receptor potential A	Drosophila melanogaster	102-107
12359138-9	2002	This finding of a novel mutation substituting cysteine with phenylalanine in one AVP-NPII gene allele supports the hypothesis that inability to form normal disulfide bonds in neurophysin II leads to ADNDI.	Disulfides	156-165	arginine vasopressin	Homo sapiens	81-89
12147243-6	2002	Circular dichroism studies on the recombinant protein indicate that the disulfide-bonded TSP1-module consists primarily of distorted beta-strands.	Disulfides	72-81	thrombospondin 1	Homo sapiens	89-93
12186542-0	2002	The different energetic state of the intra A-chain/domain disulfide of insulin and insulin-like growth factor 1 is mainly controlled by their B-chain/domain.	Disulfides	58-67	insulin	Homo sapiens	71-78
12186542-0	2002	The different energetic state of the intra A-chain/domain disulfide of insulin and insulin-like growth factor 1 is mainly controlled by their B-chain/domain.	Disulfides	58-67	insulin like growth factor 1	Homo sapiens	83-111
12186542-1	2002	Insulin and insulin-like growth factor 1 (IGF-1) share homologous sequence, similar three-dimensional structure, and weakly overlapping biological activity, but different folding information is stored in their homologous sequences: the sequence of insulin encodes one unique thermodynamically stable three-dimensional structure while that of IGF-1 encodes two disulfide isomers with different three-dimensional structure but similar thermodynamic stability.	Disulfides	360-369	insulin	Homo sapiens	0-7
12186542-1	2002	Insulin and insulin-like growth factor 1 (IGF-1) share homologous sequence, similar three-dimensional structure, and weakly overlapping biological activity, but different folding information is stored in their homologous sequences: the sequence of insulin encodes one unique thermodynamically stable three-dimensional structure while that of IGF-1 encodes two disulfide isomers with different three-dimensional structure but similar thermodynamic stability.	Disulfides	360-369	insulin like growth factor 1	Homo sapiens	12-40
12186542-1	2002	Insulin and insulin-like growth factor 1 (IGF-1) share homologous sequence, similar three-dimensional structure, and weakly overlapping biological activity, but different folding information is stored in their homologous sequences: the sequence of insulin encodes one unique thermodynamically stable three-dimensional structure while that of IGF-1 encodes two disulfide isomers with different three-dimensional structure but similar thermodynamic stability.	Disulfides	360-369	insulin like growth factor 1	Homo sapiens	42-47
12186542-1	2002	Insulin and insulin-like growth factor 1 (IGF-1) share homologous sequence, similar three-dimensional structure, and weakly overlapping biological activity, but different folding information is stored in their homologous sequences: the sequence of insulin encodes one unique thermodynamically stable three-dimensional structure while that of IGF-1 encodes two disulfide isomers with different three-dimensional structure but similar thermodynamic stability.	Disulfides	360-369	insulin	Homo sapiens	12-19
12186542-2	2002	Their different folding behavior probably resulted from the different energetic state of the intra A-chain/domain disulfide: the intra A-chain disulfide of insulin is a stable bond while that of IGF-1 is a strained bond with high energy.	Disulfides	114-123	insulin	Homo sapiens	156-163
12186542-2	2002	Their different folding behavior probably resulted from the different energetic state of the intra A-chain/domain disulfide: the intra A-chain disulfide of insulin is a stable bond while that of IGF-1 is a strained bond with high energy.	Disulfides	114-123	insulin like growth factor 1	Homo sapiens	195-200
12186542-2	2002	Their different folding behavior probably resulted from the different energetic state of the intra A-chain/domain disulfide: the intra A-chain disulfide of insulin is a stable bond while that of IGF-1 is a strained bond with high energy.	Disulfides	143-152	insulin	Homo sapiens	156-163
12186542-2	2002	Their different folding behavior probably resulted from the different energetic state of the intra A-chain/domain disulfide: the intra A-chain disulfide of insulin is a stable bond while that of IGF-1 is a strained bond with high energy.	Disulfides	143-152	insulin like growth factor 1	Homo sapiens	195-200
12186542-5	2002	Second, the disulfide stability of two global hybrids of insulin and IGF-1, Ins(A)/IGF-1(B) and Ins(B)/IGF-1(A), was investigated.	Disulfides	12-21	insulin	Homo sapiens	57-64
12186542-8	2002	One major equilibrium intermediate with two disulfides of Ins(A)/IGF-1(B) was purified and characterized.	Disulfides	44-54	insulin like growth factor 1	Homo sapiens	65-70
12186542-10	2002	Our present results suggested that the energetic state of the intra A-chain/domain disulfide of insulin and IGF-1 was not controlled by the A-chain/domain sequence close to this disulfide but was mainly controlled by the sequence of the B-chain/domain.	Disulfides	83-92	insulin	Homo sapiens	96-103
12186542-10	2002	Our present results suggested that the energetic state of the intra A-chain/domain disulfide of insulin and IGF-1 was not controlled by the A-chain/domain sequence close to this disulfide but was mainly controlled by the sequence of the B-chain/domain.	Disulfides	83-92	insulin like growth factor 1	Homo sapiens	108-113
12186542-10	2002	Our present results suggested that the energetic state of the intra A-chain/domain disulfide of insulin and IGF-1 was not controlled by the A-chain/domain sequence close to this disulfide but was mainly controlled by the sequence of the B-chain/domain.	Disulfides	178-187	insulin	Homo sapiens	96-103
12186542-10	2002	Our present results suggested that the energetic state of the intra A-chain/domain disulfide of insulin and IGF-1 was not controlled by the A-chain/domain sequence close to this disulfide but was mainly controlled by the sequence of the B-chain/domain.	Disulfides	178-187	insulin like growth factor 1	Homo sapiens	108-113
12217626-1	2002	Glutaredoxin (Grx) is a specific and efficient catalyst of glutathione-dependent deglutathionylation of protein-SS-glutathione mixed disulfides.	Disulfides	133-143	glutaredoxin	Rattus norvegicus	0-12
12217626-1	2002	Glutaredoxin (Grx) is a specific and efficient catalyst of glutathione-dependent deglutathionylation of protein-SS-glutathione mixed disulfides.	Disulfides	133-143	glutaredoxin	Rattus norvegicus	14-17
12192065-0	2002	Interdomain engineered disulfide bond permitting elucidation of mechanisms of inactivation of coagulation factor Va by activated protein C. Procoagulant factor Va (FVa) is inactivated via limited proteolysis at three Arg residues in the A2 domain by the anticoagulant serine protease, activated protein C (APC).	Disulfides	23-32	coagulation factor II, thrombin	Homo sapiens	268-283
12154226-6	2002	Although Zn(2+) binding occurs only when the protein is in the reduced form, biochemical analyses show that under oxidative conditions, the GhCesA1 zinc-finger domain and also the full-length protein dimerize via intermolecular disulfide bonds, indicating CesA dimerization can be regulated by redox state.	Disulfides	228-237	cellulose synthase A catalytic subunit 8 [UDP-forming]-like	Gossypium hirsutum	140-147
12225802-0	2002	Isolation of ovocleidin-116 from chicken eggshells, correction of its amino acid sequence and identification of disulfide bonds and glycosylated Asn.	Disulfides	112-121	matrix extracellular phosphoglycoprotein	Gallus gallus	13-27
12127077-3	2002	In this study, we determined that human VEGF(121) contains a third interchain disulfide bond between Cys116 of each monomer.	Disulfides	78-87	vascular endothelial growth factor A	Homo sapiens	40-44
12127077-6	2002	In fact, selective reduction of the Cys116 interchain disulfide bond yielded an unstable VEGF(121) molecule, which reoxidized quickly.	Disulfides	54-63	vascular endothelial growth factor A	Homo sapiens	89-93
12102725-0	2002	A novel approach to the synthesis of EGF-like domains: a method for the one-pot regioselective formation of the three disulfide bonds of a human blood coagulation factor VII EGF-1 analogue.	Disulfides	118-127	coagulation factor VII	Homo sapiens	151-173
12492154-1	2002	Aggregate formation and the structure of the aggregates of disulfide-reduced proteins were investigated using alpha-lactalbumin and lysozyme as model proteins.	Disulfides	59-68	lysozyme	Homo sapiens	132-140
12089508-0	2002	Disulfide exchange in domain 2 of CD4 is required for entry of HIV-1.	Disulfides	0-9	CD4 molecule	Homo sapiens	34-37
12146942-7	2002	Co(II) bound exclusively at the alpha5 sites is capable of rapid equilibration between the alpha3N and alpha5 sites upon reduction of the mixed disulfides in S-methylated SmtB.	Disulfides	144-154	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	0-6
12430881-1	2002	Fibrinogen is a 340-kDa plasma protein that is composed of two identical molecular halves, each consisting of three non-identical subunit polypeptides designated as A alpha, B beta- and gamma-chains held together by multiple disulfide bonds.	Disulfides	225-234	fibrinogen beta chain	Homo sapiens	0-10
12119363-3	2002	Dissection of the degradation process revealed that upon release from calnexin, extensively oxidized BACE457 transiently entered in disulfide-bonded complexes associated with the lumenal chaperones BiP and protein disulfide isomerase (PDI) before unfolding and dislocation into the cytosol for degradation.	Disulfides	132-141	heat shock protein family A (Hsp70) member 5	Homo sapiens	198-201
12182824-6	2002	To confirm the disulfide bond formation, hIL-6-HlyA(s) was purified by a single-step immunoaffinity chromatography from culture supernatant in yields of 18 microg/L culture supernatant with purity in the range of 60%.	Disulfides	15-24	interleukin 6	Homo sapiens	41-46
12182824-7	2002	These results demonstrate that codon usage has an impact on the hemolysin-mediated secretion of hIL-6 and, furthermore, provide evidence that the hemolysin system enables secretory delivery of disulfide-bridged proteins.	Disulfides	193-202	interleukin 6	Homo sapiens	96-101
12119021-10	2002	Furthermore, it was established that reaction of hBCATm with H2O2 abolished its activity and resulted in the formation of an intrasubunit disulfide bond between Cys315 and Cys318.	Disulfides	138-147	branched chain amino acid transaminase 2	Homo sapiens	49-55
12089508-5	2002	The redox state of the thiols (disulfide versus dithiol) appeared to be regulated by thioredoxin, which is secreted by CD4(+) T cells.	Disulfides	31-40	CD4 molecule	Homo sapiens	119-122
12135356-4	2002	The expressed C4BP was found to contain six disulfide-linked alpha-chains.	Disulfides	44-53	complement component 4 binding protein alpha	Homo sapiens	14-18
12135356-10	2002	Gel filtration analysis of these variants demonstrated the whole alpha-helix region to be required for the formation of stable polymers of C4BP, which were further stabilized by the formation of disulfide bonds.	Disulfides	195-204	complement component 4 binding protein alpha	Homo sapiens	139-143
12119021-9	2002	Electrospray ionization mass spectrometry analysis and UV-Vis spectroscopic studies of 5,5"-dithiobis(2-nitrobenzoic acid) labeled hBCATm showed that during labeling, an intrasubunit disulfide bond was formed in a significant portion of the protein.	Disulfides	183-192	branched chain amino acid transaminase 2	Homo sapiens	131-137
11943773-3	2002	GPIb binding sites have been assigned in the VWF A1 domain, which consists of a disulfide loop Cys1272(509)-Cys1458(695) where amino acid residues are numbered from the starting methionine as +1.	Disulfides	80-89	von Willebrand factor	Homo sapiens	45-48
11983507-2	2002	In this compound, the cysteines implied in the two insulin inter-chain disulfide bridges are replaced by two serines (residues Ser(A7) and Ser(A20)) and the intra-A-chain disulfide bridge (residues Cys(A6) and Cys(A11)) is conserved.	Disulfides	71-80	insulin	Homo sapiens	51-58
12065480-4	2002	Matrix-assisted laser desorption ionization mass-spectrometry sequence analysis revealed the 55-kDa protein to be protein disulfide isomerase (PDI), a member of the estrogen receptor complex which carries out thiol-disulfide exchange reactions at infected host cell surfaces.	Disulfides	122-131	protein disulfide isomerase family A member 2	Homo sapiens	143-146
12074582-4	2002	The overall structure of BTCe was stabilized by three disulfide bonds, a hydrophobic core, and 23 hydrogen bonds.	Disulfides	54-63	betacellulin	Homo sapiens	25-29
12089063-2	2002	Apoptotic stimuli such as tumor necrosis factor (TNF) and reactive oxygen species (ROS) activate ASK1 in part by oxidizing Trx (forming intramolecular disulfide between C32 and C35) to release Trx from ASK1.	Disulfides	151-160	tumor necrosis factor	Homo sapiens	26-47
12089063-2	2002	Apoptotic stimuli such as tumor necrosis factor (TNF) and reactive oxygen species (ROS) activate ASK1 in part by oxidizing Trx (forming intramolecular disulfide between C32 and C35) to release Trx from ASK1.	Disulfides	151-160	tumor necrosis factor	Homo sapiens	49-52
12070343-5	2002	This rate is orders of magnitude faster than the reaction of dithiol Trx with insulin disulfides.	Disulfides	86-96	insulin	Homo sapiens	78-85
12068291-3	2002	They display a distinctive, disulfide-linked Ig domain interface and are folded back asymmetrically onto the C epsilon 3 and C epsilon 4 domains, which causes an acute bend in the IgE molecule.	Disulfides	28-37	immunoglobulin heavy constant epsilon	Homo sapiens	180-183
11978783-3	2002	We report here that HLA-B27 HC also forms two types of aberrant disulfide-linked complexes (dimers) during the folding and assembly process that can be distinguished by conformation-sensitive antibodies W6/32 and HC10.	Disulfides	64-73	CYCS pseudogene 25	Homo sapiens	213-217
11937510-7	2002	By substituting each PLAP Cys by Ser, we found that disrupting the disulfide bond between Cys-121 and Cys-183 completely prevents the formation of the active enzyme, whereas the carboxyl-terminally located Cys-467-Cys-474 bond plays a lesser structural role.	Disulfides	67-76	alkaline phosphatase, placental	Homo sapiens	21-25
11907033-5	2002	The cysteine residue responsible for the disulfide bond formation between transporters (light chains) and heavy chain subunits of the heterodimeric amino acid transporter family is conserved for AGT1.	Disulfides	41-50	solute carrier family 7, (cationic amino acid transporter, y+ system) member 13	Mus musculus	195-199
11907033-11	2002	In the Western blot analysis, AGT1 was detected as a high molecular mass band in the nonreducing condition, whereas the band shifted to a 40-kDa band corresponding to the AGT1 monomer in the reducing condition, suggesting the association of AGT1 with other protein via a disulfide bond.	Disulfides	271-280	solute carrier family 7, (cationic amino acid transporter, y+ system) member 13	Mus musculus	30-34
12009896-5	2002	The loop 6/7 thrombin site allowed assessment of an intramolecular disulfide bond between the N- and C-terminal halves of the transporter.	Disulfides	67-76	coagulation factor II, thrombin	Homo sapiens	13-21
12032078-3	2002	The presence of ERp57 during class I assembly suggests it may be involved in the reduction of intrachain disulfides prior to retrotranslocation.	Disulfides	105-115	protein disulfide isomerase family A member 3	Homo sapiens	16-21
12479219-3	2002	An antimesothelin disulfide-linked Fv (SS1 Fv) was fused to a truncated mutant of Pseudomonas exotoxin A to produce the recombinant immunotoxin SS1(dsFv)-PE38, which has a high binding affinity to mesothelin (Kd = 0.7 nM).	Disulfides	18-27	major histocompatibility complex, class II, DR beta 1	Homo sapiens	39-42
12479219-3	2002	An antimesothelin disulfide-linked Fv (SS1 Fv) was fused to a truncated mutant of Pseudomonas exotoxin A to produce the recombinant immunotoxin SS1(dsFv)-PE38, which has a high binding affinity to mesothelin (Kd = 0.7 nM).	Disulfides	18-27	major histocompatibility complex, class II, DR beta 1	Homo sapiens	144-147
11877442-4	2002	In its disulfide form, the 13-kDa protein thioredoxin-2 is a substrate of thioredoxin reductase-1 (K(m) = 5.2 microm, k(cat) = 14.5 s(-1)) and in its dithiol form, an electron donor for TPx-1 (K(m) = 9 microm, k(cat) = 5.4 s(-1)).	Disulfides	7-16	peroxiredoxin 2	Homo sapiens	186-191
11980482-2	2002	We show here that Fis subunits rapidly exchange between dimers in solution by disulfide cross-linking mixtures of Fis mutants with different electrophoretic mobilities and by monitoring energy transfer between fluorescently labeled Fis subunits upon heterodimer formation.	Disulfides	78-87	long intergenic non-protein coding RNA 1554	Homo sapiens	18-21
12052074-0	2002	High-pressure refolding of disulfide-cross-linked lysozyme aggregates: thermodynamics and optimization.	Disulfides	27-36	lysozyme	Homo sapiens	50-58
18759047-0	2002	The thermodynamic stability of insulin disulfides is not affected by the C-domain of insulin-like growth factor 1.	Disulfides	39-49	insulin	Homo sapiens	31-38
18759047-3	2002	However, their folding behavior is different: insulin and its recombinant precursor (PIP) fold into one unique tertiary structure, while IGF-1 folds into two disulfides isomers with similar thermodynamic stability.	Disulfides	158-168	insulin like growth factor 1	Homo sapiens	137-142
11996901-5	2002	Calcitonin is a 32-amino-acid-long peptide with an N-terminal disulfide bridge and a C-terminal prolineamide residue.	Disulfides	62-71	calcitonin related polypeptide alpha	Homo sapiens	0-10
11931620-10	2002	It was found that analogues of 1, bearing a disulfide bridge, had increased selectivity to hsst2 and hsst5; however, they exhibited weaker affinity to hsst4 as compared to 1.	Disulfides	44-53	sulfotransferase family 2B member 1	Homo sapiens	91-96
12398152-8	2002	Under physiological conditions, thiyl radicals can react with thiolate anion yielding disulfide radical anion (RSSR)-* as an intermediate and finally disulfides and superoxide radical anion (O2-*), which is next inactivated in the reaction catalyzed by superoxide dismutase (SOD).	Disulfides	150-160	superoxide dismutase 1	Homo sapiens	253-273
12398152-8	2002	Under physiological conditions, thiyl radicals can react with thiolate anion yielding disulfide radical anion (RSSR)-* as an intermediate and finally disulfides and superoxide radical anion (O2-*), which is next inactivated in the reaction catalyzed by superoxide dismutase (SOD).	Disulfides	150-160	superoxide dismutase 1	Homo sapiens	275-278
12054642-5	2002	Despite a different arrangement of the disulfides, hBD-1(Ser35) proved as active as hBD-1 against the microorganisms tested.	Disulfides	39-49	defensin beta 1	Homo sapiens	51-62
12061718-1	2002	Previous NMR structural studies of the heparin-binding domain of vascular endothelial growth factor (VEGF165) revealed a novel fold comprising two subdomains, each containing two disulfide bridges and a short two-stranded antiparallel beta-sheet.	Disulfides	179-188	vascular endothelial growth factor A	Homo sapiens	65-99
12139771-1	2002	A high-performance liquid chromatographic (HPLC) analysis of human serum albumin (HSA) using an ion-exchange (DEAE-form) column shows three components: The principal component corresponds to human mercaptalbumin (HMA); the secondary to nonmercaptalbumin (HNA), having mixed disulfide with cystine (HNA[Cys]), or oxidized glutathione (HNA[Glut]); and the tertiary to HNA, oxidized more highly than mixed disulfide.	Disulfides	274-283	albumin	Homo sapiens	67-80
11919164-6	2002	Dimeric TFF1, linked by a disulfide bond, and monomeric TFF1 are produced by estrogen-responsive breast cancer cell lines.	Disulfides	26-35	trefoil factor 1	Homo sapiens	8-12
12139771-1	2002	A high-performance liquid chromatographic (HPLC) analysis of human serum albumin (HSA) using an ion-exchange (DEAE-form) column shows three components: The principal component corresponds to human mercaptalbumin (HMA); the secondary to nonmercaptalbumin (HNA), having mixed disulfide with cystine (HNA[Cys]), or oxidized glutathione (HNA[Glut]); and the tertiary to HNA, oxidized more highly than mixed disulfide.	Disulfides	403-412	albumin	Homo sapiens	67-80
11882357-10	2002	CONCLUSION: Disulfide bonds and the resulting 3D conformation of the CD22 molecules may have important roles in the difference of antigenicity of CD22 beta in B cells (CD22 beta 1) and basophils (CD22 beta 2).	Disulfides	12-21	CD22 molecule	Homo sapiens	146-150
11856829-8	2002	Finally, the results support a number of thermodynamic and kinetic experimental data concerning the role of the disulfide bridge between Cys65 and Cys72 in the folding of RNase A.	Disulfides	112-121	ribonuclease pancreatic	Bos taurus	171-178
11792705-7	2002	The V3-like domain of PrP is a disulfide-linked loop (Cys(179)-Cys(214)) that includes the E200K mutation site associated with familial Creutzfeldt-Jakob disease.	Disulfides	31-40	prion protein	Homo sapiens	22-25
11882357-10	2002	CONCLUSION: Disulfide bonds and the resulting 3D conformation of the CD22 molecules may have important roles in the difference of antigenicity of CD22 beta in B cells (CD22 beta 1) and basophils (CD22 beta 2).	Disulfides	12-21	CD22 molecule	Homo sapiens	146-150
11882357-10	2002	CONCLUSION: Disulfide bonds and the resulting 3D conformation of the CD22 molecules may have important roles in the difference of antigenicity of CD22 beta in B cells (CD22 beta 1) and basophils (CD22 beta 2).	Disulfides	12-21	CD22 molecule	Homo sapiens	146-150
11835989-0	2002	Antibacterial activities and conformations of bovine beta-defensin BNBD-12 and analogs:structural and disulfide bridge requirements for activity.	Disulfides	102-111	LOC100296173	Bos taurus	53-66
11868814-0	2002	Importance of glycosylation and disulfide bonds in hyaluronidase activity of macaque sperm surface PH-20.	Disulfides	32-41	sperm adhesion molecule 1	Homo sapiens	99-104
11904141-3	2002	Moreover, mutant F proteins that lacked the specific N-linked oligosaccharide chains required for disulfide bond formation showed increased association with ERp57.	Disulfides	98-107	protein disulfide isomerase family A member 3	Homo sapiens	157-162
11858710-7	2002	Introduction of the intramolecular disulfide bond together with C-terminal shortening and replacement of C-terminal residue was shown to result in increasing the thermal stability by 19 degrees C and four times enhancement of biological activity compared with intact IFN-gamma molecule.	Disulfides	35-44	interferon gamma	Homo sapiens	267-276
11847130-5	2002	ERp44 forms mixed disulfides with both hEROs and cargo folding intermediates.	Disulfides	18-28	endoplasmic reticulum protein 44	Homo sapiens	0-5
11842220-2	2002	It interacts with ERp57, a thiol-disulfide oxidoreductase that promotes the formation of disulfide bonds in glycoproteins bound by CRT.	Disulfides	33-42	protein disulfide isomerase family A member 3	Homo sapiens	18-23
11842220-2	2002	It interacts with ERp57, a thiol-disulfide oxidoreductase that promotes the formation of disulfide bonds in glycoproteins bound by CRT.	Disulfides	33-42	calreticulin	Homo sapiens	131-134
11866530-3	2002	Three classes of disulfide-constrained peptides that antagonize binding of the VEGF dimer to its receptors, KDR and Flt-1, were identified previously using phage display methods.	Disulfides	17-26	vascular endothelial growth factor A	Homo sapiens	79-83
11866530-3	2002	Three classes of disulfide-constrained peptides that antagonize binding of the VEGF dimer to its receptors, KDR and Flt-1, were identified previously using phage display methods.	Disulfides	17-26	fms related receptor tyrosine kinase 1	Homo sapiens	116-121
11830467-7	2002	Under nonreducing conditions the Pro(33)DeltaLys(611) variant migrated with a slightly decreased molecular weight compared to the Pro(33)Lys(611) isoform suggesting that DeltaLys(611) has an influence on the disulfide bonds of GPIIIa.	Disulfides	208-217	integrin subunit beta 3	Homo sapiens	227-233
11814349-1	2002	Although insulin and insulin-like growth factor 1 (IGF-1) share homologous sequence, similar tertiary structure, weakly overlapped biological activity, and a common ancestor, the two highly homologous sequences encode different folding behavior: insulin folds into one unique stable tertiary structure while IGF-1 folds into two disulfide isomers with similar thermodynamic stability.	Disulfides	329-338	insulin like growth factor 1	Homo sapiens	51-56
11814341-2	2002	We address this problem by studying the conformational propensities of reductively unfolded RNase A under folding conditions, since earlier work has indicated that the equilibrium conformational ensemble of fully reduced RNase A resembles the transient conformational ensemble of a burst-phase folding intermediate of disulfide-intact RNase A.	Disulfides	318-327	ribonuclease pancreatic	Bos taurus	92-99
11814349-3	2002	Both mini-IGF-1 and Ins(A)/IGF-1(B) fold into two thermodynamically stable disulfide isomers in vivo and in vitro just like that of IGF-1, while Ins(B)/IGF-1(A) folds into one unique thermodynamically stable tertiary structure in vivo and in vitro just like that of insulin.	Disulfides	75-84	insulin like growth factor 1	Homo sapiens	10-15
11814341-3	2002	To assess these propensities, the relative disulfide-bond populations of the 1S, 2S, and 3S ensembles of the [C40A,C95A] mutant of RNase A were measured.	Disulfides	43-52	ribonuclease pancreatic	Bos taurus	131-138
11814341-7	2002	The 65-72 disulfide bond is much more strongly favored than would be predicted by this power law, consistent with earlier peptide studies and the disulfide-bond distributions of the 1S and 2S ensembles in wild-type RNase A.	Disulfides	10-19	ribonuclease pancreatic	Bos taurus	215-222
11814349-3	2002	Both mini-IGF-1 and Ins(A)/IGF-1(B) fold into two thermodynamically stable disulfide isomers in vivo and in vitro just like that of IGF-1, while Ins(B)/IGF-1(A) folds into one unique thermodynamically stable tertiary structure in vivo and in vitro just like that of insulin.	Disulfides	75-84	insulin like growth factor 1	Homo sapiens	27-32
11814349-3	2002	Both mini-IGF-1 and Ins(A)/IGF-1(B) fold into two thermodynamically stable disulfide isomers in vivo and in vitro just like that of IGF-1, while Ins(B)/IGF-1(A) folds into one unique thermodynamically stable tertiary structure in vivo and in vitro just like that of insulin.	Disulfides	75-84	insulin like growth factor 1	Homo sapiens	27-32
11814349-3	2002	Both mini-IGF-1 and Ins(A)/IGF-1(B) fold into two thermodynamically stable disulfide isomers in vivo and in vitro just like that of IGF-1, while Ins(B)/IGF-1(A) folds into one unique thermodynamically stable tertiary structure in vivo and in vitro just like that of insulin.	Disulfides	75-84	insulin like growth factor 1	Homo sapiens	27-32
11820931-7	2002	Des-(121-124)-RNase A failed to recover activity both in the presence and absence of glutathione, due to the mismatched formation of disulfide bonds.	Disulfides	133-142	ribonuclease pancreatic	Bos taurus	14-21
11839698-4	2002	The isolated a and a" domains of PDI are good catalysts of simple thiol-disulfide interchange reactions but require additional domains to be effective as catalysts of the rate-limiting disulfide isomerizations in protein folding pathways.	Disulfides	72-81	protein disulfide isomerase family A member 2	Homo sapiens	33-36
11839698-4	2002	The isolated a and a" domains of PDI are good catalysts of simple thiol-disulfide interchange reactions but require additional domains to be effective as catalysts of the rate-limiting disulfide isomerizations in protein folding pathways.	Disulfides	185-194	protein disulfide isomerase family A member 2	Homo sapiens	33-36
11935325-9	2002	On the basis of predictions from molecular modeling of the X-ray crystallographic structure of chick smooth muscle myosin, the mutated thiol reactive group of R702C may lead to intermolecular disulfide bridges, with the consequent formation of the inclusions typical of FTNS.	Disulfides	192-201	myosin, heavy chain 9, non-muscle	Gallus gallus	115-121
11883697-2	2002	It is composed of the disulfide-stabilized Fv portion of the anti-CD22 antibody RFB4 genetically fused to a truncated form of Pseudomonas exotoxin A.	Disulfides	22-31	CD22 molecule	Homo sapiens	66-70
11820931-11	2002	The C-terminal amino acids play a significant role in the formation of the correct disulfide bonds during the refolding process, and the interaction of amino acid residues and the existence of the main chain around the C-terminal region are both important for achieving the efficient packing of the RNase A molecule.	Disulfides	83-92	ribonuclease pancreatic	Bos taurus	299-306
11698397-10	2002	SOD-catalyzed oxidation of GSH and homocysteine was enhanced by cysteine through a thiol-disulfide exchange mechanism.	Disulfides	89-98	superoxide dismutase 1	Homo sapiens	0-3
11796015-0	2002	Expression of HER2 in human gastric cancer cells directly correlates with antitumor activity of a recombinant disulfide-stabilized anti-HER2 immunotoxin.	Disulfides	110-119	erb-b2 receptor tyrosine kinase 2	Homo sapiens	14-18
11796015-0	2002	Expression of HER2 in human gastric cancer cells directly correlates with antitumor activity of a recombinant disulfide-stabilized anti-HER2 immunotoxin.	Disulfides	110-119	erb-b2 receptor tyrosine kinase 2	Homo sapiens	136-140
11560938-0	2002	The folding pathway of alpha-lactalbumin elucidated by the technique of disulfide scrambling.	Disulfides	72-81	lactalbumin alpha	Homo sapiens	23-40
11771999-11	2002	ProS and the chicken cystatin share two conserved disulfide bonds as well as a high conservation of hydrophobic residues.	Disulfides	50-59	cystatin C	Gallus gallus	21-29
11795902-4	2002	Using these procedures, we identified ERP72 and ERP60, two members of the protein disulfide isomerase family, creatine kinase, glyceraldehyde-3-phosphate dehydrogenase, phospholipase C-gamma1, and thioredoxin reductase as the targets of DA-derived H2O2.	Disulfides	82-91	protein disulfide isomerase family A, member 3	Rattus norvegicus	48-53
11694508-7	2002	The present results suggest that PDI is acting both as an isomerase and as a chaperone during folding and disulfide bond formation of proinsulin.	Disulfides	106-115	insulin	Homo sapiens	134-144
11560938-3	2002	Under strong denaturing conditions (e.g. 6 m guanidinium chloride) and in the presence of a thiol initiator, alpha-lactalbumin (alphaLA) denatures by shuffling its four native disulfide bonds and converts to an assembly of 45 species of scrambled isomers.	Disulfides	176-185	lactalbumin alpha	Homo sapiens	109-126
11754549-0	2002	Engineering nutritious proteins: improvement of stability in the designer protein MB-1 via introduction of disulfide bridges.	Disulfides	107-116	CD79a molecule	Homo sapiens	82-86
11754549-4	2002	Reported here are the synthesis and characterization of two disulfide-bridged mutants derived from the MB-1 designer protein.	Disulfides	60-69	CD79a molecule	Homo sapiens	103-107
11754549-6	2002	When the disulfide bridges were cleaved, the mutants" behavior changed: the mutants significantly unfolded, suggesting that the introduction of Cys residues was deleterious to MB-1-folding.	Disulfides	9-18	CD79a molecule	Homo sapiens	176-180
11885292-0	2002	Disulfide reduction in major histocompatibility complex class II-restricted antigen processing by interferon-gamma-inducible lysosomal thiol reductase.	Disulfides	0-9	IFI30 lysosomal thiol reductase	Homo sapiens	98-150
11928826-1	2002	Apolipoprotein(a) [apo(a)] is the distinctive glycoprotein of lipoprotein Lp(a), which is disulfide linked to the apo B100 of a low density lipoprotein particle.	Disulfides	90-99	apolipoprotein B	Homo sapiens	114-122
11928826-11	2002	These data suggest that the stringent specificity of tissue-type plasminogen activator for plasminogen requires molecular interactions with structures located remotely from the activation disulfide loop.	Disulfides	188-197	plasminogen activator, tissue type	Homo sapiens	53-86
11825568-1	2002	The presence of a disulfide bond inside the peptide binding groove of MHC class I molecules and of the thiol oxidoreductase ERp57 in the class I loading complex suggests that disulfide bond isomerization may play a role in peptide loading.	Disulfides	18-27	protein disulfide isomerase family A member 3	Homo sapiens	124-129
11825568-1	2002	The presence of a disulfide bond inside the peptide binding groove of MHC class I molecules and of the thiol oxidoreductase ERp57 in the class I loading complex suggests that disulfide bond isomerization may play a role in peptide loading.	Disulfides	175-184	protein disulfide isomerase family A member 3	Homo sapiens	124-129
11825568-2	2002	Here we show that ERp57 and tapasin are disulfide linked inside the loading complex.	Disulfides	40-49	protein disulfide isomerase family A member 3	Homo sapiens	18-23
11825568-2	2002	Here we show that ERp57 and tapasin are disulfide linked inside the loading complex.	Disulfides	40-49	TAP binding protein	Homo sapiens	28-35
11825568-5	2002	These findings suggest a role for disulfide bond isomerization in tapasin-mediated peptide loading.	Disulfides	34-43	TAP binding protein	Homo sapiens	66-73
12139377-1	2002	Biologically active IL-12 is a 70 kDa heterodimeric cytokine (IL-12 p70) mainly produced by antigen-presenting cells (APC) and made of disulfide-linked alpha (p35) and beta (p40) chains.	Disulfides	135-144	ubiquitin associated and SH3 domain containing B	Homo sapiens	68-71
11885292-1	2002	Constitutively expressed in antigen-presenting cells (APCs), interferon-gamma-inducible lysosomal thiol reductase (GILT) catalyzes disulfide bond reduction under acidic conditions.	Disulfides	131-140	IFI30 lysosomal thiol reductase	Homo sapiens	61-113
11885292-1	2002	Constitutively expressed in antigen-presenting cells (APCs), interferon-gamma-inducible lysosomal thiol reductase (GILT) catalyzes disulfide bond reduction under acidic conditions.	Disulfides	131-140	IFI30 lysosomal thiol reductase	Homo sapiens	115-119
11885292-4	2002	A well-established assay spectrophotometrically measures interchain disulfide bond reduction of insulin via the precipitation of aggregating free B chains.	Disulfides	68-77	insulin	Homo sapiens	96-103
11591708-3	2001	The cysteine residue responsible for the disulfide bond formation between transporters (light chains) and heavy chain subunits in the heterodimeric amino acid transporters is conserved for Asc-2.	Disulfides	41-50	solute carrier family 7 (cationic amino acid transporter, y+ system), member 12	Mus musculus	189-194
11591708-10	2001	In the Western blot analysis on mouse erythrocytes and kidney, Asc-2 was detected as multiple bands in the nonreducing condition, whereas the bands shifted to a single band at lower molecular weight, suggesting the association of Asc-2 with other protein(s) via a disulfide bond.	Disulfides	264-273	solute carrier family 7 (cationic amino acid transporter, y+ system), member 12	Mus musculus	230-235
11747437-0	2001	Cleavage of disulfide-bridged stalk domains during shedding of angiotensin-converting enzyme occurs at multiple juxtamembrane sites.	Disulfides	12-21	angiotensin I converting enzyme	Homo sapiens	63-92
11732921-0	2001	Folding of a disulfide-bonded protein species with free thiol(s): competition between conformational folding and disulfide reshuffling in an intermediate of bovine pancreatic ribonuclease A.	Disulfides	13-22	ribonuclease pancreatic	Bos taurus	175-189
11735415-0	2001	Role of the disulfide cleavage induced molten globule state of type a botulinum neurotoxin in its endopeptidase activity.	Disulfides	12-21	neurotoxin	Clostridium botulinum	80-90
11735415-2	2001	The endopeptidase activity of type A botulinum neurotoxin (BoNT/A) is triggered by reduction of its disulfide bond between its heavy chain and light chain.	Disulfides	100-109	neurotoxin	Clostridium botulinum	47-57
11732921-0	2001	Folding of a disulfide-bonded protein species with free thiol(s): competition between conformational folding and disulfide reshuffling in an intermediate of bovine pancreatic ribonuclease A.	Disulfides	113-122	ribonuclease pancreatic	Bos taurus	175-189
11688981-2	2001	In this study we report that treating wild type CFTR-expressing cells with oxidizing agents results in a significant reduction in the gel mobility of the protein indicative of the formation of disulfide bonds.	Disulfides	193-202	CF transmembrane conductance regulator	Homo sapiens	48-52
11090689-1	2001	The production of human proinsulin in its disulfide-intact, native form in Escherichia coli requires disulfide bond formation and the periplasmic space is the favourable compartment for oxidative folding.	Disulfides	42-51	insulin	Homo sapiens	24-34
11090689-1	2001	The production of human proinsulin in its disulfide-intact, native form in Escherichia coli requires disulfide bond formation and the periplasmic space is the favourable compartment for oxidative folding.	Disulfides	101-110	insulin	Homo sapiens	24-34
11090689-2	2001	However, the secretory expression of proinsulin is limited by its high susceptibility to proteolysis and by disulfide bond formation, which is rate-limiting for proinsulin folding.	Disulfides	108-117	insulin	Homo sapiens	37-47
11090689-2	2001	However, the secretory expression of proinsulin is limited by its high susceptibility to proteolysis and by disulfide bond formation, which is rate-limiting for proinsulin folding.	Disulfides	108-117	insulin	Homo sapiens	161-171
11090689-5	2001	As DsbA is the main catalyst of disulfide bond formation in E. coli, we expected increased yields of proinsulin by intra- or intermolecular catalysis of disulfide bond formation.	Disulfides	32-41	insulin	Homo sapiens	101-111
11090689-5	2001	As DsbA is the main catalyst of disulfide bond formation in E. coli, we expected increased yields of proinsulin by intra- or intermolecular catalysis of disulfide bond formation.	Disulfides	153-162	insulin	Homo sapiens	101-111
11090689-6	2001	In the context of the fusion protein, proinsulin was found to be stabilised, probably due to an increased solubility and faster disulfide bond formation.	Disulfides	128-137	insulin	Homo sapiens	38-48
11842239-0	2002	Effect of the intermolecular disulfide bond on the conformation and stability of glial cell line-derived neurotrophic factor.	Disulfides	29-38	glial cell derived neurotrophic factor	Homo sapiens	81-124
11842239-3	2002	Sedimentation equilibrium and velocity experiments demonstrated that, after removal of the interchain disulfide bond, GDNF remains as a non-covalent dimer and is stable at pH 7.0.	Disulfides	102-111	glial cell derived neurotrophic factor	Homo sapiens	118-122
11842239-4	2002	To investigate the effect of the intermolecular disulfide on the structure and stability of GDNF, we compared the solution structures of the wild-type protein and a cysteine-101 to alanine (C101A) mutant using Fourier transform infrared (FTIR), FT-Raman and circular dichroism (CD) spectroscopy and sedimentation analysis.	Disulfides	48-57	glial cell derived neurotrophic factor	Homo sapiens	92-96
11842239-5	2002	The elimination of the intermolecular disulfide bond causes only minor changes (approximately 4%) in the secondary structures of GDNF.	Disulfides	38-47	glial cell derived neurotrophic factor	Homo sapiens	129-133
11842239-10	2002	By comparing the Raman spectrum of wild-type GDNF with that of the C101A analog, we identified the conformation of the intermolecular disulfide as trans-gauche-trans geometry.	Disulfides	134-143	glial cell derived neurotrophic factor	Homo sapiens	45-49
11716463-3	2001	Under nonreducing conditions, native PP7 exists as a mixture of monomer with an intramolecular disulfide bridge, disulfide-linked homodimer, and possibly disulfide-linked complexes with potential partner proteins.	Disulfides	95-104	serine/threonine phosphatase 7	Arabidopsis thaliana	37-40
11716463-3	2001	Under nonreducing conditions, native PP7 exists as a mixture of monomer with an intramolecular disulfide bridge, disulfide-linked homodimer, and possibly disulfide-linked complexes with potential partner proteins.	Disulfides	113-122	serine/threonine phosphatase 7	Arabidopsis thaliana	37-40
11716463-3	2001	Under nonreducing conditions, native PP7 exists as a mixture of monomer with an intramolecular disulfide bridge, disulfide-linked homodimer, and possibly disulfide-linked complexes with potential partner proteins.	Disulfides	113-122	serine/threonine phosphatase 7	Arabidopsis thaliana	37-40
11718563-7	2001	In contrast to the isolated alpha-helical domain of alpha-lactalbumin, Lyso-alpha with two native disulfide bonds exhibits a well-defined tertiary structure, as indicated by cooperative thermal unfolding and a well-dispersed NMR spectrum.	Disulfides	98-107	lactalbumin alpha	Homo sapiens	52-69
11535606-6	2001	Although heterodimer formation does not involve intermolecular disulfide bonds, RAMP-CRLR association promotes the formation of intramolecular disulfide bonds within RAMP1.	Disulfides	143-152	calcitonin receptor like receptor	Homo sapiens	85-89
11601970-0	2001	Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1.	Disulfides	139-148	rhodopsin	Homo sapiens	71-80
11714858-4	2001	The methionine residue is oxidized to the corresponding sulfoxide, and the primary sequence peptide (residues 1-14 of apoB-100) is linked by the intramolecular disulfide bond between C-12 and C-61 to the peptide composed of residues 53-66, as we have observed previously (Yang, C-Y., T. W. Kim, S. A. Weng, B. Lee, M. Yang, and A. M. Gotto, Jr. 1990.	Disulfides	160-169	apolipoprotein B	Homo sapiens	118-126
11703593-3	2001	One protein, fibronectin (FN), associates to form an insoluble disulfide-linked matrix and possesses inherent protein-disulfide isomerase (PDI) activity.	Disulfides	63-72	fibronectin 1	Homo sapiens	13-24
11703593-3	2001	One protein, fibronectin (FN), associates to form an insoluble disulfide-linked matrix and possesses inherent protein-disulfide isomerase (PDI) activity.	Disulfides	63-72	fibronectin 1	Homo sapiens	26-28
11816713-1	2001	GPIbbeta is disulfide-linked to GPIbalpha to form GPIb, a platelet receptor for von Willebrand factor (vWF).	Disulfides	12-21	von Willebrand factor	Homo sapiens	80-101
11816713-1	2001	GPIbbeta is disulfide-linked to GPIbalpha to form GPIb, a platelet receptor for von Willebrand factor (vWF).	Disulfides	12-21	von Willebrand factor	Homo sapiens	103-106
11526117-13	2001	We conclude that a heterogeneous combination of specific proteolysis and intermolecular disulfide bond formation in the sperm head generates multiple forms of zonadhesin with differing avidities for the zona pellucida.	Disulfides	88-97	zonadhesin	Sus scrofa	159-169
11694580-5	2001	We show that Pmel17 is cleaved in a post-Golgi compartment into two disulfide-linked subunits: a large lumenal subunit, M alpha, and an integral membrane subunit, M beta.	Disulfides	68-77	premelanosome protein	Homo sapiens	13-19
11601970-7	2001	The observed disulfide bond formation rates correlate well with proximity of these residues found in the crystal structure of rhodopsin in the dark.	Disulfides	13-22	rhodopsin	Homo sapiens	126-135
11601971-0	2001	Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3, and 4.	Disulfides	139-148	rhodopsin	Homo sapiens	71-80
11601971-6	2001	Comparisons of the results from disulfide bond formation in solution with the distances observed in the rhodopsin crystal structure showed that the rates of disulfide bond formation in most cases were consistent with the amino acid proximities as revealed in crystal structure.	Disulfides	157-166	rhodopsin	Homo sapiens	104-113
11558598-1	2001	Human interleukin 6 (hIL-6), which is a cytokine involved in diverse biological activities, consists of a four-helix bundle with two disulfide bonds.	Disulfides	133-142	interleukin 6	Homo sapiens	6-19
11489908-1	2001	We report the use of thiol chemistry to define specific and reversible disulfide interactions of Cys-substituted NK2 receptor mutants with analogues of neurokinin A (NKA) containing single cysteine substitutions.	Disulfides	71-80	tachykinin precursor 1	Homo sapiens	152-164
11489908-1	2001	We report the use of thiol chemistry to define specific and reversible disulfide interactions of Cys-substituted NK2 receptor mutants with analogues of neurokinin A (NKA) containing single cysteine substitutions.	Disulfides	71-80	tachykinin precursor 1	Homo sapiens	166-169
11489908-3	2001	N-biotinyl-[Tyr1,Cys9]NKA, N-biotinyl-[Tyr1,Cys10]NKA were both found to reversibly disulfide bond to the NK2 receptor mutant Met297 --&gt; Cys.	Disulfides	84-93	tachykinin precursor 1	Homo sapiens	22-25
11489908-3	2001	N-biotinyl-[Tyr1,Cys9]NKA, N-biotinyl-[Tyr1,Cys10]NKA were both found to reversibly disulfide bond to the NK2 receptor mutant Met297 --&gt; Cys.	Disulfides	84-93	tachykinin precursor 1	Homo sapiens	50-53
11580297-0	2001	A new spectroscopic approach to examining the role of disulfide bonds in the structure and unfolding of soybean trypsin inhibitor.	Disulfides	54-63	kunitz trypsin protease inhibitor	Glycine max	112-129
11580297-2	2001	In this work, we have used a new, real-time spectroscopic approach to examine how the reduction of two disulfide bonds affects the secondary structure of soybean trypsin inhibitor (STI).	Disulfides	103-112	kunitz trypsin protease inhibitor	Glycine max	162-179
11454874-5	2001	Mutagenesis to prevent formation of this disulfide completely disrupted CD47 signaling independent of effects on ligand binding, as assessed by T cell interleukin-2 secretion and Ca(2+) responses.	Disulfides	41-50	interleukin 2	Homo sapiens	151-164
11553487-2	2001	Recently, we assembled an artificial transaminase by conjugation of intestinal fatty acid binding protein (IFABP) with a pyridoxamine derivative via a disulfide bond; the resulting construct catalyzed a transamination reaction 200-fold faster than free pyridoxamine.	Disulfides	151-160	fatty acid binding protein 2	Homo sapiens	68-105
11553487-2	2001	Recently, we assembled an artificial transaminase by conjugation of intestinal fatty acid binding protein (IFABP) with a pyridoxamine derivative via a disulfide bond; the resulting construct catalyzed a transamination reaction 200-fold faster than free pyridoxamine.	Disulfides	151-160	fatty acid binding protein 2	Homo sapiens	107-112
11591149-0	2001	Hierarchical protein folding: asymmetric unfolding of an insulin analogue lacking the A7-B7 interchain disulfide bridge.	Disulfides	103-112	insulin	Homo sapiens	57-64
11591149-3	2001	Stepwise stabilization of structural subdomains among on-pathway intermediates is proposed to underlie the disulfide pathway of proinsulin and related molecules.	Disulfides	107-116	insulin	Homo sapiens	128-138
11591149-4	2001	Here, effects of pairwise serine substitution of insulin"s exposed interchain disulfide bridge (Cys(A7)-Cys(B7)) are characterized as a model of a late intermediate.	Disulfides	78-87	insulin	Homo sapiens	49-56
11573936-0	2001	A disulfide bond is required for functional assembly of NCX1 from complementary fragments.	Disulfides	2-11	solute carrier family 8 member A1	Homo sapiens	56-60
11687299-0	2001	Interrelationships among biological activity, disulfide bonds, secondary structure, and metal ion binding for a chemically synthesized 34-amino-acid peptide derived from alpha-fetoprotein.	Disulfides	46-55	alpha fetoprotein	Homo sapiens	170-187
11473115-1	2001	We have previously shown that lipoprotein(a) (Lp(a)) assembly involves an initial noncovalent interaction between sequences within apolipoprotein(a) (apo(a)) kringle IV types 5-8 and the amino terminus of apolipoprotein B-100 (sequences between amino acids 680 and 781 in apoB-100), followed by formation of a disulfide bond.	Disulfides	310-319	apolipoprotein B	Homo sapiens	205-225
11558598-1	2001	Human interleukin 6 (hIL-6), which is a cytokine involved in diverse biological activities, consists of a four-helix bundle with two disulfide bonds.	Disulfides	133-142	interleukin 6	Homo sapiens	21-26
11478907-3	2001	A compound consisting merely of the cyclic core of hMCH with the Arg attached to the N-terminus of the disulfide ring was found to activate both hMCH-1R and hMCH-2R about as effectively as full-length hMCH.	Disulfides	103-112	pro-melanin concentrating hormone	Homo sapiens	51-55
11397793-4	2001	Grx2 exhibited 36% identity with Grx1 and had a disulfide active center containing the Cys-Ser-Tyr-Cys motif.	Disulfides	48-57	glutaredoxin 2	Homo sapiens	0-4
11766126-11	2001	Recombinant human IL-6 (rhIL-6) exposed to HD lacked the second disulfide bridge and was partially unfolded, as determined by nuclear magnetic resonance-nuclear Overhauser enhancement and exchange spectroscopy (NMR-NOESY).	Disulfides	64-73	interleukin 6	Homo sapiens	18-22
11509657-0	2001	Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation.	Disulfides	99-108	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	24-29
11509657-9	2001	Our data provide evidence for molecular mechanisms of redox signal sensing through the thiol-disulfide redox cycle coupled with the thioredoxin system in the Yap1p NES.	Disulfides	93-102	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	158-163
11518539-1	2001	The hydrogen-exchange behavior of the low-pH molten globule of human alpha-lactalbumin, containing all four disulfides, has been examined and compared with that of a single disulfide variant, [28-111] alpha-lactalbumin, and of a series of proline variants of [28-111] alpha-lactalbumin.	Disulfides	108-118	lactalbumin alpha	Homo sapiens	69-86
11518539-1	2001	The hydrogen-exchange behavior of the low-pH molten globule of human alpha-lactalbumin, containing all four disulfides, has been examined and compared with that of a single disulfide variant, [28-111] alpha-lactalbumin, and of a series of proline variants of [28-111] alpha-lactalbumin.	Disulfides	108-117	lactalbumin alpha	Homo sapiens	69-86
11500369-0	2001	Functional relevance of the disulfide-linked complex of the N-terminal PDZ domain of InaD with NorpA.	Disulfides	28-37	inactivation no afterpotential D	Drosophila melanogaster	85-89
11500369-0	2001	Functional relevance of the disulfide-linked complex of the N-terminal PDZ domain of InaD with NorpA.	Disulfides	28-37	no receptor potential A	Drosophila melanogaster	95-100
11478874-2	2001	The C-terminal part containing the three disulfide bridges CART(48-89) is the biologically active part of the molecule affecting food intake.	Disulfides	41-50	CART prepropeptide	Homo sapiens	59-63
11478907-3	2001	A compound consisting merely of the cyclic core of hMCH with the Arg attached to the N-terminus of the disulfide ring was found to activate both hMCH-1R and hMCH-2R about as effectively as full-length hMCH.	Disulfides	103-112	pro-melanin concentrating hormone	Homo sapiens	145-149
11478907-3	2001	A compound consisting merely of the cyclic core of hMCH with the Arg attached to the N-terminus of the disulfide ring was found to activate both hMCH-1R and hMCH-2R about as effectively as full-length hMCH.	Disulfides	103-112	pro-melanin concentrating hormone	Homo sapiens	145-149
11478907-3	2001	A compound consisting merely of the cyclic core of hMCH with the Arg attached to the N-terminus of the disulfide ring was found to activate both hMCH-1R and hMCH-2R about as effectively as full-length hMCH.	Disulfides	103-112	pro-melanin concentrating hormone	Homo sapiens	145-149
11468164-3	2001	The neo-Cys residues were always found to be disulfide-bridged to either an isolated Cys amino acid or to the corresponding Cys residue of another abnormal fibrinogen molecule, forming dimers.	Disulfides	45-54	fibrinogen beta chain	Homo sapiens	156-166
11459935-3	2001	Myostatin protein purified from mammalian cells consisted of a noncovalently held complex of the N-terminal propeptide and a disulfide-linked dimer of C-terminal fragments.	Disulfides	125-134	myostatin	Homo sapiens	0-9
11309389-8	2001	The GH concentration dependence for inhibition of PMA-induced GHR proteolysis paralleled that for its promotion of receptor dimerization (as monitored by formation of GHR disulfide linkage).	Disulfides	171-180	somatotropin	Oryctolagus cuniculus	4-6
11297543-5	2001	The human Grx2 sequence contains three characteristic regions of the glutaredoxin family: the dithiol/disulfide active site, CSYC, the GSH binding site, and a hydrophobic surface area.	Disulfides	102-111	glutaredoxin 2	Homo sapiens	10-14
11456492-6	2001	Thus, the trans to cis isomerization of the Tyr92-Pro93 peptide group during the regeneration of wild-type RNase A may occur after the formation of the third native disulfide bond.	Disulfides	165-174	ribonuclease pancreatic	Bos taurus	107-114
11491658-4	2001	Osmotic stress also promoted activation and disulfide-bonded dimerization of the extracellular domain-depleted mutant RET (RET-PTC-1), suggesting that the target amino acid(s) for dimerization is located intracellularly rather than in the cysteine-rich region of the extracellular domain.	Disulfides	44-53	patched 1	Homo sapiens	127-132
12750762-1	2001	Endothelins (ET-1, ET-2 and ET-3) are 21-amino-acid peptides with two disulfide bonds that belong to the sarafotoxin family.	Disulfides	70-79	endothelin 1	Homo sapiens	0-11
12750762-1	2001	Endothelins (ET-1, ET-2 and ET-3) are 21-amino-acid peptides with two disulfide bonds that belong to the sarafotoxin family.	Disulfides	70-79	endothelin 1	Homo sapiens	13-17
11223094-8	2001	In order to improve the affinity of the peptide to alpha-BTX, we designed and synthesized the peptide CRYYESSLKSYCD (Met1 and Pro12 were replaced by cysteines), which following oxidation creates a single disulfide bond and forms a cyclic structure.	Disulfides	204-213	DNA methyltransferase (cytosine-5) 1	Mus musculus	117-121
11320094-8	2001	Studies also suggest that the N and C halves of ABCR are linked through disulfide bonds.	Disulfides	72-81	ATP binding cassette subfamily A member 4	Homo sapiens	48-52
11433346-6	2001	Although FANCC lacks homology with conventional disulfide reductases, it functions by preventing the formation of inactivating disulfide bonds within GSTP1 during apoptosis.	Disulfides	48-57	FA complementation group C	Homo sapiens	9-14
11278628-5	2001	The purified laminin isoform was composed of disulfide-linked 230-, 220-, and 200-kDa subunits, which immunoblot analysis identified as the beta1, gamma1, and alpha4 chains.	Disulfides	45-54	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	140-165
11387253-0	2001	ER60/ERp57 forms disulfide-bonded intermediates with MHC class I heavy chain.	Disulfides	17-26	protein disulfide isomerase family A member 3	Homo sapiens	0-4
11387253-0	2001	ER60/ERp57 forms disulfide-bonded intermediates with MHC class I heavy chain.	Disulfides	17-26	protein disulfide isomerase family A member 3	Homo sapiens	5-10
11278637-7	2001	Expression of high concentrations of the mutant protein in wild-type mice reduced the abundance of disulfide cross-linked oligomers of endogenous SP-D in the bronchoalveolar lavage fluid and demonstrated a phenotype that partially overlapped with that of the SP-D-/- mice; the animals developed emphysema and foamy macrophages without the associated abnormalities in alveolar phospholipids typical of SP-D-/- mice.	Disulfides	99-108	surfactant associated protein D	Mus musculus	146-150
11278637-9	2001	Disulfide cross-linked SP-D oligomers are required for the regulation of surfactant phospholipid homeostasis and the prevention of emphysema and foamy macrophages in vivo.	Disulfides	0-9	surfactant associated protein D	Mus musculus	23-27
11359834-4	2001	C4BP consists of seven identical alpha-chains and one beta-chain linked together with disulfide bridges.	Disulfides	86-95	complement component 4 binding protein alpha	Homo sapiens	0-4
11699729-2	2001	Lp(a) is, however, distinguishable from LDL by the presence of an additional glycoprotein apolipoprotein(a) [apo(a)], which is covalently attached to apo B-100 by a single disulfide bond.	Disulfides	172-181	apolipoprotein B	Homo sapiens	150-159
11369801-0	2001	Limited proteolysis of a disulfide-linked apoA-I dimer in reconstituted HDL.	Disulfides	25-34	apolipoprotein A1	Homo sapiens	42-48
11340658-0	2001	Crystal structure of a mutant human lysozyme with a substituted disulfide bond.	Disulfides	64-73	lysozyme	Homo sapiens	36-44
11340658-1	2001	The three-dimensional structure of a mutant human lysozyme, W64CC65A, in which a non-native disulfide bond Cys64--Cys81 is substituted for the Cys65--Cys81 of the wild type protein by replacing Trp64 and Cys65 with Cys and Ala, respectively, was determined by X-ray crystallography and refined to an R-value of 0.181, using 33,187 reflections at 1.87-A resolution.	Disulfides	92-101	lysozyme	Homo sapiens	50-58
11139586-3	2001	A mutant GroEL(AEX) (C138S,C458S,C519S,D83C,K327C) in the oxidized form is locked in a closed conformation by an interdomain disulfide cross-link and cannot hydrolyze ATP (Murai, N., Makino, Y., and Yoshida, M. (1996) J. Biol.	Disulfides	125-134	GroEL	Escherichia coli	9-14
11278672-2	2001	Cell wall attachment of Aga2p is mediated through two disulfide bonds to Aga1p (Cappellaro, C., Baldermann, C., Rachel, R., and Tanner, W. (1994) EMBO J.	Disulfides	54-63	Aga2p	Saccharomyces cerevisiae S288C	24-29
11278672-5	2001	Aga2p co-expressed with a 149-residue fragment of Aga1p formed a disulfide-linked complex with specific activity 43-fold higher than Aga2p expressed alone.	Disulfides	65-74	Aga2p	Saccharomyces cerevisiae S288C	0-5
11368628-6	2001	The results also indicated that the aggregates and intermediates, which contained dimeric and trimeric alpha-La, were mainly formed by the intermolecular disulfide bonds.	Disulfides	154-163	lactalbumin alpha	Homo sapiens	103-111
11279016-2	2001	Human nerve growth factor beta (NGF) contains three disulfide bonds between nonconsecutive cysteine residues and forms insoluble aggregates when expressed in E. coli.	Disulfides	52-61	nerve growth factor	Homo sapiens	6-25
11279016-2	2001	Human nerve growth factor beta (NGF) contains three disulfide bonds between nonconsecutive cysteine residues and forms insoluble aggregates when expressed in E. coli.	Disulfides	52-61	nerve growth factor	Homo sapiens	32-35
11320236-0	2001	Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants.	Disulfides	99-108	rhodopsin	Homo sapiens	26-35
11320236-2	2001	Previous work has shown that misfolding is caused by the formation of a disulfide bond in the ID domain different from the native Cys-110-Cys-187 disulfide bond in native rhodopsin.	Disulfides	146-155	rhodopsin	Homo sapiens	171-180
11320237-4	2001	The reagent is attached to the SH group of cytoplasmic monocysteine rhodopsin mutants by a disulfide-exchange reaction with the pyridylthio group, and the derivatized rhodopsin then is complexed with T by illumination at lambda &gt;495 nm.	Disulfides	91-100	rhodopsin	Homo sapiens	68-77
11320237-4	2001	The reagent is attached to the SH group of cytoplasmic monocysteine rhodopsin mutants by a disulfide-exchange reaction with the pyridylthio group, and the derivatized rhodopsin then is complexed with T by illumination at lambda &gt;495 nm.	Disulfides	91-100	rhodopsin	Homo sapiens	167-176
11425803-0	2001	Neighboring cysteine residues in human fucosyltransferase VII are engaged in disulfide bridges, forming small loop structures.	Disulfides	77-86	fucosyltransferase 7	Homo sapiens	39-61
11425803-4	2001	We identified the disulfide bridges in a recombinant, soluble form of human FucT VII.	Disulfides	18-27	fucosyltransferase 7	Homo sapiens	76-84
11425803-8	2001	All six cysteines in the FucT VII sequence were shown to be disulfide-linked.	Disulfides	60-69	fucosyltransferase 7	Homo sapiens	25-33
11319555-2	2001	Here we used disulfide bond trapping to examine the proximity and mobility of cysteines substituted for aligned GABAA receptor alpha1 and beta1 M2 segment channel-lining residues in resting and activated receptors.	Disulfides	13-22	gamma-aminobutyric acid type A receptor subunit alpha1	Homo sapiens	112-146
11152681-9	2001	The results indicate that both covalent linkage by a disulfide bond and noncovalent association are involved in the formation of PRMT5 homo-oligomers.	Disulfides	53-62	protein arginine methyltransferase 5	Homo sapiens	129-134
11264172-6	2001	Homozygous expression of recombinant mutant full-length vWF resulted in additional dimers, probably through disulfide bonding at the amino-terminal multimerization site, whereas recombinant WT vWF correctly assembled into multimers.	Disulfides	108-117	von Willebrand factor	Homo sapiens	56-59
11264172-9	2001	We also confirmed previous studies that found that disulfide bonding at the vWF amino-terminal is independent of dimerization at the vWF carboxy-terminal.	Disulfides	51-60	von Willebrand factor	Homo sapiens	76-79
11254752-8	2001	Although individual disruption of disulfide bond 2 or 4 in apoB-28 and apoB-50 was previously shown to block lipoprotein assembly in vivo, these alterations had no impact on the ability of apoB-17 to bind to phospholipid vesicles in vitro or on its capacity to form recombinant lipoprotein particles.	Disulfides	34-43	apolipoprotein B	Rattus norvegicus	71-75
11118458-0	2001	The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: fractionation of conformational isomers of alpha-lactalbumin.	Disulfides	76-85	lactalbumin alpha	Homo sapiens	27-44
11118458-1	2001	The structure of denatured alpha-lactalbumin (alpha-LA) has been characterized using the method of disulfide scrambling.	Disulfides	99-108	lactalbumin alpha	Homo sapiens	27-44
11118458-1	2001	The structure of denatured alpha-lactalbumin (alpha-LA) has been characterized using the method of disulfide scrambling.	Disulfides	99-108	lactalbumin alpha	Homo sapiens	46-54
11118458-2	2001	Under denaturing conditions (urea, guanidine hydrochloride, guanidine thiocyanate, organic solvent or elevated temperature) and in the presence of thiol initiator, alpha-LA denatures by shuffling its four native disulfide bonds and converts to a mixture of fully oxidized scrambled structures.	Disulfides	212-221	lactalbumin alpha	Homo sapiens	164-172
11121408-7	2001	Interestingly, LAR expression significantly decreased the levels of disulfide-linked RET-MEN2A dimerization.	Disulfides	68-77	protein tyrosine phosphatase receptor type F	Homo sapiens	15-18
11258877-0	2001	Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro.	Disulfides	9-18	prolactin induced protein	Homo sapiens	38-63
11258877-1	2001	Although the structure of insulin has been well studied, the formation pathway of the three disulfide bridges during the refolding of insulin precursor is ambiguous.	Disulfides	92-101	insulin	Homo sapiens	134-141
11258877-2	2001	Here, we reported the in vitro disulfide-forming pathway of a recombinant porcine insulin precursor (PIP).	Disulfides	31-40	prolactin induced protein	Homo sapiens	74-99
11258877-2	2001	Here, we reported the in vitro disulfide-forming pathway of a recombinant porcine insulin precursor (PIP).	Disulfides	31-40	prolactin induced protein	Homo sapiens	101-104
11258877-7	2001	Based on the time-dependent formation and distribution of disulfide pairs in the trapped intermediates, two different forming pathways of disulfide bonds in the refolding process of PIP in vitro have been proposed.	Disulfides	58-67	prolactin induced protein	Homo sapiens	182-185
11258877-7	2001	Based on the time-dependent formation and distribution of disulfide pairs in the trapped intermediates, two different forming pathways of disulfide bonds in the refolding process of PIP in vitro have been proposed.	Disulfides	138-147	prolactin induced protein	Homo sapiens	182-185
11258877-8	2001	The first one involves the rapid formation of the intra-A disulfide bond, followed by the slower formation of one of the inter-AB disulfide bonds and then the pairing of the remaining cysteines to complete the refolding of PIP.	Disulfides	58-67	prolactin induced protein	Homo sapiens	223-226
11258877-8	2001	The first one involves the rapid formation of the intra-A disulfide bond, followed by the slower formation of one of the inter-AB disulfide bonds and then the pairing of the remaining cysteines to complete the refolding of PIP.	Disulfides	130-139	prolactin induced protein	Homo sapiens	223-226
11258877-10	2001	The nonnative two-disulfide intermediates may then slowly rearrange between CysA6, CysA7, CysA11, and CysB7, until the native disulfide bond A6-A11 or A7-B7 is formed to complete the refolding of PIP.	Disulfides	18-27	prolactin induced protein	Homo sapiens	196-199
11258980-1	2001	Thioredoxin reductase (TR), an NADPH-dependent flavoenzyme that catalyzes the reduction of many disulfide-containing substrates, plays an important role in the cellular response to oxidative stress.	Disulfides	96-105	peroxiredoxin 5	Rattus norvegicus	0-21
11258980-1	2001	Thioredoxin reductase (TR), an NADPH-dependent flavoenzyme that catalyzes the reduction of many disulfide-containing substrates, plays an important role in the cellular response to oxidative stress.	Disulfides	96-105	peroxiredoxin 5	Rattus norvegicus	23-25
11254752-8	2001	Although individual disruption of disulfide bond 2 or 4 in apoB-28 and apoB-50 was previously shown to block lipoprotein assembly in vivo, these alterations had no impact on the ability of apoB-17 to bind to phospholipid vesicles in vitro or on its capacity to form recombinant lipoprotein particles.	Disulfides	34-43	apolipoprotein B	Rattus norvegicus	59-63
11254752-8	2001	Although individual disruption of disulfide bond 2 or 4 in apoB-28 and apoB-50 was previously shown to block lipoprotein assembly in vivo, these alterations had no impact on the ability of apoB-17 to bind to phospholipid vesicles in vitro or on its capacity to form recombinant lipoprotein particles.	Disulfides	34-43	apolipoprotein B	Rattus norvegicus	71-75
11321671-0	2001	The electrochemically induced conformational transition of disulfides in bovine serum albumin studied by thin layer circular dichroism spectroelectrochemistry.	Disulfides	59-69	albumin	Homo sapiens	80-93
11321671-1	2001	The conformational transition of disulfides in bovine serum albumin (BSA) induced by electrochemical redox reaction of disulfides were monitored by in-situ circular dichroism (CD) spectroelectrochemistry, with a long optical path thin layer cell and analyzed by a singular value decomposition least square (SVDLS) method.	Disulfides	33-43	albumin	Homo sapiens	54-67
11321671-1	2001	The conformational transition of disulfides in bovine serum albumin (BSA) induced by electrochemical redox reaction of disulfides were monitored by in-situ circular dichroism (CD) spectroelectrochemistry, with a long optical path thin layer cell and analyzed by a singular value decomposition least square (SVDLS) method.	Disulfides	119-129	albumin	Homo sapiens	54-67
11237737-1	2001	Reduction of disulfide bonds in human melanocortin 1 receptor (hMC1R) with increasing concentrations of DTT (dithiothreitol) resulted in a decrease in the binding of [125I]-ACTH (adrenocorticotropic hormone, L-isomer) in an uniphasic manner and a decrease in [125I]-NDP-MSH ([Nle(4),D-Phe(7)]-alpha-melanocyte stimulating hormone; D-isomer) binding in a biphasic manner.	Disulfides	13-22	proopiomelanocortin	Homo sapiens	173-177
11237737-1	2001	Reduction of disulfide bonds in human melanocortin 1 receptor (hMC1R) with increasing concentrations of DTT (dithiothreitol) resulted in a decrease in the binding of [125I]-ACTH (adrenocorticotropic hormone, L-isomer) in an uniphasic manner and a decrease in [125I]-NDP-MSH ([Nle(4),D-Phe(7)]-alpha-melanocyte stimulating hormone; D-isomer) binding in a biphasic manner.	Disulfides	13-22	proopiomelanocortin	Homo sapiens	270-273
11310611-1	2001	Cyclic 12-, 13- and 14-membered ring angiotensin II analogues related to disulfides but encompassing methylene-dithioether bridges have been prepared.	Disulfides	73-83	angiotensinogen	Rattus norvegicus	37-51
11222545-6	2001	RS1 migrated as a single 24-kDa polypeptide under disulfide-reducing conditions and a larger complex (&gt;95 kDa) under nonreducing conditions in the membrane fraction of retinal tissue homogenates and transfected COS-1 cells.	Disulfides	50-59	retinoschisis (X-linked, juvenile) 1 (human)	Mus musculus	0-3
11222545-9	2001	CONCLUSIONS: RS1 is expressed and assembled in photoreceptors of the outer retina and bipolar cells of the inner retina as a disulfide-linked oligomeric protein complex.	Disulfides	125-134	retinoschisis (X-linked, juvenile) 1 (human)	Mus musculus	13-16
11254752-6	2001	Although normally a soluble peptide, mild reduction of apoB-17 caused its precipitation, suggesting that hydrophobic, solvent-inaccessible domains within the alpha(1) domain of apoB are stabilized by intramolecular disulfide bonds.	Disulfides	215-224	apolipoprotein B	Rattus norvegicus	55-59
11254752-6	2001	Although normally a soluble peptide, mild reduction of apoB-17 caused its precipitation, suggesting that hydrophobic, solvent-inaccessible domains within the alpha(1) domain of apoB are stabilized by intramolecular disulfide bonds.	Disulfides	215-224	apolipoprotein B	Rattus norvegicus	177-181
11226236-9	2001	We combine these results with those of earlier studies to suggest a general three-stage model of oxidative folding of RNase A and other single-domain proteins with multiple disulfide bonds.	Disulfides	173-182	ribonuclease pancreatic	Bos taurus	118-125
11642043-1	2001	Horseradish peroxidase is immobilized by a periodate method on the gold surfaces previously modified with 16-mercapto-hexadecanoic acid or with hydrogen disulfide and soybean trypsin inhibitor.	Disulfides	144-162	peroxidase	Glycine max	12-22
11162621-0	2001	Requirement of intact disulfide bonds in orexin-A-induced stimulation of gastric acid secretion that is mediated by OX1 receptor activation.	Disulfides	22-31	hypocretin neuropeptide precursor	Rattus norvegicus	41-49
11178913-2	2001	Here, we test experimentally the robustness of the src SH3-domain folding transition state to changes in topology by covalently constraining regions of the protein with disulfide crosslinks and then performing kinetic analysis on point mutations in the context of these modified proteins.	Disulfides	169-178	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	51-54
11060285-4	2001	In addition to the four cysteines that characterize most chemokines, MPIF-1 has two additional cysteines that form a disulfide bond.	Disulfides	117-126	C-C motif chemokine ligand 23	Homo sapiens	69-75
11162621-9	2001	Agonistic activity for OX1R of the three orexin-A analogues with modification of one or both disulfide bonds was significantly reduced as compared with that of orexin-A.	Disulfides	93-102	hypocretin neuropeptide precursor	Rattus norvegicus	41-49
11162621-12	2001	These results suggested that the orexin-A-induced acid stimulation requires OX1R activation and that disulfide bonds in orexin-A may have a key role in the receptor activation.	Disulfides	101-110	hypocretin neuropeptide precursor	Rattus norvegicus	33-41
11162621-12	2001	These results suggested that the orexin-A-induced acid stimulation requires OX1R activation and that disulfide bonds in orexin-A may have a key role in the receptor activation.	Disulfides	101-110	hypocretin neuropeptide precursor	Rattus norvegicus	120-128
11162621-1	2001	Orexin-A is a neuropeptide consisting of 33 amino acids with two intrachain disulfide bonds, namely Cys6-Cys12 and Cys7-Cys14, and is a potent stimulator of food consumption and gastric acid secretion.	Disulfides	76-85	hypocretin neuropeptide precursor	Rattus norvegicus	0-8
11162621-3	2001	The objective of the present study was to characterize the receptor-mediated mechanism of orexin-A-induced stimulation of gastric acid secretion using orexin-A-related peptides with modification of disulfide bonds.	Disulfides	198-207	hypocretin neuropeptide precursor	Rattus norvegicus	90-98
11162621-3	2001	The objective of the present study was to characterize the receptor-mediated mechanism of orexin-A-induced stimulation of gastric acid secretion using orexin-A-related peptides with modification of disulfide bonds.	Disulfides	198-207	hypocretin neuropeptide precursor	Rattus norvegicus	151-159
11460466-3	2001	Fibrinogen is comprised of two sets of three polypeptide chains termed A alpha, B beta, and gamma, that are joined by disulfide bridging within the N-terminal E domain.	Disulfides	118-127	fibrinogen beta chain	Homo sapiens	0-10
11251288-12	2001	CONCLUSIONS: Erythropoietin expressed in E. coli bearing specific Asn--&gt;Cys mutations at natural glycosylation sites can be glycosylated using beta-N-glycosyl iodoacetamides even in the presence of two disulfide bonds.	Disulfides	205-214	erythropoietin	Homo sapiens	13-27
11157741-3	2001	In contrast to known structures with the SH3 domain fold, MIA is a single-domain protein, and contains an additional antiparallel beta-sheet and two disulfide bonds.	Disulfides	149-158	MIA SH3 domain containing	Homo sapiens	58-61
11342210-1	2001	The fibrinogen molecule consists of two sets of Aalpha, Bbeta, and gamma chains assembled into a bilateral disulfide linked (Aalpha, Bbeta, gamma)2 structure.	Disulfides	107-116	fibrinogen beta chain	Homo sapiens	4-14
11024048-4	2001	The lack of this domain concomitantly abolished the disulfide-mediated oligomerization of GnT-V, which appears to confer the Golgi retention.	Disulfides	52-61	alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase	Homo sapiens	90-95
11460483-2	2001	The mechanism by which Lp(a) may favour this pathological state may be related to its particular structure, a plasminogen-like glycoprotein, apo(a), that is disulfide linked to the apo B100 of an atherogenic LDL-like particle.	Disulfides	157-166	apolipoprotein B	Homo sapiens	181-189
11158675-1	2001	The disulfide reducing enzymes glutathione reductase and thioredoxin reductase are highly conserved among bacteria, fungi, worms, and mammals.	Disulfides	4-13	Thioredoxin reductase-1	Drosophila melanogaster	31-52
11158675-1	2001	The disulfide reducing enzymes glutathione reductase and thioredoxin reductase are highly conserved among bacteria, fungi, worms, and mammals.	Disulfides	4-13	Thioredoxin reductase-1	Drosophila melanogaster	57-78
11141061-7	2001	In conclusion, r-RNase A under folding conditions (the R(N) state) is poised for the final folding step(s) with a native-like trace of the chain fold but a large separation between the two subdomains which is then decreased upon introduction of three of the four native disulfide cross-links.	Disulfides	270-279	ribonuclease pancreatic	Bos taurus	17-24
11460506-8	2001	Studies with recombinant systems, using deletion and substitution mutants, indicate that initial chain assembly depends on hydrophobic interactions present in the C-terminal half of the coil-coil domains and that inter- and intra-disulfide bonds that stabilize fibrinogen are needed to complete chain assembly.	Disulfides	230-239	fibrinogen beta chain	Homo sapiens	261-271
11460470-4	2001	The neo-Cys residues were found to be disulfide-bridged to either an isolated Cys amino acid or to the corresponding Cys residue of another abnormal fibrinogen molecule, forming dimers.	Disulfides	38-47	fibrinogen beta chain	Homo sapiens	149-159
11460526-1	2001	Fibrinogen, a 340-kDa plasma protein, is composed of two identical molecular halves each consisting of three non-identical A alpha-, B beta- and gamma-chain subunits held together by multiple disulfide bonds.	Disulfides	192-201	fibrinogen beta chain	Homo sapiens	0-10
11133656-5	2001	Using affinity-purified anti-peptide antisera, we determined that the molecular weight of sp56 in cauda epididymal sperm approximated that of guinea pig AM67 ( approximately 67 000 M:(r)) and that sp56 was present in a high molecular weight, disulfide-linked complex.	Disulfides	242-251	zona pellucida 3 receptor	Mus musculus	90-94
11133656-5	2001	Using affinity-purified anti-peptide antisera, we determined that the molecular weight of sp56 in cauda epididymal sperm approximated that of guinea pig AM67 ( approximately 67 000 M:(r)) and that sp56 was present in a high molecular weight, disulfide-linked complex.	Disulfides	242-251	zona pellucida 3 receptor	Mus musculus	197-201
11134959-6	2001	L. japonicus FABP-2 contains three cysteine residues, and a disulfide bond is identified between Cys-81 and Cys-92.	Disulfides	60-69	fatty acid binding protein 2	Homo sapiens	13-19
11777392-1	2001	Albumin polymers, having an average diameter of 1020 +/- 250 nm, were prepared by the disulfide polymerization of recombinant human serum albumin (rHSA) by controlling of the pH and temperature.	Disulfides	86-95	albumin	Homo sapiens	132-145
11168369-0	2001	A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.	Disulfides	142-151	albumin	Homo sapiens	108-121
11134973-6	2001	Heterogeneous proteins become cross-linked following the formation of heteromolecular interchain disulfide bonds during thermal unfolding of a mixture of of ribonuclease A and lysozyme.	Disulfides	97-106	lysozyme	Homo sapiens	176-184
11168891-4	2001	Two disulfide isomers were produced, one with an insulin-like disulfide bonding pattern and the other with a reversed chain orientation.	Disulfides	4-13	insulin	Homo sapiens	49-56
11148131-3	2001	Because these truncations involved removal of a conserved cysteine residue (Cys(186)), we hypothesized that intralumenal disulfide-mediated folding of the C terminus of SP-C(21) is required for intracellular trafficking.	Disulfides	121-130	surfactant protein C	Rattus norvegicus	169-173
11168891-4	2001	Two disulfide isomers were produced, one with an insulin-like disulfide bonding pattern and the other with a reversed chain orientation.	Disulfides	62-71	insulin	Homo sapiens	49-56
21340935-5	2001	Apo(a) is covalently linked via a disulfide bridge to apolipoprotein B-100, the major protein constituent of LDL.	Disulfides	34-43	apolipoprotein B	Homo sapiens	54-74
11119600-4	2001	The immunoprecipitated complex contained disulfide-bonded dimers of A33R protein that were noncovalently linked to A36R protein.	Disulfides	41-50	IEV transmembrane phosphoprotein	Vaccinia virus	115-119
12040418-4	2001	The peptide mapping of PIP scrambles demonstrated that PIP had shuffled its native disulfides under the condition we used.	Disulfides	83-93	prolactin induced protein	Homo sapiens	55-58
11161827-8	2001	This mutation helps to define two homologous regions of the AVP-NPII precursor bounded by disulfide bridges between C13 and C27 and between C61 and C73 that have structural homology and contain the majority of amino acid substitutions associated with ADNDI.	Disulfides	90-99	arginine vasopressin	Homo sapiens	60-68
11266594-3	2001	To explore the nature of side-chain--side-chain interactions in the alpha-lactalbumin (alpha-LA) molten globule, we determined the effective concentration for formation of the 28--111 disulfide bond in 14 double-mutant proteins, each containing two hydrophobic core residues replaced by alanine.	Disulfides	184-193	lactalbumin alpha	Homo sapiens	87-95
12040418-1	2001	Recombinant single-chain insulin (PIP) contains three disulfide bonds.	Disulfides	54-63	insulin	Homo sapiens	25-32
12040418-1	2001	Recombinant single-chain insulin (PIP) contains three disulfide bonds.	Disulfides	54-63	prolactin induced protein	Homo sapiens	34-37
12040418-2	2001	In the presence of denaturants and thiol reagents, the native structure of PIP was disturbed and its native disulfides were shuffled to form a mixture of scrambled isomers which have different degrees of unfolding.	Disulfides	108-118	prolactin induced protein	Homo sapiens	75-78
12040418-6	2001	These results show that PIP has only one thermodynamically stable disulfide linkage, and the non-natural disulfide isomers could refold in vitro efficiently to from native PIP.	Disulfides	66-75	prolactin induced protein	Homo sapiens	24-27
12040418-6	2001	These results show that PIP has only one thermodynamically stable disulfide linkage, and the non-natural disulfide isomers could refold in vitro efficiently to from native PIP.	Disulfides	105-114	prolactin induced protein	Homo sapiens	172-175
11150528-1	2000	A predominant conformational isomer of non-native alpha-lactalbumin (alpha-LA) has been purified by thermal denaturation of the native alpha-LA using the technique of disulfide scrambling.	Disulfides	167-176	lactalbumin alpha	Homo sapiens	50-67
11016937-1	2000	Thrombospondin 1 (TSP1) is a homotrimeric glycoprotein composed of 150-kDa subunits connected by disulfide bridges.	Disulfides	97-106	thrombospondin 1	Homo sapiens	0-16
11016937-1	2000	Thrombospondin 1 (TSP1) is a homotrimeric glycoprotein composed of 150-kDa subunits connected by disulfide bridges.	Disulfides	97-106	thrombospondin 1	Homo sapiens	18-22
11016937-7	2000	NoC is a disulfide bonded trimer and cleaves readily at a site of preferential proteolysis to yield monomeric N and trimeric oC.	Disulfides	9-18	nocturnin	Homo sapiens	0-3
11149825-0	2000	Nucleophilic trifluoromethylation of carbonyl compounds and disulfides with trifluoromethane and silicon-containing bases Provided that DMF (or another N,N-dialkylformamide) is present in the reaction medium, at least in a catalytic amount, fluoroform trifluoromethylates efficiently carbonyl compounds, even enolizable ones, when opposed to (TMS)(2)N(-) M(+), generated in situ from N(TMS)(3) and M(+) F(-) or RO(-) Na(+).	Disulfides	60-70	PYD and CARD domain containing	Homo sapiens	343-346
11149825-0	2000	Nucleophilic trifluoromethylation of carbonyl compounds and disulfides with trifluoromethane and silicon-containing bases Provided that DMF (or another N,N-dialkylformamide) is present in the reaction medium, at least in a catalytic amount, fluoroform trifluoromethylates efficiently carbonyl compounds, even enolizable ones, when opposed to (TMS)(2)N(-) M(+), generated in situ from N(TMS)(3) and M(+) F(-) or RO(-) Na(+).	Disulfides	60-70	PYD and CARD domain containing	Homo sapiens	386-389
11150528-1	2000	A predominant conformational isomer of non-native alpha-lactalbumin (alpha-LA) has been purified by thermal denaturation of the native alpha-LA using the technique of disulfide scrambling.	Disulfides	167-176	lactalbumin alpha	Homo sapiens	69-77
11112528-14	2000	Comparison of DKP[A6-A11](Ser) and DKP[A6-A11](Ala) supports the hypothesis that the native A1-A8 alpha-helix functions as a preformed recognition element tethered by insulin"s intrachain disulfide bridge.	Disulfides	188-197	insulin	Homo sapiens	167-174
10986287-2	2000	The heavy and light chains are linked by a disulfide bond, and P25 associates with disulfide-linked heavy and light chains by noncovalent interactions.	Disulfides	83-92	fibrohexamerin	Bombyx mori	63-66
10970898-4	2000	We report here that a single mutation in MTX, in either position 15 or 33, resulted in a shift from the MTX toward the Pi1/HsTx1 disulfide bridge pattern.	Disulfides	129-138	serpin family A member 1	Homo sapiens	119-122
11112528-0	2000	Hierarchical protein "un-design": insulin"s intrachain disulfide bridge tethers a recognition alpha-helix.	Disulfides	55-64	insulin	Homo sapiens	34-41
11106485-7	2000	The magnitude of the activation barrier between LA (ground state) and A (end state) forms of TlL (10.6 kcal/mol) is comparable to the enthalpic barriers typical for ring flips and disulfide isomerizations at ambient temperatures.	Disulfides	180-189	tolloid like 1	Homo sapiens	93-96
11120833-7	2000	These disulfide-stabilized bispecific Fab-scFv ("bibody") and trispecific Fab-(scFv)(2) ("tribody") heterodimers represent up to 90% of all secreted Ab fragments in the mammalian expression system and possess fully functional binding moieties.	Disulfides	6-15	immunglobulin heavy chain variable region	Homo sapiens	42-46
11120833-7	2000	These disulfide-stabilized bispecific Fab-scFv ("bibody") and trispecific Fab-(scFv)(2) ("tribody") heterodimers represent up to 90% of all secreted Ab fragments in the mammalian expression system and possess fully functional binding moieties.	Disulfides	6-15	immunglobulin heavy chain variable region	Homo sapiens	79-83
11106487-4	2000	Control experiments demonstrated that translocation of aFGF by the diphtheria toxin pathway, which requires extensive unfolding of the protein, was prevented by disulfide bond formation, indicating that the introduced disulfide bonds interfered with the unfolding of the growth factor.	Disulfides	161-170	fibroblast growth factor 1	Mus musculus	55-59
11106487-4	2000	Control experiments demonstrated that translocation of aFGF by the diphtheria toxin pathway, which requires extensive unfolding of the protein, was prevented by disulfide bond formation, indicating that the introduced disulfide bonds interfered with the unfolding of the growth factor.	Disulfides	218-227	fibroblast growth factor 1	Mus musculus	55-59
11106487-5	2000	On the other hand, when the growth factor as such was added to cells expressing FGF receptors, the disulfide-bonded mutants were translocated to the cytosol and the nucleus equally well as wild-type aFGF.	Disulfides	99-108	fibroblast growth factor 1	Mus musculus	80-83
11087419-2	2000	Both mixed disulfides react with the skeletal myosin motor domain (S-1) as actin site-directed agents and label exclusively and stoichiometrically Cys 540 in the hydrophobic strong actin binding helix-loop-helix motif, causing only a 1.9-2.4-fold decrease in the V(max) for acto-S-1 ATPase.	Disulfides	11-21	proteasome 26S subunit, non-ATPase 1	Homo sapiens	67-70
11090188-9	2000	Thus, gM and the UL73 gene product, which represents the gN homolog of herpesviruses, form a disulfide-linked complex in HCMV virions.	Disulfides	93-102	envelope glycoprotein N	Human betaherpesvirus 5	17-21
10964928-7	2000	In addition, we show that pro-LPC is prone to aggregation and forms large complexes linked via interchain disulfide bonds.	Disulfides	106-115	proprotein convertase subtilisin/kexin type 7	Homo sapiens	30-33
11087419-2	2000	Both mixed disulfides react with the skeletal myosin motor domain (S-1) as actin site-directed agents and label exclusively and stoichiometrically Cys 540 in the hydrophobic strong actin binding helix-loop-helix motif, causing only a 1.9-2.4-fold decrease in the V(max) for acto-S-1 ATPase.	Disulfides	11-21	proteasome 26S subunit, non-ATPase 1	Homo sapiens	279-282
10922370-9	2000	The function of Pcd1p may be to remove potentially toxic oxidized CoA disulfide from peroxisomes in order to maintain the capacity for beta-oxidation of fatty acids.	Disulfides	70-79	8-oxo-dGTP diphosphatase	Saccharomyces cerevisiae S288C	16-21
11090354-1	2000	The endoplasmic reticulum (ER) supports disulfide bond formation by a poorly understood mechanism requiring protein disulfide isomerase (PDI) and ERO1.	Disulfides	40-49	ER oxidoreductin	Saccharomyces cerevisiae S288C	146-150
11090354-4	2000	Disulfide formation proceeded by direct delivery of oxidizing equivalents from Ero1p to folding substrates via PDI.	Disulfides	0-9	ER oxidoreductin	Saccharomyces cerevisiae S288C	79-84
11093204-0	2000	Diels-Alder Type Addition of 1,3-Dienes to a Disulfide Bridging Ligand in Diruthenium Complexes Support of this work through a CREST grant of the Japan Science and Technology Corporation is gratefully acknowledged.	Disulfides	45-54	SS18L1 subunit of BAF chromatin remodeling complex	Homo sapiens	127-132
11071851-1	2000	Using the patch-clamp technique we determined that Pandinus imperator toxin Pi1, a recently described peptide toxin having four disulfide bridges instead of the usual three in scorpion toxins, blocked Kv1.3 channels of human T lymphocytes from the extracellular side with a 1:1 stoichiometry.	Disulfides	128-137	serpin family A member 1	Homo sapiens	76-79
11071851-5	2000	The fourth disulfide bridge in Pi1 had no influence on the channel binding ability of the toxin; the less effective block was due to differences in amino acid side chain properties at positions 11 and 35.	Disulfides	11-20	serpin family A member 1	Homo sapiens	31-34
11025545-3	2000	This activation is the result of the reduction of two disulfide bridges by thioredoxin m, that are located at the N- and C-terminii of the NADP malate dehydrogenase.	Disulfides	54-63	uncharacterized protein	Chlamydomonas reinhardtii	139-164
10954708-1	2000	In mammalian brain, acetylcholinesterase (AChE) exists mostly as a tetramer of 70-kDa catalytic subunits that are linked through disulfide bonds to a hydrophobic subunit P of approximately 20 kDa.	Disulfides	129-138	acetylcholinesterase (Cartwright blood group)	Homo sapiens	20-40
10954708-1	2000	In mammalian brain, acetylcholinesterase (AChE) exists mostly as a tetramer of 70-kDa catalytic subunits that are linked through disulfide bonds to a hydrophobic subunit P of approximately 20 kDa.	Disulfides	129-138	acetylcholinesterase (Cartwright blood group)	Homo sapiens	42-46
11068047-0	2000	Reversible inactivation of AT(2) angiotensin II receptor from cysteine-disulfide bond exchange.	Disulfides	71-80	angiotensinogen	Homo sapiens	33-47
11046093-3	2000	Human insulin was conjugated at a 1:1 molar ratio to iron-loaded human Tf by a disulfide linkage.	Disulfides	79-88	insulin	Homo sapiens	6-13
11046093-5	2000	The release of free insulin involved a disulfide reduction reaction that was inhibited by the pretreatment of the liver slice with a sulfhydryl-reactive reagent N-ethylmaleimide.	Disulfides	39-48	insulin	Homo sapiens	20-27
10924510-8	2000	BACE exhibited intramolecular disulfide bonding but did not form oligomeric structures by standard SDS-polyacrylamide gel electrophoresis analysis and sedimented as a monomer in sucrose velocity gradients.	Disulfides	30-39	beta-secretase 1	Homo sapiens	0-4
11035080-4	2000	The positions of cysteine residues that are important for disulfide bonds were conserved with respect to those in mammalian TNF-alpha.	Disulfides	58-67	tumor necrosis factor	Homo sapiens	124-133
11083061-0	2000	Three-dimensional solution structure of a disulfide bond isomer of the human insulin-like growth factor-I.	Disulfides	42-51	insulin like growth factor 1	Homo sapiens	77-105
11229362-3	2000	To investigate redox homeostasis further in AD, we analyzed protein disulfide isomerase (PDI), a multifunctional enzyme, which catalyzes the disruption and formation of disulfide bonds.	Disulfides	68-77	protein disulfide isomerase family A member 2	Homo sapiens	89-92
11229362-4	2000	PDI plays a pivotal role in both secreted and cell-surface-associated protein disulfide rearrangement.	Disulfides	78-87	protein disulfide isomerase family A member 2	Homo sapiens	0-3
11052759-6	2000	PS of control films was highest (P &lt; 0.05) in 2-mercaptoethanol, confirming the importance of disulfide bonds in SPI film formation.	Disulfides	97-106	chromogranin A	Homo sapiens	116-119
11013218-5	2000	The data are consistent with a model in which oxidation of Yap1 leads to disulfide bond formation with the resulting change of conformation masking recognition of the nuclear export signal by Crm1/Xpo1, thereby promoting nuclear accumulation of the protein.	Disulfides	73-82	DNA-binding transcription factor YAP1	Saccharomyces cerevisiae S288C	59-63
11013218-5	2000	The data are consistent with a model in which oxidation of Yap1 leads to disulfide bond formation with the resulting change of conformation masking recognition of the nuclear export signal by Crm1/Xpo1, thereby promoting nuclear accumulation of the protein.	Disulfides	73-82	exportin CRM1	Saccharomyces cerevisiae S288C	192-196
11013218-5	2000	The data are consistent with a model in which oxidation of Yap1 leads to disulfide bond formation with the resulting change of conformation masking recognition of the nuclear export signal by Crm1/Xpo1, thereby promoting nuclear accumulation of the protein.	Disulfides	73-82	exportin CRM1	Saccharomyces cerevisiae S288C	197-201
11083061-1	2000	The solution structure of a disulfide bond isomer of human insulin-like growth factor-I (IGF-I) was determined using homonuclear NMR methods.	Disulfides	28-37	insulin like growth factor 1	Homo sapiens	59-87
11083061-1	2000	The solution structure of a disulfide bond isomer of human insulin-like growth factor-I (IGF-I) was determined using homonuclear NMR methods.	Disulfides	28-37	insulin like growth factor 1	Homo sapiens	89-94
11083061-6	2000	A similar relationship has been described between the structure of native insulin and a homologous disulfide isomer, suggesting that these alternative folds represent general features of insulin-like sequences.	Disulfides	99-108	insulin	Homo sapiens	74-81
11083061-6	2000	A similar relationship has been described between the structure of native insulin and a homologous disulfide isomer, suggesting that these alternative folds represent general features of insulin-like sequences.	Disulfides	99-108	insulin	Homo sapiens	187-194
11083061-9	2000	Comparison of the biological activities of native and the disulfide bond isomer of human IGF-I highlight the importance of Tyr24, Phe25, Phe49-Cys52 and Phe16 in binding to the IGF-I receptor or specific IGFBPs.	Disulfides	58-67	insulin like growth factor 1	Homo sapiens	89-94
10993229-0	2000	Direct identification of a novel disulfide bond linkage system of new isolated isomer (isomer V) in recombinantly produced h-IGF-I.	Disulfides	33-42	insulin like growth factor 1	Homo sapiens	125-130
11106176-8	2000	The resulting purified disulfide-linked homodimer was demonstrated to bind to VEGF-R1 and to compete with VEGF-A for binding to this receptor.	Disulfides	23-32	fms related receptor tyrosine kinase 1	Homo sapiens	78-85
11106176-8	2000	The resulting purified disulfide-linked homodimer was demonstrated to bind to VEGF-R1 and to compete with VEGF-A for binding to this receptor.	Disulfides	23-32	vascular endothelial growth factor A	Homo sapiens	106-112
10837476-8	2000	The mutant apoB100 bound to apo(a) and formed bona fide disulfide-linked Lp(a), but Lp(a) assembly was less efficient than with wild-type human apoB100.	Disulfides	56-65	apolipoprotein B	Homo sapiens	11-18
10993229-1	2000	Insulin-like growth factor I (IGF-I or somatomedin C) is a serum polypeptide with three intramolecular disulfide bonds.	Disulfides	103-112	insulin like growth factor 1	Homo sapiens	0-28
10993229-1	2000	Insulin-like growth factor I (IGF-I or somatomedin C) is a serum polypeptide with three intramolecular disulfide bonds.	Disulfides	103-112	insulin like growth factor 1	Homo sapiens	30-35
10993229-1	2000	Insulin-like growth factor I (IGF-I or somatomedin C) is a serum polypeptide with three intramolecular disulfide bonds.	Disulfides	103-112	insulin like growth factor 1	Homo sapiens	39-52
10854422-7	2000	In addition, ASP-1 contains conserved, potential disulfide bond-forming cysteine residues and N-glycosylation sites.	Disulfides	49-58	Aspartic protease 1	Caenorhabditis elegans	13-18
10982384-0	2000	Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum.	Disulfides	93-102	ER oxidoreductin	Saccharomyces cerevisiae S288C	76-81
10982384-1	2000	In the major pathway for protein disulfide-bond formation in the endoplasmic reticulum (ER), oxidizing equivalents flow from the conserved ER-membrane protein Ero1p to secretory proteins via protein disulfide isomerase (PDI).	Disulfides	33-42	ER oxidoreductin	Saccharomyces cerevisiae S288C	159-164
10982384-2	2000	Herein, a mutational analysis of the yeast ERO1 gene identifies two pairs of conserved cysteines likely to form redox-active disulfide bonds in Ero1p.	Disulfides	125-134	ER oxidoreductin	Saccharomyces cerevisiae S288C	43-47
10982384-2	2000	Herein, a mutational analysis of the yeast ERO1 gene identifies two pairs of conserved cysteines likely to form redox-active disulfide bonds in Ero1p.	Disulfides	125-134	ER oxidoreductin	Saccharomyces cerevisiae S288C	144-149
10982384-4	2000	Substitution of Cys100 with alanine impedes the capture of Ero1p-Pdi1p mixed-disulfide complexes from yeast, and also blocks oxidation of Pdi1p in vivo.	Disulfides	77-86	ER oxidoreductin	Saccharomyces cerevisiae S288C	59-64
10982384-5	2000	Cys352 and Cys355 are required to maintain the fully oxidized redox state of Ero1p, and also play an auxiliary role in thiol-disulfide exchange with Pdi1p.	Disulfides	125-134	ER oxidoreductin	Saccharomyces cerevisiae S288C	77-82
10982384-6	2000	These results suggest a model for the function of Ero1p wherein Cys100 and Cys105 form a redox-active disulfide bond that engages directly in thiol-disulfide exchange with ER oxidoreductases.	Disulfides	102-111	ER oxidoreductin	Saccharomyces cerevisiae S288C	50-55
10982384-6	2000	These results suggest a model for the function of Ero1p wherein Cys100 and Cys105 form a redox-active disulfide bond that engages directly in thiol-disulfide exchange with ER oxidoreductases.	Disulfides	148-157	ER oxidoreductin	Saccharomyces cerevisiae S288C	50-55
11019979-9	2000	These results suggested that the interchain disulfide bonds that link the vWF homodimers near the N-termini were being reduced by a vWF reductase secreted by endothelial cells.	Disulfides	44-53	von Willebrand factor	Homo sapiens	74-77
11019979-9	2000	These results suggested that the interchain disulfide bonds that link the vWF homodimers near the N-termini were being reduced by a vWF reductase secreted by endothelial cells.	Disulfides	44-53	von Willebrand factor	Homo sapiens	132-135
10964659-8	2000	We conclude that the reducing agent as well as light break a disulfide bond resulting in activation of the rhodopsin and induction of carotenogenesis.	Disulfides	61-70	rhodopsin	Homo sapiens	107-116
10852914-2	2000	We recently identified a gamma-interferon-inducible lysosomal thiol reductase (GILT), constitutively expressed in antigen-presenting cells, that catalyzes disulfide bond reduction both in vitro and in vivo and is optimally active at acidic pH.	Disulfides	155-164	IFI30 lysosomal thiol reductase	Homo sapiens	25-77
10852914-2	2000	We recently identified a gamma-interferon-inducible lysosomal thiol reductase (GILT), constitutively expressed in antigen-presenting cells, that catalyzes disulfide bond reduction both in vitro and in vivo and is optimally active at acidic pH.	Disulfides	155-164	IFI30 lysosomal thiol reductase	Homo sapiens	79-83
10852914-5	2000	GILT may be important in disulfide bond reduction of proteins delivered to MIICs and consequently in antigen processing.	Disulfides	25-34	IFI30 lysosomal thiol reductase	Homo sapiens	0-4
10852914-6	2000	In this report we show that, like its mature form, precursor GILT reduces disulfide bonds with an acidic pH optimum, suggesting that it may also be involved in disulfide bond reduction in the endocytic pathway.	Disulfides	74-83	IFI30 lysosomal thiol reductase	Homo sapiens	61-65
10852914-6	2000	In this report we show that, like its mature form, precursor GILT reduces disulfide bonds with an acidic pH optimum, suggesting that it may also be involved in disulfide bond reduction in the endocytic pathway.	Disulfides	160-169	IFI30 lysosomal thiol reductase	Homo sapiens	61-65
10831592-0	2000	Localization of disulfide bonds in the cystine knot domain of human von Willebrand factor.	Disulfides	16-25	von Willebrand factor	Homo sapiens	68-89
11035262-2	2000	Previous studies showed that the loss of cyt c triggered superoxide production by mitochondria and contributed to the oxidation of cellular thiol-disulfide redox state.	Disulfides	146-155	cytochrome c, somatic	Homo sapiens	41-46
10959975-8	2000	In the case of CP1, a disulfide-bonded homodimer is detected and the disulfide bonding pattern elucidated using MALDI-MS coupled with on-plate enzymatic digestion.	Disulfides	22-31	cerebral peptide 1	Aplysia californica	15-18
10959975-8	2000	In the case of CP1, a disulfide-bonded homodimer is detected and the disulfide bonding pattern elucidated using MALDI-MS coupled with on-plate enzymatic digestion.	Disulfides	69-78	cerebral peptide 1	Aplysia californica	15-18
10913300-0	2000	The N-terminal fragment of human parathyroid hormone receptor 1 constitutes a hormone binding domain and reveals a distinct disulfide pattern.	Disulfides	124-133	parathyroid hormone 1 receptor	Homo sapiens	33-63
10989181-3	2000	Non-reducing immunoblots showed that rE2 is a disulfide bond-linked homodimer with at least 10-fold higher avidity for conformation-dependent anti-BVDV-E2 antibodies than its reduced monomeric counterpart.	Disulfides	46-55	dihydrolipoamide S-succinyltransferase	Rattus norvegicus	37-40
10989181-3	2000	Non-reducing immunoblots showed that rE2 is a disulfide bond-linked homodimer with at least 10-fold higher avidity for conformation-dependent anti-BVDV-E2 antibodies than its reduced monomeric counterpart.	Disulfides	46-55	dihydrolipoamide S-succinyltransferase	Rattus norvegicus	38-40
10899108-1	2000	Human interleukin-12 (IL-12, p70) is an early pro-inflammatory cytokine, comprising two disulfide-linked subunits, p35 and p40.	Disulfides	88-97	ubiquitin associated and SH3 domain containing B	Homo sapiens	29-32
10913246-6	2000	These findings indicate that the loss of ER DNA-binding function in extracts from some primary breast tumors and in ER or ER-DBD exposed to thiol-reacting oxidants results from this asymmetric zinc finger susceptibility to disulfide formation that prevents dimerization.	Disulfides	223-232	estrogen receptor 1	Homo sapiens	41-43
10913246-6	2000	These findings indicate that the loss of ER DNA-binding function in extracts from some primary breast tumors and in ER or ER-DBD exposed to thiol-reacting oxidants results from this asymmetric zinc finger susceptibility to disulfide formation that prevents dimerization.	Disulfides	223-232	estrogen receptor 1	Homo sapiens	116-118
10913246-6	2000	These findings indicate that the loss of ER DNA-binding function in extracts from some primary breast tumors and in ER or ER-DBD exposed to thiol-reacting oxidants results from this asymmetric zinc finger susceptibility to disulfide formation that prevents dimerization.	Disulfides	223-232	estrogen receptor 1	Homo sapiens	116-118
10926679-1	2000	Tris(2-carboxyethyl)phosphine (TCEP) reduces (cleaves) disulfide bonds of the renal proximal tubule type IIa Na/Pi- cotransporter (rat NaPi IIa) and thereby inhibits its function.	Disulfides	55-64	solute carrier family 34 member 1	Rattus norvegicus	135-143
10887149-6	2000	Early truncation of the A alpha chain appears to result in defective assembly or secretion of fibrinogen, probably due to the removal of the C-terminal disulfide ring residues that are critically required for the formation of a stable 3-chained half molecule.	Disulfides	152-161	fibrinogen beta chain	Homo sapiens	94-104
10779511-14	2000	The other corresponds to the "specificity-determining loop" defined in beta1 and beta3 integrins and contains the antigenic residue Glu(175) in a disulfide-bonded loop located near the "top" of the domain.	Disulfides	146-155	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	71-86
10926679-8	2000	Sequence comparisons suggest the involvement/presence of different disulfide bonds in type IIa and type IIb Na/P(i)-cotransporters.	Disulfides	67-76	ATPase, class II, type 9B	Mus musculus	104-107
10748154-5	2000	In recombinant TRAIL, Cys(230) was found engaged either in interchain disulfide bridge formation, resulting in poorly active TRAIL, or in the chelation of one zinc atom per TRAIL trimer in the active, pro-apoptotic form of TRAIL.	Disulfides	70-79	TNF superfamily member 10	Homo sapiens	15-20
10887202-11	2000	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.	Disulfides	76-85	beta-secretase 1	Homo sapiens	126-130
10801893-13	2000	This suggests that during the catalytic cycle, Acr2p forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active Acr2p reductase.	Disulfides	67-76	Arr2p	Saccharomyces cerevisiae S288C	47-52
10880522-1	2000	The B cell antigen receptor (BCR) is a large complex that consists of a disulfide-linked tetramer of two transmembrane heavy (mu) chains and two light (lambda or kappa) chains in association with a heterodimer of Igalpha and Igbeta.	Disulfides	72-81	CD79a molecule	Homo sapiens	213-220
10801877-1	2000	Conformational reorganization of the amino-terminal four-helix bundle (22-kDa fragment) of apolipoprotein E (apoE) in binding to the phospholipid dimyristoylphosphatidylcholine (DMPC) to form discoidal particles was investigated by introducing single, double, and triple interhelical disulfide bonds to restrict the opening of the bundle.	Disulfides	284-293	apolipoprotein E	Homo sapiens	91-107
10801877-1	2000	Conformational reorganization of the amino-terminal four-helix bundle (22-kDa fragment) of apolipoprotein E (apoE) in binding to the phospholipid dimyristoylphosphatidylcholine (DMPC) to form discoidal particles was investigated by introducing single, double, and triple interhelical disulfide bonds to restrict the opening of the bundle.	Disulfides	284-293	apolipoprotein E	Homo sapiens	109-113
10891074-2	2000	We have investigated the activation of the GPCR rhodopsin by the construction and analysis of a mutant which contains a total of four disulfide bonds connecting the cytoplasmic ends of helices 1 and 7, and 3 and 5, and the extracellular ends of helices 3 and 4, and 5 and 6.	Disulfides	134-143	rhodopsin	Homo sapiens	48-57
10916174-4	2000	The ALF could be composed of many kappa chains devoid of any disulfide bond.	Disulfides	61-70	general transcription factor IIA subunit 1 like	Homo sapiens	4-7
10945247-2	2000	The transferrin molecule, with a molecular mass of about 80 kDa, is folded into two similarly sized homologous N- and C-lobes that are stabilized by many intrachain disulfides.	Disulfides	165-175	transferrin	Homo sapiens	4-15
10864452-4	2000	Disulfide bridges connect Cys253 and Cys263, Cys257 and Cys287, Cys359 and Cys370, Cys570 and Cys635, and Cys676 and Cys701, forming five intrachain disulfide bridges in the heavy chain of EPO.	Disulfides	0-9	eosinophil peroxidase	Homo sapiens	189-192
10864452-6	2000	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.	Disulfides	15-24	myeloperoxidase	Canis lupus familiaris	138-141
11131146-1	2000	Unfolded bovine rhodanese, a sulfurtransferase, does not regain full activity upon refolding due to the formation of aggregates and disulfide-linked misfolded states unless a large excess of reductant such as 200 mM beta-ME and 5 mg/ml detergent are present [Tandon and Horowitz (1990), J. Biol.	Disulfides	132-141	thiosulfate sulfurtransferase	Bos taurus	16-25
10878097-2	2000	It is constituted of the type II membrane protein 4F2hc (CD98) which is covalently linked to the polytopic membrane protein LAT1 via a disulfide bridge.	Disulfides	135-144	solute carrier family 7 member 5 L homeolog	Xenopus laevis	57-61
10933493-3	2000	A concatemer of the first and second modules (LB(1-2)) folds efficiently in the presence of calcium ions, forming the same disulfide connectivities as in the isolated modules.	Disulfides	123-132	cytoskeleton associated protein 2	Homo sapiens	46-52
10878097-2	2000	It is constituted of the type II membrane protein 4F2hc (CD98) which is covalently linked to the polytopic membrane protein LAT1 via a disulfide bridge.	Disulfides	135-144	solute carrier family 7 member 5 L homeolog	Xenopus laevis	124-128
10848594-3	2000	ITF contains a unique three-looped trefoil motif formed by intrachain disulfide bonds among six conserved cysteine residues, which is thought to contribute to its marked protease resistance.	Disulfides	70-79	trefoil factor 3	Homo sapiens	0-3
10806188-0	2000	Drug-stimulated ATPase activity of human P-glycoprotein is blocked by disulfide cross-linking between the nucleotide-binding sites.	Disulfides	70-79	ATP binding cassette subfamily B member 1	Homo sapiens	41-55
10788477-3	2000	MTX possesses 53-68% sequence identity with HsTx1 and Pi1, two other K(+) channel short chain scorpion toxins cross-linked by four disulfide bridges.	Disulfides	131-140	hybrid sterility, X Chromosome QTL 1	Mus musculus	44-49
10821677-0	2000	Human CC chemokine I-309, structural consequences of the additional disulfide bond.	Disulfides	68-77	C-C motif chemokine ligand 1	Homo sapiens	19-24
10821677-1	2000	I-309 is a member of the CC subclass of chemokines and is one of only three human chemokines known to contain an additional, third disulfide bond.	Disulfides	131-140	C-C motif chemokine ligand 1	Homo sapiens	0-5
10809738-0	2000	The role of ERp57 in disulfide bond formation during the assembly of major histocompatibility complex class I in a synchronized semipermeabilized cell translation system.	Disulfides	21-30	protein disulfide isomerase family A member 3	Homo sapiens	12-17
10809738-5	2000	A later and more prolonged interaction of calreticulin, specifically with assembled, disulfide-bonded heavy chain, highlights distinct differences in the roles of these two proteins in the assembly of MHC class I molecules.	Disulfides	85-94	calreticulin	Homo sapiens	42-54
10809738-6	2000	We also demonstrate that the thiol-dependent reductase ERp57 initially interacts with nondisulfide-bonded heavy chain, but this rapidly becomes disulfide-bonded and indicates that heavy chain folding occurs during its interaction with ERp57.	Disulfides	89-98	protein disulfide isomerase family A member 3	Homo sapiens	55-60
10866303-3	2000	The treatment of this TRAIL protein with DTT, a reducing agent, abolished formation of the Mr 42,000 band, suggesting that the Mr 42,000 band was the result of intermolecular disulfide bridge formation.	Disulfides	175-184	TNF superfamily member 10	Homo sapiens	22-27
10866303-8	2000	Therefore, our data indicate that cysteine 230 is not only required for TRAIL function but also modulates the apoptotic activity of TRAIL by forming an intermolecular disulfide bridge.	Disulfides	167-176	TNF superfamily member 10	Homo sapiens	72-77
10866303-8	2000	Therefore, our data indicate that cysteine 230 is not only required for TRAIL function but also modulates the apoptotic activity of TRAIL by forming an intermolecular disulfide bridge.	Disulfides	167-176	TNF superfamily member 10	Homo sapiens	132-137
10801974-6	2000	Characterization of recombinant mutant rat TrxR with SeCys(498) replaced by Cys having a 100-fold lower k(cat) for Trx reduction revealed the C-terminal redox center was present as a dithiol when the Cys(59)-Cys(64) was a disulfide, demonstrating that the selenium atom with its larger radius is critical for formation of the unique selenenylsulfide.	Disulfides	222-231	thioredoxin 1	Rattus norvegicus	43-46
10820057-6	2000	These results suggest that BSA forms disulfide-bonded aggregates that contain available thiol groups that can catalyze the formation of differently structured alpha-La monomers, dimers, higher polymers, and adducts of alpha-La with BSA.	Disulfides	37-46	lactalbumin alpha	Homo sapiens	218-226
10806409-3	2000	We observed that, in contrast with porcine OBP-1, purified recombinant OBP-1F is a homodimer exhibiting two disulfide bonds (C44-C48 and C63-C155), a pairing close to that of hamster aphrodisin.	Disulfides	108-117	odorant binding protein I f	Rattus norvegicus	71-77
10820057-4	2000	When 10% solutions of 1:1 (w/w) mixtures of alpha-La and BSA were heated, large disulfide-bonded aggregates and SDS-monomeric BSA and alpha-La were present.	Disulfides	80-89	lactalbumin alpha	Homo sapiens	44-52
10820057-6	2000	These results suggest that BSA forms disulfide-bonded aggregates that contain available thiol groups that can catalyze the formation of differently structured alpha-La monomers, dimers, higher polymers, and adducts of alpha-La with BSA.	Disulfides	37-46	lactalbumin alpha	Homo sapiens	159-167
10775604-2	2000	This protein, secreted as a disulfide-linked homo-octamer, was recognized by a panel of anti-CD46 antibodies with varying avidities.	Disulfides	28-37	CD46 molecule	Homo sapiens	93-97
10762272-4	2000	Like pediocin PA-1, disulfide-containing sakacin P mutants had the same potency at 20 and 37 degrees C, whereas wild-type sakacin P was approximately 10 times less potent at 37 degrees C than at 20 degrees C. Reciprocal effects on target cell specificity and the temperature dependence of potency were observed upon studying the effect of removing the C-terminal disulfide bridge from pediocin PA-1 by Cys--&gt;Ser mutations.	Disulfides	20-29	PAXIP1 associated glutamate rich protein 1	Homo sapiens	394-398
10823489-2	2000	Endothelin 1 was obtained by using regioselective and random schemes of disulfide bond formation.	Disulfides	72-81	endothelin 1	Homo sapiens	0-12
10863935-0	2000	Solution synthesis and biological activity of human pleiotrophin, a novel heparin-binding neurotrophic factor consisting of 136 amino acid residues with five disulfide bonds.	Disulfides	158-167	pleiotrophin	Homo sapiens	52-64
10863935-1	2000	Human pleiotrophin (hPTN), a novel heparin-binding neurotrophic factor consisting of 136 amino acid residues with five intramolecular disulfide bonds, was synthesized by solution procedure in order to demonstrate the utility of our strategy using our newly developed solvent system, a mixture of trifluoroethanol (TFE) and dichloromethane (DCM) or chloroform (CHL).	Disulfides	134-143	pleiotrophin	Homo sapiens	6-18
10845681-1	2000	Atrial natriuretic peptide (ANP) is a peptide with 25 amino acid residues (hANP 4-28) and one intra-chain disulfide bond.	Disulfides	106-115	natriuretic peptide A	Homo sapiens	0-26
10850801-1	2000	Using a combination of theoretical sequence structure recognition predictions and experimental disulfide bond assignments, a three-dimensional (3D) model of human interleukin-7 (hIL-7) was constructed that predicts atypical surface chemistry in helix D that is important for receptor activation.	Disulfides	95-104	interleukin 7	Homo sapiens	163-176
10850801-1	2000	Using a combination of theoretical sequence structure recognition predictions and experimental disulfide bond assignments, a three-dimensional (3D) model of human interleukin-7 (hIL-7) was constructed that predicts atypical surface chemistry in helix D that is important for receptor activation.	Disulfides	95-104	interleukin 7	Homo sapiens	178-183
10938586-6	2000	The results obtained show that the 41 degrees C stress leads to formation of intermolecular disulfide bonds between apo-GR and associated heat shock proteins (Hsp90, Hsp70).	Disulfides	92-101	nuclear receptor subfamily 3 group C member 1	Homo sapiens	120-122
10756101-2	2000	Here, we used circular dichroism and disulfide exchange experiments to examine the unfolding mechanism of alpha-LA(alpha), a two- disulfide variant of human alpha-lactalbumin (alpha-LA) that adopts a molten globule conformation under near physiological conditions.	Disulfides	37-46	lactalbumin alpha	Homo sapiens	106-114
10845681-1	2000	Atrial natriuretic peptide (ANP) is a peptide with 25 amino acid residues (hANP 4-28) and one intra-chain disulfide bond.	Disulfides	106-115	natriuretic peptide A	Homo sapiens	28-31
10756101-2	2000	Here, we used circular dichroism and disulfide exchange experiments to examine the unfolding mechanism of alpha-LA(alpha), a two- disulfide variant of human alpha-lactalbumin (alpha-LA) that adopts a molten globule conformation under near physiological conditions.	Disulfides	130-139	lactalbumin alpha	Homo sapiens	106-114
10845681-8	2000	The HS- then catalyzed ANP to form the disulfide-linked multimers.	Disulfides	39-48	natriuretic peptide A	Homo sapiens	23-26
10845681-9	2000	The dehydroalanine-type ANP intermediate then reacted with another ANP molecule to form a non-disulfide-linked dimer through reaction with the side chain of tyrosine.	Disulfides	94-103	natriuretic peptide A	Homo sapiens	24-27
11232598-8	2000	This cysteine is also one of the cysteines that form the intersubunit disulfide bonds, suggesting that calmodulin binds at an intersubunit contact site.	Disulfides	70-79	calmodulin 1	Homo sapiens	103-113
10757967-1	2000	The applications of disulfide-bond chemistry to studies of protein folding, structure, and stability are reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A).	Disulfides	20-29	ribonuclease pancreatic	Bos taurus	153-167
10757967-1	2000	The applications of disulfide-bond chemistry to studies of protein folding, structure, and stability are reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A).	Disulfides	20-29	ribonuclease pancreatic	Bos taurus	169-176
10757967-3	2000	The oxidative folding of RNase A is then described, focusing on the role of structure formation in the regeneration of the native disulfide bonds.	Disulfides	130-139	ribonuclease pancreatic	Bos taurus	25-32
10803663-1	2000	Plasma lipoprotein(a) [Lp(a)]-consisting of a disulfide-linked complex of apolipoprotein B and apolipoprotein (a)--levels are considered to be an independent risk factor for coronary heart disease.	Disulfides	46-55	apolipoprotein B	Homo sapiens	74-90
10727107-5	2000	Unexpectedly, the absence of a disulfide bridge Cys31-Cys34 in [Abu 31,34]-MTX and MTX(1-29) resulted in MTX-unrelated half-cystine pairings of the three remaining disulfide bridges for the two analogs, which is likely to be responsible for their inactivity against Kv1 channel subtypes.	Disulfides	31-40	potassium voltage-gated channel subfamily A member 5	Rattus norvegicus	266-269
10805377-3	2000	We show by sequence analysis that the OvIL-4 cDNA retained the four alpha-helix structure and disulfide bonds identified in human IL-4 (HuIL-4).	Disulfides	94-103	interleukin 4	Homo sapiens	40-44
10733880-11	2000	The murine Tcl1 recombinant protein displays limited solubility and forms disulfide-linked dimers and oligomers, while the mutant murine Tcl1 C86A protein has increased solubility and does not form higher order oligomers.	Disulfides	74-83	T cell lymphoma breakpoint 1	Mus musculus	11-15
10727242-0	2000	Effect of an alternative disulfide bond on the structure, stability, and folding of human lysozyme.	Disulfides	25-34	lysozyme	Homo sapiens	90-98
10727242-1	2000	Human lysozyme has four disulfide bonds, one of which, Cys65-Cys81, is included in a long loop of the beta-domain.	Disulfides	24-33	lysozyme	Homo sapiens	6-14
10727242-3	2000	Here, using the W64CC65A mutant, we investigated the effects of an alternative disulfide bond on the structure, stability, and folding of human lysozyme using circular dichroism (CD) and fluorescence spectroscopy combined with a stopped-flow technique.	Disulfides	79-88	lysozyme	Homo sapiens	144-152
10727242-8	2000	The Gibbs" free-energy diagrams obtained from the kinetic analysis suggest that the structure around the loop region in the beta-domain of human lysozyme is formed after the transition state of folding, and thus, the effect of the alternative disulfide bond on the structure, stability, and folding of human lysozyme appears mainly in the native state.	Disulfides	243-252	lysozyme	Homo sapiens	145-153
10727242-8	2000	The Gibbs" free-energy diagrams obtained from the kinetic analysis suggest that the structure around the loop region in the beta-domain of human lysozyme is formed after the transition state of folding, and thus, the effect of the alternative disulfide bond on the structure, stability, and folding of human lysozyme appears mainly in the native state.	Disulfides	243-252	lysozyme	Homo sapiens	308-316
10890174-1	2000	This review will summarize the properties of five variant forms of human growth hormone: a disulfide dimer, a glycosylated form, 20 kD-hGH, and two peptides made up of portions of 22 kD-hGH.	Disulfides	91-100	growth hormone 1	Homo sapiens	73-87
10694412-3	2000	SecB binds both fully unfolded RNase A and BPTI as well as compact, partially folded disulfide intermediates of alpha-lactalbumin, which have 40-60% of native secondary structure.	Disulfides	85-94	lactalbumin alpha	Homo sapiens	112-129
10767776-0	2000	Mass spectrometric mapping of disulfide bonds in recombinant human interleukin-13.	Disulfides	30-39	interleukin 13	Homo sapiens	67-81
10767776-5	2000	This disulfide arrangement is similar to that observed for the analogous four internal cysteine residues in hIL-4.	Disulfides	5-14	interleukin 4	Homo sapiens	108-113
10767776-6	2000	The conservation of disulfide bond arrangements between hIL-13 and hIL-4, coupled with their alpha-helical structure and sequence homologies, confirms that IL-13 and IL-4 are structural homologues.	Disulfides	20-29	interleukin 13	Homo sapiens	56-62
10767776-6	2000	The conservation of disulfide bond arrangements between hIL-13 and hIL-4, coupled with their alpha-helical structure and sequence homologies, confirms that IL-13 and IL-4 are structural homologues.	Disulfides	20-29	interleukin 4	Homo sapiens	67-72
10767776-6	2000	The conservation of disulfide bond arrangements between hIL-13 and hIL-4, coupled with their alpha-helical structure and sequence homologies, confirms that IL-13 and IL-4 are structural homologues.	Disulfides	20-29	interleukin 13	Homo sapiens	57-62
10767776-6	2000	The conservation of disulfide bond arrangements between hIL-13 and hIL-4, coupled with their alpha-helical structure and sequence homologies, confirms that IL-13 and IL-4 are structural homologues.	Disulfides	20-29	interleukin 4	Homo sapiens	68-72
10681495-0	2000	The packing of the transmembrane segments of human multidrug resistance P-glycoprotein is revealed by disulfide cross-linking analysis.	Disulfides	102-111	ATP binding cassette subfamily B member 1	Homo sapiens	72-86
10700152-3	2000	We show that chloroplasts can express a secretory protein, human somatotropin, in a soluble, biologically active, disulfide-bonded form.	Disulfides	114-123	growth hormone 1	Homo sapiens	65-77
10933939-4	2000	Transferrin (Tf) was conjugated with PNA via a reversible disulfide bond using N-succinimidyl-3-(2-pyridyldithio)propionate.	Disulfides	58-67	transferrin	Homo sapiens	0-11
10933939-4	2000	Transferrin (Tf) was conjugated with PNA via a reversible disulfide bond using N-succinimidyl-3-(2-pyridyldithio)propionate.	Disulfides	58-67	transferrin	Homo sapiens	13-15
10666291-0	2000	Copper-dependent formation of disulfide-linked dimer of S100B protein.	Disulfides	30-39	S100 calcium binding protein B	Homo sapiens	56-61
10694815-2	2000	A chimeric protein consisting of a scFv of mAb 145.2C11, the hinge-CH2-CH3 region of human IgG1, and the transmembrane and cytosolic domains of murine CD80 formed disulfide-linked dimers on the plasma membrane of cells and specifically bound lymphocytes.	Disulfides	163-172	CD80 antigen	Mus musculus	151-155
10713556-4	2000	The interaction of PDSG with catalase in water and in phosphate buffer was accompanied by significant changes in CD spectra in the far UV-region that indicated disturbances in the secondary structure of catalase subunits induced by the bioantioxidant; the latter was suggested to initiate the reaction of thiol--disulfide exchange with the enzyme.	Disulfides	312-321	catalase	Homo sapiens	29-37
10713556-4	2000	The interaction of PDSG with catalase in water and in phosphate buffer was accompanied by significant changes in CD spectra in the far UV-region that indicated disturbances in the secondary structure of catalase subunits induced by the bioantioxidant; the latter was suggested to initiate the reaction of thiol--disulfide exchange with the enzyme.	Disulfides	312-321	catalase	Homo sapiens	203-211
10713556-5	2000	The problem of the compatibility of catalase with disulfide bioantioxidants is discussed.	Disulfides	50-59	catalase	Homo sapiens	36-44
10648821-1	2000	The G protein-coupled vasopressin V2 receptor (V2 receptor) contains a pair of conserved cysteine residues (C112 and C192) which are thought to form a disulfide bond between the first and second extracellular loops.	Disulfides	151-160	arginine vasopressin receptor 2	Homo sapiens	22-45
10655481-3	2000	The disulfide product of this inactivation was not sensitive to reduction by externally added sulfhydryl compounds, but apparently reacted with intracellular reducing agents to spontaneously regenerate active SERT.	Disulfides	4-13	solute carrier family 6 member 4	Homo sapiens	209-213
10689966-8	2000	We then applied the above procedure to the synthesis of endothelin-1 (ET-1), a peptide containing 21-amino acid residues having a C-terminal Trp residue and two disulfide bonds, by regioselective disulfide formation.	Disulfides	161-170	endothelin 1	Homo sapiens	56-68
10689966-8	2000	We then applied the above procedure to the synthesis of endothelin-1 (ET-1), a peptide containing 21-amino acid residues having a C-terminal Trp residue and two disulfide bonds, by regioselective disulfide formation.	Disulfides	161-170	endothelin 1	Homo sapiens	70-74
10689966-8	2000	We then applied the above procedure to the synthesis of endothelin-1 (ET-1), a peptide containing 21-amino acid residues having a C-terminal Trp residue and two disulfide bonds, by regioselective disulfide formation.	Disulfides	196-205	endothelin 1	Homo sapiens	56-68
10689966-8	2000	We then applied the above procedure to the synthesis of endothelin-1 (ET-1), a peptide containing 21-amino acid residues having a C-terminal Trp residue and two disulfide bonds, by regioselective disulfide formation.	Disulfides	196-205	endothelin 1	Homo sapiens	70-74
10689966-9	2000	The combination of the silyl chloride method with iodine oxidation using S-acetamidomethyl (Acm) and S-tBu groups for the regioselective double disulfide formation was successfully applied to give a highly purified ET-1.	Disulfides	144-153	endothelin 1	Homo sapiens	215-219
10716183-5	2000	The second and fourth domains of the EGF receptor, S1 and S2, consist of the modules held together by disulfide bonds, which, except for the first module of the S1 domain, form rod-like structures.	Disulfides	102-111	epidermal growth factor receptor	Homo sapiens	37-49
10893147-10	2000	In cells and virions, both M and GP5 occur in heterodimeric complexes linked by disulfide bonds.	Disulfides	80-89	glycoprotein V platelet	Homo sapiens	33-36
10620363-0	2000	Disulfide bonds in big ET-1 are essential for the specific cleavage at the Trp(21)-Val(22) bond by soluble endothelin converting enzyme-1 from baculovirus/insect cells.	Disulfides	0-9	endothelin 1	Homo sapiens	23-27
10620363-7	2000	However, when linear big ET-1, in which the formation of disulfide bonds has been prevented by alkylation of the four cysteines, was used as substrate, it was cleaved by solECE-1 at multiple sites.	Disulfides	57-66	endothelin 1	Homo sapiens	25-29
10620363-8	2000	This result indicates that secondary/tertiary structure of big ET-1 induced by disulfide bonds is essential for the specific cleavage of the Trp(21)-Val(22) bond by ECE-1.	Disulfides	79-88	endothelin 1	Homo sapiens	63-67
10606762-0	2000	Local interactions and the role of the 6-120 disulfide bond in alpha-lactalbumin: implications for formation of the molten globule state.	Disulfides	45-54	lactalbumin alpha	Homo sapiens	63-80
10606762-2	2000	A set of peptides has been prepared in order to probe the role of local interactions in the vicinity of the Cys(6)-Cys(120) disulfide bond in stabilizing the molten globule state of human alpha-lactalbumin.	Disulfides	124-133	lactalbumin alpha	Homo sapiens	188-205
10639150-0	2000	Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT).	Disulfides	23-32	IFI30 lysosomal thiol reductase	Homo sapiens	75-127
10639150-0	2000	Enzymatic reduction of disulfide bonds in lysosomes: characterization of a gamma-interferon-inducible lysosomal thiol reductase (GILT).	Disulfides	23-32	IFI30 lysosomal thiol reductase	Homo sapiens	129-133
11281283-9	2000	The reduction in eNOS sulfhydryl content and the inhibitory effect of PAO on eNOS activity were prevented by dithiothreitol, a disulfide-reducing agent.	Disulfides	127-136	nitric oxide synthase 3	Bos taurus	17-21
11281283-9	2000	The reduction in eNOS sulfhydryl content and the inhibitory effect of PAO on eNOS activity were prevented by dithiothreitol, a disulfide-reducing agent.	Disulfides	127-136	nitric oxide synthase 3	Bos taurus	77-81
10617603-0	2000	Functional analysis of a disulfide bond in the cardiac Na(+)-Ca(2+) exchanger.	Disulfides	25-34	solute carrier family 8 member A1	Homo sapiens	55-77
10623614-1	2000	The binding processes of GroEL with apo cytochrome c (apo-cyt c) and disulfide-reduced apo alpha-lactalbumin (rLA) in homogeneous solution at low concentration were analyzed by fluorescence correlation spectroscopy (FCS) with extremely high sensitivity.	Disulfides	69-78	lactalbumin alpha	Homo sapiens	91-108
11264870-5	2000	On the other hand, multimeric FN formed by disulfide bonds did not show any effect on either cell adhesion or spreading.	Disulfides	43-52	fibronectin 1	Homo sapiens	30-32
10632727-0	2000	Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A.	Disulfides	16-25	ribonuclease pancreatic	Bos taurus	90-104
10601849-7	2000	Among the hormones having a cysteine residue at their N-terminal end and intramolecular disulfide bonds, it was found that vasopressin and oxytocin, but not calcitonin and endothelins, were cleaved by the enzyme.	Disulfides	88-97	arginine vasopressin	Homo sapiens	123-134
10632727-2	2000	Bovine pancreatic ribonuclease A (RNase A) is a 124-residue enzyme that contains four interweaving disulfide bonds (Cys26-Cys84, Cys40-Cys95, Cys58-Cys110, and Cys65-Cys72) and catalyzes the cleavage of RNA.	Disulfides	99-108	ribonuclease pancreatic	Bos taurus	18-32
10632727-2	2000	Bovine pancreatic ribonuclease A (RNase A) is a 124-residue enzyme that contains four interweaving disulfide bonds (Cys26-Cys84, Cys40-Cys95, Cys58-Cys110, and Cys65-Cys72) and catalyzes the cleavage of RNA.	Disulfides	99-108	ribonuclease pancreatic	Bos taurus	34-41
10632727-3	2000	The contribution of each disulfide bond to the conformational stability and catalytic activity of RNase A has been determined by using variants in which each cystine is replaced independently with a pair of alanine residues.	Disulfides	25-34	ribonuclease pancreatic	Bos taurus	98-105
10632727-4	2000	Thermal unfolding experiments monitored by ultraviolet spectroscopy and differential scanning calorimetry reveal that wild-type RNase A and each disulfide variant unfold in a two-state process and that each disulfide bond contributes substantially to conformational stability.	Disulfides	207-216	ribonuclease pancreatic	Bos taurus	128-135
10632727-6	2000	Removing either one of the terminal disulfide bonds liberates a similar number of residues and has a similar effect on conformational stability, decreasing the midpoint of the thermal transition by almost 40 degrees C. The disulfide variants catalyze the cleavage of poly(cytidylic acid) with values of kcat/Km that are 2- to 40-fold less than that of wild-type RNase A.	Disulfides	36-45	ribonuclease pancreatic	Bos taurus	362-369
10632727-6	2000	Removing either one of the terminal disulfide bonds liberates a similar number of residues and has a similar effect on conformational stability, decreasing the midpoint of the thermal transition by almost 40 degrees C. The disulfide variants catalyze the cleavage of poly(cytidylic acid) with values of kcat/Km that are 2- to 40-fold less than that of wild-type RNase A.	Disulfides	223-232	ribonuclease pancreatic	Bos taurus	362-369
10779222-1	2000	The trefoil peptide family is comprised of three small peptides (designated pS2, SP, and ITF) exhibiting a unique motif of three intrachain loops formed by disulfide bonds.	Disulfides	156-165	trefoil factor 1	Homo sapiens	76-79
10779222-1	2000	The trefoil peptide family is comprised of three small peptides (designated pS2, SP, and ITF) exhibiting a unique motif of three intrachain loops formed by disulfide bonds.	Disulfides	156-165	trefoil factor 3	Homo sapiens	89-92
10608814-0	1999	Probing the folding pathways of long R(3) insulin-like growth factor-I (LR(3)IGF-I) and IGF-I via capture and identification of disulfide intermediates by cyanylation methodology and mass spectrometry.	Disulfides	128-137	insulin like growth factor 1	Homo sapiens	77-82
10601232-1	1999	Oxidation of the skeletal muscle Ca(2+) release channel (RYR1) increases its activity, produces intersubunit disulfide bonds, and blocks its interaction with calmodulin.	Disulfides	109-118	ryanodine receptor 1	Homo sapiens	57-61
11105248-3	2000	By C-terminal fusion of scFv molecules to the Fd- and the L-chains efficient heterodimerization in mammalian cells was obtained and a novel intermediate sized, disulfide stabilized BsAb could be efficiently produced.	Disulfides	160-169	immunglobulin heavy chain variable region	Homo sapiens	24-28
10608814-0	1999	Probing the folding pathways of long R(3) insulin-like growth factor-I (LR(3)IGF-I) and IGF-I via capture and identification of disulfide intermediates by cyanylation methodology and mass spectrometry.	Disulfides	128-137	insulin like growth factor 1	Homo sapiens	88-93
10608814-5	1999	Folding pathways of IGF-I and LR(3)IGF-I are proposed based on the time-dependent distribution and disulfide structure of the corresponding trapped intermediates.	Disulfides	99-108	insulin like growth factor 1	Homo sapiens	20-25
10608814-5	1999	Folding pathways of IGF-I and LR(3)IGF-I are proposed based on the time-dependent distribution and disulfide structure of the corresponding trapped intermediates.	Disulfides	99-108	insulin like growth factor 1	Homo sapiens	35-40
10753067-6	1999	RESULTS: After transient transfection of COS-7 cells, IFNgammaR/IgG1 and IL-4/IgG1 fusion proteins are secreted in vitro as disulfide-linked homodimers, with the expected biological activity.	Disulfides	124-133	immunoglobulin heavy constant gamma 1 (G1m marker)	Mus musculus	64-68
10633069-0	1999	Is formation of visible channels in a phospholipid bilayer by botulinum neurotoxin type B sensitive to its disulfide?	Disulfides	107-116	neurotoxin	Clostridium botulinum	72-82
10633069-6	1999	We reduced this unnicked protein and used its binding to ganglioside in a lipid layer to produce helical tubular crystals of unnicked botulinum neurotoxin type B in its disulfide-reduced state.	Disulfides	169-178	neurotoxin	Clostridium botulinum	144-154
10633069-9	1999	Although channels have been seen with disulfide-linked neurotoxin (Schmid, Robinson, and DasGupta (1993) Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles, Nature 364, 827-830), no channels were seen here, a finding which suggests that the reduced, unnicked neurotoxin is incapable of forming a visible channel.	Disulfides	38-47	neurotoxin	Clostridium botulinum	55-65
10633069-9	1999	Although channels have been seen with disulfide-linked neurotoxin (Schmid, Robinson, and DasGupta (1993) Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles, Nature 364, 827-830), no channels were seen here, a finding which suggests that the reduced, unnicked neurotoxin is incapable of forming a visible channel.	Disulfides	38-47	neurotoxin	Clostridium botulinum	139-149
10633069-9	1999	Although channels have been seen with disulfide-linked neurotoxin (Schmid, Robinson, and DasGupta (1993) Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles, Nature 364, 827-830), no channels were seen here, a finding which suggests that the reduced, unnicked neurotoxin is incapable of forming a visible channel.	Disulfides	38-47	neurotoxin	Clostridium botulinum	139-149
10600104-1	1999	We have identified specific regions of the polypeptide chain of bovine pancreatic ribonuclease A (RNase A) that are critical for stabilizing the oxidative folding intermediate des-[40-95] (with three native disulfide bonds but lacking the fourth native Cys40-Cys95 disulfide bond) in an ensemble of largely disordered three-disulfide precursors (3S if des-[40-95]).	Disulfides	207-216	ribonuclease pancreatic	Bos taurus	98-105
10600104-1	1999	We have identified specific regions of the polypeptide chain of bovine pancreatic ribonuclease A (RNase A) that are critical for stabilizing the oxidative folding intermediate des-[40-95] (with three native disulfide bonds but lacking the fourth native Cys40-Cys95 disulfide bond) in an ensemble of largely disordered three-disulfide precursors (3S if des-[40-95]).	Disulfides	265-274	ribonuclease pancreatic	Bos taurus	98-105
10600104-1	1999	We have identified specific regions of the polypeptide chain of bovine pancreatic ribonuclease A (RNase A) that are critical for stabilizing the oxidative folding intermediate des-[40-95] (with three native disulfide bonds but lacking the fourth native Cys40-Cys95 disulfide bond) in an ensemble of largely disordered three-disulfide precursors (3S if des-[40-95]).	Disulfides	265-274	ribonuclease pancreatic	Bos taurus	98-105
10600104-2	1999	A stable analogue of des-[40-95], viz., [C40A, C95A] RNase A, which contains three out of four native disulfide pairings, was previously found to have a three-dimensional structure very similar to that of the wild-type protein.	Disulfides	102-111	ribonuclease pancreatic	Bos taurus	53-60
10600104-5	1999	Comparison of the relative stabilities at specific amide sites of [C40A, C95A] RNase A at both temperatures with the corresponding values for the wild-type protein at 35 degrees C corroborates previous experimental evidence that unidentified intramolecular contacts in the vicinity of the preferentially formed native one-disulfide (C65-C72) loop are crucial for stabilizing early folding intermediates, leading to des-[40-95].	Disulfides	322-331	ribonuclease pancreatic	Bos taurus	79-86
10600104-6	1999	Moreover, values of for residues at or near the third alpha-helix, and in part of the second beta-sheet of [C40A, C95A] RNase A, indicate that these two regions of regular backbone structure contribute to stabilizing the global chain fold of the des-[40-95] disulfide-folding intermediate in the wild-type protein.	Disulfides	258-267	ribonuclease pancreatic	Bos taurus	120-127
10564764-9	1999	Refolding experiments of synthesized linear p-Cox17p revealed the existence of mostly one pattern of three intrachain disulfide bridges similar to that of native p-Cox17p, because the main oxidized p-Cox17p was completely co-eluted with the natural product.	Disulfides	118-127	cytochrome c oxidase assembly protein 17, copper chaperone	Mus musculus	46-52
10644446-6	1999	ANGPTL3 contains the four conserved cysteines implicated in the intramolecular disulfide bonds within the FHD, but it does not contain two other cysteines that are found within the FHD of angiopoietins 1, 2, and 4.	Disulfides	79-88	angiopoietin like 3	Homo sapiens	0-7
10568788-1	1999	The L-type amino acid transporter LAT1 has recently been identified as being a disulfide-linked "light chain" of the ubiquitously expressed glycoprotein 4F2hc/CD98.	Disulfides	79-88	dihydrolipoyllysine-residue acetyltransferase	Saccharomyces cerevisiae S288C	34-38
10567376-4	1999	Refolding and unfolding of hFGF-2 (155 amino acids) is very slow compared with other non-disulfide-bonded monomeric proteins of similar size.	Disulfides	89-98	fibroblast growth factor 2	Homo sapiens	27-33
10570143-2	1999	Single cysteine substitution mutants in the cytoplasmic face of rhodopsin were labeled by attachment of the trifluoroethylthio (TET), CF(3)-CH(2)-S, group through a disulfide linkage.	Disulfides	165-174	rhodopsin	Homo sapiens	64-73
10753067-6	1999	RESULTS: After transient transfection of COS-7 cells, IFNgammaR/IgG1 and IL-4/IgG1 fusion proteins are secreted in vitro as disulfide-linked homodimers, with the expected biological activity.	Disulfides	124-133	immunoglobulin heavy constant gamma 1 (G1m marker)	Mus musculus	78-82
10502286-2	1999	The presence of cystein residues in apoE2 and apoE3 allows these isoforms to form disulfide-linked complexes, such as apo(E-AII) complex and apo(AII-E-AII) complex.	Disulfides	82-91	apolipoprotein E	Homo sapiens	36-41
10557227-1	1999	After isolation of tobacco (Nicotiana tabacum) leaf mitochondria, alternative oxidase (AOX) is predominantly present as the disulfide-linked, less-active "oxidized" form.	Disulfides	124-133	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	66-85
10557227-1	1999	After isolation of tobacco (Nicotiana tabacum) leaf mitochondria, alternative oxidase (AOX) is predominantly present as the disulfide-linked, less-active "oxidized" form.	Disulfides	124-133	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	87-90
10557227-2	1999	In an in organello assay, significant AOX activity was dependent upon both the reduction of the regulatory disulfide bond (such as occurs by dithiothreitol) and upon the presence of the activator pyruvate.	Disulfides	107-116	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	38-41
10572015-5	1999	On the basis of these results, we also describe a simple protocol for identifying disulfide loops in soluble and membrane proteins, exemplified by the alpha subunit of the muscle nicotinic acetylcholine receptor (nAChR).	Disulfides	82-91	cholinergic receptor nicotinic alpha 4 subunit	Homo sapiens	213-218
10458736-5	1999	Introduction of the hinge-CH2-CH3 region of human IgG (gamma1 domain) between AFP and TM allowed efficient formation of disulfide-linked dimers.	Disulfides	120-129	alpha fetoprotein	Homo sapiens	78-81
10563507-3	1999	Using reduced/oxidized glutathione, the EGF-RGD module was folded as efficiently as the natural C1r-EGF module, resulting in formation of the appropriate disulfide bridge pattern as shown by mass spectrometry and N-terminal sequence analyses of thermolytic fragments.	Disulfides	154-163	complement C1r	Homo sapiens	96-99
10502286-2	1999	The presence of cystein residues in apoE2 and apoE3 allows these isoforms to form disulfide-linked complexes, such as apo(E-AII) complex and apo(AII-E-AII) complex.	Disulfides	82-91	apolipoprotein E	Homo sapiens	46-51
10506575-4	1999	Disulfide cross-linking analysis also showed that the immature P-gp did not exhibit ATP-induced conformational changes as found in the mature enzyme.	Disulfides	0-9	ATP binding cassette subfamily B member 1	Homo sapiens	63-67
10526086-2	1999	The structure of C5a includes a core region (N-terminal residues 1-63) consisting of four, antiparallel alpha-helices held together by three disulfide linkages and a structured C-terminal tail (residues 64-74).	Disulfides	141-150	complement C5a receptor 1	Homo sapiens	17-20
10526086-10	1999	A model of C5a receptor dimerization is presented to account for the high potency of the disulfide antagonist C5aRAD.	Disulfides	89-98	complement C5a receptor 1	Homo sapiens	11-23
10506124-2	1999	The transporter designated BAT1 (b(0, +)-type amino acid transporter 1) from rat kidney was found to be structurally related to recently identified amino acid transporters for system L, system y(+)L, and system x(-)C, which are linked, via a disulfide bond, to the other type II membrane glycoprotein, 4F2hc (4F2 heavy chain).	Disulfides	242-251	solute carrier family 7 member 9	Rattus norvegicus	27-70
10506124-2	1999	The transporter designated BAT1 (b(0, +)-type amino acid transporter 1) from rat kidney was found to be structurally related to recently identified amino acid transporters for system L, system y(+)L, and system x(-)C, which are linked, via a disulfide bond, to the other type II membrane glycoprotein, 4F2hc (4F2 heavy chain).	Disulfides	242-251	solute carrier family 3 member 2	Rattus norvegicus	302-307
10506124-2	1999	The transporter designated BAT1 (b(0, +)-type amino acid transporter 1) from rat kidney was found to be structurally related to recently identified amino acid transporters for system L, system y(+)L, and system x(-)C, which are linked, via a disulfide bond, to the other type II membrane glycoprotein, 4F2hc (4F2 heavy chain).	Disulfides	242-251	solute carrier family 3 member 2	Rattus norvegicus	309-324
10506124-4	1999	The band was shifted to 41 kDa in the reducing condition, confirming that BAT1 and rBAT are linked via a disulfide bond.	Disulfides	105-114	DExD-box helicase 39B	Rattus norvegicus	74-78
10496984-10	1999	Reduced TFPI-2/MSPI did not bind to heparin, suggesting that proper disulfide pairings and conformation are essential for matrix binding.	Disulfides	68-77	tissue factor pathway inhibitor 2	Homo sapiens	8-14
10500168-0	1999	The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule and weakens its cooperativity of folding.	Disulfides	11-20	lactalbumin alpha	Homo sapiens	41-58
10490983-2	1999	The predominant interactions between the light chain and BiP are observed early in the folding pathway, when the light chain is either completely reduced, or has only one disulfide bond.	Disulfides	171-180	heat shock protein family A (Hsp70) member 5	Homo sapiens	57-60
10504730-1	1999	Human alpha-lactalbumin (alpha-LA) is a four disulfide-bonded protein that adopts partially structured conformations under a variety of mildly denaturing conditions.	Disulfides	45-54	lactalbumin alpha	Homo sapiens	6-23
10504730-1	1999	Human alpha-lactalbumin (alpha-LA) is a four disulfide-bonded protein that adopts partially structured conformations under a variety of mildly denaturing conditions.	Disulfides	45-54	lactalbumin alpha	Homo sapiens	25-33
10504730-8	1999	These results show that the overall architecture of the protein fold of alpha-LA is determined by the polypeptide sequence itself, and not as the result of cross-linking by disulfide bonds, and provide insight into the way in which the sequence codes for the fold.	Disulfides	173-182	lactalbumin alpha	Homo sapiens	72-80
10500168-1	1999	Our aim is to determine whether the disulfide bonds of alpha-lactalbumin account for the lack of cooperative folding behavior reported for some molten globule variants, in contrast to the highly cooperative folding reported for the pH 4 molten globule of apomyoglobin.	Disulfides	36-45	lactalbumin alpha	Homo sapiens	55-72
10493584-1	1999	Recent studies of the refolding of reduced bovine pancreatic trypsin inhibitor (BPTI) have shown that a previously unidentified intermediate with a single disulfide is formed much more rapidly than any other one-disulfide species.	Disulfides	155-164	trophoblast Kunitz domain protein 1	Bos taurus	61-78
10504260-0	1999	Structure and function in rhodopsin: effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase.	Disulfides	48-57	rhodopsin	Homo sapiens	26-35
10504260-0	1999	Structure and function in rhodopsin: effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase.	Disulfides	48-57	rhodopsin	Homo sapiens	97-106
10508406-0	1999	State-dependent disulfide cross-linking in rhodopsin.	Disulfides	16-25	rhodopsin	Homo sapiens	43-52
10508406-1	1999	In previous studies, we developed a new method for detecting tertiary interactions in rhodopsin using split receptors and disulfide cross-linking.	Disulfides	122-131	rhodopsin	Homo sapiens	86-95
10493584-1	1999	Recent studies of the refolding of reduced bovine pancreatic trypsin inhibitor (BPTI) have shown that a previously unidentified intermediate with a single disulfide is formed much more rapidly than any other one-disulfide species.	Disulfides	212-221	trophoblast Kunitz domain protein 1	Bos taurus	61-78
10463612-1	1999	Thioredoxin (Trx) is a small redox-active protein that provides reducing equivalents for key cysteine residues of proteins through thiol-disulfide exchange, such as the transcription factor nuclear factor-kappaB (NF-kappaB).	Disulfides	137-146	nuclear factor kappa B subunit 1	Homo sapiens	190-211
10463612-1	1999	Thioredoxin (Trx) is a small redox-active protein that provides reducing equivalents for key cysteine residues of proteins through thiol-disulfide exchange, such as the transcription factor nuclear factor-kappaB (NF-kappaB).	Disulfides	137-146	nuclear factor kappa B subunit 1	Homo sapiens	213-222
10428976-1	1999	The process of assembly of apolipoprotein (apo) B-containing lipoprotein particles occurs co-translationally after disulfide-dependent folding of the N-terminal domain of apoB but the mechanism is not understood.	Disulfides	115-124	apolipoprotein B	Homo sapiens	171-175
10441134-0	1999	Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin.	Disulfides	8-17	coagulation factor II, thrombin	Homo sapiens	102-110
10441134-5	1999	Thrombospondin-1, known to form disulfide-linked complexes with thrombin-AT [Milev, Y., and Essex, D. W. (1999) Arch.	Disulfides	32-41	thrombospondin 1	Homo sapiens	0-16
10441134-5	1999	Thrombospondin-1, known to form disulfide-linked complexes with thrombin-AT [Milev, Y., and Essex, D. W. (1999) Arch.	Disulfides	32-41	coagulation factor II, thrombin	Homo sapiens	64-72
10441134-14	1999	In summary, these studies indicate that PDI functions to form disulfide-linked complexes of vitronectin with thrombin-AT.	Disulfides	62-71	coagulation factor II, thrombin	Homo sapiens	109-117
10465542-2	1999	It was indicated that conformational restriction of peptide via an intramolecular disulfide bond improved the binding affinity for IgE and that the peptide might have an ability to inhibit the IgE-receptor interaction.	Disulfides	82-91	immunoglobulin heavy constant epsilon	Homo sapiens	131-134
10465542-2	1999	It was indicated that conformational restriction of peptide via an intramolecular disulfide bond improved the binding affinity for IgE and that the peptide might have an ability to inhibit the IgE-receptor interaction.	Disulfides	82-91	immunoglobulin heavy constant epsilon	Homo sapiens	193-196
10609639-1	1999	kappa-Casein as purified from bovine milk exhibits a rather unique disulfide bonding pattern as revealed by SDS-PAGE.	Disulfides	67-76	casein kappa	Bos taurus	0-12
10409638-10	1999	Furthermore, we provide evidence that treatment of caspase-3 with NO can lead to mixed disulfide formation with glutathione, demonstrating the oxidative character of NO.	Disulfides	87-96	caspase 3	Homo sapiens	51-60
10423251-0	1999	Redox-dependent DNA binding of the purified androgen receptor: evidence for disulfide-linked androgen receptor dimers.	Disulfides	76-85	androgen receptor	Homo sapiens	44-61
10423251-0	1999	Redox-dependent DNA binding of the purified androgen receptor: evidence for disulfide-linked androgen receptor dimers.	Disulfides	76-85	androgen receptor	Homo sapiens	93-110
10423251-6	1999	Treatment with the sulfhydryl oxidizing reagent diamide formed the faster migrating, slower dissociating complex, indicating it represents disulfide-linked AR dimers bound to DNA.	Disulfides	139-148	androgen receptor	Homo sapiens	156-158
10413465-1	1999	Recent studies have shown that at physiological conditions (pH 7.6, 37 degrees C), the reactivity of recombinant apoE isoforms secreted by mammalian cells toward amyloid peptide beta (Abeta40) follows the order apoE2 &gt; apoE3 &gt; apoE4 for the apoE monomer and apoE2 &gt; apoE3 for apoE dimer that is formed via that intramolecular disulfide bridges.	Disulfides	335-344	apolipoprotein E	Homo sapiens	113-117
10391912-3	1999	In order to isolate thioredoxin targets related to these phenotypes, we prepared a C35S (Escherichia coli numbering) thioredoxin mutant to stabilize the intermediate disulfide bridged complex and we added a polyhistidine N-terminal extension in order to purify the complex rapidly.	Disulfides	166-175	thioredoxin 3	Arabidopsis thaliana	20-31
10336486-4	1999	In addition, reduction released a 120-kDa C-terminal MUC2 fragment, showing that proteolytic cleavage in this domain may occur and leave the fragment attached to the complex via disulfide bonds.	Disulfides	178-187	mucin 2, oligomeric mucus/gel-forming	Homo sapiens	53-57
10411467-4	1999	The obtained thiolated p(DMAEMA-co-AEMA) was conjugated to transferrin (Tf) or the F(ab") fragment of mAb 323/A3 via a disulfide linkage.	Disulfides	119-128	transferrin	Homo sapiens	59-70
10411467-4	1999	The obtained thiolated p(DMAEMA-co-AEMA) was conjugated to transferrin (Tf) or the F(ab") fragment of mAb 323/A3 via a disulfide linkage.	Disulfides	119-128	transferrin	Homo sapiens	72-74
10404027-5	1999	Western blot analysis showed that periostin is a disulfide linked 90 kDa protein secreted by osteoblasts and osteoblast-like cell lines.	Disulfides	49-58	periostin, osteoblast specific factor	Mus musculus	34-43
10422834-1	1999	Insulin-like growth factor (IGF-1) contains three disulfide bonds.	Disulfides	50-59	insulin like growth factor 1	Homo sapiens	28-33
10422834-2	1999	In the presence of denaturant and thiol catalyst, IGF-1 shuffles its native disulfide bonds and denatures to form a mixture of scrambled isomers.	Disulfides	76-85	insulin like growth factor 1	Homo sapiens	50-55
10387004-0	1999	Disulfide bridges in interleukin-8 probed using non-natural disulfide analogues: dissociation of roles in structure from function.	Disulfides	0-9	C-X-C motif chemokine ligand 8	Homo sapiens	21-34
10387004-0	1999	Disulfide bridges in interleukin-8 probed using non-natural disulfide analogues: dissociation of roles in structure from function.	Disulfides	60-69	C-X-C motif chemokine ligand 8	Homo sapiens	21-34
10387004-1	1999	The structural and functional roles of the two disulfide bridges in interleukin-8 (IL-8) were addressed using IL-8 analogues with covalently modified disulfide bridges.	Disulfides	47-56	C-X-C motif chemokine ligand 8	Homo sapiens	68-81
10387004-1	1999	The structural and functional roles of the two disulfide bridges in interleukin-8 (IL-8) were addressed using IL-8 analogues with covalently modified disulfide bridges.	Disulfides	47-56	C-X-C motif chemokine ligand 8	Homo sapiens	83-87
10387004-1	1999	The structural and functional roles of the two disulfide bridges in interleukin-8 (IL-8) were addressed using IL-8 analogues with covalently modified disulfide bridges.	Disulfides	150-159	C-X-C motif chemokine ligand 8	Homo sapiens	83-87
10387004-1	1999	The structural and functional roles of the two disulfide bridges in interleukin-8 (IL-8) were addressed using IL-8 analogues with covalently modified disulfide bridges.	Disulfides	150-159	C-X-C motif chemokine ligand 8	Homo sapiens	110-114
10387004-6	1999	Modification to the disulfide bridge between cysteines 9 and 50 had only a modest effect on IL-8 function.	Disulfides	20-29	C-X-C motif chemokine ligand 8	Homo sapiens	92-96
10390351-0	1999	Removal of the conserved disulfide bridges from the scFv fragment of an antibody: effects on folding kinetics and aggregation.	Disulfides	25-34	immunglobulin heavy chain variable region	Homo sapiens	52-56
10390351-1	1999	Fluorescence measurements and H/2H exchange experiments monitored by mass spectrometry have been applied to investigate the influence of the conserved disulfide bridges on the folding behavior and in vitro aggregation properties of the scFv fragment of the antibody hu4D5-8.	Disulfides	151-160	immunglobulin heavy chain variable region	Homo sapiens	236-240
10524776-0	1999	The intermolecular disulfide bridge of human glial cell line-derived neurotrophic factor: its selective reduction and biological activity of the modified protein.	Disulfides	19-28	glial cell derived neurotrophic factor	Homo sapiens	45-88
10415716-1	1999	Differences in proteinase susceptibility between free TIMP-1 and the TIMP-1-MMP-3 complex and mutagenesis studies suggested that the residues around the disulfide bond between Cys1 and Cys70 in TIMP-1 may interact with MMPs.	Disulfides	153-162	TIMP metallopeptidase inhibitor 1	Homo sapiens	54-60
10415716-1	1999	Differences in proteinase susceptibility between free TIMP-1 and the TIMP-1-MMP-3 complex and mutagenesis studies suggested that the residues around the disulfide bond between Cys1 and Cys70 in TIMP-1 may interact with MMPs.	Disulfides	153-162	TIMP metallopeptidase inhibitor 1	Homo sapiens	69-75
10415716-1	1999	Differences in proteinase susceptibility between free TIMP-1 and the TIMP-1-MMP-3 complex and mutagenesis studies suggested that the residues around the disulfide bond between Cys1 and Cys70 in TIMP-1 may interact with MMPs.	Disulfides	153-162	matrix metallopeptidase 3	Homo sapiens	76-81
10415716-1	1999	Differences in proteinase susceptibility between free TIMP-1 and the TIMP-1-MMP-3 complex and mutagenesis studies suggested that the residues around the disulfide bond between Cys1 and Cys70 in TIMP-1 may interact with MMPs.	Disulfides	153-162	TIMP metallopeptidase inhibitor 1	Homo sapiens	69-75
16127603-1	1999	The endothelins are a family of three potent vasoactive peptides, ET-1, -2 and -3, which comprise 21 amino acids and contain two disulfide bridges between cysteine residues.	Disulfides	129-138	endothelin 1	Homo sapiens	4-15
16127603-1	1999	The endothelins are a family of three potent vasoactive peptides, ET-1, -2 and -3, which comprise 21 amino acids and contain two disulfide bridges between cysteine residues.	Disulfides	129-138	endothelin 1	Homo sapiens	66-81
10350478-4	1999	Rhodopsin mutants containing these disulfides demonstrate nativelike absorption spectra and light-dependent activation of transducin, suggesting that large movements on the extracellular side of TM5 with respect to TM6 are not required for receptor activation.	Disulfides	35-45	rhodopsin	Homo sapiens	0-9
10329650-9	1999	Analogous with IGFBP-3, IGFBP-5, and IGFBP-6, Cys9-Cys11 and Cys10-Cys12 of IGFBP-1 are also disulfide-linked.	Disulfides	93-102	insulin like growth factor binding protein 5	Homo sapiens	24-31
10371022-0	1999	Electrochemical studies of cytochrome c disulfide at gold electrodes.	Disulfides	40-49	cytochrome c, somatic	Homo sapiens	27-39
10371022-1	1999	The electrochemistry of disulfide in cytochrome c on gold electrodes was reported.	Disulfides	24-33	cytochrome c, somatic	Homo sapiens	37-49
10371022-3	1999	Disulfide bonds in cytochrome c were strongly adsorbed onto the surface of gold electrodes and caused slow rate of electron transfer of the heme group.	Disulfides	0-9	cytochrome c, somatic	Homo sapiens	19-31
10371022-4	1999	It was found that the presence of disulfides in cytochrome c was responsible for the lack of electrochemical response of the heme group on a gold electrode.	Disulfides	34-44	cytochrome c, somatic	Homo sapiens	48-60
10069970-7	1999	A close comparison of A. albimanus salivary peroxidase with canine myeloperoxidase, for which the crystal structure is known, showed that all six disulfide bridges were conserved and demonstrated identity for all five residues associated with a Ca2+-binding site.	Disulfides	146-155	myeloperoxidase	Canis lupus familiaris	67-82
10356266-3	1999	The reduced lysozyme lacking disulfide bonds was found to have a property similar to that of the molten globule state in terms of its local hydrophobicity, which was determined with the aqueous two-phase partitioning method.	Disulfides	30-39	lysozyme	Homo sapiens	13-21
10356266-4	1999	The reduced lysozyme was more clearly retarded on the ILC column than the native and 1 M guanidinium hydrochloride (GuHCl)-treated lysozymes with intact disulfide bonds.	Disulfides	154-163	lysozyme	Homo sapiens	13-21
10187802-3	1999	The large interaction interface in the TIMP-1.MMP-3 complex includes a contiguous region of TIMP-1 around the disulfide bond between Cys1 and Cys70 that inserts into the active site of MMP-3.	Disulfides	110-119	TIMP metallopeptidase inhibitor 1	Homo sapiens	39-45
10187802-3	1999	The large interaction interface in the TIMP-1.MMP-3 complex includes a contiguous region of TIMP-1 around the disulfide bond between Cys1 and Cys70 that inserts into the active site of MMP-3.	Disulfides	110-119	matrix metallopeptidase 3	Homo sapiens	46-51
10187802-3	1999	The large interaction interface in the TIMP-1.MMP-3 complex includes a contiguous region of TIMP-1 around the disulfide bond between Cys1 and Cys70 that inserts into the active site of MMP-3.	Disulfides	110-119	TIMP metallopeptidase inhibitor 1	Homo sapiens	92-98
10187802-3	1999	The large interaction interface in the TIMP-1.MMP-3 complex includes a contiguous region of TIMP-1 around the disulfide bond between Cys1 and Cys70 that inserts into the active site of MMP-3.	Disulfides	110-119	matrix metallopeptidase 3	Homo sapiens	185-190
10209036-0	1999	SHP2-interacting transmembrane adaptor protein (SIT), a novel disulfide-linked dimer regulating human T cell activation.	Disulfides	62-71	signaling threshold regulating transmembrane adaptor 1	Homo sapiens	0-46
10209036-0	1999	SHP2-interacting transmembrane adaptor protein (SIT), a novel disulfide-linked dimer regulating human T cell activation.	Disulfides	62-71	signaling threshold regulating transmembrane adaptor 1	Homo sapiens	48-51
10209036-3	1999	SIT is a disulfide-linked homodimeric glycoprotein that is expressed in lymphocytes.	Disulfides	9-18	signaling threshold regulating transmembrane adaptor 1	Homo sapiens	0-3
10092664-0	1999	A disulfide-bridged mutant of natriuretic peptide receptor-A displays constitutive activity.	Disulfides	2-11	natriuretic peptide receptor 1	Homo sapiens	30-60
10092664-6	1999	Since NPR-A displays a pair of juxtamembrane cysteines separated by 8 residues, we hypothesized that the removal of one of those cysteines would leave the other unpaired and reactive, thus susceptible to form an interchain disulfide bridge and to favor the dimeric interactions.	Disulfides	223-232	natriuretic peptide receptor 1	Homo sapiens	6-11
10085090-10	1999	Disulfide-dependent dimerization may be a physiologically significant regulatory mechanism controlling S100A8-provoked leukocyte recruitment.	Disulfides	0-9	S100 calcium binding protein A8 (calgranulin A)	Mus musculus	103-109
10085090-4	1999	Electrospray mass spectrometry and SDS-polyacrylamide gel electrophoresis analysis indicated that low concentrations of hypochlorite (40 microM) converted 70-80% of S100A8 to the disulfide-linked homodimer.	Disulfides	179-188	S100 calcium binding protein A8 (calgranulin A)	Mus musculus	165-171
10077638-7	1999	ORFV2-VEGF was found to be a disulfide-linked homodimer with a subunit of approximately 25 kDa.	Disulfides	29-38	vascular endothelial growth factor A	Homo sapiens	6-10
9951525-0	1999	Probing the disulfide folding pathway of insulin-like growth factor-I.	Disulfides	12-21	insulin like growth factor 1	Homo sapiens	41-69
9951525-2	1999	This problem is exemplified by insulin-like growth factor (IGF)-I which when refolded in vitro produces the native three-disulfide structure, an alternative structure with mispaired disulfide bonds and other isomeric forms.	Disulfides	121-130	insulin like growth factor 1	Homo sapiens	31-65
9951525-6	1999	In addition to non-native intermediates, three native-like intermediates were identified, that appear to have a major role in the in vitro refolding pathway of Long-[Arg3]IGF-I; a single-disulfide Cys18-Cys61 intermediate, an intermediate with Cys18-Cys61 and Cys6-Cys48 disulfide bonds and another with Cys18-Cys61 and Cys47-Cys52 disulfide bonds.	Disulfides	187-196	insulin like growth factor 1	Homo sapiens	171-176
9951525-6	1999	In addition to non-native intermediates, three native-like intermediates were identified, that appear to have a major role in the in vitro refolding pathway of Long-[Arg3]IGF-I; a single-disulfide Cys18-Cys61 intermediate, an intermediate with Cys18-Cys61 and Cys6-Cys48 disulfide bonds and another with Cys18-Cys61 and Cys47-Cys52 disulfide bonds.	Disulfides	271-280	insulin like growth factor 1	Homo sapiens	171-176
9951525-6	1999	In addition to non-native intermediates, three native-like intermediates were identified, that appear to have a major role in the in vitro refolding pathway of Long-[Arg3]IGF-I; a single-disulfide Cys18-Cys61 intermediate, an intermediate with Cys18-Cys61 and Cys6-Cys48 disulfide bonds and another with Cys18-Cys61 and Cys47-Cys52 disulfide bonds.	Disulfides	271-280	insulin like growth factor 1	Homo sapiens	171-176
10077597-1	1999	We recently demonstrated that the G protein-coupled, extracellular calcium-sensing receptor (CaR) forms disulfide-linked dimers.	Disulfides	104-113	calcium sensing receptor	Homo sapiens	67-91
10077638-7	1999	ORFV2-VEGF was found to be a disulfide-linked homodimer with a subunit of approximately 25 kDa.	Disulfides	29-38	superoxide dismutase 1	Homo sapiens	46-55
10077597-1	1999	We recently demonstrated that the G protein-coupled, extracellular calcium-sensing receptor (CaR) forms disulfide-linked dimers.	Disulfides	104-113	calcium sensing receptor	Homo sapiens	93-96
10066758-2	1999	Although several of the early steps leading to fibronectin deposition have been identified, the mechanisms leading to the accumulation of fibronectin in disulfide-stabilized multimers are largely unknown.	Disulfides	153-162	fibronectin 1	Homo sapiens	138-149
10066782-0	1999	Disulfide bond structure and N-glycosylation sites of the extracellular domain of the human interleukin-6 receptor.	Disulfides	0-9	interleukin 6 receptor	Homo sapiens	92-114
10066758-3	1999	Disulfide-stabilized fibronectin multimers are thought to arise through intra- or intermolecular disulfide exchange.	Disulfides	0-9	fibronectin 1	Homo sapiens	21-32
10066758-3	1999	Disulfide-stabilized fibronectin multimers are thought to arise through intra- or intermolecular disulfide exchange.	Disulfides	97-106	fibronectin 1	Homo sapiens	21-32
10066758-5	1999	The twelfth type I module of fibronectin (I12) contains a Cys-X-X-Cys motif, suggesting that fibronectin may have the intrinsic ability to catalyze disulfide bond rearrangement.	Disulfides	148-157	fibronectin 1	Homo sapiens	29-40
10066758-5	1999	The twelfth type I module of fibronectin (I12) contains a Cys-X-X-Cys motif, suggesting that fibronectin may have the intrinsic ability to catalyze disulfide bond rearrangement.	Disulfides	148-157	fibronectin 1	Homo sapiens	93-104
10051572-1	1999	The disulfide bond between Cys-110 and Cys-187 in the intradiscal domain is required for correct folding in vivo and function of mammalian rhodopsin.	Disulfides	4-13	rhodopsin	Homo sapiens	139-148
10051572-2	1999	Misfolding in rhodopsin, characterized by the loss of ability to bind 11-cis-retinal, has been shown to be caused by an intradiscal disulfide bond different from the above native disulfide bond.	Disulfides	132-141	rhodopsin	Homo sapiens	14-23
10052952-0	1999	Conformational unfolding studies of three-disulfide mutants of bovine pancreatic ribonuclease A and the coupling of proline isomerization to disulfide redox reactions.	Disulfides	42-51	ribonuclease pancreatic	Bos taurus	81-95
10052953-11	1999	Finally, the cysteines constituting the PON1 disulfide bond (C41 and C352) were essential, but the glycan chains linked to Asn 252 and 323 were not essential for PON1 secretion and activity.	Disulfides	45-54	paraoxonase 1	Homo sapiens	40-44
10051572-2	1999	Misfolding in rhodopsin, characterized by the loss of ability to bind 11-cis-retinal, has been shown to be caused by an intradiscal disulfide bond different from the above native disulfide bond.	Disulfides	179-188	rhodopsin	Homo sapiens	14-23
10051572-6	1999	C185A allows the formation of a C110-C187 disulfide bond, with wild-type-like rhodopsin phenotype.	Disulfides	42-51	rhodopsin	Homo sapiens	78-87
10319440-3	1999	Our previous studies with specific antibodies against L-chain and P25 have shown that L-chain and H-chain are linked by disulfide bond(s) but P25 is not covalently linked to H-chain.	Disulfides	120-129	fibrohexamerin	Bombyx mori	66-69
9920905-7	1999	Analysis of wild-type MBP-A and MBP-A containing the substitution Cys6 --&gt; Ser suggests that polypeptides within each trimeric structural unit are mostly linked by disulfide bonds between cysteine residues at positions 13 and 18 arranged in an asymmetrical configuration.	Disulfides	167-176	mannose binding lectin 1	Rattus norvegicus	32-37
10495900-0	1999	[Directed and spontaneous disulfide bond closure using hydrogen peroxide in the synthesis of endothelins-1 and -3].	Disulfides	26-35	endothelin 1	Homo sapiens	93-113
10099541-1	1999	Recombinant human interleukin-6 (hIL-6), a pleiotropic cytokine containing two intramolecular disulfide bonds, was expressed in Escherichia coli as an insoluble inclusion body, before being refolded and purified in high yield providing sufficient qualities for clinical use.	Disulfides	94-103	interleukin 6	Homo sapiens	33-38
10099541-2	1999	Quantitative reconstitution of the native disulfide bonds of hIL-6 from the fully denatured E. coli extracts could be performed by glutathione-assisted oxidation in a completely denaturating condition (6M guanidinium chloride) at protein concentrations higher than 1 mg/mL, preventing aggregation of reduced hIL-6.	Disulfides	42-51	interleukin 6	Homo sapiens	61-66
10099541-2	1999	Quantitative reconstitution of the native disulfide bonds of hIL-6 from the fully denatured E. coli extracts could be performed by glutathione-assisted oxidation in a completely denaturating condition (6M guanidinium chloride) at protein concentrations higher than 1 mg/mL, preventing aggregation of reduced hIL-6.	Disulfides	42-51	interleukin 6	Homo sapiens	308-313
10024465-11	1999	The absorption of 250-nm light by disulfide bonds also provided information regarding the proper folding of rat prolactin and bovine alpha-lactalbumin.	Disulfides	34-43	prolactin	Rattus norvegicus	112-121
10089129-7	1999	The purified recombinant rat IL-6 had a molecular mass of 21 756.38+/-0.25 Da, which is within 0.01% of the predicted value, taking into account cleavage of the N-terminal methionine residue and the formation of two disulfide bridges.	Disulfides	216-225	interleukin 6	Rattus norvegicus	29-33
9926405-5	1999	Furthermore, changes of the pattern of protonated molecules caused by temperature effects and by protein unfolding due to disulfide bond reduction have been studied with the model proteins cytochrome c and hen eggwhite lysozyme.	Disulfides	122-131	cytochrome c, somatic	Homo sapiens	189-201
10333293-3	1999	Bactericidal/permeability-increasing protein, which is a member of the same gene family, contains an essential disulfide bond between Cys135 and Cys175; these residues, which correspond to Cys129 and Cys168 in PLTP, are conserved among all known members of the gene family.	Disulfides	111-120	phospholipid transfer protein	Homo sapiens	210-214
10195449-4	1999	We previously confirmed that the synthetic EGF-like peptides SDGF(38-80) and AR(44-84), corresponding to the EGF-like domain of mouse SDGF and human AR, respectively, formed similar disulfide bond patterns to that of EGF.	Disulfides	182-191	amphiregulin	Mus musculus	61-65
10195449-4	1999	We previously confirmed that the synthetic EGF-like peptides SDGF(38-80) and AR(44-84), corresponding to the EGF-like domain of mouse SDGF and human AR, respectively, formed similar disulfide bond patterns to that of EGF.	Disulfides	182-191	amphiregulin	Mus musculus	77-79
10024465-7	1999	Human growth hormone, 22 kDa; human prolactin, 23 kDa; and bovine prolactin, 23 kDa, contain two, three, and three disulfides, respectively, and are folded correctly by air oxidation performed during renaturation under alkaline conditions.	Disulfides	115-125	growth hormone 1	Homo sapiens	6-20
10024465-7	1999	Human growth hormone, 22 kDa; human prolactin, 23 kDa; and bovine prolactin, 23 kDa, contain two, three, and three disulfides, respectively, and are folded correctly by air oxidation performed during renaturation under alkaline conditions.	Disulfides	115-125	prolactin	Homo sapiens	36-45
10025946-0	1999	Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions.	Disulfides	82-92	insulin like growth factor 1	Homo sapiens	0-36
10024465-7	1999	Human growth hormone, 22 kDa; human prolactin, 23 kDa; and bovine prolactin, 23 kDa, contain two, three, and three disulfides, respectively, and are folded correctly by air oxidation performed during renaturation under alkaline conditions.	Disulfides	115-125	prolactin	Bos taurus	66-75
10024465-8	1999	Proper disulfide bond formation of rat prolactin, 23 kDa, containing three disulfide bonds required the addition of a reducing agent at the initiation of renaturation.	Disulfides	7-16	prolactin	Rattus norvegicus	39-48
10024465-8	1999	Proper disulfide bond formation of rat prolactin, 23 kDa, containing three disulfide bonds required the addition of a reducing agent at the initiation of renaturation.	Disulfides	75-84	prolactin	Rattus norvegicus	39-48
10025946-1	1999	Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al.	Disulfides	81-90	insulin like growth factor 1	Homo sapiens	0-34
10025946-4	1999	The results indicate that the previously described thermodynamic disulfide exchange folding problem of IGF-I in vitro is also present in vivo.	Disulfides	65-74	insulin like growth factor 1	Homo sapiens	103-108
10025946-5	1999	Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance.	Disulfides	49-58	insulin like growth factor 1	Homo sapiens	82-87
10025946-5	1999	Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance.	Disulfides	174-183	insulin like growth factor 1	Homo sapiens	82-87
9989245-9	1999	MPP(+)-induced pore opening and cytochrome c release were blocked by CsA, the Ca2+ uniporter inhibitor ruthenium red, the hydrophobic disulfide reagent N-ethylmaleimide, butacaine, and the free radical scavenging enzymes catalase and superoxide dismutase.	Disulfides	134-143	cytochrome c, somatic	Homo sapiens	32-44
9882436-0	1999	Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III.	Disulfides	8-17	thrombospondin 1	Homo sapiens	85-101
10226519-1	1999	We have deleted the interchain disulfide bonds in a chimeric anti-CEA antibody (chT84.66) by mutating two cysteines in the heavy chain to glycine residues.	Disulfides	31-40	carcinoembryonic antigen gene family	Mus musculus	66-69
9882436-0	1999	Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III.	Disulfides	8-17	coagulation factor II, thrombin	Homo sapiens	107-115
9882436-12	1999	In summary, these data are consistent with a role for PDI-catalyzed formation of disulfide-linked complexes of TSP with other proteins.	Disulfides	81-90	thrombospondin 1	Homo sapiens	111-114
9886297-5	1999	Finally, p11 forms a disulfide-linked tetramer in both types of crystals thus suggesting a model for an oxidized form of other S100 proteins that have been found in the extracellular milieu.	Disulfides	21-30	S100 calcium binding protein A10	Homo sapiens	9-12
10609876-7	1999	Inactivation of this regulator by a TNF-induced reduction of NAD(P)H levels and/or formation of intraprotein disulfides would be responsible for ROS generation.	Disulfides	109-119	tumor necrosis factor	Mus musculus	36-39
9852116-7	1998	A disulfide bond between Cys18 and Cys138 using a fully N-deglycosylated mutant of human angiotensinogen was identified by tryptic digestion and mass spectrometry.	Disulfides	2-11	angiotensinogen	Homo sapiens	89-104
9886286-4	1999	This fold is primarily dictated by disulfide bonds formed by eight conserved cysteines, with a characteristic spacing, and thus is likely to be shared by most of the type I and II receptors for the TGFbeta family.	Disulfides	35-44	transforming growth factor beta 1	Homo sapiens	198-205
9922141-2	1998	Libraries of short disulfide-constrained peptides yielded three distinct classes of peptides that bind to the receptor-binding domain of VEGF with micromolar affinities.	Disulfides	19-28	vascular endothelial growth factor A	Homo sapiens	137-141
9920403-6	1998	The stable IgA/SC complex consists of a structure with a disulfide bond between IgA and SC apparently in equilibrium with a structure in which this bond is absent.	Disulfides	57-66	CD79a molecule	Homo sapiens	11-14
9920403-6	1998	The stable IgA/SC complex consists of a structure with a disulfide bond between IgA and SC apparently in equilibrium with a structure in which this bond is absent.	Disulfides	57-66	CD79a molecule	Homo sapiens	80-83
9920403-10	1998	Our results support a mechanism for optimal binding of IgA to SC, that can occur both in vitro and in vivo, in which a thiol disulfide interchange occurs between a free IgA thiol and a sensitive SC disulfide following the initial non-covalent interaction.	Disulfides	125-134	CD79a molecule	Homo sapiens	55-58
9920403-10	1998	Our results support a mechanism for optimal binding of IgA to SC, that can occur both in vitro and in vivo, in which a thiol disulfide interchange occurs between a free IgA thiol and a sensitive SC disulfide following the initial non-covalent interaction.	Disulfides	125-134	CD79a molecule	Homo sapiens	169-172
9826515-1	1998	Air re-oxidation of fully reduced human endothelin-1 under optimized conditions yields the natural isomer with parallel disulfide bridges and the non-natural isomer with crossed disulfide bridges at a ratio of 3:1.	Disulfides	120-129	endothelin 1	Homo sapiens	40-52
9862285-3	1998	In these cytochrome P-450-dependent lipid peroxidation systems, pretreatment of microsome with trisulfide derivatives (cystine trisulfide and thiocyclam) significantly inhibited TBA-RS formation and oxygen consumption compared with disulfide or thiol analogs (cystine, nereistoxin, or cysteine).	Disulfides	232-241	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	9-25
9826515-1	1998	Air re-oxidation of fully reduced human endothelin-1 under optimized conditions yields the natural isomer with parallel disulfide bridges and the non-natural isomer with crossed disulfide bridges at a ratio of 3:1.	Disulfides	178-187	endothelin 1	Homo sapiens	40-52
9843414-1	1998	Rat SP-A is a heterooligomer of two closely related isoforms, that requires interchain disulfide linkage for several functions including SP-A-mediated phospholipid vesicle aggregation and modulation of surfactant secretion and uptake by isolated alveolar type II cells.	Disulfides	87-96	surfactant protein A1	Rattus norvegicus	4-8
9843414-2	1998	While the Cys6 disulfide bond of rat SP-A is known to be critical for function, the importance of the second interchain disulfide linkage within the N-terminal Isoleucine-3-Lysine-Cysteine-1 (IKC) sequence of the alternatively processed isoform is not clear.	Disulfides	15-24	surfactant protein A1	Rattus norvegicus	37-41
9804847-6	1998	To characterize this interaction, we studied the binding of the thrombin-cleaved N-terminal disulfide knot of fibrin (NDSK II), a dimeric fragment with exposed beta15-42, to HUVEC in three separate assay systems.	Disulfides	92-101	coagulation factor II, thrombin	Homo sapiens	64-72
9826543-4	1998	The candidates that might form disulfide bonds with actin were identified by monoclonal antibody to be GpIIb and/or GpIIIa.	Disulfides	31-40	integrin subunit beta 3	Homo sapiens	116-122
9787167-0	1998	Formation of the human fibrinogen subclass fib420: disulfide bonds and glycosylation in its unique (alphaE chain) domains.	Disulfides	51-60	fibrinogen beta chain	Homo sapiens	23-33
9799507-7	1998	Determination of the C-terminus of soluble ACE-JMEGF revealed that, surprisingly, cleavage occurred at a Gly-Phe bond between the fifth and sixth cysteines within the third disulfide loop of the EGF-like domain.	Disulfides	173-182	angiotensin-converting enzyme	Cricetulus griseus	43-46
9784253-1	1998	Human glial cell line-derived neurotrophic factor is a single polypeptide of 134 amino acids and functions as a disulfide-linked dimer.	Disulfides	112-121	glial cell derived neurotrophic factor	Homo sapiens	6-49
9737972-0	1998	Disulfide bonding and cysteine accessibility in the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluRD.	Disulfides	0-9	glutamate ionotropic receptor AMPA type subunit 4	Homo sapiens	126-131
9737972-4	1998	Using biochemical techniques, this disulfide is shown to exist in the ligand-binding domain of the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor subunit GluRD, although GluRD homomeric receptors are not modulated by DTT.	Disulfides	35-44	glutamate ionotropic receptor AMPA type subunit 4	Homo sapiens	180-185
9737972-4	1998	Using biochemical techniques, this disulfide is shown to exist in the ligand-binding domain of the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor subunit GluRD, although GluRD homomeric receptors are not modulated by DTT.	Disulfides	35-44	glutamate ionotropic receptor AMPA type subunit 4	Homo sapiens	196-201
9710621-0	1998	Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.	Disulfides	39-48	erb-b2 receptor tyrosine kinase 2	Homo sapiens	14-17
9751809-3	1998	MOX maintains many of the structural features of DBH, as evidenced by the retention of most of the disulfide linkages and all of the peptidyl ligands to the active site copper atoms.	Disulfides	99-108	dopamine beta hydroxylase	Mus musculus	49-52
9710621-0	1998	Activation of Neu (ErbB-2) mediated by disulfide bond-induced dimerization reveals a receptor tyrosine kinase dimer interface.	Disulfides	39-48	erb-b2 receptor tyrosine kinase 2	Homo sapiens	19-25
9725916-3	1998	Disulfide bonding between LAP and latent TGF-beta-binding protein (LTBP) produces the most common form of latent TGF-beta, the large latent complex.	Disulfides	0-9	transforming growth factor beta 1	Homo sapiens	26-29
9724700-0	1998	Molecular localization of a redox-modulated process regulating plant mitochondrial electron transport Using in organellar assays, we found that significant tobacco alternative oxidase (AOX) activity is dependent on both reduction of a putative regulatory disulfide bond and the presence of pyruvate, which may interact with a Cys sulfhydryl. This redox modulation and pyruvate activation thus may be important in determining the partitioning of electrons to AOX in vivo.	Disulfides	256-265	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	165-184
9725916-3	1998	Disulfide bonding between LAP and latent TGF-beta-binding protein (LTBP) produces the most common form of latent TGF-beta, the large latent complex.	Disulfides	0-9	transforming growth factor beta 1	Homo sapiens	41-49
9725916-3	1998	Disulfide bonding between LAP and latent TGF-beta-binding protein (LTBP) produces the most common form of latent TGF-beta, the large latent complex.	Disulfides	0-9	transforming growth factor beta 1	Homo sapiens	113-121
9724700-0	1998	Molecular localization of a redox-modulated process regulating plant mitochondrial electron transport Using in organellar assays, we found that significant tobacco alternative oxidase (AOX) activity is dependent on both reduction of a putative regulatory disulfide bond and the presence of pyruvate, which may interact with a Cys sulfhydryl. This redox modulation and pyruvate activation thus may be important in determining the partitioning of electrons to AOX in vivo.	Disulfides	256-265	ubiquinol oxidase 1, mitochondrial	Nicotiana tabacum	186-189
9712858-5	1998	The misfolded LRP molecules migrate as high molecular weight aggregates under nonreducing SDS-polyacrylamide gel electrophoresis, suggesting the formation of intermolecular disulfide bonds.	Disulfides	173-182	LDL receptor related protein 1	Homo sapiens	14-17
9685721-1	1998	The binding constants between disulfide-intact or various disulfide-reduced bovine alpha-lactalbumins and an Escherichia coli chaperonin, GroEL, were determined by using the equilibrium dialysis method.	Disulfides	30-39	GroEL	Escherichia coli	138-143
9685721-1	1998	The binding constants between disulfide-intact or various disulfide-reduced bovine alpha-lactalbumins and an Escherichia coli chaperonin, GroEL, were determined by using the equilibrium dialysis method.	Disulfides	58-67	GroEL	Escherichia coli	138-143
9685721-6	1998	The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL.	Disulfides	10-19	GroEL	Escherichia coli	111-116
9685721-6	1998	The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL.	Disulfides	36-45	GroEL	Escherichia coli	111-116
9668102-4	1998	The thioredoxin domain of TRP32 has thioredoxin-like reducing activity, which can reduce the interchain disulfide bridges of insulin in vitro.	Disulfides	104-113	insulin	Homo sapiens	125-132
9685721-6	1998	The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL.	Disulfides	36-45	GroEL	Escherichia coli	324-329
9685721-6	1998	The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL.	Disulfides	36-45	GroEL	Escherichia coli	111-116
9685721-6	1998	The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL.	Disulfides	36-45	GroEL	Escherichia coli	324-329
9658097-0	1998	Moloney murine leukemia virus envelope protein subunits, gp70 and Pr15E, form a stable disulfide-linked complex.	Disulfides	87-96	embigin	Homo sapiens	57-61
9753780-10	1998	This disulfide bond(s) is essential for full XET activity.	Disulfides	5-14	xyloglucan:xyloglucosyl transferase 33	Arabidopsis thaliana	45-48
9703976-1	1998	Protein disulfide isomerase (PDI), the product of the essential PDI1 gene of Saccharomyces cerevisiae catalyzes oxidization of thiols, reduction of disulfide bonds, and isomerization of disulfides.	Disulfides	8-17	protein disulfide isomerase family A member 2	Homo sapiens	29-32
9703976-1	1998	Protein disulfide isomerase (PDI), the product of the essential PDI1 gene of Saccharomyces cerevisiae catalyzes oxidization of thiols, reduction of disulfide bonds, and isomerization of disulfides.	Disulfides	186-196	protein disulfide isomerase family A member 2	Homo sapiens	29-32
9658097-3	1998	We found that all cell-associated gp70 molecules are disulfide linked to Pr15E whereas only a small amount of free gp70 is released by the cells.	Disulfides	53-62	embigin	Homo sapiens	34-38
9658097-4	1998	The complexes were resistant to treatment with reducing agents in vivo, indicating that the presence and stability of the disulfide interaction between gp70 and Pr15E are not dependent on the cellular redox state.	Disulfides	122-131	embigin	Homo sapiens	152-156
9658097-7	1998	The possibility that alkylating agents induce the formation of the intersubunit disulfide linkage was excluded by showing that disulfide-linked gp70-Pr15E complexes exist in freshly made lysates of nonalkylated cells and that disruption of the complexes can be prevented by lowering the pH.	Disulfides	127-136	embigin	Homo sapiens	144-148
9658097-8	1998	Together, these data establish that gp70 and Pr15E form a stable disulfide-linked complex in vivo.	Disulfides	65-74	embigin	Homo sapiens	36-40
9668062-10	1998	This insoluble MUC2 mucin was recovered by immunoprecipitation after reduction of disulfide bonds.	Disulfides	82-91	mucin 2, oligomeric mucus/gel-forming	Homo sapiens	15-19
9657753-0	1998	Binding of factor VIII to von willebrand factor is enabled by cleavage of the von Willebrand factor propeptide and enhanced by formation of disulfide-linked multimers.	Disulfides	140-149	von Willebrand factor	Homo sapiens	26-47
9657753-9	1998	Our results indicate that high-affinity factor VIII binding sites are located on N-terminal disulfide-linked vWF subunits from which the propeptide has been cleaved.	Disulfides	92-101	von Willebrand factor	Homo sapiens	109-112
9657753-2	1998	Prior reports suggest that posttranslational modifications of vWF, including formation of N-terminal intersubunit disulfide bonds and subsequent cleavage of the propeptide, influence availability and/or affinity of factor VIII binding sites.	Disulfides	114-123	von Willebrand factor	Homo sapiens	62-65
9657753-3	1998	We found that deletion of the vWF propeptide produced a dimeric vWF molecule lacking N-terminal intersubunit disulfide bonds.	Disulfides	109-118	von Willebrand factor	Homo sapiens	30-33
9667953-5	1998	Upon partial reduction of human growth hormone (hGH) with dithiothreitol, its C-terminal disulfide bond between residues 182 and 189 was cleaved and the nascent thiol groups were modified with [125I]ASDPE to yield [125I]ASET-hGH [1-(thio-hGH)-2-(3"-[125I]iodo-5"-azidosalicylamido)ethane].	Disulfides	89-98	growth hormone 1	Homo sapiens	32-46
9688536-0	1998	Specific reduction of insulin disulfides by macrophage migration inhibitory factor (MIF) with glutathione and dihydrolipoamide: potential role in cellular redox processes.	Disulfides	30-40	insulin	Homo sapiens	22-29
9688536-3	1998	Here we further investigated this function by examining the reduction of insulin disulfides by wild-type human MIF (wtMIF) using various substrates, namely glutathione (GSH), dihydrolipoamide, L-cysteine, beta-mercaptoethanol and dithiothreitol.	Disulfides	81-91	insulin	Homo sapiens	73-80
9688536-6	1998	Reduction of insulin disulfides by MIF was closely dependent on the presence of the Cys57-Ala-Leu-Cys60 (CALC) motif-forming cysteines C57 and C60, whereas C81 was not involved (activities: 51+/-13%, 14+/-5%, and 70+/-12% of wtMIF, respectively, and 20+/-3% for the double mutant C57S/C60S).	Disulfides	21-31	insulin	Homo sapiens	13-20
9653039-4	1998	In order to understand the mechanism for formation of the native-like tertiary topology, we substituted alanine for each of the 23 buried residues in the alpha-helical domain of alpha-LA and determined the effect of these substitutions on the Ceff for formation of the 28-111 disulfide bond.	Disulfides	276-285	lactalbumin alpha	Homo sapiens	178-186
9692918-2	1998	However, it was able to activate a mutant malate dehydrogenase where only the most exposed disulfide was retained.	Disulfides	91-100	uncharacterized protein	Chlamydomonas reinhardtii	42-62
9675066-13	1998	These results indicated that KIVt9 couples to the Cys-apoB-100 peptides through a disulfide linkage.	Disulfides	82-91	apolipoprotein B	Homo sapiens	54-62
9684889-0	1998	Transition state in the folding of alpha-lactalbumin probed by the 6-120 disulfide bond.	Disulfides	73-82	lactalbumin alpha	Homo sapiens	35-52
9675066-2	1998	Lp(a) particles are generated through the formation of a disulfide bond between Cys4057 of kringle IV type 9, (KIVt9), of the multikringle apolipoprotein(a) [apo(a)] and a cysteine in apoB-100 low-density lipoprotein (LDL).	Disulfides	57-66	apolipoprotein B	Homo sapiens	184-192
9684889-1	1998	The guanidine hydrochloride concentration dependence of the folding and unfolding rate constants of a derivative of alpha-lactalbumin, in which the 6-120 disulfide bond is selectively reduced and S-carboxymethylated, was measured and compared with that of disulfide-intact alpha-lactalbumin.	Disulfides	154-163	lactalbumin alpha	Homo sapiens	116-133
9684889-1	1998	The guanidine hydrochloride concentration dependence of the folding and unfolding rate constants of a derivative of alpha-lactalbumin, in which the 6-120 disulfide bond is selectively reduced and S-carboxymethylated, was measured and compared with that of disulfide-intact alpha-lactalbumin.	Disulfides	256-265	lactalbumin alpha	Homo sapiens	116-133
9636055-4	1998	The isomer with the crossed disulfide pairing was a better thrombin inhibitor and was more strongly affected by calcium binding than the uncrossed [1-2, 3-4] isomer.	Disulfides	28-37	coagulation factor II, thrombin	Homo sapiens	59-67
9603957-13	1998	This ability of the amino-terminal region of mucin to aid in the assembly of multimers is consistent with its amino acid identities to the amino-terminal region of human von Willebrand factor, which also serves to form disulfide-linked multimers of this protein.	Disulfides	219-228	von Willebrand factor	Homo sapiens	170-191
9652114-0	1998	Rapid verification of disulfide linkages in recombinant human growth hormone by tandem column tryptic mapping.	Disulfides	22-31	growth hormone 1	Homo sapiens	62-76
9601051-1	1998	Lipoprotein(a) [Lp(a)] particle formation is a two-step process in which initial noncovalent interactions between apolipoprotein(a) [apo(a)] and the apolipoprotein B-100 (apoB-100) component of low-density lipoprotein (LDL) precede disulfide bond formation.	Disulfides	232-241	apolipoprotein B	Homo sapiens	149-169
9601051-1	1998	Lipoprotein(a) [Lp(a)] particle formation is a two-step process in which initial noncovalent interactions between apolipoprotein(a) [apo(a)] and the apolipoprotein B-100 (apoB-100) component of low-density lipoprotein (LDL) precede disulfide bond formation.	Disulfides	232-241	apolipoprotein B	Homo sapiens	171-179
9628846-2	1998	Amino acid residues 420-434 of the first disulfide loop of the sex hormone binding globulinlike domain of protein S are involved in the interaction of protein S with C4BP.	Disulfides	41-50	complement component 4 binding protein alpha	Homo sapiens	166-170
9631517-1	1998	The active N-terminal domain of the mouse tissue inhibitor of metalloproteinases-1 is a 14.1-kDa polypeptide with three disulfide bonds.	Disulfides	120-129	tissue inhibitor of metalloproteinase 1	Mus musculus	42-82
9652114-1	1998	An automated tryptic mapping method was developed for characterization of disulfide linkages in recombinant human growth hormone (rhGH).	Disulfides	74-83	growth hormone 1	Homo sapiens	114-128
9608841-2	1998	A genetically altered E. coli dihydrofolate reductase (DHFR-ASC) was attached to a carboxymethyldextran matrix layer covering the sensor surface of an SPR biosensor through a disulfide linkage at the engineered protein"s C-terminus.	Disulfides	175-184	dihydrofolate reductase	Escherichia coli	55-59
9637257-0	1998	An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly.	Disulfides	77-86	immunglobulin heavy chain variable region	Homo sapiens	33-37
9585534-1	1998	The extracellular domain of transmembrane Abeta amyloid precursor protein (APP) has a Cu(II) reducing activity upon Cu(II) binding associated with the formation of a new disulfide bridge.	Disulfides	170-179	amyloid beta precursor protein	Homo sapiens	48-73
9575190-6	1998	PCI has a special disulfide scaffold called a T-knot that is also present in several growth factors including EGF and transforming growth factor alpha.	Disulfides	18-27	tumor necrosis factor	Homo sapiens	118-150
9585571-0	1998	Kinetic folding pathway of a three-disulfide mutant of bovine pancreatic ribonuclease A missing the [40-95] disulfide bond.	Disulfides	35-44	ribonuclease pancreatic	Bos taurus	73-87
9585571-0	1998	Kinetic folding pathway of a three-disulfide mutant of bovine pancreatic ribonuclease A missing the [40-95] disulfide bond.	Disulfides	108-117	ribonuclease pancreatic	Bos taurus	73-87
9585571-3	1998	It was found that the disulfide intermediates formed during regeneration reach a steady-state distribution after a short period of preequilibration similar to that in the regeneration of wild-type RNase A.	Disulfides	22-31	ribonuclease pancreatic	Bos taurus	197-204
9637257-1	1998	A fully functional cysteine-free derivative of the intrinsically stable anti-HER2 scFv fragment hu4D5-8 was generated by replacing the disulfide forming cysteine residues in VH and VL with the amino acid combination valine-alanine in both domains.	Disulfides	135-144	erb-b2 receptor tyrosine kinase 2	Homo sapiens	77-81
9637257-1	1998	A fully functional cysteine-free derivative of the intrinsically stable anti-HER2 scFv fragment hu4D5-8 was generated by replacing the disulfide forming cysteine residues in VH and VL with the amino acid combination valine-alanine in both domains.	Disulfides	135-144	immunglobulin heavy chain variable region	Homo sapiens	82-86
9637257-3	1998	The thermodynamic stability of the disulfide-containing scFv of 8.1 kcal/mol is decreased upon complete reduction of both disulfides to 2.7 kcal/mol, while that of the valine-alanine variant is somewhat higher (about 3.8 kcal/ mol).	Disulfides	35-44	immunglobulin heavy chain variable region	Homo sapiens	56-60
9637257-3	1998	The thermodynamic stability of the disulfide-containing scFv of 8.1 kcal/mol is decreased upon complete reduction of both disulfides to 2.7 kcal/mol, while that of the valine-alanine variant is somewhat higher (about 3.8 kcal/ mol).	Disulfides	122-132	immunglobulin heavy chain variable region	Homo sapiens	56-60
9637257-4	1998	Our results suggest that, in principle, a disulfide-free fully functional derivative of any scFv can be obtained, as long as the corresponding disulfide-containing scFv has a high enough thermodynamic stability.	Disulfides	42-51	immunglobulin heavy chain variable region	Homo sapiens	92-96
9637257-4	1998	Our results suggest that, in principle, a disulfide-free fully functional derivative of any scFv can be obtained, as long as the corresponding disulfide-containing scFv has a high enough thermodynamic stability.	Disulfides	42-51	immunglobulin heavy chain variable region	Homo sapiens	164-168
9637257-4	1998	Our results suggest that, in principle, a disulfide-free fully functional derivative of any scFv can be obtained, as long as the corresponding disulfide-containing scFv has a high enough thermodynamic stability.	Disulfides	143-152	immunglobulin heavy chain variable region	Homo sapiens	92-96
9637257-4	1998	Our results suggest that, in principle, a disulfide-free fully functional derivative of any scFv can be obtained, as long as the corresponding disulfide-containing scFv has a high enough thermodynamic stability.	Disulfides	143-152	immunglobulin heavy chain variable region	Homo sapiens	164-168
9571241-9	1998	Thus, Grx1 and Grx2 function differently in the cell, and we suggest that glutaredoxins may act as one of the primary defenses against mixed disulfides formed following oxidative damage to proteins.	Disulfides	141-151	dithiol glutaredoxin GRX1	Saccharomyces cerevisiae S288C	6-10
9558384-2	1998	The truncated Aalpha-chain of fibrinogen Marburg is partly linked with albumin by a disulfide bond.	Disulfides	84-93	fibrinogen beta chain	Homo sapiens	30-40
9556602-0	1998	Disulfide bond structure of human epidermal growth factor receptor.	Disulfides	0-9	epidermal growth factor receptor	Homo sapiens	34-66
9572853-6	1998	The complex could be degraded to a fragment containing two disulfide-linked peptides from uPA, one of which included the active site Ser, while PAI-1 was left undegraded.	Disulfides	59-68	plasminogen activator, urokinase	Homo sapiens	90-93
9548568-0	1998	Mechanism of protein kinase CK2 association with nuclear matrix: role of disulfide bond formation.	Disulfides	73-82	casein kinase 2 beta	Rattus norvegicus	28-31
9605332-5	1998	We also report the crystal structure of the C[40, 95]A variant, which is an analog of the major rate-determining three-disulfide intermediate in the oxidative folding of RNase A, missing the 40-95 disulfide bond.	Disulfides	119-128	ribonuclease pancreatic	Bos taurus	170-177
9631401-8	1998	We postulate that the immediate extracellular domain of beta-sarcoglycan may be important for the assembly and/or maintenance of this complex, potentially mediated by disulfide-bond formation to another sarcoglycan via the single cysteine residue in that domain.	Disulfides	167-176	sarcoglycan beta	Homo sapiens	56-72
9605332-5	1998	We also report the crystal structure of the C[40, 95]A variant, which is an analog of the major rate-determining three-disulfide intermediate in the oxidative folding of RNase A, missing the 40-95 disulfide bond.	Disulfides	197-206	ribonuclease pancreatic	Bos taurus	170-177
9575986-9	1998	STC1 was a glycosylated, 42-kDa disulfide-linked dimer, with a high affinity for ConA.	Disulfides	32-41	stanniocalcin-1	Salmo salar	0-4
9548753-0	1998	Formation of native disulfide bonds in endothelin-1.	Disulfides	20-29	endothelin 1	Homo sapiens	39-51
9548753-2	1998	The [Lys-Arg]-endothelin-1 analogue (KR-ET-1) yields almost selectively the native disulfide pattern (96%), in contrast to endothelin-1 (ET-1) that gives at least 25% of the non-native disulfide pattern.	Disulfides	83-92	endothelin 1	Homo sapiens	14-26
9548753-2	1998	The [Lys-Arg]-endothelin-1 analogue (KR-ET-1) yields almost selectively the native disulfide pattern (96%), in contrast to endothelin-1 (ET-1) that gives at least 25% of the non-native disulfide pattern.	Disulfides	83-92	endothelin 1	Homo sapiens	40-44
9548753-2	1998	The [Lys-Arg]-endothelin-1 analogue (KR-ET-1) yields almost selectively the native disulfide pattern (96%), in contrast to endothelin-1 (ET-1) that gives at least 25% of the non-native disulfide pattern.	Disulfides	185-194	endothelin 1	Homo sapiens	14-26
9548753-2	1998	The [Lys-Arg]-endothelin-1 analogue (KR-ET-1) yields almost selectively the native disulfide pattern (96%), in contrast to endothelin-1 (ET-1) that gives at least 25% of the non-native disulfide pattern.	Disulfides	185-194	endothelin 1	Homo sapiens	40-44
9548753-11	1998	Assuming that the formation of disulfide bonds occurs in a thermodynamically controlled step, we have hypothesized that the Arg(-1)-Asp8 salt bridge and concomitant interactions could be responsible for the increase in yield of the native isomer of KR-ET-1.	Disulfides	31-40	endothelin 1	Homo sapiens	252-256
9548753-16	1998	Altogether, these results allow us to hypothesize that the salt bridge between two highly conserved residues, one belonging to the prosequence [Arg(-1)] and the other to the mature sequence [Asp8], is involved in the formation of the native disulfide isomer of ET-1.	Disulfides	241-250	endothelin 1	Homo sapiens	261-265
9548753-17	1998	The involvement of the prosequence in the formation of the native disulfide isomer strongly suggests that, in the maturation pathway of ET-1, cleavage of the Arg52-Cys53 amide bond occurs after native disulfide bond formation.	Disulfides	66-75	endothelin 1	Homo sapiens	136-140
9548753-17	1998	The involvement of the prosequence in the formation of the native disulfide isomer strongly suggests that, in the maturation pathway of ET-1, cleavage of the Arg52-Cys53 amide bond occurs after native disulfide bond formation.	Disulfides	201-210	endothelin 1	Homo sapiens	136-140
9521769-11	1998	The formation of the 65-72 disulfide loop in the regeneration of wild-type RNase A appears to facilitate the subsequent folding events.	Disulfides	27-36	ribonuclease pancreatic	Bos taurus	75-82
9560003-1	1998	Ten overlapping 15-mer peptides, spanning the entire inner disulfide loop of human C-reactive protein (residues 36-97), were used to isolate a potent inhibitor of the enzymes human leukocyte elastase and human leukocyte cathepsin G, which are associated with chronic inflammatory tissue damage.	Disulfides	59-68	C-reactive protein	Homo sapiens	83-101
9521769-0	1998	Regeneration of three-disulfide mutants of bovine pancreatic ribonuclease A missing the 65-72 disulfide bond: characterization of a minor folding pathway of ribonuclease A and kinetic roles of Cys65 and Cys72.	Disulfides	22-31	ribonuclease pancreatic	Bos taurus	61-75
9587963-7	1998	Deglycosylation of IFN-beta-1a produced a decrease in total activity that was primarily caused by the formation of an insoluble disulfide-linked IFN precipitate.	Disulfides	128-137	interferon alpha 1	Homo sapiens	19-22
9587963-7	1998	Deglycosylation of IFN-beta-1a produced a decrease in total activity that was primarily caused by the formation of an insoluble disulfide-linked IFN precipitate.	Disulfides	128-137	interferon alpha 1	Homo sapiens	145-148
9488661-7	1998	The results suggest that p53 can form disulfides and that these disulfides must be reduced in order for the protein to function as a transcription factor.	Disulfides	38-48	tumor protein p53	Homo sapiens	25-28
9516417-0	1998	Functional analysis of disulfide linkages clustered within the amino terminus of human apolipoprotein B.	Disulfides	23-32	apolipoprotein B	Homo sapiens	87-103
9516417-1	1998	We tested the involvement of N-terminal six disulfide bonds (Cys-1 through Cys-12) of human apolipoprotein (apo) B in the assembly and secretion of lipoproteins using two C-terminal-truncated apoB variants, namely B50 and B18.	Disulfides	44-53	apolipoprotein B	Homo sapiens	92-114
9516417-7	1998	Expression of these mutants showed that disruption of disulfide bond formation within Cys-5 to Cys-8 diminished apoB secretion, whereas within Cys-1 to Cys-4 or Cys-9 to Cys-12 had lesser or no effect.	Disulfides	54-63	apolipoprotein B	Homo sapiens	112-116
9521695-0	1998	Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike three-disulfide intermediates involved in separate pathways.	Disulfides	89-98	ribonuclease pancreatic	Bos taurus	34-48
9521695-1	1998	During the regeneration of bovine pancreatic ribonuclease A (RNase A) from the reduced to the native form with mixtures of oxidized and reduced dithiothreitol at 25 degrees C, pH 8.0, the disulfide-containing protein intermediates achieve a steady-state distribution.	Disulfides	188-197	ribonuclease pancreatic	Bos taurus	45-59
9521696-1	1998	The regeneration of bovine pancreatic ribonuclease A (RNase A) from the reduced to the native form with mixtures of oxidized and reduced dithiothreitol at 25 degrees C, pH 8.0, proceeds through two separate pathways in which separate nativelike three-disulfide species are populated.	Disulfides	251-260	ribonuclease pancreatic	Bos taurus	38-52
9521696-1	1998	The regeneration of bovine pancreatic ribonuclease A (RNase A) from the reduced to the native form with mixtures of oxidized and reduced dithiothreitol at 25 degrees C, pH 8.0, proceeds through two separate pathways in which separate nativelike three-disulfide species are populated.	Disulfides	251-260	ribonuclease pancreatic	Bos taurus	54-61
9521769-0	1998	Regeneration of three-disulfide mutants of bovine pancreatic ribonuclease A missing the 65-72 disulfide bond: characterization of a minor folding pathway of ribonuclease A and kinetic roles of Cys65 and Cys72.	Disulfides	94-103	ribonuclease pancreatic	Bos taurus	61-75
9521769-1	1998	The oxidative regeneration pathways of two three-disulfide mutants of bovine pancreatic ribonuclease A (RNase A) missing the 65-72 disulfide bond, [C65S,C72S] and [C65A,C72A], have been studied by using oxidized dithiothreitol (DTTox) as an oxidizing agent and 2-aminoethylmethanethiosulfonate (AEMTS) as a thiol-blocking agent at 25 degrees C and pH 8.0.	Disulfides	49-58	ribonuclease pancreatic	Bos taurus	88-102
9521769-1	1998	The oxidative regeneration pathways of two three-disulfide mutants of bovine pancreatic ribonuclease A (RNase A) missing the 65-72 disulfide bond, [C65S,C72S] and [C65A,C72A], have been studied by using oxidized dithiothreitol (DTTox) as an oxidizing agent and 2-aminoethylmethanethiosulfonate (AEMTS) as a thiol-blocking agent at 25 degrees C and pH 8.0.	Disulfides	49-58	ribonuclease pancreatic	Bos taurus	104-111
9521769-1	1998	The oxidative regeneration pathways of two three-disulfide mutants of bovine pancreatic ribonuclease A (RNase A) missing the 65-72 disulfide bond, [C65S,C72S] and [C65A,C72A], have been studied by using oxidized dithiothreitol (DTTox) as an oxidizing agent and 2-aminoethylmethanethiosulfonate (AEMTS) as a thiol-blocking agent at 25 degrees C and pH 8.0.	Disulfides	131-140	ribonuclease pancreatic	Bos taurus	88-102
9521769-1	1998	The oxidative regeneration pathways of two three-disulfide mutants of bovine pancreatic ribonuclease A (RNase A) missing the 65-72 disulfide bond, [C65S,C72S] and [C65A,C72A], have been studied by using oxidized dithiothreitol (DTTox) as an oxidizing agent and 2-aminoethylmethanethiosulfonate (AEMTS) as a thiol-blocking agent at 25 degrees C and pH 8.0.	Disulfides	131-140	ribonuclease pancreatic	Bos taurus	104-111
9488661-7	1998	The results suggest that p53 can form disulfides and that these disulfides must be reduced in order for the protein to function as a transcription factor.	Disulfides	64-74	tumor protein p53	Homo sapiens	25-28
9538236-4	1998	The refolding intermediates of RNase B, as compared with those of RNase A, seemed to contain much less impaired disulfide linkages.	Disulfides	112-121	ribonuclease pancreatic	Bos taurus	66-73
9473222-6	1998	Both mutations are within the large disulfide loop between Cys509 and Cys695 in the A1 domain that mediates vWF interaction with platelet glycoprotein Ib.	Disulfides	36-45	von Willebrand factor	Homo sapiens	108-111
9514162-7	1998	Moreover, two-dimensional gel analysis showed that BiP associated especially well with intracellular Tg containing mispaired disulfide bonds, thought to represent early Tg folding intermediates.	Disulfides	125-134	heat shock protein family A (Hsp70) member 5	Homo sapiens	51-54
9533958-3	1998	This Spatzle carboxyterminal fragment is a disulfide-linked dimer and modelling suggests that the core disulfide bonds and dimer arrangement of this fragment are highly similar to vertebrate nerve growth factor.	Disulfides	43-52	spatzle	Drosophila melanogaster	5-12
9533958-3	1998	This Spatzle carboxyterminal fragment is a disulfide-linked dimer and modelling suggests that the core disulfide bonds and dimer arrangement of this fragment are highly similar to vertebrate nerve growth factor.	Disulfides	103-112	spatzle	Drosophila melanogaster	5-12
9477956-0	1998	Disulfide bond exchange in rhodopsin.	Disulfides	0-9	rhodopsin	Homo sapiens	27-36
9518460-4	1998	Detailed structural characterization confirms that KGF-a contains a single amino acid sequence predicted from cDNA sequence and the molecule has two intramolecular disulfide bridges, Cys1-Cys15 and Cys102-Cys106.	Disulfides	164-173	fibroblast growth factor 7	Homo sapiens	51-54
9518466-9	1998	Mass spectrometry and a chemical assay for free sulfhydryls indicated that the four cysteine residues of interleukin-13 are involved in two intramolecular disulfide bonds.	Disulfides	155-164	interleukin 13	Homo sapiens	105-119
9468524-0	1998	Localization of an insulin-like growth factor (IGF) binding site of bovine IGF binding protein-2 using disulfide mapping and deletion mutation analysis of the C-terminal domain.	Disulfides	103-112	insulin like growth factor binding protein 2	Bos taurus	75-96
9461574-12	1998	Intrasubunit disulfide-bridged S100B monomer and disulfide-bonded S100B dimer are phosphorylated by the catalytic CKII-alpha subunit on Ser-62 with a Km of 0.5 microM and a Vmax of 10 pmol/min/100 pmol of S100B.	Disulfides	13-22	S100 calcium binding protein B	Homo sapiens	31-36
9461574-15	1998	In addition, the phosphorylated intrasubunit disulfide-bridged S100B monomer retains apparent mitogenic activity toward C6 glial cells, and hence, 32P-labeled S100B should be a useful probe for characterizing the mechanisms by which extracellular oxidized S100B functions.	Disulfides	45-54	S100 calcium binding protein B	Homo sapiens	63-68
9461574-15	1998	In addition, the phosphorylated intrasubunit disulfide-bridged S100B monomer retains apparent mitogenic activity toward C6 glial cells, and hence, 32P-labeled S100B should be a useful probe for characterizing the mechanisms by which extracellular oxidized S100B functions.	Disulfides	45-54	S100 calcium binding protein B	Homo sapiens	159-164
9461574-15	1998	In addition, the phosphorylated intrasubunit disulfide-bridged S100B monomer retains apparent mitogenic activity toward C6 glial cells, and hence, 32P-labeled S100B should be a useful probe for characterizing the mechanisms by which extracellular oxidized S100B functions.	Disulfides	45-54	S100 calcium binding protein B	Homo sapiens	159-164
9461574-16	1998	Finally, we show that formation of intrasubunit disulfide-bridged S100B monomer is stimulated by peroxynitrite anion, suggesting that production of mitogenic S100B species could be enhanced in neuropathology associated with peroxynitrite anion production.	Disulfides	48-57	S100 calcium binding protein B	Homo sapiens	66-71
9461574-16	1998	Finally, we show that formation of intrasubunit disulfide-bridged S100B monomer is stimulated by peroxynitrite anion, suggesting that production of mitogenic S100B species could be enhanced in neuropathology associated with peroxynitrite anion production.	Disulfides	48-57	S100 calcium binding protein B	Homo sapiens	158-163
9477952-0	1998	Secretion efficiency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability.	Disulfides	104-113	trophoblast Kunitz domain protein 1	Bos taurus	70-87
9477956-1	1998	Rhodopsin contains two cysteines (Cys110 and Cys187) that are highly conserved among members of the G protein coupled receptor family and that form a disulfide bond connecting helixes 3 and 4 on the extracellular side of the protein.	Disulfides	150-159	rhodopsin	Homo sapiens	0-9
9477956-2	1998	However, recent work on a rhodopsin mutant split in the cytoplasmic loop connecting helixes 3 and 4 has shown that the amino- and carboxy-terminal fragments of this split protein do not comigrate on nonreducing SDS-PAGE gels, suggesting that the native Cys110-Cys187 disulfide bond is not present in this mutant [Ridge et al.	Disulfides	267-276	rhodopsin	Homo sapiens	26-35
9477956-9	1998	We show here that the inability to observe the disulfide bond on SDS gels is the result of a disulfide bond exchange reaction which occurs when this split rhodopsin is denatured in preparation for SDS-PAGE.	Disulfides	47-56	rhodopsin	Homo sapiens	155-164
9477956-9	1998	We show here that the inability to observe the disulfide bond on SDS gels is the result of a disulfide bond exchange reaction which occurs when this split rhodopsin is denatured in preparation for SDS-PAGE.	Disulfides	93-102	rhodopsin	Homo sapiens	155-164
9477956-11	1998	If the sulfhydryl-specific reagent N-ethylmaleimide is included in the sample during preparation for electrophoresis or if Cys185 is changed to Ser, the two fragments do comigrate with full-length rhodopsin on SDS gels and, therefore, are connected by the native Cys110-Cys187 disulfide bond.	Disulfides	277-286	rhodopsin	Homo sapiens	197-206
9535269-0	1998	Environmental effects on disulfide bonding patterns of bovine kappa-casein.	Disulfides	25-34	casein kappa	Bos taurus	62-74
9570526-1	1998	IL-12p70, a 70- to 75-kDa heterodimer consisting of disulfide-bonded 35-kDa (p35) and 40-kDa (p40) subunits, enhances Th1 development primarily by its ability to induce IFN-gamma production by NK and Th1 cells.	Disulfides	52-61	negative elongation factor complex member C/D, Th1l	Mus musculus	118-121
9570526-1	1998	IL-12p70, a 70- to 75-kDa heterodimer consisting of disulfide-bonded 35-kDa (p35) and 40-kDa (p40) subunits, enhances Th1 development primarily by its ability to induce IFN-gamma production by NK and Th1 cells.	Disulfides	52-61	interferon gamma	Mus musculus	169-178
9570526-1	1998	IL-12p70, a 70- to 75-kDa heterodimer consisting of disulfide-bonded 35-kDa (p35) and 40-kDa (p40) subunits, enhances Th1 development primarily by its ability to induce IFN-gamma production by NK and Th1 cells.	Disulfides	52-61	negative elongation factor complex member C/D, Th1l	Mus musculus	200-203
9491903-2	1998	It is similar to low-density lipoprotein with an additional molecule of apo A covalently linked to apo B-100 by one disulfide bridge.	Disulfides	116-125	apolipoprotein B	Homo sapiens	99-108
9535269-1	1998	Bovine kappa-casein, the stabilizing protein of the colloidal milk protein complex, has a unique disulfide bonding pattern.	Disulfides	97-106	casein kappa	Bos taurus	7-19
9422790-1	1998	Chromogranins A and B, two widespread neuroendocrine secretory proteins, contain a homologous N-terminal disulfide-bonded loop that is required for sorting to secretory granules.	Disulfides	105-114	chromogranin A	Homo sapiens	0-21
9466939-1	1998	Escherichia coli RTEM beta-lactamase, in which both cysteine residues which form the single disulfide bond have been mutated to alanine residues, can form stable reversible complexes with GroEL under two different sets of conditions.	Disulfides	92-101	GroEL	Escherichia coli	188-193
9422786-3	1998	We found that substitution of Cys-86, Cys-91, and Cys-96 in betac but not of Cys-100 or Cys-234 abrogated disulfide-linked IL-3 receptor dimerization.	Disulfides	106-115	interleukin 3	Mus musculus	123-127
9490014-1	1998	Interaction of S100a and S100b with duck gizzard caldesmon was investigated by means of native gel electrophoresis, fluorescent spectroscopy and disulfide crosslinking.	Disulfides	145-154	S100 calcium binding protein B	Homo sapiens	25-30
9419208-3	1998	Sequence analysis revealed a TSP1 recognition motif, previously defined for the CD36 gene family of cell adhesion receptors, in conserved regions flanking the disulfide-linked cysteine residues of the V3 loop of HIV envelope glycoprotein gp120, important for HIV binding to its high affinity cellular receptor CD4.	Disulfides	159-168	thrombospondin 1	Homo sapiens	29-33
9422790-3	1998	Reduction of the disulfide bond or the addition of an excess of an N-terminal chromogranin A fragment containing the loop (CgA1-60) resulted in the dissociation into monomers of the chromogranin A dimer found at pH 7.4 and 6.4 and of the chromogranin tetramer found at pH 5.4.	Disulfides	17-26	chromogranin A	Homo sapiens	182-196
9422790-5	1998	Fluorescence energy transfer experiments using fluorescently labeled CgA1-60 showed that the N-terminal disulfide-bonded loop has a high affinity for homodimerization (KD = 20 nM at pH 6.4), which was sufficient to mediate dimerization of full-length chromogranin A.	Disulfides	104-113	chromogranin A	Homo sapiens	251-265
9759493-5	1998	VWF is assembled from identical approximately 250 kDa subunits into disulfide-linked multimers that may be &gt; 20,000 kDa.	Disulfides	68-77	von Willebrand factor	Homo sapiens	0-3
9562549-3	1998	RESULTS: RNase A has four disulfide bonds, whereas cytochrome c, with a covalently bound heme group, has no disulfide bond.	Disulfides	26-35	ribonuclease pancreatic	Bos taurus	9-16
9562549-7	1998	CONCLUSIONS: These results indicate that the heat-denatured RNase A and cytochrome c are substantially unfolded according to the criteria of solution X-ray scattering, although the heat-denatured RNase A remains compact because of the presence of the disulfide bonds.	Disulfides	251-260	ribonuclease pancreatic	Bos taurus	60-67
9761676-3	1998	In the scFv fragment derived from this antibody, the stabilizing effect of Gln H6 over Glu was found to be as large as the effect of reintroducing the disulfide bond.	Disulfides	151-160	immunglobulin heavy chain variable region	Homo sapiens	7-11
9451015-6	1998	Each of the precursors of MUC2, MUC5AC, MUC5B, and MUC6 formed a single species of disulfide-linked homo-oligomer within 1 h after pulse labeling.	Disulfides	83-92	mucin 2, oligomeric mucus/gel-forming	Homo sapiens	26-30
9546612-9	1998	Intra-B-chain disulfides in alpha-thrombin were essential for binding but not catalytic H363 or residues R382-N394 and R443-G475.	Disulfides	14-24	coagulation factor II, thrombin	Homo sapiens	34-42
21374461-3	1998	These complexities include variations in the degree of sialylation on the sugar chains and complex formation with low molecular weight thiols by disulfide bridges of the reactive single cysteine (6) Hereditary deficiency of alpha-1-anti-T predisposes to degenerative lung disease and liver disease (7,8).Nucleotide sequence studies of alpha-1-anti-T have shown single or two-base substitution or dinucleotide deletion with subsequent single amino acid substitutions or deletions.	Disulfides	145-154	serpin family A member 1	Homo sapiens	224-238
21374461-3	1998	These complexities include variations in the degree of sialylation on the sugar chains and complex formation with low molecular weight thiols by disulfide bridges of the reactive single cysteine (6) Hereditary deficiency of alpha-1-anti-T predisposes to degenerative lung disease and liver disease (7,8).Nucleotide sequence studies of alpha-1-anti-T have shown single or two-base substitution or dinucleotide deletion with subsequent single amino acid substitutions or deletions.	Disulfides	145-154	serpin family A member 1	Homo sapiens	335-349
9407080-0	1997	Disulfide bond assignment in human interleukin-7 by matrix-assisted laser desorption/ionization mass spectroscopy and site-directed cysteine to serine mutational analysis.	Disulfides	0-9	interleukin 7	Homo sapiens	35-48
9659913-2	1998	In a temperature-sensitive ero1-1 mutant, newly synthesized carboxypeptidase Y is retained in the ER and lacks disulfide bonds, as shown by thiol modification with AMS.	Disulfides	111-120	ER oxidoreductin	Saccharomyces cerevisiae S288C	27-33
9659913-6	1998	We show that glutathione is not required for CPY folding and conclude that Ero1p functions in a novel mechanism that sustains the ER oxidizing potential, supporting net formation of protein disulfide bonds.	Disulfides	190-199	ER oxidoreductin	Saccharomyces cerevisiae S288C	75-80
9407080-1	1997	Interleukin-7 (IL-7) is a proteinaceous biological response modifier that has a bioactive tertiary structure dependent on disulfide bond formation.	Disulfides	122-131	interleukin 7	Homo sapiens	0-13
9407080-1	1997	Interleukin-7 (IL-7) is a proteinaceous biological response modifier that has a bioactive tertiary structure dependent on disulfide bond formation.	Disulfides	122-131	interleukin 7	Homo sapiens	15-19
9407080-2	1997	Disulfide bond assignments in human (h)IL-7 are based upon the results of matrix-assisted laser desorption/ionization (MALDI) mass spectroscopy and Cys to Ser mutational analyses.	Disulfides	0-9	interleukin 7	Homo sapiens	39-43
9407080-5	1997	Many of the anticipated hIL-7 tryptic fragments were detected including one with a molecular mass equivalent to the sum of two polypeptides linked through a disulfide bond formed from Cys residues (Cys3 and Cys142).	Disulfides	157-166	interleukin 7	Homo sapiens	24-29
9407080-8	1997	In contrast, a family of single disulfide bond-forming variants of hIL-7 were constructed by reintroducing Cys pairs (Cys3-Cys142, Cys35-Cys130, and Cys48-Cys93), and each could stimulate cell proliferation with an EC50 of 4 x 10(-9), 2 x 10(-8), and 2 x 10(-9) M, respectively.	Disulfides	32-41	interleukin 7	Homo sapiens	67-72
9407080-9	1997	In single disulfide bond-forming mutants of hIL-7, the ability to stimulate cell proliferation was abolished in the presence of 2 mM dithiothreitol.	Disulfides	10-19	interleukin 7	Homo sapiens	44-49
9407080-10	1997	The results presented strongly suggest that only a single disulfide bond is required for hIL-7 to form a tertiary structure capable of stimulating precursor B-cell proliferation.	Disulfides	58-67	interleukin 7	Homo sapiens	89-94
9398310-12	1997	These results suggest that inactivation of AR by GSNO is due to the selective formation of a single mixed disulfide between glutathione and Cys-298 located at the NADP(H)-binding site of the enzyme.	Disulfides	106-115	aldo-keto reductase family 1 member B	Homo sapiens	43-45
9388210-5	1997	The affinity of other IGFBPs for insulin can be enhanced by modifications that disrupt disulfide bonds or remove the conserved COOH terminus.	Disulfides	87-96	insulin	Homo sapiens	33-40
9388228-5	1997	Trx2 together with thioredoxin reductase and NADPH is an efficient electron donor for the essential enzyme ribonucleotide reductase and is also able to reduce the interchain disulfide bridges of insulin.	Disulfides	174-183	insulin	Homo sapiens	195-202
9487987-1	1997	Amylin, calcitonin (CT) and calcitonin gene-related peptide (CGRP) share limited structural homology including amino-terminal ring structures linked by a disulfide bridge and amidated carboxy-termini.	Disulfides	154-163	calcitonin related polypeptide alpha	Homo sapiens	28-59
9437520-7	1997	In this case protein mixed disulfide formation between DSF and caspase-1 was directly demonstrated using 35S-labeled DSF.	Disulfides	27-36	caspase 1	Homo sapiens	63-72
9437520-8	1997	The physiological disulfide GSSG was also observed to influence the activity of caspases.	Disulfides	18-27	caspase 1	Homo sapiens	80-88
9405235-1	1997	Reduction and alkylation of disulfide bonds are known to affect substrate translocation by and antidepressant binding to the serotonin transporter (SERT).	Disulfides	28-37	solute carrier family 6 member 4	Rattus norvegicus	125-146
9405235-1	1997	Reduction and alkylation of disulfide bonds are known to affect substrate translocation by and antidepressant binding to the serotonin transporter (SERT).	Disulfides	28-37	solute carrier family 6 member 4	Rattus norvegicus	148-152
9487987-1	1997	Amylin, calcitonin (CT) and calcitonin gene-related peptide (CGRP) share limited structural homology including amino-terminal ring structures linked by a disulfide bridge and amidated carboxy-termini.	Disulfides	154-163	calcitonin related polypeptide alpha	Homo sapiens	61-65
9398631-5	1997	Under these conditions IGFBP-3 and IGFBP-5, but not the other IGFBPs, formed high molecular weight disulfide-linked multimers.	Disulfides	99-108	insulin like growth factor binding protein 5	Homo sapiens	35-42
9365927-0	1997	Covalent structure of botulinum neurotoxin type E: location of sulfhydryl groups, and disulfide bridges and identification of C-termini of light and heavy chains.	Disulfides	86-95	neurotoxin	Clostridium botulinum	32-42
9368005-6	1997	In this report we describe the use of cyanogen bromide and protease digestion of the exon 11 plus form of the receptor ectodomain to identify disulfide linkages between the beta-chain residues Cys798 and Cys807 and between the alpha-chain Cys647 and the beta-chain Cys872.	Disulfides	142-151	Fc gamma receptor and transporter	Homo sapiens	227-238
9409285-2	1997	Disruption of disulfide bond formation in newly synthesized apoB molecules through the use of the reducing agent DTT resulted in a decrease in the secretion of apoB-containing lipoproteins from HepG2 cells compared with control cells.	Disulfides	14-23	apolipoprotein B	Homo sapiens	60-64
9409285-2	1997	Disruption of disulfide bond formation in newly synthesized apoB molecules through the use of the reducing agent DTT resulted in a decrease in the secretion of apoB-containing lipoproteins from HepG2 cells compared with control cells.	Disulfides	14-23	apolipoprotein B	Homo sapiens	160-164
9404661-8	1997	Our study with anti-CD19 scFv immunotoxin indicates that the formation of a disulfide-linked scFv immunotoxin is an alternative to the recombinant method of producing scFv immunotoxin.	Disulfides	76-85	immunglobulin heavy chain variable region	Homo sapiens	25-29
9404661-8	1997	Our study with anti-CD19 scFv immunotoxin indicates that the formation of a disulfide-linked scFv immunotoxin is an alternative to the recombinant method of producing scFv immunotoxin.	Disulfides	76-85	immunglobulin heavy chain variable region	Homo sapiens	93-97
9404661-8	1997	Our study with anti-CD19 scFv immunotoxin indicates that the formation of a disulfide-linked scFv immunotoxin is an alternative to the recombinant method of producing scFv immunotoxin.	Disulfides	76-85	immunglobulin heavy chain variable region	Homo sapiens	93-97
9418137-4	1997	Biochemical analysis showed that CD79 beta on pro-B cells existed either as monomers or as disulfide-linked heterodimers with CD79 alpha, non-covalently associated with four unidentified membrane molecules.	Disulfides	91-100	CD79B antigen	Mus musculus	33-42
9418137-4	1997	Biochemical analysis showed that CD79 beta on pro-B cells existed either as monomers or as disulfide-linked heterodimers with CD79 alpha, non-covalently associated with four unidentified membrane molecules.	Disulfides	91-100	CD79A antigen (immunoglobulin-associated alpha)	Mus musculus	126-136
9385634-1	1997	Lipoprotein(a) [Lp(a)] is a low-density lipoprotein complex consisting of apolipoprotein(a) [apo(a)] disulfide-linked to apolipoprotein B-100.	Disulfides	101-110	apolipoprotein B	Homo sapiens	121-141
9389317-2	1997	CD101 was first described in our laboratory using two different monoclonal antibodies, BA27 and BB27, recognizing a 140-kDa disulfide-bonded homodimeric polypeptide on a small subset of circulating T lymphocytes and on most activated T cells in vitro.	Disulfides	124-133	CD101 molecule	Homo sapiens	0-5
9346903-7	1997	We therefore hypothesized that the small subunit of MTP, protein-disulfide isomerase (PDI), plays a role in apoB secretion by facilitating correct disulfide bond formation.	Disulfides	65-74	apolipoprotein B	Homo sapiens	108-112
9295301-3	1997	Although apoB100 cysteine 4326 is required for the disulfide linkage with apo(a), other structural features, aside from a single free cysteine residue, must be important for apoB"s initial interaction with apo(a) and for facilitating the formation of the disulfide bond.	Disulfides	51-60	apolipoprotein B	Homo sapiens	9-16
9346940-2	1997	Surface biotinylation followed by wheat germ agglutinin column chromatography and anti-CD44-mediated immunoprecipitation indicate that both CD44s and p185(HER2) are expressed on the cell surface and most importantly, that these two molecules are physically linked to each other via interchain disulfide bonds.	Disulfides	293-302	erb-b2 receptor tyrosine kinase 2	Homo sapiens	155-159
9335525-0	1997	Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A.	Disulfides	71-80	ribonuclease pancreatic	Bos taurus	123-137
9335525-1	1997	The major rate-determining step in the oxidative regeneration of bovine pancreatic ribonuclease A (RNase A) proceeds through des-[40-95] RNase A, a three-disulfide intermediate lacking the Cys40-Cys95 disulfide bond.	Disulfides	154-163	ribonuclease pancreatic	Bos taurus	83-97
9335525-1	1997	The major rate-determining step in the oxidative regeneration of bovine pancreatic ribonuclease A (RNase A) proceeds through des-[40-95] RNase A, a three-disulfide intermediate lacking the Cys40-Cys95 disulfide bond.	Disulfides	154-163	ribonuclease pancreatic	Bos taurus	99-106
9335525-1	1997	The major rate-determining step in the oxidative regeneration of bovine pancreatic ribonuclease A (RNase A) proceeds through des-[40-95] RNase A, a three-disulfide intermediate lacking the Cys40-Cys95 disulfide bond.	Disulfides	154-163	ribonuclease pancreatic	Bos taurus	137-144
9335525-1	1997	The major rate-determining step in the oxidative regeneration of bovine pancreatic ribonuclease A (RNase A) proceeds through des-[40-95] RNase A, a three-disulfide intermediate lacking the Cys40-Cys95 disulfide bond.	Disulfides	201-210	ribonuclease pancreatic	Bos taurus	83-97
9335525-1	1997	The major rate-determining step in the oxidative regeneration of bovine pancreatic ribonuclease A (RNase A) proceeds through des-[40-95] RNase A, a three-disulfide intermediate lacking the Cys40-Cys95 disulfide bond.	Disulfides	201-210	ribonuclease pancreatic	Bos taurus	99-106
9351627-3	1997	A two-domain structure with similar amino acid sequences, four intradomain disulfide bonds, and high proline content, which are characteristics common to human and porcine SLPI, was also found in the mouse protein.	Disulfides	75-84	secretory leukocyte peptidase inhibitor	Homo sapiens	172-176
9344363-6	1997	RESULTS: The protein AgBM8, isolated from rabbit corneal stromal and epithelial tissues, was identified as the long-splice variant form of type XII collagen based on its size (approximately 340 kDa disulfide-linked subunits), the presence of collagenous domain(s) and a noncollagenous domain of approximately 300 kDa in its subunit structure, and its internal amino acid sequences.	Disulfides	198-207	collagen alpha-1(XII) chain	Oryctolagus cuniculus	139-156
9346948-6	1997	The SP-Ahyp,C6S was also oligomeric in solution and formed disulfide-dependent dimers, indicating the presence of at least one additional interchain disulfide bond.	Disulfides	59-68	surfactant protein A1	Rattus norvegicus	4-11
9346948-6	1997	The SP-Ahyp,C6S was also oligomeric in solution and formed disulfide-dependent dimers, indicating the presence of at least one additional interchain disulfide bond.	Disulfides	149-158	surfactant protein A1	Rattus norvegicus	4-11
9346948-11	1997	We conclude that: 1) the Cys6 interchain disulfide bond of SP-A is required for aggregation of liposomes and for potent inhibition of surfactant secretion.	Disulfides	41-50	surfactant protein A1	Rattus norvegicus	59-63
9335569-0	1997	Regeneration studies of an analog of ribonuclease A missing disulfide bonds 65-72 and 40-95.	Disulfides	60-69	ribonuclease pancreatic	Bos taurus	37-51
9398415-2	1997	Investigation of C1s and S2p photoelectron line energies shows this increase to be due largely to oxidative cleavage of native disulfide bonds to form sulfonic acid groups together with some formation of COOH/COOR on the wool fiber surfaces.	Disulfides	127-136	complement C1s	Homo sapiens	17-20
9336411-2	1997	This effect is markedly dependent on the disulfide-bond conformation of TSP1, with one isoform, TSP1(0.1), being the most potent.	Disulfides	41-50	thrombospondin 1	Homo sapiens	72-76
9336411-2	1997	This effect is markedly dependent on the disulfide-bond conformation of TSP1, with one isoform, TSP1(0.1), being the most potent.	Disulfides	41-50	thrombospondin 1	Homo sapiens	96-100
9336411-3	1997	The aims of this study were to examine the expression of different disulfide-bonded isoforms of TSP1 in inflammatory environments in which elastase and cathepsin G are present in variable amounts, and to determine the relationship between these proteinases and their potential inhibitor.	Disulfides	67-76	thrombospondin 1	Homo sapiens	96-100
9295301-3	1997	Although apoB100 cysteine 4326 is required for the disulfide linkage with apo(a), other structural features, aside from a single free cysteine residue, must be important for apoB"s initial interaction with apo(a) and for facilitating the formation of the disulfide bond.	Disulfides	51-60	apolipoprotein B	Homo sapiens	9-13
9287323-5	1997	Mutation of highly conserved cysteines in the amino-terminal domain and third extracellular loop of CCR2, but not in the fusion protein, resulted in a dramatic loss of MCP-1 binding, suggesting the existence of a critical intramolecular disulfide bond that positions the amino-terminal protein for ligand interaction.	Disulfides	237-246	C-C motif chemokine receptor 2	Homo sapiens	100-104
9308901-0	1997	Cancer cells release a covalent complex containing disulfide-linked domains from urinary plasminogen activator, neural cell adhesion molecule, and haptoglobin alpha and beta chains.	Disulfides	51-60	haptoglobin	Homo sapiens	147-158
9299452-3	1997	rHDL containing apolipoprotein A-I (apoA-I), the disulfide-linked form of the apoA-IMilano variant, or apoA-II, were all effective in inhibiting the expression of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 in TNF alpha- or LPS-stimulated HUVEC.	Disulfides	49-58	vascular cell adhesion molecule 1	Homo sapiens	163-196
9299452-3	1997	rHDL containing apolipoprotein A-I (apoA-I), the disulfide-linked form of the apoA-IMilano variant, or apoA-II, were all effective in inhibiting the expression of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 in TNF alpha- or LPS-stimulated HUVEC.	Disulfides	49-58	vascular cell adhesion molecule 1	Homo sapiens	198-204
9299452-3	1997	rHDL containing apolipoprotein A-I (apoA-I), the disulfide-linked form of the apoA-IMilano variant, or apoA-II, were all effective in inhibiting the expression of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 in TNF alpha- or LPS-stimulated HUVEC.	Disulfides	49-58	tumor necrosis factor	Homo sapiens	247-256
9268305-6	1997	Furthermore, the ring-open intermolecular disulfide form of DTTox, 2-hydroxyethyl disulfide, was only a weak inducer of grp78 and gadd153 but was a strong inducer of hsp70 mRNA and a potent oxidant that lowered the NADPH/NADP+ ratio and depleted reduced glutathione (GSH).	Disulfides	42-51	heat shock 70 kDa protein 6	Sus scrofa	166-171
9315320-6	1997	Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione.	Disulfides	49-58	glutathione peroxidase 3	Homo sapiens	159-188
9315320-6	1997	Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione.	Disulfides	49-58	glutathione peroxidase 3	Homo sapiens	226-255
9315320-6	1997	Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione.	Disulfides	93-102	glutathione peroxidase 3	Homo sapiens	159-188
9315320-6	1997	Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione.	Disulfides	93-102	glutathione peroxidase 3	Homo sapiens	226-255
9294820-15	1997	Human IGF-I appears to dimerize covalently by both disulfide scrambling and by a radical-promoted nondisulfide pathway.	Disulfides	51-60	insulin like growth factor 1	Homo sapiens	6-11
9268350-3	1997	Mutations that produce the largest increases in the Ki for a C-terminally truncated form of stromelysin 1, MMP-3(DeltaC), but do not disturb the conformation involve substitutions of residues that are located in a ridge that is centered around the disulfide bond between Cys1 and Cys70.	Disulfides	248-257	matrix metallopeptidase 3	Homo sapiens	92-105
9268356-9	1997	The disulfide bond at Cys40-58 is located in an N-terminal extension of about 160 amino acids which has no homology to other amylases but to the proposed peptide binding domain of GroEL, the Hsp60 of E. coli.	Disulfides	4-13	GroEL	Escherichia coli	180-185
9312001-6	1997	When the folding of transferrin in microsomes was analyzed, UDP-glucose enhanced the amount of folded transferrin and reduced the disulfide-linked aggregates.	Disulfides	130-139	transferrin	Homo sapiens	20-31
9268634-0	1997	The human beta-defensin-1 and alpha-defensins are encoded by adjacent genes: two peptide families with differing disulfide topology share a common ancestry.	Disulfides	113-122	defensin beta 1	Homo sapiens	10-25
9244387-0	1997	Disulfide structure of the heparin binding domain in vascular endothelial growth factor: characterization of posttranslational modifications in VEGF.	Disulfides	0-9	vascular endothelial growth factor A	Homo sapiens	53-87
9208169-12	1997	Significantly, dithiothreitol reduction of the DC disulfide abolished its inhibition of in vitro proenzyme processing, thereby demonstrating thiol-disulfide exchange between the DC disulfide and a free thiol group on an activator(s) of caspase-3.	Disulfides	50-59	caspase 3	Homo sapiens	236-245
9232643-3	1997	The mGK-13 structure is similar to other members of the mammalian serine protease family, having five conserved disulfide bonds and an active site located in the cleft between two beta-barrel domains.	Disulfides	112-121	kallikrein related-peptidase 13	Mus musculus	4-10
9232643-3	1997	The mGK-13 structure is similar to other members of the mammalian serine protease family, having five conserved disulfide bonds and an active site located in the cleft between two beta-barrel domains.	Disulfides	112-121	coagulation factor II, thrombin	Homo sapiens	66-81
9188686-7	1997	Although the structural comparison of wt RNase A and this analog of an oxidative folding intermediate indicates only localized effects around the Cys65 and Cys72 sites, these thermodynamic measurements indicate that formation of the fourth disulfide bond, Cys65-Cys72, on this oxidative folding pathway results in global stabilization of the native chain fold.	Disulfides	240-249	ribonuclease pancreatic	Bos taurus	41-48
9188686-9	1997	More generally, our study indicates that the C65-C72 disulfide bond of RNase A contributes significantly in stabilizing the structure of the hydrophobic core of the native protein.	Disulfides	53-62	ribonuclease pancreatic	Bos taurus	71-78
9188699-1	1997	The biological functions of rat surfactant protein A (SP-A), an oligomer composed of 18 polypeptide subunits derived from a single gene, are dependent on intact disulfide bonds.	Disulfides	161-170	surfactant protein A1	Rattus norvegicus	32-52
9188699-1	1997	The biological functions of rat surfactant protein A (SP-A), an oligomer composed of 18 polypeptide subunits derived from a single gene, are dependent on intact disulfide bonds.	Disulfides	161-170	surfactant protein A1	Rattus norvegicus	54-58
9188699-3	1997	However, the reported primary structure of rat SP-A predicts that only Cys6 in this region is available for interchain disulfide formation.	Disulfides	119-128	surfactant protein A1	Rattus norvegicus	47-51
9188699-9	1997	Sequencing of both native rat SP-A and human SP-A also revealed isoforms with disulfide-forming NH2-terminal extensions.	Disulfides	78-87	surfactant protein A1	Rattus norvegicus	30-34
9257707-0	1997	A disulfide bond between conserved cysteines in the extracellular loops of the human VIP receptor is required for binding and activation.	Disulfides	2-11	vasoactive intestinal peptide	Homo sapiens	85-88
9271208-4	1997	On the other hand, Raman spectra reveal pronounced CPT-induced local structural modifications of the HSA molecule, involving changes in configuration of the two disulfide bonds and transfer of a single Trp-residue to hydrophilic environment.	Disulfides	161-170	albumin	Homo sapiens	101-104
9186491-1	1997	Insulin-like growth factor-I (IGF-I) has three disulfide bonds and refolding of the fully reduced molecule generates varying ratios of correctly (PII) and incorrectly (PI) folded forms via several intermediates.	Disulfides	47-56	insulin like growth factor 1	Homo sapiens	0-28
9186491-1	1997	Insulin-like growth factor-I (IGF-I) has three disulfide bonds and refolding of the fully reduced molecule generates varying ratios of correctly (PII) and incorrectly (PI) folded forms via several intermediates.	Disulfides	47-56	insulin like growth factor 1	Homo sapiens	30-35
9186491-7	1997	It was concluded from these results that the intermediate forms of IGF-1 can rapidly reshuffle between different disulfide structures, and that formation of the last disulfide bond is not as favorable a process as the conversion to other intermediates.	Disulfides	113-122	insulin like growth factor 1	Homo sapiens	67-72
9188686-1	1997	A three-disulfide intermediate, des-[65-72] RNase A, lacking the disulfide bond between Cys65 and Cys72, is formed in one of the rate-determining steps of the oxidative regeneration pathways of bovine pancreatic ribonuclease A (RNase A).	Disulfides	8-17	ribonuclease pancreatic	Bos taurus	44-51
9188686-1	1997	A three-disulfide intermediate, des-[65-72] RNase A, lacking the disulfide bond between Cys65 and Cys72, is formed in one of the rate-determining steps of the oxidative regeneration pathways of bovine pancreatic ribonuclease A (RNase A).	Disulfides	8-17	ribonuclease pancreatic	Bos taurus	212-226
9188686-1	1997	A three-disulfide intermediate, des-[65-72] RNase A, lacking the disulfide bond between Cys65 and Cys72, is formed in one of the rate-determining steps of the oxidative regeneration pathways of bovine pancreatic ribonuclease A (RNase A).	Disulfides	8-17	ribonuclease pancreatic	Bos taurus	228-235
9188686-1	1997	A three-disulfide intermediate, des-[65-72] RNase A, lacking the disulfide bond between Cys65 and Cys72, is formed in one of the rate-determining steps of the oxidative regeneration pathways of bovine pancreatic ribonuclease A (RNase A).	Disulfides	65-74	ribonuclease pancreatic	Bos taurus	44-51
9208169-13	1997	Since T cell apoptosis involves the generation of mature caspase-3 and requires caspase-3-like activity, we propose that (1) DC disulfides are the active agents behind DC inhibition of apoptosis and (2) their site of action is the proteolytic activation of this enzyme.	Disulfides	128-138	caspase 3	Homo sapiens	57-66
9208169-13	1997	Since T cell apoptosis involves the generation of mature caspase-3 and requires caspase-3-like activity, we propose that (1) DC disulfides are the active agents behind DC inhibition of apoptosis and (2) their site of action is the proteolytic activation of this enzyme.	Disulfides	128-138	caspase 3	Homo sapiens	80-89
9185759-3	1997	In some TGF-beta expressing cell types this cytokine is released as a large molecular weight complex containing in addition to the TGF-beta latency associated peptide (LAP) a disulfide bonded latent TGF-beta binding protein (LTBP), of which the existence and function in liver is hitherto unknown.	Disulfides	175-184	transforming growth factor, beta 1	Rattus norvegicus	8-16
9211223-0	1997	Synthesis and biological activity of novel backbone-bicyclic substance-P analogs containing lactam and disulfide bridges.	Disulfides	103-112	tachykinin precursor 1	Homo sapiens	61-72
9129011-2	1997	These extremely adhesive vWF multimers may arise due to deficiency of a "depolymerase" cleaving vWF to smaller molecular forms, either by reducing the interdimeric disulfide bridges or by proteolytic degradation.	Disulfides	164-173	von Willebrand factor	Homo sapiens	25-28
9129011-2	1997	These extremely adhesive vWF multimers may arise due to deficiency of a "depolymerase" cleaving vWF to smaller molecular forms, either by reducing the interdimeric disulfide bridges or by proteolytic degradation.	Disulfides	164-173	von Willebrand factor	Homo sapiens	96-99
9183005-6	1997	Prothrombin x alpha1-microglobulin were 1:2 and 1:1 complexes which carried approximately 1% of total alpha1-microglobulin, had molecular masses of about 145 kDa and 110 kDa upon SDS/PAGE and dissociated completely to free alpha1-microglobulin and prothrombin (72 kDa) when reducing agents were added, suggesting that the complexes were stabilized by disulfide bonds.	Disulfides	351-360	coagulation factor II, thrombin	Homo sapiens	0-11
9144244-1	1997	Thioredoxin, a ubiquitous 12-kDa regulatory disulfide protein, was found to reduce disulfide bonds of allergens (convert S-S to 2 SH) and thereby mitigate the allergenicity of commercial wheat preparations.	Disulfides	44-53	thioredoxin H4-2	Triticum aestivum	0-11
9144244-1	1997	Thioredoxin, a ubiquitous 12-kDa regulatory disulfide protein, was found to reduce disulfide bonds of allergens (convert S-S to 2 SH) and thereby mitigate the allergenicity of commercial wheat preparations.	Disulfides	83-92	thioredoxin H4-2	Triticum aestivum	0-11
9144244-8	1997	As in previous studies, thioredoxin was particularly effective in the reduction of intramolecular (intrachain) disulfide bonds.	Disulfides	111-120	thioredoxin H4-2	Triticum aestivum	24-35
9177849-1	1997	We have designed and tested specific peptide linkers for the glutathione-mediated reductive release of the angiotensin II analog N-acetyl-CGDKVYIHPF attached to recombinant human hemoglobin mutants by a disulfide bond.	Disulfides	203-212	angiotensinogen	Homo sapiens	107-121
9182804-6	1997	PSD-95 and its relative chapsyn-110 exist as disulfide-linked complexes in rat brain, consistent with head-to-head multimerization of these proteins in vivo.	Disulfides	45-54	discs large MAGUK scaffold protein 2	Rattus norvegicus	24-35
9150447-4	1997	LAP is disulfide linked to another protein, latent TGF-beta binding protein (LTBP).	Disulfides	7-16	transforming growth factor beta 1	Homo sapiens	0-3
9150447-4	1997	LAP is disulfide linked to another protein, latent TGF-beta binding protein (LTBP).	Disulfides	7-16	transforming growth factor beta 1	Homo sapiens	51-59
9132026-0	1997	Correlation between disulfide reduction and conformational unfolding in bovine pancreatic trypsin inhibitor.	Disulfides	20-29	trophoblast Kunitz domain protein 1	Bos taurus	90-107
9111002-5	1997	The elastase-induced fragmentation of apo(a) was the same whether free or as a member of Lp(a), indicating that the disulfide bond between apo(a) and the apoB100 component of Lp(a) did not hinder the elastase action.	Disulfides	116-125	apolipoprotein B	Homo sapiens	154-161
9111002-6	1997	Lp(a) fragments containing kringle IV-9 retained the linkage to apoB100 via the disulfide bond, forming mini-Lp(a) particles in which the size of apo(a) varied according to the size of the fragments produced by the elastase digestion.	Disulfides	80-89	apolipoprotein B	Homo sapiens	64-71
9109671-0	1997	Disulfide exchange folding of disulfide mutants of insulin-like growth factor I in vitro.	Disulfides	0-9	insulin like growth factor 1	Homo sapiens	51-79
9109671-0	1997	Disulfide exchange folding of disulfide mutants of insulin-like growth factor I in vitro.	Disulfides	30-39	insulin like growth factor 1	Homo sapiens	51-79
9109671-1	1997	We have previously concluded that insulin-like growth factor-I (IGF-I) is thermodynamically unable to quantitatively form its disulfide bonds under reversible redox conditions in vitro.	Disulfides	126-135	insulin like growth factor 1	Homo sapiens	64-69
9109671-2	1997	From detailed analyses it was hypothesized that the 47-52 disulfide is energetically unfavorable in the native IGF-I structure [Hober et al.	Disulfides	58-67	insulin like growth factor 1	Homo sapiens	111-116
9109671-4	1997	In this paper, this hypothesis has been tested by refolding of IGF-I mutant proteins lacking either the 47-52 or 6-48 disulfide bond.	Disulfides	118-127	insulin like growth factor 1	Homo sapiens	63-68
9109671-5	1997	The disulfide exchange folding equilibrium behavior of these mutated IGF-I variants were examined in a glutathione redox buffer.	Disulfides	4-13	insulin like growth factor 1	Homo sapiens	69-74
9109671-6	1997	The mutant protein IGF-I(C47A,C52A) was demonstrated to form both remaining native disulfide bonds.	Disulfides	83-92	insulin like growth factor 1	Homo sapiens	19-24
9109671-7	1997	In contrast, IGF-I(C6A,C48A) was unable to quantitatively form both of its disulfides and was shown to accumulate a one disulfide variant lacking the 47-52 disulfide bond.	Disulfides	75-85	insulin like growth factor 1	Homo sapiens	13-18
9109671-7	1997	In contrast, IGF-I(C6A,C48A) was unable to quantitatively form both of its disulfides and was shown to accumulate a one disulfide variant lacking the 47-52 disulfide bond.	Disulfides	75-84	insulin like growth factor 1	Homo sapiens	13-18
9109671-7	1997	In contrast, IGF-I(C6A,C48A) was unable to quantitatively form both of its disulfides and was shown to accumulate a one disulfide variant lacking the 47-52 disulfide bond.	Disulfides	120-129	insulin like growth factor 1	Homo sapiens	13-18
9109671-8	1997	These folding data corroborate the hypothesis that the 47-52 disulfide bond of IGF-I is energetically unfavorable also in the absence of the 6-48 disulfide bond.	Disulfides	61-70	insulin like growth factor 1	Homo sapiens	79-84
9109671-9	1997	The two IGF-I variants were purified in oxidized forms where both native disulfides are formed.	Disulfides	73-83	insulin like growth factor 1	Homo sapiens	8-13
9109671-11	1997	Further, binding affinities to the IGF binding protein 1 and a soluble IGF type I receptor, respectively, were severely lowered in both disulfide mutant proteins compared to the native IGF-I molecule.	Disulfides	136-145	insulin like growth factor 1	Homo sapiens	185-190
9109671-13	1997	Thus, the structural changes due to removal of the 6-48 or 47-52 disulfide bonds, respectively, yield structural changes in different regions of the IGF-I molecule reflected in the different binding activities.	Disulfides	65-74	insulin like growth factor 1	Homo sapiens	149-154
9152227-6	1997	CONCLUSIONS: Like rhodopsin, the folding of the cone opsins appears to be dependent on the formation of a disulfide bond between the third transmembrane helix and the second extracellular loop.	Disulfides	106-115	rhodopsin	Homo sapiens	18-27
9092813-4	1997	We examine the hypothesis that, in spite of these differences, cripto can adopt the characteristic EGF-like 1-3, 2-4, 5-6 disulfide bond pattern.	Disulfides	122-131	teratocarcinoma-derived growth factor 1	Homo sapiens	63-69
9141135-1	1997	The characteristic CXC chemokine disulfide core of interleukin-8 (IL-8) has been rearranged in a variant replacing the 9-50 disulfide with a 9-38 disulfide.	Disulfides	33-42	C-X-C motif chemokine ligand 8	Homo sapiens	51-64
9141135-1	1997	The characteristic CXC chemokine disulfide core of interleukin-8 (IL-8) has been rearranged in a variant replacing the 9-50 disulfide with a 9-38 disulfide.	Disulfides	33-42	C-X-C motif chemokine ligand 8	Homo sapiens	66-70
9075770-4	1997	The expressed protein, mIL-10:HFc, is secreted as a disulfide-bonded homodimer.	Disulfides	52-61	interleukin 10	Mus musculus	23-29
9125178-1	1997	Apolipoprotein A-IMilano is a molecular variant of apoA-I, containing the Arg173--&gt;Cys substitution that forms a disulfide linked homodimer (A-IM/A-IM).	Disulfides	116-125	apolipoprotein A1	Homo sapiens	51-57
9054431-12	1997	Inhibition of peptidylprolyl isomerase through the use of cyclosporin A and disruption of disulfide bond formation using dithiothreitol reduced the percentage of translocated apoB by 37 and 63%, respectively.	Disulfides	90-99	apolipoprotein B	Homo sapiens	175-179
9165076-5	1997	The linear peptide uPA(19-31) and its more stable disulfide-bridged cyclic form (cyclo(19,31)uPA(19-31)) displayed uPAR-binding activity whereas other peptides such as uPA(18-30), uPA(20-32) or uPA(20-30) did not react with uPAR.	Disulfides	50-59	plasminogen activator, urokinase	Homo sapiens	93-96
9054543-0	1997	Disruption of the disulfide bonds of recombinant murine interleukin-6 induces formation of a partially unfolded state.	Disulfides	18-27	interleukin 6	Mus musculus	56-69
9054543-1	1997	A chemical modification approach was used to investigate the role of the two disulfide bonds of recombinant murine interleukin-6 (mIL-6) in terms of biological activity and conformational stability.	Disulfides	77-86	interleukin 6	Mus musculus	115-128
9054543-1	1997	A chemical modification approach was used to investigate the role of the two disulfide bonds of recombinant murine interleukin-6 (mIL-6) in terms of biological activity and conformational stability.	Disulfides	77-86	interleukin 6	Mus musculus	130-135
9054543-2	1997	Disruption of the disulfide bonds of mIL-6 by treatment with iodoacetic acid (IAA-IL-6) or iodoacetamide (IAM-IL-6) reduced the biological activity, in the murine hybridoma growth factor assay, by 500- and 200-fold, respectively.	Disulfides	18-27	interleukin 6	Mus musculus	37-42
9054543-2	1997	Disruption of the disulfide bonds of mIL-6 by treatment with iodoacetic acid (IAA-IL-6) or iodoacetamide (IAM-IL-6) reduced the biological activity, in the murine hybridoma growth factor assay, by 500- and 200-fold, respectively.	Disulfides	18-27	interleukin 6	Mus musculus	38-42
9054543-2	1997	Disruption of the disulfide bonds of mIL-6 by treatment with iodoacetic acid (IAA-IL-6) or iodoacetamide (IAM-IL-6) reduced the biological activity, in the murine hybridoma growth factor assay, by 500- and 200-fold, respectively.	Disulfides	18-27	interleukin 6	Mus musculus	82-86
9165076-5	1997	The linear peptide uPA(19-31) and its more stable disulfide-bridged cyclic form (cyclo(19,31)uPA(19-31)) displayed uPAR-binding activity whereas other peptides such as uPA(18-30), uPA(20-32) or uPA(20-30) did not react with uPAR.	Disulfides	50-59	plasminogen activator, urokinase	Homo sapiens	93-96
9057631-1	1997	The response of a B cell to antigen is dependent on the surface expression of a clonotypic B-cell receptor complex (BCR) consisting of membrane-bound Ig and disulfide-linked heterodimers of Ig alpha/beta.	Disulfides	157-166	CD79a molecule	Homo sapiens	190-198
9165076-5	1997	The linear peptide uPA(19-31) and its more stable disulfide-bridged cyclic form (cyclo(19,31)uPA(19-31)) displayed uPAR-binding activity whereas other peptides such as uPA(18-30), uPA(20-32) or uPA(20-30) did not react with uPAR.	Disulfides	50-59	plasminogen activator, urokinase	Homo sapiens	93-96
9165076-5	1997	The linear peptide uPA(19-31) and its more stable disulfide-bridged cyclic form (cyclo(19,31)uPA(19-31)) displayed uPAR-binding activity whereas other peptides such as uPA(18-30), uPA(20-32) or uPA(20-30) did not react with uPAR.	Disulfides	50-59	plasminogen activator, urokinase	Homo sapiens	93-96
9133623-1	1997	alpha-Lactalbumin in which all the disulfide bonds are fully reduced (RLA) is known to bind strongly to the chaperonin GroEL.	Disulfides	35-44	lactalbumin alpha	Homo sapiens	0-17
9063896-15	1997	Together with the increased MTS reactivity of C200S, these results support the possibility that C200 and C209 may be linked by a disulfide bond in the second external loop of SERT.	Disulfides	129-138	solute carrier family 6 member 4	Homo sapiens	175-179
15739408-8	1997	This indicates PE2 may be composed of two chains joined by disulfide bond, which is further proved from the latter amino acid composition analysis.	Disulfides	59-68	ETS2 repressor factor	Homo sapiens	15-18
9029107-3	1997	The most potent peptide, C*WLDVC* (where * indicates disulfide-linked residues), inhibited alpha 4 beta 1-dependent binding of lymphocytes to VCAM-1 and CS1 with half-maximal inhibition achieved at 1 to 3 microM of peptide.	Disulfides	53-62	vascular cell adhesion molecule 1	Homo sapiens	142-148
9037180-5	1997	Combined peptide mapping and mass spectrometric analysis indicated that the proinsulin contained the correct disulfide bridging pattern.	Disulfides	109-118	insulin	Homo sapiens	76-86
9041643-4	1997	An engineered human IgG4 specific for human tumor necrosis factor-alpha (CDP571) is similar to human myeloma IgG4 in that it is secreted as both disulfide bonded tetramers (approximately 75% of the total amount of IgG) and as tetramers composed of nondisulfide bonded half-IgG4 (heavy chain disulfide bonded to light chain) molecules.	Disulfides	145-154	tumor necrosis factor	Homo sapiens	44-71
9041643-4	1997	An engineered human IgG4 specific for human tumor necrosis factor-alpha (CDP571) is similar to human myeloma IgG4 in that it is secreted as both disulfide bonded tetramers (approximately 75% of the total amount of IgG) and as tetramers composed of nondisulfide bonded half-IgG4 (heavy chain disulfide bonded to light chain) molecules.	Disulfides	251-260	tumor necrosis factor	Homo sapiens	44-71
9006939-8	1997	Trx2 possessed a dithiol-reducing enzymatic activity and, with mammalian thioredoxin reductase and NADPH, was able to reduce the interchain disulfide bridges of insulin.	Disulfides	140-149	thioredoxin 1	Rattus norvegicus	73-84
9006939-8	1997	Trx2 possessed a dithiol-reducing enzymatic activity and, with mammalian thioredoxin reductase and NADPH, was able to reduce the interchain disulfide bridges of insulin.	Disulfides	140-149	insulin	Homo sapiens	161-168
9006956-1	1997	Thyroglobulin (Tg), the major protein secreted by thyroid epithelial cells and precursor of thyroid hormones, is a large dimeric glycoprotein with multiple disulfide bonds.	Disulfides	156-165	thyroglobulin	Rattus norvegicus	0-13
9006956-1	1997	Thyroglobulin (Tg), the major protein secreted by thyroid epithelial cells and precursor of thyroid hormones, is a large dimeric glycoprotein with multiple disulfide bonds.	Disulfides	156-165	thyroglobulin	Rattus norvegicus	15-17
9006956-10	1997	This protein was subsequently identified as thrombospondin, which, like Tg, is a large oligomeric secreted glycoprotein with multiple disulfide bonds.	Disulfides	134-143	thyroglobulin	Rattus norvegicus	72-74
9030770-7	1997	The six Cys residues of EPV20 were found to be disulfide-linked in a 1-6, 2-3 and 4 5 pattern.	Disulfides	47-56	NPC intracellular cholesterol transporter 2	Bos taurus	24-29
9016719-4	1997	Fibrinogen is a 340 kDa glycoprotein composed of six polypeptide chains, (alphabetagamma)2, held together by 29 disulfide bonds.	Disulfides	112-121	fibrinogen beta chain	Homo sapiens	0-10
9030770-9	1997	Therefore, EPV20 represents a new structure among the large group of proteins containing domains with three disulfide bonds.	Disulfides	108-117	NPC intracellular cholesterol transporter 2	Bos taurus	11-16
9043672-6	1997	Disulfide compounds were also remarkably inhibitory against HIV-EP1 and Sp1 also at 30 microM whereas the shorter-chain disulfides 7 and 9 were effective only for HIV-EP1.	Disulfides	0-9	HIVEP zinc finger 1	Homo sapiens	60-67
9026037-3	1997	FVS191cys (scFv")2 was formed through a disulfide bond between two FVS191cys molecules.	Disulfides	40-49	immunglobulin heavy chain variable region	Homo sapiens	11-15
9001397-1	1997	Here we describe the basic features of the interaction of K+ channels with Pi1, a recently described 35 amino acid scorpion toxin, which has four disulfide bridges instead of the three commonly found in all the other known scorpion toxins.	Disulfides	146-155	serpin family A member 1	Homo sapiens	75-78
9043672-6	1997	Disulfide compounds were also remarkably inhibitory against HIV-EP1 and Sp1 also at 30 microM whereas the shorter-chain disulfides 7 and 9 were effective only for HIV-EP1.	Disulfides	120-130	HIVEP zinc finger 1	Homo sapiens	163-170
9046058-1	1997	Fibronectin (Fn) matrix assembly is a dynamic cellular process in which the soluble dimeric Fn molecules are assembled into insoluble, disulfide bond stabilized fibrillar polymeric matrix.	Disulfides	135-144	fibronectin 1	Homo sapiens	0-11
9215802-2	1997	This is the second non-disulfide substrate, after dehydroascorbic acid, described for thioltransferase.	Disulfides	23-32	glutaredoxin-1	Sus scrofa	86-102
9046058-1	1997	Fibronectin (Fn) matrix assembly is a dynamic cellular process in which the soluble dimeric Fn molecules are assembled into insoluble, disulfide bond stabilized fibrillar polymeric matrix.	Disulfides	135-144	fibronectin 1	Homo sapiens	13-15
9046058-1	1997	Fibronectin (Fn) matrix assembly is a dynamic cellular process in which the soluble dimeric Fn molecules are assembled into insoluble, disulfide bond stabilized fibrillar polymeric matrix.	Disulfides	135-144	fibronectin 1	Homo sapiens	92-94
8969219-0	1996	Specifically targeted modification of human aldose reductase by physiological disulfides.	Disulfides	78-88	aldo-keto reductase family 1 member B	Homo sapiens	44-60
9144023-2	1997	Apolipoprotein(a), which shares a high degree of sequence homology with the fibrinolytic proenzyme plasminogen, is linked to the apolipoprotein B-100 component of low-density lipoprotein via a disulfide bond and confers distinct biochemical and metabolic properties to lipoprotein(a).	Disulfides	193-202	apolipoprotein B	Homo sapiens	129-149
9055206-9	1997	The disulfide bonds have been identified by peptide mapping and sequence analysis, and are in the positions predicted by homology to interleukin-8 and platelet factor 4.	Disulfides	4-13	C-X-C motif chemokine ligand 8	Homo sapiens	133-146
8985427-6	1997	The viral counterpart of IL-6 (vIL-6) has conserved important features such as cysteine residues involved in disulfide bridging or an amino-terminal signal peptide.	Disulfides	109-118	interleukin 6	Homo sapiens	25-29
8988018-0	1996	Glial cell line-derived neurotrophic factor: selective reduction of the intermolecular disulfide linkage and characterization of its disulfide structure.	Disulfides	87-96	glial cell derived neurotrophic factor	Homo sapiens	0-43
8988018-0	1996	Glial cell line-derived neurotrophic factor: selective reduction of the intermolecular disulfide linkage and characterization of its disulfide structure.	Disulfides	133-142	glial cell derived neurotrophic factor	Homo sapiens	0-43
8969219-1	1996	Aldose reductase is inactivated by physiological disulfides such as GSSG and cystine.	Disulfides	49-59	aldo-keto reductase family 1 member B	Homo sapiens	0-16
8980650-2	1996	Newly synthesized 31 kDa monomers of the B-chain (p31) dimerized rapidly via disulfide bonds to a p54 species (t1/2 &lt; 30 min).	Disulfides	77-86	ATPase H+ transporting V1 subunit E1	Homo sapiens	50-53
9084209-1	1996	We report the production of human mucus proteinase inhibitor (MPI) by the filamentous fungus Aspergillus niger to test the ability of this host organism to secrete low molecular weight, highly disulfide-bonded proteins in biologically active conformation.	Disulfides	193-202	secretory leukocyte peptidase inhibitor	Homo sapiens	34-60
9003757-3	1996	Disulfide linked to the light chain is the catalytic domain, which is generally trypsin-like but contains a large insertion loop at the edge of the active site, a third helical segment, a prominent cationic patch analogous to the anion binding exosite I of thrombin and a trypsin-like Ca[II] binding site.	Disulfides	0-9	coagulation factor II, thrombin	Homo sapiens	257-265
8943374-2	1996	We now demonstrate that CD94 glycoproteins form disulfide-bonded heterodimers with the NKG2A/B, NKG2C, and NKG2E glycoproteins.	Disulfides	48-57	killer cell lectin like receptor C2	Homo sapiens	96-101
8977462-9	1996	In summary, the results of our study indicate that apo(a) kringle IV types 7 and 8 are required for maximal efficiency of Lp(a) formation, likely by virtue of their ability to mediate lysine-dependent non-covalent interactions with apoB-100 that precede disulfide bond formation.	Disulfides	254-263	apolipoprotein B	Homo sapiens	232-240
9012504-3	1996	Here we report the cloning and characterization of mouse VEGF-C, which is produced as a disulfide-linked dimer of 415 amino acid residue polypeptides, sharing an 85% identity with the human VEGF-C amino acid sequence.	Disulfides	88-97	vascular endothelial growth factor C	Mus musculus	57-63
8943374-2	1996	We now demonstrate that CD94 glycoproteins form disulfide-bonded heterodimers with the NKG2A/B, NKG2C, and NKG2E glycoproteins.	Disulfides	48-57	killer cell lectin like receptor C3	Homo sapiens	107-112
8961144-1	1996	Insulin, acylated with dimethylmaleic anhydride, was conjugated to transferrin (Tf) via a disulfide linkage.	Disulfides	90-99	insulin	Homo sapiens	0-7
8961144-1	1996	Insulin, acylated with dimethylmaleic anhydride, was conjugated to transferrin (Tf) via a disulfide linkage.	Disulfides	90-99	transferrin	Homo sapiens	67-78
8961144-1	1996	Insulin, acylated with dimethylmaleic anhydride, was conjugated to transferrin (Tf) via a disulfide linkage.	Disulfides	90-99	transferrin	Homo sapiens	80-82
8914835-0	1996	S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione.	Disulfides	49-59	glutaredoxin-1	Sus scrofa	91-103
10168548-2	1996	It consists of one molecule of low density lipoprotein and an additional molecule of apo(a) linked to apoB-100 by a disulfide bridge.	Disulfides	116-125	apolipoprotein B	Homo sapiens	102-110
8942648-9	1996	Two unique disulfides are formed between the four cysteines in the cytokine domain of TPO: Cys7-Cys151 and Cys29-Cys85.	Disulfides	11-21	thrombopoietin	Homo sapiens	86-89
8942655-6	1996	An oxidized adduct of ICE with glutathione, formed by disulfide rearrangement with oxidized glutathione to inhibit and stabilize the enzyme during purification, was rapidly reduced upon exposure to 5 mM DTT.	Disulfides	54-63	caspase 1	Homo sapiens	22-25
8916456-4	1996	Recently, a trisulfide bond was reported to occur in the minor loop disulfide at Cys182-Cys189 in human growth hormone.	Disulfides	68-77	growth hormone 1	Homo sapiens	104-118
8916456-5	1996	We have detected a trisulfide structure in methionyl human growth hormone in the major loop disulfide Cys53-Cys165.	Disulfides	92-101	growth hormone 1	Homo sapiens	59-73
8944748-2	1996	Reduction-carboxamidomethylation of HDL3 entirely converts the disulfide-linked apoA-II dimers into monomers, without affecting the structure, composition and particle size distribution of HDL3.	Disulfides	63-72	HDL3	Homo sapiens	36-40
9055015-6	1996	In the light of recent evidence on the role of nef gene defects/attenuations in long-term survival of HIV-1 infected patients, it may be that the nef gene defect created by gene duplication, which eliminated the cysteine-206 crucial in disulfide bond formation, may play a role in chronic HIV-1 infection in this patient.	Disulfides	236-245	S100 calcium binding protein B	Homo sapiens	146-149
8914841-0	1996	Positions of disulfide bonds in yam (Dioscorea japonica) acidic class IL (class IV) chitinase.	Disulfides	13-22	Chi	Hordeum vulgare	84-93
8914841-2	1996	The positions of disulfide bonds in this chitinase were examined.	Disulfides	17-26	Chi	Hordeum vulgare	41-50
8914841-3	1996	Chitinase protein was digested with acid protease and thermolysin, and the resulting disulfide bond containing peptides were separated by reversed-phase HPLC and detected using the SBD-F (7-fluorobenzo-2-oxa-1,3-diazole-4-sulfonic acid ammonium salt) method.	Disulfides	85-94	Chi	Hordeum vulgare	0-9
8914841-5	1996	Location of disulfide bonds in the catalytic domain was identical to that of barley class II chitinase but different from rye class II chitinase at the C-terminal.	Disulfides	12-21	Chi	Hordeum vulgare	93-102
8914835-1	1996	The disulfide-reducing activities of glutaredoxin, thioredoxin, protein disulfide isomerase, glutathione, and cysteine were directly compared with a mixture of hepatocyte 35S-glutathiolated proteins as the substrate.	Disulfides	4-13	glutaredoxin-1	Sus scrofa	37-49
8914835-19	1996	Thus, protein disulfide isomerase and thioredoxin are more effective than glutaredoxin as reductants of insulin protein disulfides.	Disulfides	120-130	glutaredoxin-1	Sus scrofa	74-86
8914835-23	1996	A glutathione binding site at the dithiol region of glutaredoxin may be of primary importance for its function in protein dethiolation, while a different specific peptide binding site in thioredoxin may be more suited to certain protein disulfide structures.	Disulfides	237-246	glutaredoxin-1	Sus scrofa	52-64
8910397-2	1996	Fibrinogen is a plasma protein consisting of six polypeptide chains which are linked by disulfide bonds.	Disulfides	88-97	fibrinogen beta chain	Homo sapiens	0-10
8837741-1	1996	beta-Microseminoprotein is a small, nonglycosylated protein, rich in disulfide bonds, which is present in the secretions of the airways, the gastrointestinal tract, and the urogenital tract.	Disulfides	69-78	microseminoprotein, beta	Rattus norvegicus	0-23
8982855-0	1996	Rat liver fatty acid-binding protein: identification of a molecular species having a mixed disulfide with cysteine at cysteine-69 and enhanced protease susceptibility.	Disulfides	91-100	glutamic-oxaloacetic transaminase 2	Rattus norvegicus	10-36
8982855-8	1996	The presence of a relatively large amount of cysteine (but not of glutathione) mixed-disulfide form of FABP suggests some physiological role of this modification related to the redox status of the cell [Thomas, J.A., Poland, B., and Honzatko, R. (1995) Arch.	Disulfides	85-94	glutamic-oxaloacetic transaminase 2	Rattus norvegicus	103-107
8824263-2	1996	Transferrin was linked to PE via a disulfide bond.	Disulfides	35-44	transferrin	Homo sapiens	0-11
8864113-3	1996	Disulfide cross-linking of the helices prevented activation of transducin, which suggests the importance of this movement for activation of rhodopsin.	Disulfides	0-9	rhodopsin	Homo sapiens	140-149
8931130-0	1996	Engineered disulfide bonds in recombinant human interferon-gamma: the impact of the N-terminal helix A and the AB-loop on protein stability.	Disulfides	11-20	interferon gamma	Homo sapiens	48-64
8944550-2	1996	The enzyme activity depended on the presence of reduced glutathione (GSH), glutathione reductase (GR) and NADPH to reduce the disulfide bond in a synthetic substrate, hydroxyl ethyl disulfide (HEDS).	Disulfides	126-135	glutathione-disulfide reductase	Sus scrofa	75-96
8944550-2	1996	The enzyme activity depended on the presence of reduced glutathione (GSH), glutathione reductase (GR) and NADPH to reduce the disulfide bond in a synthetic substrate, hydroxyl ethyl disulfide (HEDS).	Disulfides	126-135	glutathione-disulfide reductase	Sus scrofa	98-100
8897385-1	1996	Lipoprotein(a) (Lp(a)) is bound to apolipoprotein B-100 by disulfide linkage and is associated in the upper density range of low density lipoprotein cholesterol.	Disulfides	59-68	apolipoprotein B	Homo sapiens	35-55
8888292-4	1996	Characterization of this protein revealed that it was platelet surface glycoprotein V (GPV) because it was not affected by a disulfide bond reduction but was cleaved by thrombin.	Disulfides	125-134	glycoprotein V platelet	Homo sapiens	71-85
8888292-4	1996	Characterization of this protein revealed that it was platelet surface glycoprotein V (GPV) because it was not affected by a disulfide bond reduction but was cleaved by thrombin.	Disulfides	125-134	glycoprotein V platelet	Homo sapiens	87-90
8931130-1	1996	Insertion sites for cysteines with optimal stereochemistry for the formation of unstrained disulfide bridges were identified in recombinant human interferon-gamma (rhu-IFN-gamma) by computer modelling.	Disulfides	91-100	interferon gamma	Homo sapiens	146-162
8784206-2	1996	We have previously shown that a single-disulfide variant of human IL-6, lacking 22 N-terminal amino acids and the disulfide bond connecting Cys-45 and Cys-51 in the 185-residue chain of the wild-type protein, fully retains the conformational, stability, and functional properties of the full-length human IL-6 [Breton et al.	Disulfides	39-48	interleukin 6	Homo sapiens	66-70
8841458-1	1996	Vascular permeability factor, also known as vascular endothelial growth factor (VPF/VEGF), is a disulfide-linked dimeric glycoprotein of about 40 kDa that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells.	Disulfides	96-105	vascular endothelial growth factor A	Homo sapiens	0-28
8841458-1	1996	Vascular permeability factor, also known as vascular endothelial growth factor (VPF/VEGF), is a disulfide-linked dimeric glycoprotein of about 40 kDa that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells.	Disulfides	96-105	vascular endothelial growth factor A	Homo sapiens	44-78
8841458-1	1996	Vascular permeability factor, also known as vascular endothelial growth factor (VPF/VEGF), is a disulfide-linked dimeric glycoprotein of about 40 kDa that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells.	Disulfides	96-105	vascular endothelial growth factor A	Homo sapiens	80-83
8841458-1	1996	Vascular permeability factor, also known as vascular endothelial growth factor (VPF/VEGF), is a disulfide-linked dimeric glycoprotein of about 40 kDa that enhances vascular permeability, induces chemotaxis and activation of monocytes/macrophages, and promotes growth of vascular endothelial cells.	Disulfides	96-105	vascular endothelial growth factor A	Homo sapiens	84-88
8703036-13	1996	These results suggest that these interactions may be important for proper folding of LRP by ensuring the formation of proper intradomain, but not intermolecular or interdomain, disulfide bonds.	Disulfides	177-186	LDL receptor related protein 1	Homo sapiens	85-88
8784206-2	1996	We have previously shown that a single-disulfide variant of human IL-6, lacking 22 N-terminal amino acids and the disulfide bond connecting Cys-45 and Cys-51 in the 185-residue chain of the wild-type protein, fully retains the conformational, stability, and functional properties of the full-length human IL-6 [Breton et al.	Disulfides	114-123	interleukin 6	Homo sapiens	66-70
8812848-1	1996	Lipoprotein(a) is a macromolecular complex consisting of a low-density lipoprotein-like particle with an additional glycoprotein, apolipoprotein(a) [apo(a)], linked to apolipoprotein B-100 via a disulfide bond.	Disulfides	195-204	apolipoprotein B	Homo sapiens	168-188
8806626-4	1996	vWF bound to bitiscetin but not to botrocetin electroblotted to a PVDF membrane after SDS-PAGE and this binding was diminished after reduction of disulfide bonds of bitiscetin.	Disulfides	146-155	von Willebrand factor	Homo sapiens	0-3
8814219-0	1996	Identification of monoclonal antibodies that recognize different disulfide bonded forms of thrombospondin 1.	Disulfides	65-74	thrombospondin 1	Homo sapiens	91-107
8814219-3	1996	We have identified murine monoclonal antibodies that recognized different disulfide-bonded forms of TSP1, made by preparing TSP1 in buffers containing either 0.1 mM or 2 mM Ca2+.	Disulfides	74-83	thrombospondin 1	Homo sapiens	100-104
8814219-7	1996	These results suggested that different disulfide-bonded forms of TSP1 were being expressed in different areas of inflamed tissue.	Disulfides	39-48	thrombospondin 1	Homo sapiens	65-69
8765230-8	1996	These results suggest that though the intra-A chain disulfide bond is deleted, the other two inter-chain disulfide bonds are still correctly paired, and that the intra-A chain disulfide bond is essential for insulin displaying its biological activity.	Disulfides	52-61	insulin	Homo sapiens	208-215
8765230-8	1996	These results suggest that though the intra-A chain disulfide bond is deleted, the other two inter-chain disulfide bonds are still correctly paired, and that the intra-A chain disulfide bond is essential for insulin displaying its biological activity.	Disulfides	105-114	insulin	Homo sapiens	208-215
8765230-8	1996	These results suggest that though the intra-A chain disulfide bond is deleted, the other two inter-chain disulfide bonds are still correctly paired, and that the intra-A chain disulfide bond is essential for insulin displaying its biological activity.	Disulfides	105-114	insulin	Homo sapiens	208-215
8765649-7	1996	The proposed scheme of bFGF oxidation with DTNB revealed that the difference in the aggregate structural forms was probably due either to the presence of covalently bound residues of nitrobenzoic acid in the products of oxidation, or to the participation of sulfhydryl groups in disulfide bond formation.	Disulfides	279-288	fibroblast growth factor 2	Homo sapiens	23-27
8707860-11	1996	Thus, the intracellular location of cysteine transport activity may be cell lineage-dependent, and its presence may, in part, determine whether an organelle is a productive site of processing antigens with disulfide bonds that is necessary for CD4+ cell activation.	Disulfides	206-215	CD4 molecule	Homo sapiens	244-247
8960116-3	1996	The alpha-chain was disulfide-linked to the gamma-chain and the beta-chain was non-covalently associated with the alpha-gamma chain, in fair agreement with mammalian C8.	Disulfides	20-29	Fc gamma receptor and transporter	Homo sapiens	4-15
8889820-0	1996	Selective cleavage and modification of the intersubunit disulfide bonds of bovine dopamine beta-monooxygenase: conversion of tetramer to active dimer.	Disulfides	56-65	dopamine beta-hydroxylase	Bos taurus	82-109
8889820-1	1996	Bovine dopamine beta-monooxygenase is a tetramer consisting of two disulfide-linked dimers.	Disulfides	67-76	dopamine beta-hydroxylase	Bos taurus	7-34
8895096-10	1996	The oligomers of alpha-lactalbumin are stabilized mainly by nonnative interchain disulfide bridges.	Disulfides	81-90	lactalbumin alpha	Homo sapiens	17-34
9237217-5	1996	The cyclized, disulfide-bonded form of one such peptide, SCLRWGKWSNCGS, bound CaM better than its reduced form or an analogue in which the cysteine residues were replaced by serine.	Disulfides	14-23	calmodulin	Bos taurus	78-81
8703948-0	1996	Catalysis of disulfide isomerization in thrombospondin 1 by protein disulfide isomerase.	Disulfides	13-22	thrombospondin 1	Homo sapiens	40-56
8703948-2	1996	The structure and some functional properties of thrombospondin 1 are regulated by disulfide interchange in the Ca(2+)-binding repeats and C-globular domain.	Disulfides	82-91	thrombospondin 1	Homo sapiens	48-64
8703948-3	1996	The recent identification of the enzyme, protein disulfide isomerase, on the platelet surface suggested that protein disulfide isomerase may catalyze disulfide isomerization in platelet thrombospondin 1.	Disulfides	49-58	thrombospondin 1	Homo sapiens	186-202
8703948-4	1996	Protein disulfide isomerase was found to form disulfide-linked complexes with thrombospondin 1, which is consistent with protein disulfide isomerase-mediated rearrangement of disulfide bonds in thrombospondin 1.	Disulfides	8-17	thrombospondin 1	Homo sapiens	78-94
8703948-4	1996	Protein disulfide isomerase was found to form disulfide-linked complexes with thrombospondin 1, which is consistent with protein disulfide isomerase-mediated rearrangement of disulfide bonds in thrombospondin 1.	Disulfides	8-17	thrombospondin 1	Homo sapiens	194-210
8703948-4	1996	Protein disulfide isomerase was found to form disulfide-linked complexes with thrombospondin 1, which is consistent with protein disulfide isomerase-mediated rearrangement of disulfide bonds in thrombospondin 1.	Disulfides	46-55	thrombospondin 1	Homo sapiens	78-94
8703948-4	1996	Protein disulfide isomerase was found to form disulfide-linked complexes with thrombospondin 1, which is consistent with protein disulfide isomerase-mediated rearrangement of disulfide bonds in thrombospondin 1.	Disulfides	46-55	thrombospondin 1	Homo sapiens	194-210
8703948-5	1996	To quantitate disulfide interchange in thrombospondin 1, perturbation of the enzyme inhibitory properties of platelet thrombospondin 1 were measured, specifically changes in the apparent dissociation constant for inhibition of neutrophil cathepsin G by thrombospondin 1.	Disulfides	14-23	thrombospondin 1	Homo sapiens	39-55
8703948-7	1996	The rate of protein disulfide isomerase-catalyzed disulfide interchange in thrombospondin 1 increased linearly with protein disulfide isomerase concentration and the K(m) for reduced glutathione was 0.4 +/- 0.2 mM.	Disulfides	20-29	thrombospondin 1	Homo sapiens	75-91
8703948-8	1996	Disulfide isomerization in both platelet and fibroblast thrombospondin 1 was probed by measuring perturbation in epitopes for two anti-thrombospondin 1 monoclonal antibodies.	Disulfides	0-9	thrombospondin 1	Homo sapiens	56-72
8703948-8	1996	Disulfide isomerization in both platelet and fibroblast thrombospondin 1 was probed by measuring perturbation in epitopes for two anti-thrombospondin 1 monoclonal antibodies.	Disulfides	0-9	thrombospondin 1	Homo sapiens	135-151
8703948-11	1996	In summary, protein disulfide isomerase catalyzes disulfide interchange in thrombospondin 1 which alters binding of neutrophil cathepsin G and antibody D4.6 to thrombospondin 1.	Disulfides	20-29	thrombospondin 1	Homo sapiens	75-91
8703948-11	1996	In summary, protein disulfide isomerase catalyzes disulfide interchange in thrombospondin 1 which alters binding of neutrophil cathepsin G and antibody D4.6 to thrombospondin 1.	Disulfides	20-29	thrombospondin 1	Homo sapiens	160-176
8662901-8	1996	Swapping of the disulfide bridges in IGF-I and the C-region mutants decreased the affinity dramatically for IGFBP-3, primarily by decreasing the association rate.	Disulfides	16-25	insulin like growth factor 1	Homo sapiens	37-42
8663382-4	1996	However, refolding of denatured/reduced lysozyme into buffer that lacks thiol/disulfide reagents leads to aggregation.	Disulfides	78-87	lysozyme	Homo sapiens	40-48
8755737-0	1996	Assignment of free and disulfide-bonded cysteine residues in testis angiotensin-converting enzyme: functional implications.	Disulfides	23-32	angiotensin I converting enzyme	Homo sapiens	68-97
8679613-3	1996	The solution structure of the 25 kDa disulfide-linked TGF-beta 1 homodimer was calculated from over 3200 distance and dihedral angle restraints.	Disulfides	37-46	transforming growth factor beta 1	Homo sapiens	54-64
8895088-1	1996	kappa-Casein as purified from bovine milk exhibits a rather unique disulfide bonding pattern as revealed by SDS-PAGE.	Disulfides	67-76	casein kappa	Bos taurus	0-12
8662732-10	1996	These studies indicate that amino-terminal disulfides are required to stabilize dodecamers, and support our hypothesis that the oligomerization of trimeric subunits contributes to the anti-microbial properties of SP-D.	Disulfides	43-53	pulmonary surfactant-associated protein D	Cricetulus griseus	213-217
8842749-10	1996	The binding of TGF beta 1 to the type I kinase subunit appears to require an intact disulfide-linked ligand dimer in the absence of a type III subunit.	Disulfides	84-93	transforming growth factor beta 1	Homo sapiens	15-25
8786998-0	1996	Computer-aided modeling of structure stabilizing disulfide bonds in recombinant human interferon-gamma.	Disulfides	49-58	interferon gamma	Homo sapiens	86-102
8753066-7	1996	Total synthesis of human insulin, a two chain peptide containing three disulfide bonds, was achieved unambiguously by sequential and selective formation of disulfide bonds in the protein for the first time.	Disulfides	71-80	insulin	Homo sapiens	25-32
8753066-7	1996	Total synthesis of human insulin, a two chain peptide containing three disulfide bonds, was achieved unambiguously by sequential and selective formation of disulfide bonds in the protein for the first time.	Disulfides	156-165	insulin	Homo sapiens	25-32
8753066-10	1996	Using three orthogonal thiol protecting groups, Trt, Acm, and But, three disulfide bonds of human insulin were efficiently constructed by the successive reactions using thiolysis, iodine oxidation, and the sily1 chloride method.	Disulfides	73-82	insulin	Homo sapiens	98-105
8643565-9	1996	As a result, the LCs that were bound to BiP mutants were unable to undergo complete disulfide bond formation and were retained in the ER.	Disulfides	84-93	heat shock protein family A (Hsp70) member 5	Homo sapiens	40-43
8639560-2	1996	Key to this process appears to be the interaction of the tyrosine kinase SH2 domains with the tyrosine-phosphorylated cytoplasmic domain of Ig-alpha, a disulfide-bonded heterodimeric (with Ig-beta or Ig-gamma) transmembrane protein that noncovalently associates with the antigen receptor immunoglobin chains.	Disulfides	152-161	CD79a molecule	Homo sapiens	140-148
8647881-14	1996	Taken together, these results indicate that in addition to disulfide bonds, noncovalent interactions of other amino-terminal amino acid residues in the three fibrinogen chains also participate in dimer formation.	Disulfides	59-68	fibrinogen beta chain	Homo sapiens	158-168
8639781-14	1996	Purified vWF was incubated with the protease, and the degraded material subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis after disulfide reduction.	Disulfides	149-158	von Willebrand factor	Homo sapiens	9-12
8637013-3	1996	The binding constant was estimated to be in the order of 10(5) M-1 by analyzing the kinetic data quantitatively and was found to be much weaker than the binding between GroEL and disulfide-bond reduced alpha-lactalbumin, whose binding constant is in the order of 10(7) M-1.	Disulfides	179-188	lactalbumin alpha	Homo sapiens	202-219
8634257-3	1996	Previous studies have suggested that disulfide-linked homodimers of peripherin/rds and rom-1 can associate noncovalently to form higher order structures.	Disulfides	37-46	peripherin	Bos taurus	68-78
8626682-3	1996	Both I-1 and I-2 contain a native-like disulfide bond, Cys4-Cys89 and Cys43-Cys138, respectively, and I-3 forms a mispaired disulfide, Cys43-Cys89.	Disulfides	39-48	protein phosphatase 1 regulatory inhibitor subunit 1A	Homo sapiens	5-16
8639542-1	1996	A peptide band of approximately 105 kDa migrating near the gamma dimer position of disulfide bond reduced human plasma fibrinogen prepared from fresh single donor or outdated plasma was identified by SDS-PAGE.	Disulfides	83-92	fibrinogen beta chain	Homo sapiens	119-129
8626682-7	1996	I-4 and I-5, which are disulfide-linked dimers, are in equilibrium with reduced rhSCF and other intermediates and may not play an important role in rhSCF folding.	Disulfides	23-32	PPP1R2C family member C	Homo sapiens	0-11
8626682-10	1996	Gel filtration/light-scattering experiments indicate that reduced rhSCF and iodoacetate-trapped I-1, I-2, and I-3 exist as dimeric forms, indicating that rhSCF dimerization precedes formation of disulfide bonds.	Disulfides	195-204	protein phosphatase 1 regulatory inhibitor subunit 1A	Homo sapiens	96-99
8626683-9	1996	In vitro, the disulfide-linked dimer exhibits approximately 3-fold higher biological activity in supporting growth of a hematopoietic cell line and stimulating hematopoietic cell colony formation from enriched human CD34+ cells.	Disulfides	14-23	CD34 molecule	Homo sapiens	216-220
8797087-0	1996	Structural and functional characterization of a novel tumor-derived rat galectin-1 having transforming growth factor (TGF) activity: the relationship between intramolecular disulfide bridges and TGF activity.	Disulfides	173-182	galectin 1	Rattus norvegicus	72-82
8647251-2	1996	Part of synovial fluid alpha1-proteinase inhibitor forms a mixed disulfide with immunoglobulin A, which has been postulated to lack inhibitory activity.	Disulfides	65-74	serpin family A member 1	Bos taurus	23-50
8689720-2	1996	Solid phase synthesis of fibrinogen-related peptides with disulfide bond formed on solid support.	Disulfides	58-67	fibrinogen beta chain	Homo sapiens	25-35
8647100-6	1996	These two parallel disulfide bridges stabilised a beta-sheet structure which comprised two antiparallel strands (residues 5-9 and 12-16) linked by a distorted beta-turn (residues 9-12).	Disulfides	19-28	amyloid beta precursor protein	Homo sapiens	48-54
8797087-9	1996	Chemical modification of sulfhydryl groups in purified t-galectin-1 with [14C]-iodoacetamide suggested the presence of intramolecular disulfide bonds.	Disulfides	134-143	galectin 1	Rattus norvegicus	57-67
8797087-10	1996	MALDI-TOF mass spectrometric analysis of the native and reduced forms of the tryptic peptides from t-galectin-1 showed that t-galectin-1 has two intramolecular disulfide bonds (Cys2-Cys16 and Cys42-Cys60).	Disulfides	160-169	galectin 1	Rattus norvegicus	126-136
8797087-11	1996	These studies suggest that these intramolecular disulfide bonds of t-galectin-1 are essential for its mitogenic activity and that the different activities may be regulated by structural changes caused by intramolecular disulfide bond-breakage.	Disulfides	48-57	galectin 1	Rattus norvegicus	69-79
8797087-11	1996	These studies suggest that these intramolecular disulfide bonds of t-galectin-1 are essential for its mitogenic activity and that the different activities may be regulated by structural changes caused by intramolecular disulfide bond-breakage.	Disulfides	219-228	galectin 1	Rattus norvegicus	69-79
8633035-2	1996	CAIII forms a disulfide link between glutathione and two of its five cysteine residues, a process termed S-glutathiolation.	Disulfides	14-23	carbonic anhydrase 3	Homo sapiens	0-5
8627518-4	1996	Anti-transferrin receptor antibody-rsCD4 conjugates were synthesized with a disulfide linkage and characterized in vitro.	Disulfides	76-85	transferrin	Rattus norvegicus	5-16
11536727-1	1996	We describe a protease, named "thiocalsin," that is activated by  calcium but only after reductive activation by thioredoxin, a small protein with a redox-active disulfide group that functions widely in regulation.	Disulfides	162-171	thioredoxin H4-2	Triticum aestivum	113-124
8622978-5	1996	Insect cells infected with recombinant baculovirus expressing normal vWF sequence secreted a disulfide linked dimeric molecule with an apparent molecular mass of 150 kDa before reduction, yielding a single band of 80 kDa after disulfide bond reduction.	Disulfides	93-102	von Willebrand factor	Homo sapiens	69-72
8622978-5	1996	Insect cells infected with recombinant baculovirus expressing normal vWF sequence secreted a disulfide linked dimeric molecule with an apparent molecular mass of 150 kDa before reduction, yielding a single band of 80 kDa after disulfide bond reduction.	Disulfides	227-236	von Willebrand factor	Homo sapiens	69-72
8622978-7	1996	We conclude that CyS2010 is essential for normal dimerization of vWF subunits through disulfide bonding of carboxyl-terminal domains and that a heterozygous mutation in the corresponding codon is responsible for defective multimer formation in type III) von Willebrand disease.	Disulfides	86-95	von Willebrand factor	Homo sapiens	65-68
11536727-4	1996	The disulfide groups of the enzyme, as well as its protein substrates, were reduced by thioredoxin via NADPH and the associated enzyme, NADP-thioredoxin reductase.	Disulfides	4-13	thioredoxin H4-2	Triticum aestivum	87-98
8603822-0	1996	Improved tumor detection by anti-CEA chimeric Fab oligomers with disulfide linkages in a pancreatic-carcinoma-xenograft model.	Disulfides	65-74	carcinoembryonic antigen gene family	Mus musculus	33-36
11536727-4	1996	The disulfide groups of the enzyme, as well as its protein substrates, were reduced by thioredoxin via NADPH and the associated enzyme, NADP-thioredoxin reductase.	Disulfides	4-13	thioredoxin H4-2	Triticum aestivum	141-152
8648630-5	1996	Each module has the same disulfide bond connections Cys1-Cys3 (loop a), Cys2-Cys4 (loop b), Cys5-Cys6 (loop c) and Cys7-Cys8 (loop d), the first three being identical to epidermal growth factor (EGF).	Disulfides	25-34	cystin 1	Mus musculus	52-56
9026359-7	1996	Granulocytic protein p25 was found to be a product of oxidative cleavage of disulfide bridges in the p50 dimer.	Disulfides	76-85	nuclear factor kappa B subunit 1	Homo sapiens	101-104
8631777-0	1996	Blocking the Ca2+-induced conformational transitions in calmodulin with disulfide bonds.	Disulfides	72-81	calmodulin 1	Homo sapiens	56-66
8609174-12	1996	Both unfolded III-10 and unfolded III-1 could support fibronectin binding, but only III-10 could promote the formation of disulfide-bonded multimers of fibronectin in the absence of cells.	Disulfides	122-131	fibronectin 1	Homo sapiens	152-163
8637916-3	1996	VEGF-B formed cell-surface-associated disulfide-linked homodimers and heterodimerized with VEGF when coexpressed.	Disulfides	38-47	vascular endothelial growth factor A	Homo sapiens	0-4
8631818-0	1996	A disulfide-bonded dimer of the Golgi beta-galactoside alpha2,6-sialyltransferase is catalytically inactive yet still retains the ability to bind galactose.	Disulfides	2-11	ST6 beta-galactoside alpha-2,6-sialyltransferase 2	Bos taurus	55-81
8631818-2	1996	Here we show that 30% of the total rat liver Golgi alpha2,6-sialyltransferase forms a disulfide-bonded 100-kDa species that can be converted to the 50-kDa monomer form of the enzyme upon reduction.	Disulfides	86-95	ST6 beta-galactoside alpha-2,6-sialyltransferase 2	Bos taurus	51-77
8631818-3	1996	Limited proteolysis of both enzyme forms demonstrates that the 100-kDa species is a disulfide-bonded homodimer of the alpha2,6-sialyltransferase.	Disulfides	84-93	ST6 beta-galactoside alpha-2,6-sialyltransferase 2	Bos taurus	118-144
8631818-4	1996	The alpha2,6-sialyltransferase disulfide-bonded dimer is found in bovine liver Golgi membranes and in Golgi membranes prepared and solubilized in the presence of 100 mM iodoacetamide, suggesting that it is not unique to rat liver or formed aberrantly upon membrane lysis.	Disulfides	31-40	ST6 beta-galactoside alpha-2,6-sialyltransferase 2	Bos taurus	4-30
8631818-7	1996	These results suggest that the alpha2,6-sialyltransferase disulfide-bonded dimer lacks catalytic activity due to a weak affinity for its sugar nucleotide donor, CMP-NeuAc, and that this catalytically inactive form of the enzyme may act as a galactose-specific lectin in the Golgi.	Disulfides	58-67	ST6 beta-galactoside alpha-2,6-sialyltransferase 2	Bos taurus	31-57
8619817-1	1996	Midkine (MK) is a heparin binding growth/differentiation factor different from fibroblast growth factors (FGFs), and is largely composed of two domains which are found by a folded polypeptide chain interconnected by disulfide bridges.	Disulfides	216-225	midkine	Homo sapiens	0-7
8619605-4	1996	The ability of isolated rat liver mitochondria to reduce disulfides was examined by the reduction of 5,5"-dithiobis-(2 nitro-benzoic acid) (DTNB), the reaction catalyzed by thioredoxin reductase and glutathione reductase.	Disulfides	57-67	peroxiredoxin 5	Rattus norvegicus	173-194
8605162-0	1996	Role of a disulfide-bonded peptide loop within human complement C9 in the species-selectivity of complement inhibitor CD59.	Disulfides	10-19	CD59 molecule (CD59 blood group)	Homo sapiens	118-122
8608123-0	1996	Recombinant immunotoxin containing a disulfide-stabilized Fv directed at erbB2 that does not require proteolytic activation.	Disulfides	37-46	erb-b2 receptor tyrosine kinase 2	Homo sapiens	73-78
8603589-4	1996	Data suggest intermolecular disulfide bridges and/or intermolecular ionic interactions, as thiols, urea, and chelators increase monomerization of the majority of granule PRL.	Disulfides	28-37	prolactin	Rattus norvegicus	170-173
8577771-1	1996	B1(dsFv)-PE33 is a recombinant immunotoxin composed of a mutant form of Pseudomonas exotoxin (PE) that does not need proteolytic activation and a disulfide-stabilized Fv fragment of the anti-Lewis(y) monoclonal antibody B1, which recognizes a carbohydrate epitope on human carcinoma cells.	Disulfides	146-155	immunoglobulin kappa variable 7-3 (pseudogene)	Homo sapiens	0-13
8649796-9	1996	Using two-dimensional gel electrophoresis, bax complexes were disrupted under reducing conditions to reveal homo- and heterodimers of 18 and 21 kDa suggesting that disulfide interactions were required for complex formation.	Disulfides	164-173	BCL2 associated X, apoptosis regulator	Homo sapiens	43-46
8734474-5	1996	Abolition by mutagenesis (C4S) of the N-terminal disulfide bond increased by 50% the PRL secretion rate (medium to cell ratio) and multiplied by 5 the specific activity of medium PRL from pulse-labeled cells.	Disulfides	49-58	prolactin	Rattus norvegicus	85-88
8734474-5	1996	Abolition by mutagenesis (C4S) of the N-terminal disulfide bond increased by 50% the PRL secretion rate (medium to cell ratio) and multiplied by 5 the specific activity of medium PRL from pulse-labeled cells.	Disulfides	49-58	prolactin	Rattus norvegicus	179-182
8734474-6	1996	These results support the hypothesis that N-terminal disulfide bond plays a role in the control of PRL intracellular transit and storage.	Disulfides	53-62	prolactin	Rattus norvegicus	99-102
8619817-1	1996	Midkine (MK) is a heparin binding growth/differentiation factor different from fibroblast growth factors (FGFs), and is largely composed of two domains which are found by a folded polypeptide chain interconnected by disulfide bridges.	Disulfides	216-225	midkine	Homo sapiens	9-11
9026538-0	1996	Role of intramolecular disulfide bond formation in the assembly and secretion of apolipoprotein B-100-containing lipoproteins.	Disulfides	23-32	apolipoprotein B	Homo sapiens	81-101
8601717-1	1996	Laminins represent a growing family of disulfide-linked heterotrimers constituted by the association of three genetically different polypeptides, the alpha, beta, and gamma chains.	Disulfides	39-48	laminin subunit beta 2	Homo sapiens	0-8
9026538-3	1996	Although apoB contains eight known disulfide bonds, seven of which are positioned in the amino-terminal 21% of the protein, its assembly and secretion was only partially blocked in cells treated with 2 mM DTT, a condition that fully blocks the secretion of other disulfide-bonded proteins.	Disulfides	35-44	apolipoprotein B	Homo sapiens	9-13
9026538-3	1996	Although apoB contains eight known disulfide bonds, seven of which are positioned in the amino-terminal 21% of the protein, its assembly and secretion was only partially blocked in cells treated with 2 mM DTT, a condition that fully blocks the secretion of other disulfide-bonded proteins.	Disulfides	263-272	apolipoprotein B	Homo sapiens	9-13
9026538-4	1996	Nonreducing gel electrophoresis of an apoB-derived proteolytic peptide revealed that apoB escapes the secretory block normally caused by DTT because its amino-terminal disulfide bonds undergo maturation to a DTT-resistant form after completing synthesis of only the first approximately 20-25% of the protein.	Disulfides	168-177	apolipoprotein B	Homo sapiens	38-42
9026538-4	1996	Nonreducing gel electrophoresis of an apoB-derived proteolytic peptide revealed that apoB escapes the secretory block normally caused by DTT because its amino-terminal disulfide bonds undergo maturation to a DTT-resistant form after completing synthesis of only the first approximately 20-25% of the protein.	Disulfides	168-177	apolipoprotein B	Homo sapiens	85-89
9026538-6	1996	Reduced forms of apoB were extremely labile and, unlike other disulfide-bonded proteins, incapable of achieving secretion competence posttranslationally.	Disulfides	62-71	apolipoprotein B	Homo sapiens	17-21
9026538-7	1996	These results indicate that disulfide bond formation within the amino-terminus of apoB is essential for the proper folding and assembly of its downstream lipophilic sequences.	Disulfides	28-37	apolipoprotein B	Homo sapiens	82-86
8547266-0	1996	Disulfide determinants of calcium-induced packing in alpha-lactalbumin.	Disulfides	0-9	lactalbumin alpha	Homo sapiens	53-70
8547266-4	1996	alpha-LA(alpha) contains only the two disulfide bonds in the alpha-helical domain of alpha-LA, while alpha-LA(beta) contains only the beta-sheet domain and interdomain disulfide bonds.	Disulfides	38-47	lactalbumin alpha	Homo sapiens	0-8
8547266-4	1996	alpha-LA(alpha) contains only the two disulfide bonds in the alpha-helical domain of alpha-LA, while alpha-LA(beta) contains only the beta-sheet domain and interdomain disulfide bonds.	Disulfides	38-47	lactalbumin alpha	Homo sapiens	85-93
8547266-4	1996	alpha-LA(alpha) contains only the two disulfide bonds in the alpha-helical domain of alpha-LA, while alpha-LA(beta) contains only the beta-sheet domain and interdomain disulfide bonds.	Disulfides	38-47	lactalbumin alpha	Homo sapiens	85-93
8547266-7	1996	Thus, specific interactions within alpha-LA imposed by the beta-sheet domain and interdomain disulfide bonds, as opposed to the two alpha-helical domain disulfides, are necessary for the calcium-induced progression from the molten globule toward more native-like structure.	Disulfides	93-102	lactalbumin alpha	Homo sapiens	35-43
15251573-1	1995	The major apoproteins of Lp(a)--apo(a) and apo B-100--are linked by only one intermolecular disulfide bond.	Disulfides	92-101	apolipoprotein B	Homo sapiens	43-52
8552654-0	1996	The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: presence of a disulfide bond.	Disulfides	128-137	tachykinin precursor 1	Homo sapiens	32-43
8552654-0	1996	The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: presence of a disulfide bond.	Disulfides	128-137	tachykinin precursor 1	Homo sapiens	101-112
9075580-3	1996	We have used site directed mutagenesis to explore three aspects of the structure of CD59: 1) the role of the disulfide bridges in expression and function of the molecule; 2) the location of epitopes reacting with monoclonal antibodies to the molecule; and 3) the parts of the molecule that are critical to its function in inhibiting complement lysis.	Disulfides	109-118	CD59 molecule (CD59 blood group)	Homo sapiens	84-88
8852563-0	1996	Distance distributions from the tyrosyl to disulfide residues in the oxytocin and [Arg8]-vasopressin measured using frequency-domain fluorescence resonance energy transfer.	Disulfides	43-52	arginine vasopressin	Homo sapiens	89-100
8807712-3	1996	Glycoprotein Ib is an integral membrane protein composed of two disulfide-linked chains noncovalently associated to glycoproteins IX and V. As the receptor of the von Willebrand factor (vWF), GPIb plays a main role in platelet adhesion to the subendothelium.	Disulfides	64-73	von Willebrand factor	Homo sapiens	163-184
8807712-3	1996	Glycoprotein Ib is an integral membrane protein composed of two disulfide-linked chains noncovalently associated to glycoproteins IX and V. As the receptor of the von Willebrand factor (vWF), GPIb plays a main role in platelet adhesion to the subendothelium.	Disulfides	64-73	von Willebrand factor	Homo sapiens	186-189
8713797-6	1996	Reduction of the disulfide bonds in GPIIIa greatly reduced its reactivity, suggesting that the negative charges in the epitope are arranged in a particular conformation.	Disulfides	17-26	integrin subunit beta 3	Homo sapiens	36-42
8713801-6	1996	The studies presented in this paper demonstrated that the A1 domain of bovine vWF contained the GPIb, heparin, botrocetin as well as collagen binding sites and that integrity of the disulfide bond (Cys 509-Cys 695), did not seem to be essential for binding of bovine vWF fragment to GPIb.	Disulfides	182-191	von Willebrand factor	Bos taurus	78-81
8566530-7	1996	In spite of an initial expectation that the structure recognized by an Escherichia coli chaperone, GroEL, is the molten globule, the interaction of GroEL with alpha-lactalbumin in the molten globule state is much weaker than the interaction with more unfolded states of alpha-lactalbumin, a disulfide-reduced form, and disulfide rearranged species.	Disulfides	291-300	GroEL	Escherichia coli	148-153
8566530-7	1996	In spite of an initial expectation that the structure recognized by an Escherichia coli chaperone, GroEL, is the molten globule, the interaction of GroEL with alpha-lactalbumin in the molten globule state is much weaker than the interaction with more unfolded states of alpha-lactalbumin, a disulfide-reduced form, and disulfide rearranged species.	Disulfides	319-328	GroEL	Escherichia coli	148-153
8838586-5	1996	MPAbs to the Cys4190 region of apoB-100, a second or alternative disulfide link-site between apo[a] and apoB-100, were also isolated using a synthetic peptide (G4182IYTREELSTMFIREVG4198) affinity resin.	Disulfides	65-74	apolipoprotein B	Homo sapiens	31-39
8838586-7	1996	In contrast, MPAbs to the apoB-100 region 4182-4198 which contains Cys4190, a second or alternative disulfide link-site between apo[a] and apoB-100, displayed a less significant difference in binding to Lp[a] and LDL.	Disulfides	100-109	apolipoprotein B	Homo sapiens	26-34
8739350-4	1996	Another analog LK-802 was designed by introduction of additional pair of mutations (Cys95Cys148) into LK-801 in order to prepare disulfide linked TNF trimers.	Disulfides	129-138	tumor necrosis factor	Mus musculus	146-149
8840431-1	1996	Adriamycin (ADM) was chemically conjugated to a murine monoclonal antibody, A0011, which recognizes the c-erbB-2 product, via a disulfide bond using N-succinimidyl-3-(2-pyridyldithio) propionate (SPDP) and 2-iminothiolane (2-IT).	Disulfides	128-137	erb-b2 receptor tyrosine kinase 2	Homo sapiens	104-112
7473749-1	1995	The three-dimensional solution structure of bombyxin-II, an insulin-like two-chain peptide produced by the brain of the silkworm Bombyx mori, has been determined by simulated annealing calculations based on 535 distance constraints and 24 torsion-angle constraints derived from NMR data and three distance constraints of the disulfide bonds.	Disulfides	325-334	bombyxin A-6	Bombyx mori	44-55
7592581-1	1995	In the formation of the lipoprotein(a) (Lp(a)) particle, apolipoprotein(a) (apo(a)) and apolipoprotein B (apoB) are covalently linked via a disulfide bond in both humans and human-apo(a)/apoB transgenic mice.	Disulfides	140-149	apolipoprotein B	Homo sapiens	88-104
8567176-1	1995	Endothelin-1 (ET), the most potent vasoconstrictor yet discovered, is a peptide containing 21 amino acids with two intrachain disulfide bridges.	Disulfides	126-135	endothelin 1	Homo sapiens	0-12
8567176-1	1995	Endothelin-1 (ET), the most potent vasoconstrictor yet discovered, is a peptide containing 21 amino acids with two intrachain disulfide bridges.	Disulfides	126-135	endothelin 1	Homo sapiens	14-16
8680650-1	1995	A type I ribosome inactivating protein, gelonin, was linked to Lym-1, a murine monoclonal antibody reactive with a polymorphic determinant of class II HLA-DR histocompatibility leukocyte antigen (HLA) on human lymphoma cells, via a disulfide linkage using the heterobifunctional cross-linking agent, N-succinimidyl-3-(2-pyridyldithio) propionate.	Disulfides	232-241	Fc receptor, IgG, low affinity IIb	Mus musculus	63-68
8587043-9	1995	The data indicate the dimerization mechanism to involve an initial reduction of the Cys7-Cys161 disulfide bond and subsequent random reoxidation of the free thiols across two EPO molecules.	Disulfides	96-105	erythropoietin	Homo sapiens	175-178
7479743-1	1995	Lipoprotein(a) [Lp(a)] is a lipoprotein formed by the disulfide linkage of apolipoprotein (apo) B100 of a low density lipoprotein particle to apolipoprotein(a).	Disulfides	54-63	apolipoprotein B	Homo sapiens	75-100
7479743-2	1995	Prior studies have suggested that one of the C-terminal Cys residues of apo-B100 is involved in the disulfide linkage of apo-B100 to apo(a).	Disulfides	100-109	apolipoprotein B	Homo sapiens	72-80
7479743-2	1995	Prior studies have suggested that one of the C-terminal Cys residues of apo-B100 is involved in the disulfide linkage of apo-B100 to apo(a).	Disulfides	100-109	apolipoprotein B	Homo sapiens	121-129
7548065-4	1995	As a first step toward an understanding of the structure and function of LB repeats, we have expressed the amino-terminal ligand-binding repeat (LB1) of the human LDLR as a recombinant peptide (rLB1) and have determined its disulfide-pairing scheme.	Disulfides	224-233	cytoskeleton associated protein 2	Homo sapiens	145-148
7592581-1	1995	In the formation of the lipoprotein(a) (Lp(a)) particle, apolipoprotein(a) (apo(a)) and apolipoprotein B (apoB) are covalently linked via a disulfide bond in both humans and human-apo(a)/apoB transgenic mice.	Disulfides	140-149	apolipoprotein B	Homo sapiens	106-110
7592581-1	1995	In the formation of the lipoprotein(a) (Lp(a)) particle, apolipoprotein(a) (apo(a)) and apolipoprotein B (apoB) are covalently linked via a disulfide bond in both humans and human-apo(a)/apoB transgenic mice.	Disulfides	140-149	apolipoprotein B	Homo sapiens	187-191
7595472-4	1995	The coordination of the gamma-carboxylate group of 4-Glu-oxytocin and a disulfide sulfur atom of GlyGlyGly-Lys8-vasopressin was reported to occur in the 2N-complexes over medium pH range.	Disulfides	72-81	arginine vasopressin	Homo sapiens	112-123
7557016-2	1995	Thioredoxin reductase contains a redox active disulfide and is a member of the pyridine nucleotide-disulfide oxidoreductase family of flavoenzymes that includes lipoamide dehydrogenase, glutathione reductase, trypanothione reductase, mercuric reductase, and NADH peroxidase.	Disulfides	46-55	mercuric reductase	Escherichia coli	234-252
8554907-6	1995	We propose that differences in the modes of interactions of the V3 disulfide loops with CD4 in SIV and HIV may be responsible for the observed different neutralizing properties of the two V3 loops.	Disulfides	67-76	CD4 molecule	Homo sapiens	88-91
7472433-1	1995	The immunoreactivity for thioredoxin, which catalyzes protein disulfide reductions, has previously been shown to exist in nerve cells and their axons.	Disulfides	62-71	thioredoxin 1	Rattus norvegicus	25-36
7657617-3	1995	We examined proinsulin conformational maturation by monitoring accessibility of protein disulfide bonds.	Disulfides	88-97	insulin	Homo sapiens	12-22
8520114-7	1995	On the other hand, the BDNF purified from the precipitate had low biological activity (EC50 of 2 ng/ml) and incorrect disulfide bonds.	Disulfides	118-127	brain derived neurotrophic factor	Gallus gallus	23-27
9816075-0	1995	Characterization of B1(Fv)PE38 and B1(dsFv)PE38: single-chain and disulfide-stabilized Fv immunotoxins with increased activity that cause complete remissions of established human carcinoma xenografts in nude mice.	Disulfides	66-75	immunoglobulin kappa variable 7-3 (pseudogene)	Homo sapiens	20-30
9816075-0	1995	Characterization of B1(Fv)PE38 and B1(dsFv)PE38: single-chain and disulfide-stabilized Fv immunotoxins with increased activity that cause complete remissions of established human carcinoma xenografts in nude mice.	Disulfides	66-75	immunoglobulin kappa variable 7-3 (pseudogene)	Homo sapiens	35-47
9816075-7	1995	The half-lives in the blood of mice of B1(Fv)PE38 (single-chain) and B1(dsFv)PE38 (disulfide-stabilized) are 23 and 27 min, respectively.	Disulfides	83-92	immunoglobulin kappa variable 7-3 (pseudogene)	Homo sapiens	39-49
9816075-7	1995	The half-lives in the blood of mice of B1(Fv)PE38 (single-chain) and B1(dsFv)PE38 (disulfide-stabilized) are 23 and 27 min, respectively.	Disulfides	83-92	immunoglobulin kappa variable 7-3 (pseudogene)	Homo sapiens	69-81
7657617-5	1995	With t1/2 approximately 10 min, newly synthesized proinsulin becomes resistant to disulfide reduction, correlating with endoplasmic reticulum (ER) export.	Disulfides	82-91	insulin	Homo sapiens	50-60
7657617-8	1995	Employing 30 mM dithiothreitol in vivo, a further decrease in disulfide accessibility is observed following proinsulin conversion to insulin.	Disulfides	62-71	insulin	Homo sapiens	108-118
7657617-8	1995	Employing 30 mM dithiothreitol in vivo, a further decrease in disulfide accessibility is observed following proinsulin conversion to insulin.	Disulfides	62-71	insulin	Homo sapiens	111-118
7657617-9	1995	Incubation of islets with chloroquine or zinc enhances and diminishes accessibility of insulin disulfides, respectively.	Disulfides	95-105	insulin	Homo sapiens	87-94
8528075-3	1995	Modifications within the disulfide-bonded loop containing the activation site and the adjacent hexadecapeptide upstream sequence showed that uPA recognition elements encompassed R29 at the activation site and multiple elements extending upstream to perhaps 13 residues, all maintained in specific conformational register by surrounding pairs of disulfide bonds.	Disulfides	345-354	proline rich acidic protein 1	Homo sapiens	141-144
7662677-2	1995	A disulfide bond linking helices 2 and 3 of the four-helix bundle amino-terminal domain was introduced by mutating threonine-57 to cysteine (Thr57--&gt;Cys) in apoE3 (cysteine at position 112) to determine the influence of the disulfide bond on the properties of this domain.	Disulfides	2-11	apolipoprotein E	Homo sapiens	160-165
8528075-3	1995	Modifications within the disulfide-bonded loop containing the activation site and the adjacent hexadecapeptide upstream sequence showed that uPA recognition elements encompassed R29 at the activation site and multiple elements extending upstream to perhaps 13 residues, all maintained in specific conformational register by surrounding pairs of disulfide bonds.	Disulfides	25-34	proline rich acidic protein 1	Homo sapiens	141-144
7662677-2	1995	A disulfide bond linking helices 2 and 3 of the four-helix bundle amino-terminal domain was introduced by mutating threonine-57 to cysteine (Thr57--&gt;Cys) in apoE3 (cysteine at position 112) to determine the influence of the disulfide bond on the properties of this domain.	Disulfides	227-236	apolipoprotein E	Homo sapiens	160-165
7626644-1	1995	A single, intramolecular disulfide promotes GLUT1 tetramerization.	Disulfides	25-34	solute carrier family 2, facilitated glucose transporter member 1	Cricetulus griseus	44-49
7544344-6	1995	CD59 was found to specifically bind to a peptide corresponding to residues 334-385 of the human C8 alpha-subunit, and to require a disulfide bond between Cys345 and Cys369.	Disulfides	131-140	CD59 molecule (CD59 blood group)	Homo sapiens	0-4
8846437-1	1995	Calcitonin, calcitonin gene related peptide, amylin, and adrenomedullin are structurally related polypeptides characterized by a six or seven amino acid ring structure linked by a disulfide bridge and an amidated C-terminus.	Disulfides	180-189	calcitonin related polypeptide alpha	Homo sapiens	0-10
7638166-3	1995	In purified human PON, residues Cys-41 and Cys-352 form an intramolecular disulfide bond and neither could function as an active-center cysteine.	Disulfides	74-83	paraoxonase 1	Homo sapiens	18-21
8846437-1	1995	Calcitonin, calcitonin gene related peptide, amylin, and adrenomedullin are structurally related polypeptides characterized by a six or seven amino acid ring structure linked by a disulfide bridge and an amidated C-terminus.	Disulfides	180-189	calcitonin related polypeptide alpha	Homo sapiens	12-22
7627335-1	1995	Calcitonin, calcitonin gene-related peptide, adrenomedullin and amylin are structurally related peptides with N-terminal 6-7 amino acid ring structures linked by a disulfide bridge and with amidated C-termini.	Disulfides	164-173	calcitonin related polypeptide alpha	Homo sapiens	0-10
7627335-1	1995	Calcitonin, calcitonin gene-related peptide, adrenomedullin and amylin are structurally related peptides with N-terminal 6-7 amino acid ring structures linked by a disulfide bridge and with amidated C-termini.	Disulfides	164-173	calcitonin related polypeptide alpha	Homo sapiens	12-22
7558597-3	1995	A significant contribution from a slow rotational component supports either the persistence, on the nano-second timescale at least, of a non-flexible alpha-helical structure for the C-terminal tail residues of endothelin-1 in water as solvent, as seen in the X-ray crystallographic structure, or the interaction of the C-terminal tail residues 16-21 with the constrained disulfide-bridged core residues 1-15.	Disulfides	371-380	endothelin 1	Homo sapiens	210-222
8527874-4	1995	The structure of hCGRP is characterized by a rigid N-terminal disulfide-bonded loop followed by helix segments (Val8-Leu16), a gamma-turn (Ser19-Gly21) and several local hydrogen-bonded patterns.	Disulfides	62-71	calcitonin related polypeptide alpha	Homo sapiens	17-22
7558602-5	1995	Analysis of the structures indicates that the residues Tyr5 and Arg9 exhibit similar side chain orientation as that in the corresponding disulfide loop of human transforming growth factor-alpha.	Disulfides	137-146	tumor necrosis factor	Homo sapiens	161-193
8590602-6	1995	These results demonstrate that the disulfide pairings in each of the three domains of human tissue factor pathway inhibitor purified from Escherichia coli are homologous to each other and also to those in bovine pancreatic trypsin inhibitor.	Disulfides	35-44	trophoblast Kunitz domain protein 1	Bos taurus	223-240
17974429-4	1995	Human plasma fibronectin is a high molecular weight (440-530 kD) glycoprotein, consisting of two nearly identical subunits disulfide-bridged close to their C-terminal ends.	Disulfides	123-132	fibronectin 1	Homo sapiens	13-24
7598720-6	1995	It is also concluded that the six crucial cysteine residues, e.g., Cys50, Cys63, Cys72, Cys86, Cys105 and Cys122 in the N-terminal extracellular domain, may be functionally important by forming intramolecular disulfide bonds which help to maintain the topology for ligand binding in human VIP 1 receptors.	Disulfides	209-218	vasoactive intestinal peptide	Homo sapiens	289-292
8578449-5	1995	Our data underline the crucial role of the 509-695 disulfide bond in the binding of vWF to GPIb and discriminate the specificity of each Cys in this binding.	Disulfides	51-60	von Willebrand factor	Homo sapiens	84-87
7794252-4	1995	Most of the recombinant IGF1 molecules, secreted from yeast, are a conglomeration of inactive multimers which are either disulfide-linked or mere physical aggregates.	Disulfides	121-130	insulin like growth factor 1	Homo sapiens	24-28
7541042-1	1995	A disulfide-linked homodimer binds two CD86 molecules.	Disulfides	2-11	superoxide dismutase 1	Homo sapiens	19-28
15714754-1	1995	In the last stage of fibrinogen synthesis, two Aalpha-Bbeta-gamma half-molecules are disulfide linked in their N-terminal regions to form a dimeric fibrinogen molecule.	Disulfides	85-94	fibrinogen beta chain	Homo sapiens	21-31
15714754-1	1995	In the last stage of fibrinogen synthesis, two Aalpha-Bbeta-gamma half-molecules are disulfide linked in their N-terminal regions to form a dimeric fibrinogen molecule.	Disulfides	85-94	fibrinogen beta chain	Homo sapiens	148-158
7539791-8	1995	Based on sequence analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and reaction with specific antibodies, one is shown to be a 2:2 disulfide-bound complex (approximately 200 kDa) between proMBP and angiotensinogen.	Disulfides	151-160	angiotensinogen	Homo sapiens	218-233
7539426-10	1995	These results, and the locations of von Willebrand disease type 2B mutations, suggest that two acidic regions containing the Cys-509-Cys-695 disulfide (Glu-497-Arg-511, Arg-687-Val-698) and one predominantly basic region (Met-540-Arg-578) cooperate to inhibit a distinct GPIb binding site in the VWF A1 domain.	Disulfides	141-150	von Willebrand factor	Homo sapiens	296-299
7779780-4	1995	This domain was linked by a disulfide bond to apo B100.	Disulfides	28-37	apolipoprotein B	Homo sapiens	46-54
7756638-4	1995	However, disruption of disulfide bonds located at or near the N-terminus of GPIIIa abolished the binding of all the anti-PlA1 alloantibodies tested.	Disulfides	23-32	integrin subunit beta 3	Homo sapiens	76-82
7539971-3	1995	Sedimentation analysis and nonreducing SDS-PAGE revealed that NS2 of all three orbiviruses is a 7S multimer with both inter- and intramolecular disulfide bonds, probably consisting of six or more NS2 molecules.	Disulfides	144-153	NS2	Homo sapiens	62-65
7607216-9	1995	MelT, an adduct of melarsen oxide and dihydrotrypanothione which is a competitive inhibitor of the disulfide binding site of trypanothione reductase, confers protection against Triostam.	Disulfides	99-108	trypanothione reductase	Leishmania donovani	125-148
7659790-0	1995	Disulfide bridges in extracellular domains of angiotensin II receptor type IA.	Disulfides	0-9	angiotensinogen	Rattus norvegicus	46-60
7567962-5	1995	The published data on the alignments for the fibronectin type III repeat region of the INSR together with previous cysteine mutagenesis studies indicated that there were two disulfide bonds linking the alpha and beta chains of the INSR, but only one alpha-beta linkage in the insulin-like growth factor 1 receptor (IG1R).	Disulfides	174-183	fibronectin 1	Homo sapiens	45-56
7659790-1	1995	Angiotensin II receptor type IA (AT1A) has a cysteine (Cys) residue in each of four extracellular domains, and these Cys residues are believed to form two disulfide bridges.	Disulfides	155-164	angiotensinogen	Rattus norvegicus	0-14
7759526-3	1995	TSP1 trimer formation is mediated by interchain disulfide linkage involving two NH2-terminal cysteines.	Disulfides	48-57	thrombospondin 1	Homo sapiens	0-4
7766603-6	1995	We propose that the fluorescence changes as well as the changes in affinity for gelatin or the collagen fragment result from structural changes secondary to the breakage of disulfide bonds, as a consequence of energy transfer from nearby tryptophans in one or more of the Fn type I repeats in the gelatin binding region of fibronectin.	Disulfides	173-182	fibronectin 1	Homo sapiens	323-334
7538125-6	1995	However, coexpression of the hCG-alpha gene enhanced folding and formation of disulfide bonds 23-72, 93-100, and 26-110 of hCG-beta lacking N-linked glycans.	Disulfides	78-87	chromogranin A	Homo sapiens	29-38
7766677-1	1995	Tick anticoagulant peptide (TAP) is a disulfide rich potent inhibitor of factor Xa.	Disulfides	38-47	nuclear RNA export factor 1	Rattus norvegicus	28-31
7766677-5	1995	Disulfide bonds play a significant role in the folding and structural stability of rTAP.	Disulfides	0-9	nuclear RNA export factor 1	Rattus norvegicus	83-87
7766677-6	1995	This is apparent from the resistance of rTAP to fluorescence-detected unfolding by guanidinium chloride (Gdn-HCl), unless disulfides are first reduced.	Disulfides	122-132	nuclear RNA export factor 1	Rattus norvegicus	40-44
7766681-3	1995	The rate constant for the reaction of GSSG with thioltransferase to form a thioltransferase-glutathione mixed disulfide and GSH was estimated to be &gt; or = 7.1(+/- 0.4).10(5) M-1 s-1.	Disulfides	110-119	glutaredoxin-1	Sus scrofa	48-64
7744853-3	1995	The decrease in DNA binding activity is due to the formation of disulfide bond(s), formed between two specific cysteine residues located outside the TTF-1 homeodomain; hence, oxidation does not appear to directly hinder TTF-1/DNA contacts.	Disulfides	64-73	NK2 homeobox 1	Homo sapiens	149-154
7744853-4	1995	Disulfide bond formation seems to stabilize preexisting, loosely associated, TTF-1 dimers, which, upon oxidation, proceed in the formation of specific, higher order oligomers.	Disulfides	0-9	NK2 homeobox 1	Homo sapiens	77-82
7766681-3	1995	The rate constant for the reaction of GSSG with thioltransferase to form a thioltransferase-glutathione mixed disulfide and GSH was estimated to be &gt; or = 7.1(+/- 0.4).10(5) M-1 s-1.	Disulfides	110-119	glutaredoxin-1	Sus scrofa	75-91
7766681-4	1995	This reaction is proposed to be the first step in the mechanism by which the activity of some proteins is modulated by the thioltransferase-catalyzed formation of protein-glutathione mixed disulfides.	Disulfides	189-199	glutaredoxin-1	Sus scrofa	123-139
7766681-9	1995	The results suggest that the gamma-L-glutamyl-L-cysteinyl moiety of GSSG and of GSH-containing mixed disulfides is essential for their recognition by thioltransferase.	Disulfides	101-111	glutaredoxin-1	Sus scrofa	150-166
7771788-5	1995	In the presence of various pyridine nucleotide-dependent substrates, mitochondria are able to reduce the disulfide 5,5"-dithiobis (2-nitrobenzoic acid) (DTNB) to an extent far larger than that calculated from the theoretical amount of total mitochondrial thiol groups, indicating the occurrence of a catalytic system.	Disulfides	105-114	dystrobrevin, beta	Rattus norvegicus	153-157
7707501-0	1995	Constitutive activation of a variant of the env-mpl oncogene product by disulfide-linked homodimerization.	Disulfides	72-81	MPL proto-oncogene, thrombopoietin receptor	Homo sapiens	48-51
7707501-7	1995	We show here that a mutation converting this cysteine to a glycine completely abolishes del3-mpl oncogenicity and that the del3-mpl oncogene product is constitutively activated by disulfide-linked homodimerization.	Disulfides	180-189	MPL proto-oncogene, thrombopoietin receptor	Homo sapiens	69-72
7718556-1	1995	Addition of the Lys(-2)-Arg(-1) dipeptide, present in the precursor protein, to the N-terminus of endothelin-1 (ET-1), to form a 23-residue peptide (KR-ET-1) has been shown to greatly improve formation of native disulfide bridges and to dramatically decrease biological activity.	Disulfides	212-221	endothelin 1	Homo sapiens	112-116
7718582-9	1995	In hITF (monomer) six of the seven cysteines are disulfide-linked to form 3 disulfide bridges.	Disulfides	76-85	trefoil factor 3	Homo sapiens	3-7
7664466-2	1995	Lp(a) is a low-density lipoprotein (LDL)-like particle which contains a glycoprotein (apoprotein(a)) disulfide linked to apo B-100.	Disulfides	101-110	apolipoprotein B	Homo sapiens	121-130
7721858-2	1995	Intestinal trefoil factor (ITF) is a small peptide bearing the unique motif of intrachain disulfide bonds characteristic of the trefoil family.	Disulfides	90-99	trefoil factor 3	Homo sapiens	0-25
7721858-2	1995	Intestinal trefoil factor (ITF) is a small peptide bearing the unique motif of intrachain disulfide bonds characteristic of the trefoil family.	Disulfides	90-99	trefoil factor 3	Homo sapiens	27-30
7718556-0	1995	[Lys(-2)-Arg(-1)]endothelin-1 solution structure by two-dimensional 1H-NMR: possible involvement of electrostatic interactions in native disulfide bridge formation and in biological activity decrease.	Disulfides	137-146	endothelin 1	Homo sapiens	17-29
7718556-11	1995	In vitro, native disulfide bond formation improvement observed for KR-ET-1 could be ascribed to electrostatic interactions and more specifically to the Arg(-1)-Glu10 salt bridge.	Disulfides	17-26	endothelin 1	Homo sapiens	70-74
7718582-11	1995	Sequence and mass spectrometry analyses as well as peptide mapping showed that the dimer form of both hITF and rITF is mediated by a disulfide bridge between Cys-57 residues of two monomers.	Disulfides	133-142	trefoil factor 3	Homo sapiens	102-106
7718582-9	1995	In hITF (monomer) six of the seven cysteines are disulfide-linked to form 3 disulfide bridges.	Disulfides	49-58	trefoil factor 3	Homo sapiens	3-7
7786412-1	1995	The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers.	Disulfides	255-264	interleukin 2	Homo sapiens	81-85
7747964-5	1995	The apparent migration of this enterotoxin determined by SDS-PAGE did not shift in the presence of a disulfide reducing agent, indicating that it is composed of a single-chain protein.	Disulfides	101-110	Enterotoxin	Staphylococcus aureus	31-42
7749627-1	1995	Haptoglobin (Hp), a hemoglobin-binding protein in plasma, consists of alpha and beta subunits and has a tetra-chain arrangement (beta-alpha-alpha-beta) connected by disulfide bridges in most mammals so far examined.	Disulfides	165-174	haptoglobin	Canis lupus familiaris	0-11
7542260-8	1995	In contrast, fibronectin monomers in the same lysates are gradually formed into disulfide-bonded dimers.	Disulfides	80-89	fibronectin 1	Homo sapiens	13-24
7703261-8	1995	Constraining these molecules to the unimolecular quadruplex/duplex structure by bridging the 5" and 3" ends of the duplex motif with either triethylene glycol or disulfide bonds improved their thrombin inhibitory activity.	Disulfides	162-171	coagulation factor II, thrombin	Homo sapiens	193-201
7546247-3	1995	Biologically active TGF-beta represents a family of 25-kDa homodimeric proteins linked with disulfide bonds.	Disulfides	92-101	transforming growth factor beta 1	Homo sapiens	20-28
7724183-0	1995	Disruption of conserved rhodopsin disulfide bond by Cys187Tyr mutation causes early and severe autosomal dominant retinitis pigmentosa.	Disulfides	34-43	rhodopsin	Homo sapiens	24-33
7724183-4	1995	RESULTS: Affected family members are heterozygous for a unique Cys187Tyr rhodopsin mutation which disrupts a highly conserved disulfide bond essential to normal rhodopsin function.	Disulfides	126-135	rhodopsin	Homo sapiens	73-82
7724183-4	1995	RESULTS: Affected family members are heterozygous for a unique Cys187Tyr rhodopsin mutation which disrupts a highly conserved disulfide bond essential to normal rhodopsin function.	Disulfides	126-135	rhodopsin	Homo sapiens	161-170
7724183-10	1995	CONCLUSION: An early onset, blinding form of autosomal dominant RP results from a rhodopsin Cys187Tyr mutation that eliminates a residue necessary for the formation of a highly conserved disulfide bond essential to normal rhodopsin function.	Disulfides	187-196	rhodopsin	Homo sapiens	82-91
7724183-10	1995	CONCLUSION: An early onset, blinding form of autosomal dominant RP results from a rhodopsin Cys187Tyr mutation that eliminates a residue necessary for the formation of a highly conserved disulfide bond essential to normal rhodopsin function.	Disulfides	187-196	rhodopsin	Homo sapiens	222-231
7786412-1	1995	The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers.	Disulfides	139-148	interleukin 2	Homo sapiens	81-85
7788295-0	1995	Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B.	Disulfides	51-60	nuclear factor kappa B subunit 1	Homo sapiens	136-146
7788295-2	1995	It has recently been shown to be responsible for activating the DNA-binding properties of the cellular transcription factor, NF kappa B, by reducing a disulfide bond involving Cys62 of the p50 subunit.	Disulfides	151-160	nuclear factor kappa B subunit 1	Homo sapiens	125-135
7788295-2	1995	It has recently been shown to be responsible for activating the DNA-binding properties of the cellular transcription factor, NF kappa B, by reducing a disulfide bond involving Cys62 of the p50 subunit.	Disulfides	151-160	nuclear factor kappa B subunit 1	Homo sapiens	189-192
7880817-4	1995	Thus, residues 18-177 in SHBG encompass a region required for its steroid-binding activity, and a disulfide bridge normally present between Cys-164 and Cys-188 in SHBG is not obviously essential for steroid binding.	Disulfides	98-107	sex hormone binding globulin	Homo sapiens	163-167
7880819-7	1995	Our results suggest that molten globules contain regions with varying degrees of specificity for native-like structure and that the core region surrounding the 28-111 disulfide bond plays an important role in alpha-LA folding by stabilizing the molten globule intermediate.	Disulfides	167-176	lactalbumin alpha	Homo sapiens	209-217
7788295-3	1995	Using multidimensional heteronuclear-edited and hetero-nuclear-filtered NMR spectroscopy, we have solved the solution structure of a complex of human thioredoxin and a 13-residue peptide extending from residues 56-68 of p50, representing a kinetically stable mixed disulfide intermediate along the reaction pathway.	Disulfides	265-274	nuclear factor kappa B subunit 1	Homo sapiens	220-223
7788295-6	1995	CONCLUSIONS: In addition to the intermolecular disulfide bridge between Cys32 of human thioredoxin and Cys62 of the peptide, the complex is stabilized by numerous hydrogen-bonding, electrostatic and hydrophobic interactions which involve residues 57-65 of the NF kappa B peptide and confer substrate specificity.	Disulfides	47-56	nuclear factor kappa B subunit 1	Homo sapiens	260-270
7887985-3	1995	Inhibition of ID-1 was attributed initially to the formation of a mixed disulfide between PTU and a putative cysteine residue at the active site.	Disulfides	72-81	inhibitor of DNA binding 1, HLH protein	Rattus norvegicus	14-18
7876253-6	1995	This demonstrated that folding and disulfide bond formation of t-PA determines its extent of core N-linked glycosylation.	Disulfides	35-44	plasminogen activator, tissue type	Homo sapiens	63-67
7876253-7	1995	When dithiothreitol was removed from the cells, the reduced and overglycosylated t-PA formed disulfide bonds, folded, and was secreted.	Disulfides	93-102	plasminogen activator, tissue type	Homo sapiens	81-85
7853497-3	1995	E1, which folds into its mature conformation via at least three intermediates differing in the configurations of their disulfide bonds, was found to interact strongly and transiently with BiP after synthesis.	Disulfides	119-128	heat shock protein family A (Hsp70) member 5	Homo sapiens	188-191
7853497-6	1995	These results suggest that the ATP-regulated binding and release of BiP have a role in modulating disulfide bond formation during E1 folding.	Disulfides	98-107	heat shock protein family A (Hsp70) member 5	Homo sapiens	68-71
7850810-11	1995	Together, these data suggest that sialyl-Lex antigen in colon, colon carcinoma, and the sera of patients with this tumor is located on the MUC2 molecule, consisting of several subunits with an apparent M(r) 880,000, linked via disulfide bridges.	Disulfides	227-236	mucin 2, oligomeric mucus/gel-forming	Homo sapiens	139-143
7536892-2	1995	Considering five disulfide bridges of CD59, we divided the molecule into two portions and synthesized the two peptides.	Disulfides	17-26	CD59 molecule (CD59 blood group)	Homo sapiens	38-42
7849060-5	1995	The conformation of an ETB receptor-specific agonist, IRL 1620, which lacks the N-terminal seven residues and the two intrachain disulfides, was found by NMR and circular dichroism spectroscopy to be predominantly random coil, despite the fact that its affinity for the ETB receptor almost equals that of ET1.	Disulfides	129-139	endothelin receptor type B	Homo sapiens	23-26
7882997-0	1995	A genetic variant of albumin (albumin Asola; Tyr140-->Cys) with no free -SH group but with an additional disulfide bridge.	Disulfides	105-114	albumin	Homo sapiens	21-28
7772282-2	1995	The current model suggests a two-site binding motif in which part of the amino-terminal extracellular domain of the receptor is recognized first by the amino-terminal end and disulfide-linked core of the C5a ligand.	Disulfides	175-184	complement C5a receptor 1	Homo sapiens	204-214
7702187-8	1995	These peptides share structural features with CDD/ANP with regard to their 17-amino-acid-exhibiting loop bridged by a disulfide bond.	Disulfides	118-127	natriuretic peptide A	Homo sapiens	46-49
7702187-8	1995	These peptides share structural features with CDD/ANP with regard to their 17-amino-acid-exhibiting loop bridged by a disulfide bond.	Disulfides	118-127	natriuretic peptide A	Homo sapiens	50-53
7796045-1	1995	Endothelin-1, a bicyclic 21-amino acid peptide with disulfide bridges between cysteines 1 and 15 as well as between cysteines 3 and 11, has been reported to be partially helical based on both CD and NMR data.	Disulfides	52-61	endothelin 1	Homo sapiens	0-12
7529790-4	1995	Under reducing conditions, there was an apparent decrease in the molecular mass of the alpha-chain, which is likely to result from the release of a protein of 20 to 30 kDa linked by internal disulfide bond to the alpha v-chain.	Disulfides	191-200	Fc gamma receptor and transporter	Homo sapiens	87-98
7852537-2	1995	There was no activity detected in the absence of reduced glutathione, which indicates that insulin is cleaved in human adipose tissue through reduction of the disulfide bridge between the chains.	Disulfides	159-168	insulin	Homo sapiens	91-98
7819243-5	1995	Insulin was selected since unfolding can be triggered by reduction of the interchain disulfide bonds, a treatment that does not affect alpha-crystallin.	Disulfides	85-94	insulin	Homo sapiens	0-7
7851440-0	1995	Structure, stability and biological properties of a N-terminally truncated form of recombinant human interleukin-6 containing a single disulfide bond.	Disulfides	135-144	interleukin 6	Homo sapiens	101-114
7851440-2	1995	The 163-residue protein des-(A1-S22)-[C45S, C51S]interleukin-6, containing a single disulfide bridge, formed inclusion bodies.	Disulfides	84-93	interleukin 6	Homo sapiens	49-62
7851654-10	1995	These studies indicate that AM50 is first assembled into a disulfide-cross-linked complex and subsequently processed into mature AM50.	Disulfides	59-68	neuronal pentraxin-2	Cavia porcellus	28-32
7734198-6	1995	In addition, because significantly higher levels of the Nef oligomers were consistently observed under the nonreducing SDS-PAGE condition, site-specific mutagenesis was also used to examine the role of cysteine residues in generating disulfide-linked Nef dimers in vitro.	Disulfides	234-243	S100 calcium binding protein B	Homo sapiens	56-59
7734198-6	1995	In addition, because significantly higher levels of the Nef oligomers were consistently observed under the nonreducing SDS-PAGE condition, site-specific mutagenesis was also used to examine the role of cysteine residues in generating disulfide-linked Nef dimers in vitro.	Disulfides	234-243	S100 calcium binding protein B	Homo sapiens	251-254
7734198-8	1995	Therefore, these results demonstrate that the leucine zipper-type motif in the HIV-2 Nef protein mediates stable homooligomer formation in vitro, and also establish a role for covalent disulfide bonds in the formation of linked Nef dimers and thermal stability of the monomer Nef in vitro.	Disulfides	185-194	S100 calcium binding protein B	Homo sapiens	85-88
7734198-8	1995	Therefore, these results demonstrate that the leucine zipper-type motif in the HIV-2 Nef protein mediates stable homooligomer formation in vitro, and also establish a role for covalent disulfide bonds in the formation of linked Nef dimers and thermal stability of the monomer Nef in vitro.	Disulfides	185-194	S100 calcium binding protein B	Homo sapiens	228-231
7734198-8	1995	Therefore, these results demonstrate that the leucine zipper-type motif in the HIV-2 Nef protein mediates stable homooligomer formation in vitro, and also establish a role for covalent disulfide bonds in the formation of linked Nef dimers and thermal stability of the monomer Nef in vitro.	Disulfides	185-194	S100 calcium binding protein B	Homo sapiens	228-231
7835433-5	1995	Furthermore, as isolated the thioredoxin domains of CaBP1 and CaBP2 were in disulfide form as judged by stoichiometric oxidation of 2 and 3 mol of NADPH in CaBP1 and CaBP2, respectively.	Disulfides	76-85	thioredoxin 1	Rattus norvegicus	29-40
7835433-5	1995	Furthermore, as isolated the thioredoxin domains of CaBP1 and CaBP2 were in disulfide form as judged by stoichiometric oxidation of 2 and 3 mol of NADPH in CaBP1 and CaBP2, respectively.	Disulfides	76-85	calcium binding protein 2	Rattus norvegicus	62-67
7835433-6	1995	The redox potential of the active site disulfide/dithiol was estimated from the equilibrium with a mutant E. coli Trx, P34H Trx, with a known redox potential (-235 mV).	Disulfides	39-48	thioredoxin 1	Rattus norvegicus	114-117
7835433-6	1995	The redox potential of the active site disulfide/dithiol was estimated from the equilibrium with a mutant E. coli Trx, P34H Trx, with a known redox potential (-235 mV).	Disulfides	39-48	thioredoxin 1	Rattus norvegicus	124-127
7835433-7	1995	This showed that CaBP1 and CaBP2, like PDI, have a much higher redox potential than wild type thioredoxin (-270 mV) in agreement with a role in formation of protein disulfide bonds.	Disulfides	165-174	calcium binding protein 2	Rattus norvegicus	27-32
7805042-0	1995	Development of a humanized disulfide-stabilized anti-p185HER2 Fv-beta-lactamase fusion protein for activation of a cephalosporin doxorubicin prodrug.	Disulfides	27-36	erb-b2 receptor tyrosine kinase 2	Homo sapiens	57-61
8527160-1	1995	Vascular endothelial growth factor (VEGF) is a glycoprotein consisting of two identical polypeptide chains linked by a disulfide bond.	Disulfides	119-128	vascular endothelial growth factor A	Homo sapiens	0-34
8527160-1	1995	Vascular endothelial growth factor (VEGF) is a glycoprotein consisting of two identical polypeptide chains linked by a disulfide bond.	Disulfides	119-128	vascular endothelial growth factor A	Homo sapiens	36-40
8913924-3	1995	The receptors consist of a disulfide rich domain which recognizes TNF, a transmembrane helix, and a cytoplasmic domain.	Disulfides	27-36	tumor necrosis factor	Homo sapiens	66-69
8688495-5	1995	Our data thus indicates that the protein disulfide isomerase not only facilitates the correct formation of disulfide-bonds of the antibody molecule, but also the correct refolding of the TNF moiety in vitro.	Disulfides	41-50	tumor necrosis factor	Homo sapiens	187-190
7814634-2	1995	The characteristic form of AChE in the end-plate basal lamina has the catalytic subunits disulfide linked to a collagen-like tail unit.	Disulfides	89-98	acetylcholinesterase (Cartwright blood group)	Homo sapiens	27-31
7811279-5	1994	Cysteine 524 is most likely involved in a class I disulfide bond and receptors mutated at this site displayed unusual insulin binding properties only in the cellular environment.	Disulfides	50-59	insulin	Homo sapiens	118-125
7838126-5	1995	With the natriuretic peptide analogs we tested, human NPR-A is less sensitive than rat or mouse NPR-A to changes in the 17-amino acid, disulfide-bonded ring of ANP and to the species differences in brain natriuretic peptide (BNP) but is more sensitive to deletions in the carboxyl tail of ANP.	Disulfides	135-144	natriuretic peptide receptor 1	Homo sapiens	54-59
7766047-11	1995	RPP13-1 produced in Escherichia coli was reactive to antiserum against wheat thioredoxin h. Both E. coli-produced RPP13-1 and the phloem sap proteins catalyzed the reduction of the disulfide bonds of insulin in the presence of dithiothreitol.	Disulfides	181-190	thioredoxin H4-2	Triticum aestivum	77-88
7798266-3	1994	Apexin consists of disulfide-linked 50-kDa subunits that give rise to an oligomeric protein.	Disulfides	19-28	neuronal pentraxin-2	Cavia porcellus	0-6
7798222-1	1994	A baculovirus system was used to express full-length recombinant mouse thrombospondin 2 (rTSP2) as a disulfide-bonded homotrimer with an NH2 terminus beginning with Asp20.rTSP2, like TSP1, was more sensitive to trypsin digestion if depleted of calcium ion.	Disulfides	101-110	thrombospondin 2	Rattus norvegicus	89-94
7806542-6	1994	Immunoblotting with antibodies directed against serum albumin demonstrated the presence of albumin covalently linked to fibrinogen via a disulfide bridge.	Disulfides	137-146	albumin	Homo sapiens	54-61
7806514-5	1994	Cysteine residues 2 and 4 in VPF were found to be directly involved in anti-parallel interchain disulfide bonds, as in PDGF.	Disulfides	96-105	vascular endothelial growth factor A	Homo sapiens	29-32
7806542-6	1994	Immunoblotting with antibodies directed against serum albumin demonstrated the presence of albumin covalently linked to fibrinogen via a disulfide bridge.	Disulfides	137-146	albumin	Homo sapiens	91-98
7806518-4	1994	While the basic fold is similar to that seen for interleukin-8 (IL-8) (Clore, G. M., Appella, E., Yamada, M., Matsushima, K., and Gronenborn, A. M. (1990) Biochemistry, 29, 1689-1696), there are differences in the ELR motif (residues 6-8), the turn involving residues 31-36, which is linked to the NH2-terminal region through the 9-35 disulfide bond.	Disulfides	335-344	C-X-C motif chemokine ligand 8	Homo sapiens	64-68
7721329-3	1994	Specific GTPoxi labeling of CD3-zeta was found in all murine T cells in which a complete CD3-zeta polypeptide chain was expressed, including cells in which CD3-zeta was disulfide bridged to the Fc epsilon R1 gamma chain.	Disulfides	169-178	CD247 antigen	Mus musculus	28-36
7821796-1	1994	The Marek"s disease virus (MDV) glycoprotein B (gB) precursor, gp100, is proteolytically cleaved into two disulfide-linked subunits, gp60 and gp49.	Disulfides	106-115	premelanosome protein	Homo sapiens	63-68
7929084-2	1994	Lipoprotein(a) (Lp(a)) is a lipoprotein formed by the disulfide linkage of apolipoprotein(a) (apo(a)) to the apoB100 of a low density lipoprotein particle.	Disulfides	54-63	apolipoprotein B	Homo sapiens	109-116
7969090-3	1994	However, here we show that rapid (10-min) uptake inhibitions by AA or by ROS generated by the xanthine plus xanthine oxidase (XO) reaction are selectively abolished by distinct agents; bovine serum albumin (BSA) acts only on AA, whereas the scavenger enzymes superoxide dismutase (SOD) and catalase (CAT) and the disulfide-reducing agent dithiothreitol (DTT) act only on ROS.	Disulfides	313-322	albumin	Homo sapiens	192-205
8083969-5	1994	The binding of measles virus to MCP was abolished after cleavage of the disulfide bonds by reducing agents as well as after enzymatic release of N-linked oligosaccharides.	Disulfides	72-81	CD46 molecule	Homo sapiens	32-35
8083969-7	1994	These data indicate that the receptor determinant of MCP is dependent on a conformation of the protein that is maintained by disulfide bonds and N-glycans present in the complement binding domains.	Disulfides	125-134	CD46 molecule	Homo sapiens	53-56
7947973-9	1994	Most of the DTT-susceptible disulfides were within the C9a fragment (an N-terminal peptide derived by thrombin).	Disulfides	28-38	coagulation factor II, thrombin	Homo sapiens	102-110
7957261-0	1994	A kinetic study on pantetheinase inhibition by disulfides.	Disulfides	47-57	vanin 1	Homo sapiens	19-32
7957261-6	1994	Data reported here indicate that pantetheinase reacts irreversibly with various disulfides in a time-dependent manner with the formation of a mixed disulfide apparently preceeded by a conformational change, giving a modified E* form with new kinetic parameters.	Disulfides	80-90	vanin 1	Homo sapiens	33-46
7957261-6	1994	Data reported here indicate that pantetheinase reacts irreversibly with various disulfides in a time-dependent manner with the formation of a mixed disulfide apparently preceeded by a conformational change, giving a modified E* form with new kinetic parameters.	Disulfides	80-89	vanin 1	Homo sapiens	33-46
7929206-6	1994	Purified CTLA-2 beta exists in solution primarily as a dimer but also as a disulfide-linked tetramer as judged by size exclusion chromatography.	Disulfides	75-84	cytotoxic T lymphocyte-associated protein 2 beta	Mus musculus	9-20
7983787-2	1994	The basic structure of the insulin receptor is a disulfide-linked tetramer, composed of the alpha subunit (135 kDa), which is extracellular and provides the binding site for insulin, and the beta subunit (95 kDa), contains the transmembrane domain, tyrosine kinase domain and C-terminal domain.	Disulfides	49-58	insulin	Homo sapiens	174-211
7827508-3	1994	The secreted Fd-BCCP* fusion and L chain proteins were found to be disulfide linked and Fab-BCCP* complexes of an IgG1 antibody (Mab4) to human tumor necrosis factor alpha (TNF) were shown to retain both antigen and streptavidin-binding activities.	Disulfides	67-76	tumor necrosis factor	Homo sapiens	173-176
7925967-3	1994	It is shown that spinach DHA reductase and soybean trypsin inhibitor are both capable of reducing dehydroascorbate when in the reduced (thiol) form but acquire trypsin-inhibiting activity in the oxidized (disulfide) state.	Disulfides	205-214	kunitz trypsin protease inhibitor	Glycine max	51-68
7918370-0	1994	Complete assignment of disulfide bonds in bovine dopamine beta-hydroxylase.	Disulfides	23-32	dopamine beta-hydroxylase	Bos taurus	49-74
7918370-10	1994	We propose that these five internal disulfide bonds define two Cu2+ binding domains that make up the active site of a dopamine beta-hydroxylase monomer.	Disulfides	36-45	dopamine beta-hydroxylase	Bos taurus	118-143
7918378-6	1994	The IL4 mutants were then each conjugated through a disulfide bond to PE35, a truncated form of PE which contains a single cysteine.	Disulfides	52-61	interleukin 4	Homo sapiens	4-7
7929084-3	1994	Earlier site-directed mutagenesis studies of apo(a) demonstrated that apo(a) cysteine 4057 is required for the disulfide linkage; however, the cysteine residue within apoB100 that is involved in the disulfide bond has not been identified.	Disulfides	199-208	apolipoprotein B	Homo sapiens	167-174
8068945-6	1994	Results unambiguously demonstrated that the presence of a disulfide bridge (Cys509-Cys695) within this domain downregulates the affinity of vWF to GPIb.	Disulfides	58-67	von Willebrand factor	Homo sapiens	140-143
7727378-1	1994	Three insulin-like compounds consisting of two disulfide-linked polypeptide chains have been synthesized.	Disulfides	47-56	insulin	Homo sapiens	6-13
7727388-0	1994	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.	Disulfides	4-13	superoxide dismutase 1	Homo sapiens	91-100
7727388-2	1994	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.	Disulfides	36-45	superoxide dismutase 1	Homo sapiens	53-62
7978820-0	1994	Human TIMP-1 binds to pro-M(r) 92K GL (gelatinase B, MMP-9) through the "second disulfide knot".	Disulfides	80-89	TIMP metallopeptidase inhibitor 1	Homo sapiens	6-12
7987222-0	1994	Two-step selective formation of three disulfide bridges in the synthesis of the C-terminal epidermal growth factor-like domain in human blood coagulation factor IX.	Disulfides	38-47	coagulation factor IX	Homo sapiens	142-163
8064238-9	1994	Although this fragment probably exists at a very low level under normal physiological conditions due to the disulfide bond between flanking cysteine residues (6Cys-11Cys), a reducing compound such as methimazole may cleave the disulfide bond in vivo and allow DR alpha-DRB1*0406 complex on antigen-presenting cells to bind much of the linear fragment of insulin alpha chain, which may lead to the activation of self-insulin-specific T-helper cells.	Disulfides	108-117	major histocompatibility complex, class II, DR beta 1	Homo sapiens	269-273
8064238-9	1994	Although this fragment probably exists at a very low level under normal physiological conditions due to the disulfide bond between flanking cysteine residues (6Cys-11Cys), a reducing compound such as methimazole may cleave the disulfide bond in vivo and allow DR alpha-DRB1*0406 complex on antigen-presenting cells to bind much of the linear fragment of insulin alpha chain, which may lead to the activation of self-insulin-specific T-helper cells.	Disulfides	108-117	insulin	Homo sapiens	354-361
8064238-9	1994	Although this fragment probably exists at a very low level under normal physiological conditions due to the disulfide bond between flanking cysteine residues (6Cys-11Cys), a reducing compound such as methimazole may cleave the disulfide bond in vivo and allow DR alpha-DRB1*0406 complex on antigen-presenting cells to bind much of the linear fragment of insulin alpha chain, which may lead to the activation of self-insulin-specific T-helper cells.	Disulfides	108-117	insulin	Homo sapiens	416-423
8064238-9	1994	Although this fragment probably exists at a very low level under normal physiological conditions due to the disulfide bond between flanking cysteine residues (6Cys-11Cys), a reducing compound such as methimazole may cleave the disulfide bond in vivo and allow DR alpha-DRB1*0406 complex on antigen-presenting cells to bind much of the linear fragment of insulin alpha chain, which may lead to the activation of self-insulin-specific T-helper cells.	Disulfides	227-236	major histocompatibility complex, class II, DR beta 1	Homo sapiens	269-273
8064238-9	1994	Although this fragment probably exists at a very low level under normal physiological conditions due to the disulfide bond between flanking cysteine residues (6Cys-11Cys), a reducing compound such as methimazole may cleave the disulfide bond in vivo and allow DR alpha-DRB1*0406 complex on antigen-presenting cells to bind much of the linear fragment of insulin alpha chain, which may lead to the activation of self-insulin-specific T-helper cells.	Disulfides	227-236	insulin	Homo sapiens	354-361
8064238-9	1994	Although this fragment probably exists at a very low level under normal physiological conditions due to the disulfide bond between flanking cysteine residues (6Cys-11Cys), a reducing compound such as methimazole may cleave the disulfide bond in vivo and allow DR alpha-DRB1*0406 complex on antigen-presenting cells to bind much of the linear fragment of insulin alpha chain, which may lead to the activation of self-insulin-specific T-helper cells.	Disulfides	227-236	insulin	Homo sapiens	416-423
8068682-7	1994	In order to determine the role of des-[65-72]-RNase A, i.e. of the 65-72 disulfide bond, in the structural folding/unfolding processes of RNase A, the stability and structure of this unfolding intermediate were determined by examining its thermal transition curve and by using two- and three-dimensional homonuclear 1H NMR spectroscopy.	Disulfides	73-82	ribonuclease pancreatic	Bos taurus	46-53
8068682-7	1994	In order to determine the role of des-[65-72]-RNase A, i.e. of the 65-72 disulfide bond, in the structural folding/unfolding processes of RNase A, the stability and structure of this unfolding intermediate were determined by examining its thermal transition curve and by using two- and three-dimensional homonuclear 1H NMR spectroscopy.	Disulfides	73-82	ribonuclease pancreatic	Bos taurus	138-145
8052635-2	1994	A carbene-generating photoactivatable group was linked by a disulfide bond to the cysteine sulfhydryl group of each of the rhodopsin mutants.	Disulfides	60-69	rhodopsin	Homo sapiens	123-132
7804129-0	1994	Intra-A chain disulfide bond (A6-11) of insulin is essential for displaying its activity.	Disulfides	14-23	insulin	Homo sapiens	40-47
7804129-1	1994	The mutant proinsulin gene was constructed with the codons for A6 and A11 Cys changed to Ser to delete intra-A chain disulfide bond.	Disulfides	117-126	insulin	Homo sapiens	11-21
7804129-6	1994	This intra-chain disulfide bond is essential for insulin displaying its activity.	Disulfides	17-26	insulin	Homo sapiens	49-56
7971710-5	1994	This method employs molecular conjugate consisting of a cognate moiety, in this case IgG which recognizes the macrophage Fc receptor, covalently linked to the enzyme catalase via the reversible disulfide linkage.	Disulfides	194-203	catalase	Homo sapiens	166-174
7987222-1	1994	The 45-residue C-terminal EGF-like domain in human blood coagulation factor IX has been synthesized by a 2-step method to form selectively 3 disulfide bridges.	Disulfides	141-150	coagulation factor IX	Homo sapiens	57-78
8034677-1	1994	Cultured fibroblasts express binding sites for the amino-terminal region of fibronectin on their cell surface that mediate the assembly of soluble fibronectin into disulfide-stabilized fibrils.	Disulfides	164-173	fibronectin 1	Homo sapiens	76-87
8034704-3	1994	Based on the three-dimensional structure of TGF-beta 2, we deduced Cys80 in activin A to form the intermolecular disulfide bond.	Disulfides	113-122	transforming growth factor, beta 2	Mus musculus	44-54
7518446-2	1994	TIMP-1 consists of six loops, held in place by six disulfide bonds arranged in three knotlike structures.	Disulfides	51-60	TIMP metallopeptidase inhibitor 1	Homo sapiens	0-6
8034657-4	1994	Disulfide bond reduction separated each of the M(r) 130,000-170,000 proteins into M(r) 105,000 (p105) and M(r) 45,000 (p45) subunits, indicating that these high M(r) proteins are related.	Disulfides	0-9	caspase-1	Sus scrofa	119-122
8034677-1	1994	Cultured fibroblasts express binding sites for the amino-terminal region of fibronectin on their cell surface that mediate the assembly of soluble fibronectin into disulfide-stabilized fibrils.	Disulfides	164-173	fibronectin 1	Homo sapiens	147-158
8013369-5	1994	The biological activity of CGA-(1-40) was markedly reduced after reduction and alkylation, which resulted in disruption of the single disulfide bond between Cys17 and Cys38.	Disulfides	134-143	chromogranin A	Bos taurus	27-30
7913461-0	1994	Improved binding and antitumor activity of a recombinant anti-erbB2 immunotoxin by disulfide stabilization of the Fv fragment.	Disulfides	83-92	erb-b2 receptor tyrosine kinase 2	Homo sapiens	62-67
8055938-9	1994	We show that intrachain disulfide bonds form within the purified p53 molecules during storage in the absence of reducing agent.	Disulfides	24-33	tumor protein p53	Homo sapiens	65-68
8054474-11	1994	These findings obtained by the modeling of ET-1 showed an important role for the stabilization of peptide conformation with disulfide bonds.	Disulfides	124-133	endothelin 1	Homo sapiens	43-47
8013347-0	1994	Treatment of IM-9 cells with human growth hormone (GH) promotes rapid disulfide linkage of the GH receptor.	Disulfides	70-79	growth hormone 1	Homo sapiens	35-49
8013347-0	1994	Treatment of IM-9 cells with human growth hormone (GH) promotes rapid disulfide linkage of the GH receptor.	Disulfides	70-79	growth hormone 1	Homo sapiens	51-53
8011632-2	1994	RNase T1 and alpha-lactalbumin were reduced and converted to mixed disulfide derivatives, named GS-RNase T1 and GS-alpha-lactalbumin, in good yield; the molecular masses of the derivatives were confirmed by electrospray mass spectrometry.	Disulfides	67-76	lactalbumin alpha	Homo sapiens	13-30
8011632-2	1994	RNase T1 and alpha-lactalbumin were reduced and converted to mixed disulfide derivatives, named GS-RNase T1 and GS-alpha-lactalbumin, in good yield; the molecular masses of the derivatives were confirmed by electrospray mass spectrometry.	Disulfides	67-76	GNAS complex locus	Homo sapiens	112-120
8206938-3	1994	The COOH-terminal bradykinin cleavage occurred first both in the absence and presence of DxSO4, producing a 103-kDa HK intermediate consisting of disulfide-linked heavy and light chains that retained the kinin moiety.	Disulfides	146-155	kininogen 1	Homo sapiens	18-28
8206938-3	1994	The COOH-terminal bradykinin cleavage occurred first both in the absence and presence of DxSO4, producing a 103-kDa HK intermediate consisting of disulfide-linked heavy and light chains that retained the kinin moiety.	Disulfides	146-155	kininogen 1	Homo sapiens	116-118
8069219-0	1994	Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme.	Disulfides	7-16	lysozyme	Homo sapiens	90-98
7515683-1	1994	Insulin-like growth factor I (IGF-I) is thermodynamically unable to quantitatively form its native disulfides under reversible redox conditions in vitro [Hober et al.	Disulfides	99-109	insulin like growth factor 1	Homo sapiens	0-28
7515683-1	1994	Insulin-like growth factor I (IGF-I) is thermodynamically unable to quantitatively form its native disulfides under reversible redox conditions in vitro [Hober et al.	Disulfides	99-109	insulin like growth factor 1	Homo sapiens	30-35
7515683-5	1994	However, correct disulfide bonds are formed very efficiently when insulin-like growth factor binding protein 1 is added in equimolar amounts to IGF-I to the refolding mixture.	Disulfides	17-26	insulin like growth factor 1	Homo sapiens	144-149
7515683-6	1994	On the basis of these results, we propose that one important function of at least one of the six homologous insulin-like growth factor binding proteins is to assist in the formation and maintenance of the native disulfides of IGF-I.	Disulfides	212-222	insulin like growth factor 1	Homo sapiens	226-231
8069219-2	1994	Within the first 4 ms of folding, lysozyme with intact disulfide bonds already had a far-UV CD spectrum reflecting large amounts of secondary structure.	Disulfides	55-64	lysozyme	Homo sapiens	34-42
8069219-4	1994	Thus, native disulfide bonds not only stabilize the cfinal conformation of lysozyme but also provide, in early folding intermediates, the necessary stabilization that favors the formation of secondary structure.	Disulfides	13-22	lysozyme	Homo sapiens	75-83
8175738-1	1994	Relaxin and insulin are disulfide homologues with divergent functions and antigenicity.	Disulfides	24-33	insulin	Homo sapiens	12-19
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	Disulfides	271-281	protein disulfide isomerase family A member 2	Homo sapiens	136-139
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	Disulfides	271-281	protein disulfide isomerase family A member 2	Homo sapiens	179-182
7513556-0	1994	Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin.	Disulfides	23-32	trophoblast Kunitz domain protein 1	Bos taurus	62-79
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	Disulfides	271-281	protein disulfide isomerase family A member 2	Homo sapiens	179-182
8181566-2	1994	Here, we establish that the four cysteines of oxidized aSFP form two disulfide bridges between nearest-neighbour residues.	Disulfides	69-78	spermadhesin-1	Bos taurus	55-59
8183947-4	1994	The results imply that HIV and its target cell engage in a thiol-disulfide interchange mediated by PDI and that the reduction of critical disulfides in viral envelope glycoproteins may be the initial event that triggers conformational changes required for HIV entry and cell infection.	Disulfides	65-74	protein disulfide isomerase family A member 2	Homo sapiens	99-102
8183947-4	1994	The results imply that HIV and its target cell engage in a thiol-disulfide interchange mediated by PDI and that the reduction of critical disulfides in viral envelope glycoproteins may be the initial event that triggers conformational changes required for HIV entry and cell infection.	Disulfides	138-148	protein disulfide isomerase family A member 2	Homo sapiens	99-102
8172900-3	1994	Apa-1 contains the native disulfide bond between Cys1 and Cys11.	Disulfides	26-35	zinc finger protein 410	Homo sapiens	0-5
8182519-5	1994	In the presence of the disulfide-reducing agent dithiothreitol (0.5 mM), which led to the inactivation of about 70% of the Ang II receptors in the rat portal vein, BIBS 222 (10(-6) M) shifted the concentration-response curve for Ang II to the right and reduced the maximal response by 24 +/- 4.4% (P &lt; .05).	Disulfides	23-32	angiotensinogen	Rattus norvegicus	123-129
7961597-2	1994	After pepsin digestion of the type I procollagen, a portion of the alpha 1(I) chains was recovered as a disulfide-bonded dimer.	Disulfides	104-113	collagen type I alpha 2 chain	Homo sapiens	30-48
8172889-0	1994	Roles of disulfide bonds in recombinant human interleukin 6 conformation.	Disulfides	9-18	interleukin 6	Homo sapiens	46-59
8172889-1	1994	Human IL-6 has two disulfide bonds linking Cys45 to Cys51 and Cys74 to Cys84, respectively.	Disulfides	19-28	interleukin 6	Homo sapiens	6-10
8172889-3	1994	To address the structural importance of these disulfide bonds in the formation and stabilization of IL-6 secondary and tertiary structures, we have generated a panel of disulfide bond-deficient rIL-6 analogs both by chemical reduction and alkylation as well as by site-directed mutagenesis.	Disulfides	46-55	interleukin 6	Homo sapiens	100-104
8172889-3	1994	To address the structural importance of these disulfide bonds in the formation and stabilization of IL-6 secondary and tertiary structures, we have generated a panel of disulfide bond-deficient rIL-6 analogs both by chemical reduction and alkylation as well as by site-directed mutagenesis.	Disulfides	169-178	interleukin 6	Rattus norvegicus	194-199
8172889-10	1994	Our results suggest that the second disulfide bridge plays a critical role in maintaining the spatial relationship between the putative IL-6 A and D helices.	Disulfides	36-45	interleukin 6	Homo sapiens	136-140
8163562-1	1994	Endothelin-1 (ET-1) is an endothelium-derived 21 amino acid vasoconstrictor peptide possessing two intrachain disulfide bridges.	Disulfides	110-119	endothelin 1	Homo sapiens	0-12
8163562-1	1994	Endothelin-1 (ET-1) is an endothelium-derived 21 amino acid vasoconstrictor peptide possessing two intrachain disulfide bridges.	Disulfides	110-119	endothelin 1	Homo sapiens	14-18
7986344-0	1994	Folding pathway of guanidine-denatured disulfide-intact wild-type and mutant bovine pancreatic ribonuclease A.	Disulfides	39-48	ribonuclease pancreatic	Bos taurus	95-109
7986345-2	1994	Secondary structural changes of the cleaved alpha-lactalbumin, in which the two separated polypeptides were joined by disulfide bridges, were examined in solutions of sodium dodecyl sulfate (SDS), urea, and guanidine hydrochloride.	Disulfides	118-127	lactalbumin alpha	Homo sapiens	44-61
8171015-0	1994	Naturally processed heterodimeric disulfide-linked insulin peptides bind to major histocompatibility class II molecules on thymic epithelial cells.	Disulfides	34-43	insulin	Homo sapiens	51-58
8164648-8	1994	First, the N51/IL-8I hybrid in which the N51/KC sequence between cysteines 2 and 3 (or first disulfide bond) is replaced by the corresponding sequence in IL-8 shows IL-8-like properties, indicating that this region is important for specific receptor recognition.	Disulfides	93-102	C-X-C motif chemokine ligand 8	Homo sapiens	15-19
8171015-1	1994	We determined whether disulfide-linked insulin peptides that are immunogenic in vitro for CD4+ T cells bind to major histocompatibility complex class II in vivo.	Disulfides	22-31	insulin	Homo sapiens	39-46
8171030-0	1994	Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.	Disulfides	120-129	rhodopsin	Homo sapiens	26-35
8171030-0	1994	Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.	Disulfides	120-129	rhodopsin	Homo sapiens	138-147
8171030-1	1994	A disulfide bond that is evidently conserved in the guanine nucleotide-binding protein-coupled receptors is present in rhodopsin between Cys-110 and Cys-187.	Disulfides	2-11	rhodopsin	Homo sapiens	119-128
8144509-4	1994	Proteolytic cleavage in domain 4 to release bradykinin causes a conformational change, exposing a surface-binding region (domain 5) on the disulfide-linked light chain.	Disulfides	139-148	kininogen 1	Homo sapiens	44-54
8120035-0	1994	Disulfide bonds required to assemble functional von Willebrand factor multimers.	Disulfides	0-9	von Willebrand factor	Homo sapiens	48-69
8144568-0	1994	Stabilization of an active dimeric form of the epidermal growth factor receptor by introduction of an inter-receptor disulfide bond.	Disulfides	117-126	epidermal growth factor receptor	Homo sapiens	47-79
8144568-4	1994	To stabilize homodimers of EGFR, we have generated a mutated form of the receptor by inserting a cysteine residue in the extracellular juxtamembranous region, in order to cross-link the extracellular domains of two receptors via disulfide bond formation.	Disulfides	229-238	epidermal growth factor receptor	Homo sapiens	27-31
8132629-1	1994	Following sequestration into the endoplasmic reticulum, wheat high molecular weight glutenin subunits (HMW-GS) assemble into polymers through intermolecular disulfide bond formation.	Disulfides	157-166	low-molecular-weight glutenin subunit group 5 type III	Triticum aestivum	67-102
8125943-4	1994	When the enzyme was treated with limiting amounts of o-iodosobenzoate, which oxidizes vicinal sulfhydryls to disulfides, stimulation by Ca2+ and calmodulin was eliminated at concentrations which did not affect basal adenylyl cyclase activity.	Disulfides	109-119	calmodulin 1	Homo sapiens	145-155
8125943-5	1994	Calmodulin stimulation of the enzyme was restored by treatment with dithiothreitol or glutathione which reduce disulfides to free thiols.	Disulfides	111-121	calmodulin 1	Homo sapiens	0-10
8126706-2	1994	[1,15 Aba]-ET-1 is an analogue of endothelin (ET-1) in which the disulfide bridge linking residues 1 and 15 has been removed by replacement of the cysteine residues with the mimicking group alpha-aminobutyric acid (Aba).	Disulfides	65-74	endothelin 1	Homo sapiens	11-15
8126706-2	1994	[1,15 Aba]-ET-1 is an analogue of endothelin (ET-1) in which the disulfide bridge linking residues 1 and 15 has been removed by replacement of the cysteine residues with the mimicking group alpha-aminobutyric acid (Aba).	Disulfides	65-74	endothelin 1	Homo sapiens	46-50
8120035-1	1994	The hemostatic functions of human von Willebrand Factor (vWF) depend on the normal assembly of disulfide-linked multimers from approximately 250-kDa subunits.	Disulfides	95-104	von Willebrand factor	Homo sapiens	34-55
8120035-1	1994	The hemostatic functions of human von Willebrand Factor (vWF) depend on the normal assembly of disulfide-linked multimers from approximately 250-kDa subunits.	Disulfides	95-104	von Willebrand factor	Homo sapiens	57-60
8120035-4	1994	Previous studies of plasma vWF and recombinant vWF fragments indicate that 1 or more of the Cys residues at position 459, 462, and 464 form intersubunit disulfide bonds.	Disulfides	153-162	von Willebrand factor	Homo sapiens	27-30
8120035-4	1994	Previous studies of plasma vWF and recombinant vWF fragments indicate that 1 or more of the Cys residues at position 459, 462, and 464 form intersubunit disulfide bonds.	Disulfides	153-162	von Willebrand factor	Homo sapiens	47-50
8120035-11	1994	By Edman degradation, amino acid composition, and mass spectrometry, a disulfide bond was demonstrated between Cys379 residues of adjacent vWF subunits.	Disulfides	71-80	von Willebrand factor	Homo sapiens	139-142
8120035-12	1994	Thus, intersubunit disulfide bonds involving Cys379 and 1 or more of the Cys residues at positions 459, 462, and 464 connect the NH2-terminal ends of the vWF subunits in a parallel orientation.	Disulfides	19-28	von Willebrand factor	Homo sapiens	154-157
8131275-1	1994	Lipoprotein(a) [Lp(a)] is a low-density lipoprotein (LDL)-like particle in which apolipoprotein(a) [apo(a)] is disulfide-linked to apolipoprotein B (apoB).	Disulfides	111-120	apolipoprotein B	Homo sapiens	131-147
8312273-0	1994	Disulfide-rearranged molten globule state of alpha-lactalbumin.	Disulfides	0-9	lactalbumin alpha	Homo sapiens	45-62
8056752-0	1994	Cell-free formation of disulfide-bonded multimer from isolated plasma fibronectin in the presence of a low concentration of SH reagent under a physiological condition.	Disulfides	23-32	fibronectin 1	Homo sapiens	70-81
7509003-2	1994	The Env-Sea oncoprotein is synthesized as a precursor of 155 kDa which undergoes proteolytic processing to generate a disulfide-linked complex of the proteins gp85 and gp70.	Disulfides	118-127	embigin	Homo sapiens	168-172
7509788-5	1994	The alpha ALB mRNA sequence encodes a predicted secreted protein with the typical triple domain disulfide cross-linked structure.	Disulfides	96-105	albumin	Homo sapiens	10-13
7509843-6	1994	Immunoprecipitation of the LGL-1 antigen reveals a highly disulfide-linked 40-kDa homodimer subunit that is N-glycosylated.	Disulfides	58-67	LLGL1 scribble cell polarity complex component	Mus musculus	27-32
8167469-11	1994	Studies on the redox status of the 10 cysteine residues of bovine brain HBNF and the refolded recombinant protein indicate that all cysteines are engaged in disulfide bond formation.	Disulfides	157-166	pleiotrophin	Homo sapiens	72-76
8307967-1	1994	Inactivation of rat liver S-adenosylhomocysteine hydrolase by the site-directed reagent 5"-p-fluorosulfonylbenzoyladenosine (FSBA) is associated with the formation of a disulfide bond between Cys-78 and Cys-112 (Takata, Y., and Fujioka, M. (1984) Biochemistry 23, 4357-4362; Gomi, T., Ogawa, H., and Fujioka, M. (1986) J. Biol.	Disulfides	169-178	adenosylhomocysteinase	Rattus norvegicus	26-58
8308001-8	1994	Based on the structural analysis of the 8-9th domains, a heptadecapeptide corresponding to the sequence Thr535-Glyl551 of Fn, which resided at the large disulfide loop of domain (I-9), was designed and synthesized.	Disulfides	153-162	fibronectin 1	Homo sapiens	122-124
8114670-8	1994	It is shown that either 1) the redox state (sulfhydryl/disulfide status) or 2) the accessibility of the hyperreactive thiols on the RyR and triadin is determined by the conformational state of the channel.	Disulfides	55-64	ryanodine receptor 1	Homo sapiens	132-135
8302836-1	1994	Porcine pancreatic spasmolytic polypeptide (PSP) belongs to a large family of homologous growth factor-like polypeptides characterized by a disulfide-linked "trefoil motif," duplicated and conserved in various family members.	Disulfides	140-149	regenerating family member 1 alpha	Homo sapiens	44-47
8276866-0	1994	Role of interchain disulfide bonds on the assembly and secretion of human fibrinogen.	Disulfides	19-28	fibrinogen beta chain	Homo sapiens	74-84
8294424-1	1994	The hepatocyte growth factor (HGF) receptor (p190MET) is a tyrosine kinase composed of two disulfide-linked chains, alpha of 50 kDa and beta of 145 kDa.	Disulfides	91-100	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	4-43
8300576-12	1994	The results indicate that both CaBP2 and CaBP1 can catalyze the formation of disulfide bonds and protein disulfide isomerization and may thus be involved in the folding of nascent proteins in the secretory pathway.	Disulfides	77-86	calcium binding protein 2	Rattus norvegicus	31-36
8300576-12	1994	The results indicate that both CaBP2 and CaBP1 can catalyze the formation of disulfide bonds and protein disulfide isomerization and may thus be involved in the folding of nascent proteins in the secretory pathway.	Disulfides	105-114	calcium binding protein 2	Rattus norvegicus	31-36
8290551-6	1994	Malignant astrocytomas also expressed an alternatively spliced form of FGFR-1 (FGFR-1 beta) containing two immunoglobulin-like disulfide loops, whereas normal human adult and fetal brains expressed a receptor form (FGFR-1 alpha) containing three immunoglobulin-like disulfide loops.	Disulfides	127-136	fibroblast growth factor receptor 1	Homo sapiens	71-77
8290551-6	1994	Malignant astrocytomas also expressed an alternatively spliced form of FGFR-1 (FGFR-1 beta) containing two immunoglobulin-like disulfide loops, whereas normal human adult and fetal brains expressed a receptor form (FGFR-1 alpha) containing three immunoglobulin-like disulfide loops.	Disulfides	127-136	fibroblast growth factor receptor 1	Homo sapiens	79-85
8290551-6	1994	Malignant astrocytomas also expressed an alternatively spliced form of FGFR-1 (FGFR-1 beta) containing two immunoglobulin-like disulfide loops, whereas normal human adult and fetal brains expressed a receptor form (FGFR-1 alpha) containing three immunoglobulin-like disulfide loops.	Disulfides	127-136	fibroblast growth factor receptor 1	Homo sapiens	79-85
8290551-6	1994	Malignant astrocytomas also expressed an alternatively spliced form of FGFR-1 (FGFR-1 beta) containing two immunoglobulin-like disulfide loops, whereas normal human adult and fetal brains expressed a receptor form (FGFR-1 alpha) containing three immunoglobulin-like disulfide loops.	Disulfides	266-275	fibroblast growth factor receptor 1	Homo sapiens	71-77
8276866-8	1994	Disruption of both disulfide rings at either end of the coiled-coil region disallows assembly of half-molecules and of dimeric fibrinogen.	Disulfides	19-28	fibrinogen beta chain	Homo sapiens	127-137
8011288-4	1994	Components of this disulfide linked heterodimeric complex, Ig-alpha and Ig-beta, contain an approximately 26 residue sequence motif termed ARH1, also known as TAM, which binds to cytoplasmic effectors, including src-family tyrosine kinases, and contains all structural information needed for signal transduction.	Disulfides	19-28	CD79a molecule	Homo sapiens	59-67
8011288-4	1994	Components of this disulfide linked heterodimeric complex, Ig-alpha and Ig-beta, contain an approximately 26 residue sequence motif termed ARH1, also known as TAM, which binds to cytoplasmic effectors, including src-family tyrosine kinases, and contains all structural information needed for signal transduction.	Disulfides	19-28	low density lipoprotein receptor adaptor protein 1	Homo sapiens	139-143
8011288-4	1994	Components of this disulfide linked heterodimeric complex, Ig-alpha and Ig-beta, contain an approximately 26 residue sequence motif termed ARH1, also known as TAM, which binds to cytoplasmic effectors, including src-family tyrosine kinases, and contains all structural information needed for signal transduction.	Disulfides	19-28	Myeloproliferative syndrome, transient (transient abnormal myelopoiesis)	Homo sapiens	159-162
7764512-3	1994	The cystatin consists of 111 amino acid residues with two disulfide linkages formed between 66-75 and 89-109, and has 43% identical sequences with chicken egg-white cystatin with consensus sequences of reactive sites, Gly(4), Gln-X-Val-X-Gly (48-52), and Ile(Val)-Pro-Trp (96-98).	Disulfides	58-67	cystatin C	Gallus gallus	4-12
8199238-1	1994	To synthesize a glucose-sensitive insulin-releasing protein device, insulin was esterified with methanol and connected to glucose oxidase with intervention of a disulfide compound, 5,5"-dithiobis(2-nitrobenzoic acid).	Disulfides	161-170	insulin	Homo sapiens	34-41
8199238-1	1994	To synthesize a glucose-sensitive insulin-releasing protein device, insulin was esterified with methanol and connected to glucose oxidase with intervention of a disulfide compound, 5,5"-dithiobis(2-nitrobenzoic acid).	Disulfides	161-170	insulin	Homo sapiens	68-75
8199239-1	1994	Conjugates of IL-2 with the ribosome-inactivating protein gelonin were prepared using heterobifunctional reagents to link the proteins via disulfide, acid-labile, and noncleavable linkers.	Disulfides	139-148	interleukin 2	Homo sapiens	14-18
7515032-1	1994	Western blot analysis proved that all cluster-2 MAbs recognize identical or overlapping disulfide-bond-dependent epitopes, indicating the presence of a disulfide-bond-stabilized EGP-2 domain carrying highly immunodominant non-linear epitopes.	Disulfides	152-161	epithelial cell adhesion molecule	Mus musculus	178-183
8187250-4	1994	Using high-performance liquid chromatographic techniques, we have identified sulfhydryl and disulfide groups of apoB-100 from LDL.	Disulfides	92-101	apolipoprotein B	Homo sapiens	112-120
8187250-5	1994	Sixteen of the 25 cysteine residues in apoB-100 exist in disulfide form.	Disulfides	57-66	apolipoprotein B	Homo sapiens	39-47
8187250-6	1994	All 14 cysteine residues within the N terminal end of apoB-100 are linked in disulfide bridges.	Disulfides	77-86	apolipoprotein B	Homo sapiens	54-62
8187208-3	1994	However, Lp[a-], formed by reduction of the disulfide bond between apo[a] and apoB, behaves much like homologous LDL, whether or not apo[a] is removed from the mixture, and in spite of the fact that one or more apoB disulfides may also have been cleaved.	Disulfides	44-53	apolipoprotein B	Homo sapiens	78-82
7964981-8	1994	Glioblastomas also expressed an alternatively spliced form of FGFR1 containing two immunoglobulin-like disulfide loops (FGFR1 beta), whereas normal human adult and fetal brain expressed a form of the receptor containing three immunoglobulin-like disulfide loops (FGFR1 alpha).	Disulfides	103-112	fibroblast growth factor receptor 1	Homo sapiens	62-67
7964981-8	1994	Glioblastomas also expressed an alternatively spliced form of FGFR1 containing two immunoglobulin-like disulfide loops (FGFR1 beta), whereas normal human adult and fetal brain expressed a form of the receptor containing three immunoglobulin-like disulfide loops (FGFR1 alpha).	Disulfides	246-255	fibroblast growth factor receptor 1	Homo sapiens	62-67
8011071-0	1994	Covalent structure of botulinum neurotoxin type A: location of sulfhydryl groups, and disulfide bridges and identification of C-termini of light and heavy chains.	Disulfides	86-95	neurotoxin	Clostridium botulinum	32-42
8011071-3	1994	The mature dichain neurotoxin is made of a approximately 50-kD light chain and a approximately 100-kD heavy chain connected by a disulfide bridge.	Disulfides	129-138	neurotoxin	Clostridium botulinum	19-29
8140052-4	1994	The covalent process has been elucidated to be intermolecular thiol-catalyzed disulfide interchange following beta-elimination of an intact disulfide bridge in the insulin molecule.	Disulfides	78-87	insulin	Homo sapiens	164-171
8140052-4	1994	The covalent process has been elucidated to be intermolecular thiol-catalyzed disulfide interchange following beta-elimination of an intact disulfide bridge in the insulin molecule.	Disulfides	140-149	insulin	Homo sapiens	164-171
8257688-3	1993	The molecular size of the nonreduced hybrid receptor was approximately 350K, indicating that the IGF-I and insulin receptor alpha beta halves were disulfide-linked.	Disulfides	147-156	insulin like growth factor 1	Homo sapiens	97-102
8253791-1	1993	Previous studies have shown that CD8 can be present at the cell surface either as a disulfide-linked homodimer of CD8 alpha or as a disulfide-linked heterodimer of CD8 alpha and CD8 beta.	Disulfides	132-141	CD8b molecule	Homo sapiens	178-186
7505444-2	1993	It has been hypothesized that a disulfide bond might exist between Cys4057 of apolipoprotein(a) and Cys3734 in apolipoprotein B-100.	Disulfides	32-41	apolipoprotein B	Homo sapiens	111-131
7505444-8	1993	Our results strongly suggest the existence of a disulfide bridge between Cys4057 of apolipoprotein(a) and apolipoprotein B-100 within recombinant lipoprotein(a) particles.	Disulfides	48-57	apolipoprotein B	Homo sapiens	106-126
8257688-3	1993	The molecular size of the nonreduced hybrid receptor was approximately 350K, indicating that the IGF-I and insulin receptor alpha beta halves were disulfide-linked.	Disulfides	147-156	insulin	Homo sapiens	107-114
8223645-3	1993	Using SDS/PAGE cruciferin was shown to be composed of different subunits consisting of alpha S and beta S polypeptides, which were disulfide linked, and also closely related free alpha f and beta f polypeptides which were not covalently linked.	Disulfides	131-140	cruciferin	Brassica napus	15-25
8256869-1	1993	Methodology is described for characterization of the kinetics and equilibria of thiol/disulfide interchange reactions of the disulfide bonds in the neurohypophyseal peptide hormones arginine vasopressin and oxytocin and the related peptides pressinoic acid and tocinoic acid.	Disulfides	86-95	arginine vasopressin	Homo sapiens	191-202
8256869-1	1993	Methodology is described for characterization of the kinetics and equilibria of thiol/disulfide interchange reactions of the disulfide bonds in the neurohypophyseal peptide hormones arginine vasopressin and oxytocin and the related peptides pressinoic acid and tocinoic acid.	Disulfides	125-134	arginine vasopressin	Homo sapiens	191-202
8256869-6	1993	To illustrate application of the methodology, rate and equilibrium constants are reported for the thiol/disulfide interchange reactions of cysteine with arginine vasopressin at pH 7.0.	Disulfides	104-113	arginine vasopressin	Homo sapiens	162-173
8256869-7	1993	Cysteine reacts with arginine vasopressin to form two mixed disulfides, which in turn react with another molecule of cysteine to give the dithiol form of arginine vasopressin and cystine.	Disulfides	60-70	arginine vasopressin	Homo sapiens	30-41
8223645-6	1993	N-terminal amino acid sequence determinations revealed that these reactions were related to particular cruciferin subunit beta chains having an additional cysteine residue (position 11) near the residue (position 7) implicated in the inter-chain disulfide bridges.	Disulfides	246-255	cruciferin	Brassica napus	103-113
8226803-2	1993	HGF activator purified from human serum has a molecular mass of 34 kDa and consists of two chains held together by a disulfide bond.	Disulfides	117-126	HGF activator	Homo sapiens	0-13
8310443-0	1993	Disulfide formation in reduced tetanus toxin by thioredoxin: the pharmacological role of interchain covalent and noncovalent bonds.	Disulfides	0-9	thioredoxin 1	Rattus norvegicus	48-59
8310443-1	1993	The interchain disulfide bond of tetanus toxin is known to be cleaved by reduced thioredoxin and by rat brain homogenate.	Disulfides	15-24	thioredoxin 1	Rattus norvegicus	81-92
8264155-1	1993	Vascular permeability factor, or vascular endothelial growth factor (VPF/VEGF) is a disulfide-linked dimeric glycoprotein of about 40 kD that promotes fluid and protein leakage from blood vessels.	Disulfides	84-93	vascular endothelial growth factor A	Homo sapiens	0-67
8264155-1	1993	Vascular permeability factor, or vascular endothelial growth factor (VPF/VEGF) is a disulfide-linked dimeric glycoprotein of about 40 kD that promotes fluid and protein leakage from blood vessels.	Disulfides	84-93	vascular endothelial growth factor A	Homo sapiens	69-72
8264155-1	1993	Vascular permeability factor, or vascular endothelial growth factor (VPF/VEGF) is a disulfide-linked dimeric glycoprotein of about 40 kD that promotes fluid and protein leakage from blood vessels.	Disulfides	84-93	vascular endothelial growth factor A	Homo sapiens	73-77
7693660-1	1993	Transforming growth factors beta (TGF-beta s) are disulfide-linked dimers.	Disulfides	50-59	transforming growth factor, beta 1	Rattus norvegicus	34-42
8276756-0	1993	Determination of carboxyl-terminal residue and disulfide bonds of MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein.	Disulfides	47-56	CD59 molecule (CD59 blood group)	Homo sapiens	66-71
8399391-6	1993	The formation of two interchain disulfide bridges at Cys(A5)-Cys(B21) and Cys(A18)-Cys(B10), and two intrachain disulfide bridges at Cys(B11)-Cys(B59) and Cys(B23)-Cys(B67) were determined by amino-acid sequencing and composition analysis of cystine-containing peptides isolated by HPLC.	Disulfides	32-41	cytohesin 1	Homo sapiens	61-68
8402912-1	1993	We describe a novel signal-transducing protein complex, which consists of the T cell receptor (TCR) beta chain that is disulfide linked to a 33 kd glycoprotein and noncovalently associated with proteins of the CD3 complex on the surface of the pre-T cell line SCB.29.	Disulfides	119-128	CD247 antigen	Mus musculus	210-213
8276756-0	1993	Determination of carboxyl-terminal residue and disulfide bonds of MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein.	Disulfides	47-56	CD59 molecule (CD59 blood group)	Homo sapiens	73-77
8276756-8	1993	The pattern of disulfide bonds of MACIF was also determined with the membrane form as well as the soluble form.	Disulfides	15-24	CD59 molecule (CD59 blood group)	Homo sapiens	34-39
7902878-1	1993	Human growth hormone (hGH) is a single chain, 22 kd-protein with two intramolecular disulfide bonds.	Disulfides	84-93	growth hormone 1	Homo sapiens	6-20
8245722-4	1993	Of particular interest was the demonstration of the existence of the disulfide-linked species apolipoprotein B-100:A-II and B-100:C-IIToronto in the very low density and low density lipoproteins in subjects who were carriers of apoC-IIToronto.	Disulfides	69-78	apolipoprotein B	Homo sapiens	94-114
8245722-4	1993	Of particular interest was the demonstration of the existence of the disulfide-linked species apolipoprotein B-100:A-II and B-100:C-IIToronto in the very low density and low density lipoproteins in subjects who were carriers of apoC-IIToronto.	Disulfides	69-78	NLR family pyrin domain containing 3	Homo sapiens	115-119
8366120-8	1993	Using site-directed mutagenesis, we demonstrated that Cys4057 in apo(a) is involved in disulfide linkage with apoB-100 in Lp(a) particles.	Disulfides	87-96	apolipoprotein B	Homo sapiens	110-118
8376405-2	1993	Eight different missense mutations that cause this phenotype have been reported within the disulfide loop defined by Cys-509 and Cys-695 of the mature vWF subunit; this disulfide loop is required for normal binding of vWF to platelet glycoprotein Ib.	Disulfides	91-100	von Willebrand factor	Homo sapiens	151-154
8376405-2	1993	Eight different missense mutations that cause this phenotype have been reported within the disulfide loop defined by Cys-509 and Cys-695 of the mature vWF subunit; this disulfide loop is required for normal binding of vWF to platelet glycoprotein Ib.	Disulfides	91-100	von Willebrand factor	Homo sapiens	218-221
8376405-2	1993	Eight different missense mutations that cause this phenotype have been reported within the disulfide loop defined by Cys-509 and Cys-695 of the mature vWF subunit; this disulfide loop is required for normal binding of vWF to platelet glycoprotein Ib.	Disulfides	169-178	von Willebrand factor	Homo sapiens	151-154
8376405-2	1993	Eight different missense mutations that cause this phenotype have been reported within the disulfide loop defined by Cys-509 and Cys-695 of the mature vWF subunit; this disulfide loop is required for normal binding of vWF to platelet glycoprotein Ib.	Disulfides	169-178	von Willebrand factor	Homo sapiens	218-221
8376405-8	1993	The His-505--&gt;Asp mutation lies outside the disulfide loop affected by other type IIB vWD mutations and implicates a new segment of vWF in the regulation of platelet glycoprotein Ib binding.	Disulfides	47-56	von Willebrand factor	Homo sapiens	135-138
8356046-2	1993	HMW and LMW vWF preparations were subjected to reduction of interdimeric disulfide bridges under mild reducing conditions.	Disulfides	73-82	von Willebrand factor	Homo sapiens	12-15
8214027-0	1993	Disulfide-linked aggregation of thyroglobulin normally occurs during nascent protein folding.	Disulfides	0-9	thyroglobulin	Rattus norvegicus	32-45
8360678-6	1993	It is shown that in tetrameric AChE, not all of the subunits are disulfide-bonded and that two populations of tetramers exist, one carrying one and the other carrying two hydrophobic anchors.	Disulfides	65-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	31-35
8364028-4	1993	Chemical analysis was used to determine that both recombinant human and recombinant murine IL-10 contain two disulfide bonds.	Disulfides	109-118	interleukin 10	Mus musculus	91-96
8364028-12	1993	These studies indicate that IL-10 is a highly alpha-helical protein containing two disulfide bonds, either one or both of which are critical for its structure and function.	Disulfides	83-92	interleukin 10	Mus musculus	28-33
8395519-6	1993	These data are consistent with a trimeric organization of the CISP molecule in which 195-kDa monomers would be linked together by disulfide bonds.	Disulfides	130-139	thrombospondin 2	Bos taurus	62-66
8168608-4	1993	The aggregate, which can be observed in carbamylated gamma 1-crystallin on SDS-PAGE, may be related to the formation of disulfide and non-disulfide covalent bonds, and it seems that gamma 2 and gamma 3-crystallins can not be aggregated to any great extend.	Disulfides	120-129	tryptophanyl-tRNA synthetase 1	Homo sapiens	182-201
8168608-4	1993	The aggregate, which can be observed in carbamylated gamma 1-crystallin on SDS-PAGE, may be related to the formation of disulfide and non-disulfide covalent bonds, and it seems that gamma 2 and gamma 3-crystallins can not be aggregated to any great extend.	Disulfides	138-147	tryptophanyl-tRNA synthetase 1	Homo sapiens	182-201
8394346-0	1993	Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen activator.	Disulfides	20-29	plasminogen activator, urokinase	Homo sapiens	98-134
8356046-4	1993	Our results suggest that the slowest migrating band of the dimeric triplet set of LMW vWF represents an asymmetric structure composed of an intact subunit to which one NH2-terminal and one COOH-terminal fragment are linked by disulfide bridges.	Disulfides	226-235	von Willebrand factor	Homo sapiens	86-89
8344427-1	1993	A mutant human lysozyme, designated as C77A-a, in which glutathione is bound to Cys95, has been shown to mimic an intermediate in the formation of a disulfide bond during folding of human (h)-lysozyme.	Disulfides	149-158	lysozyme	Homo sapiens	15-23
8344427-1	1993	A mutant human lysozyme, designated as C77A-a, in which glutathione is bound to Cys95, has been shown to mimic an intermediate in the formation of a disulfide bond during folding of human (h)-lysozyme.	Disulfides	149-158	lysozyme	Homo sapiens	192-200
8340419-2	1993	On the basis of its primary sequence and the location of its disulfide bonds, we propose a structural model of the erythropoietic hormone erythropoietin (Epo) which predicts a four alpha-helical bundle motif, in common with other cytokines.	Disulfides	61-70	erythropoietin	Homo sapiens	138-152
8344427-2	1993	Protein disulfide isomerase (PDI), which is believed to catalyze disulfide bond formation and associated protein folding in the endoplasmic reticulum, attacked the glutathionylated h-lysozyme C77A-a to dissociate the glutathione molecule.	Disulfides	8-17	lysozyme	Homo sapiens	183-191
8344436-5	1993	[Dpr1-Asp15]Et-1, an antagonist homologous to Et but with an amide link replacing one of the disulfides, bound to Et receptors reversibly, but binding of Et-1 was less reversible.	Disulfides	93-103	endothelin 1	Homo sapiens	12-16
8373743-0	1993	Reactivity of 42 disulfides with thiol group of human haemoglobin and human serum albumin.	Disulfides	17-27	albumin	Homo sapiens	76-89
8373743-1	1993	The reactivities of disulfides of different compound families towards thiol groups of human haemoglobin and human serum albumin were determined at physiological pH 7.4 by anion-exchange liquid chromatography.	Disulfides	20-30	albumin	Homo sapiens	114-127
18613043-6	1993	Absence of free thiols indicated that the two Cys residues of CBD(Cex) form a disulfide bridge.	Disulfides	78-87	cloacin lysis protein	Escherichia coli	66-69
8340419-2	1993	On the basis of its primary sequence and the location of its disulfide bonds, we propose a structural model of the erythropoietic hormone erythropoietin (Epo) which predicts a four alpha-helical bundle motif, in common with other cytokines.	Disulfides	61-70	erythropoietin	Homo sapiens	154-157
8329446-5	1993	Moreover, the PRL contains three disulfide bonds homologous to those of tetrapod PRLs and differs from teleost PRLs which lack the amino-terminal disulfide bond.	Disulfides	33-42	prolactin	Homo sapiens	14-17
7688303-7	1993	After reduction of brain DS-AChE by dithiothreitol, the mAb no longer reacted with the antigen, indicating that a disulfide bridge is important for the epitope.	Disulfides	114-123	acetylcholinesterase (Cartwright blood group)	Homo sapiens	28-32
8329446-5	1993	Moreover, the PRL contains three disulfide bonds homologous to those of tetrapod PRLs and differs from teleost PRLs which lack the amino-terminal disulfide bond.	Disulfides	146-155	prolactin	Homo sapiens	14-17
8510224-4	1993	Using transient transfection of a human liver cell line with constructs expressing wild-type p17 or a series of Cys mutants of p17, we show that Cys-7 forms an intramolecular S-S bond to Cys61, which in assembly-competent core proteins is available for intermolecular disulfide bonds between two neighboring subunits.	Disulfides	268-277	family with sequence similarity 72 member B	Homo sapiens	127-130
7687640-4	1993	They reacted specifically in an immunoblot of interleukin-2 (IL-2) stimulated PBMNC with a disulfide-linked homodimer of 43 kDa consisting of 28 kDa subunits.	Disulfides	91-100	interleukin 2	Homo sapiens	46-59
7687640-4	1993	They reacted specifically in an immunoblot of interleukin-2 (IL-2) stimulated PBMNC with a disulfide-linked homodimer of 43 kDa consisting of 28 kDa subunits.	Disulfides	91-100	interleukin 2	Homo sapiens	61-65
8401394-2	1993	In a preceding report, incubation of Fbg with cis-DDP under physiological conditions resulted in the cleavage of disulfide (S-S) bonds (N. Ohta, T. Yotsuyanagi and K. Ikeda, J.	Disulfides	113-122	fibrinogen beta chain	Homo sapiens	37-40
8391797-3	1993	These reagents were shown to be covalently bound to reductase SH-groups via the reaction of thiol-disulfide exchange resulting in the loss of reducing activity for cytochrome c.	Disulfides	98-107	cytochrome c, somatic	Homo sapiens	164-176
7691276-6	1993	Thus, giantin appears to be an integral component of the Golgi membrane with a disulfide-linked lumenal domain.	Disulfides	79-88	golgin B1	Homo sapiens	6-13
8494897-3	1993	This observation is of particular interest in light of the recent demonstration that two of the three disulfide bonds in native IGF-1 rearrange in the presence of dithiothreitol [Hober, S., et al.	Disulfides	102-111	insulin like growth factor 1	Homo sapiens	128-133
7685767-4	1993	The positions of methionine residues in alpha 2MR/LRP suggested that the ligand-binding CNBr fragment contained three disulfide-linked peptides comprising the residues 776-1399.	Disulfides	118-127	LDL receptor related protein 1	Homo sapiens	40-53
8511589-2	1993	Binding of IL-6 to IL-6R induced disulfide-linked homodimerization of gp130.	Disulfides	33-42	interleukin 6	Homo sapiens	11-15
8511589-2	1993	Binding of IL-6 to IL-6R induced disulfide-linked homodimerization of gp130.	Disulfides	33-42	interleukin 6 receptor	Homo sapiens	19-24
8510156-8	1993	A cluster of disulfide bridges, including the TGF-beta knot, connects the beta-strands with each other as well as the alpha-helix.	Disulfides	13-22	transforming growth factor beta 1	Homo sapiens	46-54
8515427-2	1993	Analogs of angiotensin II which contain a disulfide bridge between the side chains of residues 3 and 5 retain significant activity consistent with this hypothesis.	Disulfides	42-51	angiotensinogen	Homo sapiens	11-25
8504750-10	1993	p45 is not disulfide linked and is not a degradation product of higher mol wt polypeptides.	Disulfides	11-20	nuclear factor, erythroid 2	Homo sapiens	0-3
8397784-0	1993	Mutation of Arg55/56 to Leu55/Ala56 in insulin-like growth factor-I results in two forms different in disulfide structure and native conformation but similar under reverse-phase conditions.	Disulfides	102-111	insulin like growth factor 1	Homo sapiens	39-67
8493557-2	1993	Glial cell line-derived neurotrophic factor (GDNF) is a glycosylated, disulfide-bonded homodimer that is a distantly related member of the transforming growth factor-beta superfamily.	Disulfides	70-79	glial cell derived neurotrophic factor	Homo sapiens	0-43
8493557-2	1993	Glial cell line-derived neurotrophic factor (GDNF) is a glycosylated, disulfide-bonded homodimer that is a distantly related member of the transforming growth factor-beta superfamily.	Disulfides	70-79	glial cell derived neurotrophic factor	Homo sapiens	45-49
8493557-2	1993	Glial cell line-derived neurotrophic factor (GDNF) is a glycosylated, disulfide-bonded homodimer that is a distantly related member of the transforming growth factor-beta superfamily.	Disulfides	70-79	superoxide dismutase 1	Homo sapiens	87-96
8494898-0	1993	Role of native disulfide bonds in the structure and activity of insulin-like growth factor 1: genetic models of protein-folding intermediates.	Disulfides	15-24	insulin like growth factor 1	Homo sapiens	64-92
8494898-2	1993	Here we examine the role of these disulfide bonds in the folding and function of one family member, human insulin-like growth factor 1 (IGF-1).	Disulfides	34-43	insulin like growth factor 1	Homo sapiens	106-134
8494898-2	1993	Here we examine the role of these disulfide bonds in the folding and function of one family member, human insulin-like growth factor 1 (IGF-1).	Disulfides	34-43	insulin like growth factor 1	Homo sapiens	136-141
8494898-4	1993	An analogue lacking all three disulfide bonds (designated des-Cys-IGF-1) is inactive and unfolded.	Disulfides	30-39	insulin like growth factor 1	Homo sapiens	66-71
8473304-0	1993	1H NMR-based determination of the three-dimensional structure of the human plasma fibronectin fragment containing inter-chain disulfide bonds.	Disulfides	126-135	fibronectin 1	Homo sapiens	82-93
8477803-5	1993	The mu/psi L chain complex is associated with disulfide-linked molecules that are homologous or identical to the mb-1 and B29 proteins, known to be integral components of membrane Ig receptors on mature B cells.	Disulfides	46-55	CD79a molecule	Homo sapiens	113-125
8486673-1	1993	Rat C-reactive protein (CRP) is a pentameric glycoprotein composed of five apparently identical monomers, two of which form a disulfide-linked dimer (Rasosouli, M., Sambasivam, H., Azadi, P., Dell, A., Morris, H. R., Nagpurkar, A., Mookerjea, S., and Murray, R. K. (1992) J. Biol.	Disulfides	126-135	C-reactive protein	Rattus norvegicus	4-22
8486673-1	1993	Rat C-reactive protein (CRP) is a pentameric glycoprotein composed of five apparently identical monomers, two of which form a disulfide-linked dimer (Rasosouli, M., Sambasivam, H., Azadi, P., Dell, A., Morris, H. R., Nagpurkar, A., Mookerjea, S., and Murray, R. K. (1992) J. Biol.	Disulfides	126-135	C-reactive protein	Rattus norvegicus	24-27
8339345-5	1993	The circular dichroism (CD) spectra revealed that the analogs containing the two disulfide bridges took a beta-sheet structure and that the analogs without the disulfide bridges took a random coil conformation.	Disulfides	81-90	amyloid beta precursor protein	Homo sapiens	104-110
8484780-2	1993	We have determined the redox status and the disulfide arrangement of the cysteine residues in HBNF from bovine brain and refolded human recombinant protein produced in E. coli.	Disulfides	44-53	pleiotrophin	Homo sapiens	94-98
8484780-4	1993	The disulfide linkages of human recombinant and bovine brain HBNF, as determined after proteolytic digestions of the non-reduced proteins by peptide mapping and sequence analysis are: Cys15-Cys44, Cys23-Cys53, Cys30-Cys57, Cys67-Cys99 and Cys77-Cys109.	Disulfides	4-13	pleiotrophin	Homo sapiens	61-65
8484780-5	1993	Thus, recombinant HBNF has the same disulfide arrangement as the native brain-derived protein.	Disulfides	36-45	pleiotrophin	Homo sapiens	18-22
8473304-7	1993	We have now determined the three-dimensional structure for a substantial portion of a trypsin-digested interchain disulfide-linked 52-residue (6 kDa) fragment of the carboxyl-terminal of human plasma fibronectin (which includes the above-mentioned heptapeptide dimer) using two-dimensional NMR methods and a new strategy for NMR-based protein structure determination.	Disulfides	114-123	fibronectin 1	Homo sapiens	200-211
8463206-0	1993	Formation of inter- and intramolecular disulfide bonds can activate cardiac troponin C.	Disulfides	39-48	troponin C1, slow skeletal and cardiac type	Homo sapiens	68-86
8463206-2	1993	We report here that spontaneous formation of an intramolecular disulfide bond between Cys-35 and Cys-84, or dimerization via an intermolecular disulfide bond between Cys-84 in cardiac troponin C, renders the protein Ca(2+)-independent when assayed in fast skeletal muscle myofibrils but to a much lesser extent in cardiac myofibrils.	Disulfides	63-72	troponin C1, slow skeletal and cardiac type	Homo sapiens	176-194
8463206-2	1993	We report here that spontaneous formation of an intramolecular disulfide bond between Cys-35 and Cys-84, or dimerization via an intermolecular disulfide bond between Cys-84 in cardiac troponin C, renders the protein Ca(2+)-independent when assayed in fast skeletal muscle myofibrils but to a much lesser extent in cardiac myofibrils.	Disulfides	143-152	troponin C1, slow skeletal and cardiac type	Homo sapiens	176-194
8463206-4	1993	These disulfide bonds constrain the protein into a conformation that either resembles or can substitute for the Ca(2+)-bound form of cardiac troponin C in fast skeletal muscle myofibrils.	Disulfides	6-15	troponin C1, slow skeletal and cardiac type	Homo sapiens	133-151
8473507-6	1993	Immunoblot analysis of plasma fibrinogen demonstrated that a substantial part of the fibrinogen Dusart molecules were disulfide-linked to albumin.	Disulfides	118-127	fibrinogen beta chain	Homo sapiens	85-95
8473507-9	1993	These data indicate that the molecular abnormality in fibrinogen Dusart (A alpha 554 Arg-->Cys) results in defective lateral association of the fibrin fibers and disulfide-linked complex formation with albumin, and is associated with a family history of recurrent thrombosis in the affected individuals.	Disulfides	162-171	fibrinogen beta chain	Homo sapiens	54-64
8506265-4	1993	In addition, we explored the relative role of the disulfide bridges within the IL-6 portion of DAB389-IL-6 in the stabilization of structure required for receptor-binding.	Disulfides	50-59	interleukin 6	Homo sapiens	102-106
7681323-0	1993	Probing the determinants of disulfide stability in native pancreatic trypsin inhibitor.	Disulfides	28-37	trophoblast Kunitz domain protein 1	Bos taurus	69-86
8454636-0	1993	Characterization of the disulfide motif in BNBD-12, an antimicrobial beta-defensin peptide from bovine neutrophils.	Disulfides	24-33	LOC100296173	Bos taurus	69-82
8448123-4	1993	The disulfide-containing protein intermediates achieve a steady-state distribution after which the native protein regenerates at a rate comparable to the rates observed previously during the regeneration of RNase A with glutathione.	Disulfides	4-13	ribonuclease pancreatic	Bos taurus	207-214
8448124-8	1993	The analysis reveals that RNase A regenerates with oxidized and reduced dithiothreitol (DTTox and DTTred, respectively) through a rearrangement pathway involving one or more three-disulfide species; i.e., multiple pathways could be involved.	Disulfides	180-189	ribonuclease pancreatic	Bos taurus	26-33
8450210-2	1993	The B29 gene is specifically expressed in all cells of the B lymphocyte lineage, and the B29 protein is disulfide-linked to the protein product of at least one other gene, known as mb-1.	Disulfides	104-113	CD79B antigen	Mus musculus	89-92
8464068-2	1993	Human plasma fibronectin is a high molecular weight (530,000), multi-domain, modular glycoprotein, consisting of two nearly identical subunits disulfide-bridged close to their C-terminal ends.	Disulfides	143-152	fibronectin 1	Homo sapiens	13-24
8450210-10	1993	We found that extraction with Triton X-100 revealed an additional pair of 52- to 58-kDa heterodimers, where B29 was disulfide-bonded to a protein of approximately 23 kDa.	Disulfides	116-125	CD79B antigen	Mus musculus	108-111
8443392-2	1993	Excision of the vasoactive peptide bradykinin by plasma kallikrein results in kinin-free HK that consists of a 65-Kd N-terminal heavy chain (HK-HC) linked to the C-terminal 45-Kd light chain (HK-LC) by a disulfide bridge.	Disulfides	204-213	kininogen 1	Homo sapiens	35-45
8443182-0	1993	Alignment of disulfide bonds of the extracellular domain of the interferon gamma receptor and investigation of their role in biological activity.	Disulfides	13-22	interferon gamma	Homo sapiens	64-80
8443182-1	1993	The extracellular ligand binding domain of the human interferon gamma receptor includes eight cysteine residues forming four disulfide bonds.	Disulfides	125-134	interferon gamma	Homo sapiens	53-69
8443182-3	1993	We investigated the alignment of the disulfide bonds, using an enzymatically deglycosylated form of a soluble interferon gamma receptor, produced in baculovirus-infected insect cells.	Disulfides	37-46	interferon gamma	Homo sapiens	110-126
8386013-2	1993	In the amino acid sequence of apo bd, Cys4057 located within a plasminogen kringle 4-like repeat sequence (3991-4068) is believed to form a disulfide bond with a specific cysteine residue in apo B-100.	Disulfides	140-149	apolipoprotein B	Homo sapiens	191-200
8386013-6	1993	The result strongly implicates Cys3734 of apo B-100 as the residue forming the disulfide linkage with Cys4057 of apo[a].	Disulfides	79-88	apolipoprotein B	Homo sapiens	42-51
7679746-12	1993	Preliminary results suggest that a fraction of E1 is associated with E2 and E2-NS2 via disulfide linkages.	Disulfides	87-96	NS2	Homo sapiens	79-82
8386013-8	1993	The Cys4057 residue (henceforth designated as Cys67 in the LPaK9 sequence) is believed to form an intermolecular disulfide bond with a cysteine of apo B-100.	Disulfides	113-122	apolipoprotein B	Homo sapiens	147-156
8386013-13	1993	These results support and extend previously suggested mechanisms for a complex interaction between apo[a] and apo B-100 that involve more than a simple covalent disulfide bond.	Disulfides	161-170	apolipoprotein B	Homo sapiens	110-119
8440700-1	1993	The unoccupied insulin receptor is a structurally symmetric, disulfide-linked dimer, comprising two alpha beta halves, each with a potential insulin binding alpha subunit and a kinase active beta subunit.	Disulfides	61-70	insulin	Homo sapiens	15-22
8428978-2	1993	C4BP is composed of seven alpha-chains (70 kDa) and one beta-chain (45 kDa) joined by disulfide bonds.	Disulfides	86-95	complement component 4 binding protein alpha	Homo sapiens	0-4
8427591-4	1993	An analysis of the fibrinogen synthesized in transfected baby hamster kidney (BHK) cells employing various combinations of these mutations revealed that alpha-Cys36 and beta-Cys65 form disulfide bonds between two alpha beta gamma half-molecules, rather than within the same half-molecule; furthermore, these two disulfide bonds are sufficient to hold the two alpha beta gamma half-molecules together as intact fibrinogen.	Disulfides	185-194	fibrinogen beta chain	Homo sapiens	19-29
8431444-1	1993	Fibronectin is a large modular protein that is assembled into fibrils in a stepwise process that involves the binding of soluble fibronectin to the cell surface and formation of fibronectin multimers that are stabilized by disulfides.	Disulfides	223-233	fibronectin 1	Homo sapiens	0-11
8431444-1	1993	Fibronectin is a large modular protein that is assembled into fibrils in a stepwise process that involves the binding of soluble fibronectin to the cell surface and formation of fibronectin multimers that are stabilized by disulfides.	Disulfides	223-233	fibronectin 1	Homo sapiens	178-189
8431444-2	1993	Fibronectin contains two types of disulfide-containing repeat modules, types I and II.	Disulfides	34-43	fibronectin 1	Homo sapiens	0-11
8431444-12	1993	Expression of I-12 as a fusion protein with the gelatin binding part of fibronectin indicated that this module folds independently and that the most likely disulfide pairing is 1-4, 2-6, 3-5.	Disulfides	156-165	fibronectin 1	Homo sapiens	72-83
7679102-0	1993	Disulfide bond requirements for assembly of the platelet glycoprotein Ib-binding domain of von Willebrand factor.	Disulfides	0-9	von Willebrand factor	Homo sapiens	91-112
7679102-7	1993	The disulfide arrangement in r116 is similar, if not identical, to the proposed arrangement within the corresponding region of plasma vWF, and these studies document the inherent Cys-dependent maturation of an isolated vWF domain.	Disulfides	4-13	von Willebrand factor	Homo sapiens	219-222
8427591-0	1993	The role of amino-terminal disulfide bonds in the structure and assembly of human fibrinogen.	Disulfides	27-36	fibrinogen beta chain	Homo sapiens	82-92
8427591-1	1993	Human fibrinogen contains two half-molecules, each composed of an alpha, beta, and gamma chain linked by disulfide bonds.	Disulfides	105-114	fibrinogen beta chain	Homo sapiens	6-16
8427591-5	1993	Disulfide bonds formed by gamma-Cys8 and 9 were also sufficient to hold the two fibrinogen alpha beta gamma half-molecules together, while the disulfide bond between the two alpha-Cys28 residues failed to form in the absence of the disulfide bonds linking the alpha and beta chains and the two gamma chains.	Disulfides	0-9	fibrinogen beta chain	Homo sapiens	80-90
7678252-8	1993	The amino-terminal region of VN and the thrombin moiety of the TAT complex were found to be responsible for their interaction, which was stabilized by disulfide bridges.	Disulfides	151-160	coagulation factor II, thrombin	Homo sapiens	40-48
8443589-10	1993	Finally, the PDB structure database is examined to determine the extrinsic topologies of polypeptides containing disulfide bonds.	Disulfides	113-122	PDB1	Homo sapiens	13-16
8424645-3	1993	In the present study, GST-P mutants whose cysteine residues were independently substituted with alanine (C14A, C47A, C101A, and C169A) by site-directed mutagenesis were used to identify the cysteine residues responsible for the disulfide bond formation.	Disulfides	228-237	glutathione S-transferase pi 1	Rattus norvegicus	22-27
1463721-7	1992	In plasma, C4BP alpha exists as disulfide-linked multimers consisting of seven C4BP alpha chains and a single C4BP beta chain.	Disulfides	32-41	C4b-binding protein beta chain	Sus scrofa	110-119
1472507-0	1992	Contribution of the 6-120 disulfide bond of alpha-lactalbumin to the stabilities of its native and molten globule states.	Disulfides	26-35	lactalbumin alpha	Homo sapiens	44-61
1483466-7	1992	The mature IGF-1, which is secreted from the intracellular pool of precursor proteins, is predominantly an active, monomeric molecule, corroborating observations that early removal of the pro region before folding in the ER helps to prevent aberrant intermolecular disulfide-bond formation in IGF-1.	Disulfides	265-274	insulin like growth factor 1	Homo sapiens	11-16
1472507-1	1992	The unfolding and refolding of a derivative of alpha-lactalbumin, in which the disulfide bond between Cys6 and Cys120 is selectively reduced and S-carboxymethylated, are investigated by equilibrium and kinetic circular dichroism measurements.	Disulfides	79-88	lactalbumin alpha	Homo sapiens	47-64
1479288-10	1992	Disulfide-linked heterodimers of apoD and apoB-100 were also found in low and very low density lipoproteins, and in whole plasma.	Disulfides	0-9	apolipoprotein B	Homo sapiens	42-50
1420327-0	1992	Disulfide-linked S100 beta dimers and signal transduction.	Disulfides	0-9	S100 calcium binding protein B	Homo sapiens	17-26
1444441-9	1992	265, 534-538, 1988) includes a dissociable complex of thrombin with released platelet protease nexin, leading to formation of a nondissociable thrombin-nexin complex that then becomes disulfide linked to thrombospondin.	Disulfides	184-193	coagulation factor II, thrombin	Homo sapiens	54-62
1444441-10	1992	This disulfide-linked complex is converted back to the thrombin-nexin complex by reduction of disulfide bonds.	Disulfides	5-14	coagulation factor II, thrombin	Homo sapiens	55-63
1444441-10	1992	This disulfide-linked complex is converted back to the thrombin-nexin complex by reduction of disulfide bonds.	Disulfides	94-103	coagulation factor II, thrombin	Homo sapiens	55-63
1444441-12	1992	After longer periods of incubation or after incubation with higher concentrations of thrombin, the amount of thrombin complexed with thrombospondin exceeded the amount of thrombin-nexin complex recovered after reduction of disulfide bonds.	Disulfides	223-232	coagulation factor II, thrombin	Homo sapiens	85-93
1444441-12	1992	After longer periods of incubation or after incubation with higher concentrations of thrombin, the amount of thrombin complexed with thrombospondin exceeded the amount of thrombin-nexin complex recovered after reduction of disulfide bonds.	Disulfides	223-232	coagulation factor II, thrombin	Homo sapiens	109-117
1444441-12	1992	After longer periods of incubation or after incubation with higher concentrations of thrombin, the amount of thrombin complexed with thrombospondin exceeded the amount of thrombin-nexin complex recovered after reduction of disulfide bonds.	Disulfides	223-232	coagulation factor II, thrombin	Homo sapiens	109-117
1444441-14	1992	It was concluded that there is a nexin-independent as well as the faster nexin-dependent disulfide linkage of thrombin to thrombospondin.	Disulfides	89-98	coagulation factor II, thrombin	Homo sapiens	110-118
1420327-2	1992	These extracellular trophic activities of S100 beta require a disulfide-linked, dimeric form of the protein.	Disulfides	62-71	S100 calcium binding protein B	Homo sapiens	42-51
1420327-4	1992	We also report a simplified procedure for preparation of pharmacological amounts of biologically active S100 beta dimers, based on the finding that formation of disulfide-linked S100 beta dimers can be stimulated by the presence of calcium or lipid.	Disulfides	161-170	S100 calcium binding protein B	Homo sapiens	104-113
1420327-4	1992	We also report a simplified procedure for preparation of pharmacological amounts of biologically active S100 beta dimers, based on the finding that formation of disulfide-linked S100 beta dimers can be stimulated by the presence of calcium or lipid.	Disulfides	161-170	S100 calcium binding protein B	Homo sapiens	178-187
1420173-0	1992	Role of disulfide exchange in alpha 1-protease inhibitor.	Disulfides	8-17	serpin family A member 1	Homo sapiens	30-56
1420173-1	1992	The major endogenous inhibitor of neutrophil elastase in the plasma, alpha 1-protease inhibitor (alpha 1-PI), has a single cysteine residue which has been shown to form mixed disulfides with a number of thiols in vitro.	Disulfides	175-185	serpin family A member 1	Homo sapiens	69-95
1420173-1	1992	The major endogenous inhibitor of neutrophil elastase in the plasma, alpha 1-protease inhibitor (alpha 1-PI), has a single cysteine residue which has been shown to form mixed disulfides with a number of thiols in vitro.	Disulfides	175-185	serpin family A member 1	Homo sapiens	97-107
1420173-2	1992	Under normal physiological conditions, the plasma concentrations of reduced and oxidized thiols are such that a major fraction of alpha 1-PI in the circulation in vivo is in the form of mixed disulfides [Laurell, C.-B.	Disulfides	192-202	serpin family A member 1	Homo sapiens	130-140
1420173-5	1992	We show here that the mixed disulfide between glutathione or cysteine and alpha 1-PI (alpha 1-PI-SSG or alpha 1-PI-SScys) has an intrinsic fluorescence which distinguishes it from the reduced form of alpha 1-PI.	Disulfides	28-37	serpin family A member 1	Homo sapiens	74-84
1358197-3	1992	On intact human embryonic kidney 293 cells, in the absence of ANP, recombinant human NPR-A is self-aggregated through disulfide bonds in an M(r) &gt; 500,000, possibly tetrameric, complex.	Disulfides	118-127	natriuretic peptide receptor 1	Homo sapiens	85-90
1420173-5	1992	We show here that the mixed disulfide between glutathione or cysteine and alpha 1-PI (alpha 1-PI-SSG or alpha 1-PI-SScys) has an intrinsic fluorescence which distinguishes it from the reduced form of alpha 1-PI.	Disulfides	28-37	serpin family A member 1	Homo sapiens	86-96
1420173-5	1992	We show here that the mixed disulfide between glutathione or cysteine and alpha 1-PI (alpha 1-PI-SSG or alpha 1-PI-SScys) has an intrinsic fluorescence which distinguishes it from the reduced form of alpha 1-PI.	Disulfides	28-37	serpin family A member 1	Homo sapiens	86-96
1420173-5	1992	We show here that the mixed disulfide between glutathione or cysteine and alpha 1-PI (alpha 1-PI-SSG or alpha 1-PI-SScys) has an intrinsic fluorescence which distinguishes it from the reduced form of alpha 1-PI.	Disulfides	28-37	serpin family A member 1	Homo sapiens	86-96
1289495-0	1992	Disulfide bond cleavage of human fibrinogen by cis-diamminedichloroplatinum(II).	Disulfides	0-9	fibrinogen beta chain	Homo sapiens	33-43
1416967-3	1992	The results showed that during the beginning of renaturation almost all reduced and denatured lysozyme is converted to forms possessing lower compactness than native lysozyme, probably as a result of formation of only one or two disulfide bonds.	Disulfides	229-238	lysozyme	Homo sapiens	94-102
1416967-4	1992	Kinetic analysis of lysozyme during renaturation showed that the generation of lysozyme with four disulfide bonds was not necessarily equivalent to the formation lysozyme with native-like catalytic properties.	Disulfides	98-107	lysozyme	Homo sapiens	79-87
1416967-4	1992	Kinetic analysis of lysozyme during renaturation showed that the generation of lysozyme with four disulfide bonds was not necessarily equivalent to the formation lysozyme with native-like catalytic properties.	Disulfides	98-107	lysozyme	Homo sapiens	79-87
1416967-5	1992	It appeared that the formation rate of the structures of the structures of the substrate binding site and of the catalytic site were limited by the generation of four disulfide bonds containing lysozyme.	Disulfides	167-176	lysozyme	Homo sapiens	194-202
1289495-1	1992	Disulfide bridges in fibrinogen (Fbg) were cleaved by cis-diamminedichloroplatinum(II) (cis-DDP).	Disulfides	0-9	fibrinogen beta chain	Homo sapiens	21-31
1289495-1	1992	Disulfide bridges in fibrinogen (Fbg) were cleaved by cis-diamminedichloroplatinum(II) (cis-DDP).	Disulfides	0-9	fibrinogen beta chain	Homo sapiens	33-36
1401917-2	1992	Studies of murine B cells conducted in several laboratories, including our own, suggest that products of the mb-1 (IgM-alpha or IgD-alpha) and B29 (Ig-beta, Ig-gamma) genes occur as disulfide-linked alpha/beta and alpha/gamma heterodimers that are noncovalently associated with mIgM and mIgD.	Disulfides	182-191	CD79B antigen	Mus musculus	148-155
1289495-4	1992	The result indicates that calcium, which has three high affinity sites on Fbg, protects disulfide bridges from the rupture.	Disulfides	88-97	fibrinogen beta chain	Homo sapiens	74-77
1400449-8	1992	Both cysteine-rich subdomains of this mucin have sequence similarity with von Willebrand factor, a serum protein that exists as a disulfide-linked polymer.	Disulfides	130-139	von Willebrand factor	Homo sapiens	74-95
1391954-7	1992	Fibrinogen Marburg contained a substantial amount of albumin linked to the fibrinogen molecule by disulfide bonds, and these fibrinogen-albumin complexes were also present in plasma.	Disulfides	98-107	fibrinogen beta chain	Homo sapiens	0-10
1390775-1	1992	The fibronectin C-terminal interchain disulfide-linked heptapeptide dimer (Val-Asn-Cys-Pro-Ile-Glu-Cys)2 has been investigated via 1H NMR spectroscopy in both water and dimethyl sulfoxide (DMSO) solutions.	Disulfides	38-47	fibronectin 1	Homo sapiens	4-15
1391954-7	1992	Fibrinogen Marburg contained a substantial amount of albumin linked to the fibrinogen molecule by disulfide bonds, and these fibrinogen-albumin complexes were also present in plasma.	Disulfides	98-107	fibrinogen beta chain	Homo sapiens	75-85
1384063-1	1992	We have shown previously that during the oxidative folding of bovine pancreatic trypsin inhibitor only intermediates with native disulfide bonds are well populated.	Disulfides	129-138	trophoblast Kunitz domain protein 1	Bos taurus	80-97
1400422-2	1992	The Amb V allergens are small, highly disulfide-bonded ragweed pollen allergens that serve as useful models for understanding the molecular basis of the human immune response.	Disulfides	38-47	hypothetical protein Amb	Escherichia coli	4-7
1400429-3	1992	Recently, missense mutations that cause type IIB von Willebrand disease (vWD) were described, clustered within a disulfide loop in the A1 domain of vWF that has binding sites for GPIb, collagen, and heparin.	Disulfides	113-122	von Willebrand factor	Homo sapiens	148-151
1439759-2	1992	The transducer-transporter substructure is composed of disulfide-linked dimers of immunoglobulin (Ig)-alpha and Ig-beta/gamma subunits that are products of the mb-1(alpha) and B29 (beta/gamma) genes.	Disulfides	55-64	CD79a molecule	Homo sapiens	82-107
1390644-1	1992	The Cys-71-Cys-81 disulfide bond of the cysteine proteinase inhibitor, chicken cystatin, was specifically reduced by thioredoxin or low concentrations of dithiothreitol.	Disulfides	18-27	cystatin C	Gallus gallus	79-87
1285848-1	1992	The unfolded states of serum albumin, lysozyme and ribonuclease denatured in GuHCl with their disulfide bridges intact or reduced and carboxyamidomethylated have been compared by their circular dichroism, second-derivative and difference spectra in the ultraviolet region.	Disulfides	94-103	albumin	Homo sapiens	23-36
1390644-0	1992	Different roles of the two disulfide bonds of the cysteine proteinase inhibitor, chicken cystatin, for the conformation of the active protein.	Disulfides	27-36	cystatin C	Gallus gallus	89-97
1283335-10	1992	Furthermore, we demonstrate that reduction of the disulfide bonds of a pre-processed A-loop containing heterodimeric insulin peptide is required to further process insulin into a T cell epitope.	Disulfides	50-59	insulin	Homo sapiens	117-124
1283335-10	1992	Furthermore, we demonstrate that reduction of the disulfide bonds of a pre-processed A-loop containing heterodimeric insulin peptide is required to further process insulin into a T cell epitope.	Disulfides	50-59	insulin	Homo sapiens	164-171
1478936-5	1992	In non-reduced gels p58 migrated as two kinetically related, high relative molecular mass forms, apparently corresponding to disulfide-linked homo-dimers and -hexamers.	Disulfides	125-134	DNA primase subunit 2	Rattus norvegicus	20-23
1390878-8	1992	The addition of disulfides to PBS markedly enhanced the ability of SOD to inhibit oxidation.	Disulfides	16-26	superoxide dismutase 1	Homo sapiens	67-70
1390644-4	1992	In contrast, reduction of both disulfide bonds of cystatin by higher concentrations of dithiothreitol and subsequent alkylation led to the slow conversion of the inhibitor into two forms lacking proteinase binding ability, indicative of more extensive conformational changes.	Disulfides	31-40	cystatin C	Gallus gallus	50-58
1390644-5	1992	Together, these results suggest that the less accessible Cys-95-Cys-115 disulfide bond of chicken cystatin, but not the more accessible Cys-71-Cys-81 bond, is of importance for maintaining the conformation of the inhibitor required for binding of target proteinases.	Disulfides	72-81	cystatin C	Gallus gallus	98-106
1525170-0	1992	Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95.	Disulfides	63-72	lysozyme	Homo sapiens	44-52
1387699-1	1992	Lipoprotein(a) or Lp(a), is a member of the plasma lipoproteins with general properties of LDL but with a protein moiety represented by apoB100 disulfide linked to apolipoprotein(a) or apo(a).	Disulfides	144-153	apolipoprotein B	Homo sapiens	136-143
1384348-9	1992	These results indicate that monoclonal antibodies 5G2 and 4C10 cross-react with a species-specific region of the amino-terminal disulfide loop of bovine prolactin.	Disulfides	128-137	prolactin	Bos taurus	153-162
1438162-4	1992	The maintenance of the native state of insulin was shown to be important in protecting the disulfides from reduction by dithiothreitol and implicitly from the disulfide interchange reaction that occurs during storage.	Disulfides	91-101	insulin	Homo sapiens	39-46
1438162-4	1992	The maintenance of the native state of insulin was shown to be important in protecting the disulfides from reduction by dithiothreitol and implicitly from the disulfide interchange reaction that occurs during storage.	Disulfides	91-100	insulin	Homo sapiens	39-46
1438162-7	1992	A significant positive correlation (R2 = 0.8 and P less than 0.0005) exists between the conformational stability and chemical stability of these analogs, indicating that the chemical stability of insulin"s disulfides is under the thermodynamic control of the conformational equilibria.	Disulfides	206-216	insulin	Homo sapiens	196-203
1353499-5	1992	Much of the Tg released from BiP by the addition of Mg-ATP was found in aggregates containing interchain disulfide bonds; other BiP-associated Tg represented non-covalent aggregates and unfolded free monomers.	Disulfides	105-114	heat shock protein family A (Hsp70) member 5	Homo sapiens	29-32
1499565-4	1992	It was demonstrated that complete disulfide bond formation in murine IL-6 occurred during the early urea washing/guanidine hydrochloride extraction steps, so no refolding step was required.	Disulfides	34-43	interleukin 6	Mus musculus	69-73
1499565-5	1992	When fully reduced murine IL-6 was dissolved in 8 M guanidine hydrochloride and allowed to air-oxidize, complete disulfide bond formation, monitored by analytical reversed-phase HPLC, was shown to occur within 13 h at 6 degrees C. About 25 mg pure protein was obtained from 37 g wet cells.	Disulfides	113-122	interleukin 6	Mus musculus	26-30
1379247-0	1992	Disulfides modulate RGD-inhibitable cell adhesive activity of thrombospondin.	Disulfides	0-10	thrombospondin 1	Homo sapiens	62-76
1422223-2	1992	The first group contains four full-length IL-6 molecules that differ in the presence of cysteine residues involved in disulfide bridges.	Disulfides	118-127	interleukin 6	Homo sapiens	42-46
1379247-2	1992	The RGD sequence is located in the type 3 repeat region of TSP that has multiple Ca2+ binding sites and is subject to a complex intramolecular thiol-disulfide isomerization.	Disulfides	149-158	thrombospondin 1	Homo sapiens	59-62
1433985-2	1992	TGF-beta is a disulfide-bonded homodimer of a subunit of 12.5 kD that is derived from a much larger precursor.	Disulfides	14-23	transforming growth factor beta 1	Homo sapiens	0-8
1422223-7	1992	The yield of soluble and properly refolded IL-6 was the highest when the disulfide bond between the cysteines at positions 74 and 84 was present in the mutein form, which also lacked the 22 N-terminal amino acids.	Disulfides	73-82	interleukin 6	Homo sapiens	43-47
1379719-0	1992	The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.	Disulfides	75-84	trophoblast Kunitz domain protein 1	Bos taurus	122-139
1495977-3	1992	We show here that TCR gamma-IgH and TCR delta-IgH chimeric chains are produced intracellularly in significant amounts, that the two chains can assemble correctly to form disulfide-linked, glycosylated heterodimers, and that a selective mechanism allows secretion of correctly paired receptor chains into the medium.	Disulfides	170-179	T cell receptor delta chain	Mus musculus	36-45
1634518-1	1992	The conformation of the fully disulfide-reduced state of human serum albumin was investigated by tryptophan fluorescence spectrum, CD analyses, and size-exclusion chromatography.	Disulfides	30-39	albumin	Homo sapiens	63-76
1379719-1	1992	The best-characterized protein folding pathway is that of bovine pancreatic trypsin inhibitor, which folds from the reduced form through a series of disulfide bond intermediates.	Disulfides	149-158	trophoblast Kunitz domain protein 1	Bos taurus	76-93
1379719-2	1992	The crucial one-disulfide intermediate of bovine pancreatic trypsin inhibitor with the disulfide bond between Cys-30 and Cys-51 is shown here to have a partially folded conformation in which the major elements of secondary structure interact via a core of apolar side chains, which resembles part of the native conformation.	Disulfides	16-25	trophoblast Kunitz domain protein 1	Bos taurus	60-77
1379719-2	1992	The crucial one-disulfide intermediate of bovine pancreatic trypsin inhibitor with the disulfide bond between Cys-30 and Cys-51 is shown here to have a partially folded conformation in which the major elements of secondary structure interact via a core of apolar side chains, which resembles part of the native conformation.	Disulfides	87-96	trophoblast Kunitz domain protein 1	Bos taurus	60-77
1634518-0	1992	Partially folded state of the disulfide-reduced form of human serum albumin as an intermediate for reversible denaturation.	Disulfides	30-39	albumin	Homo sapiens	62-75
1634518-4	1992	The conformation of disulfide-reduced serum albumin was highly variable depending on pH and ionic strength conditions.	Disulfides	20-29	albumin	Homo sapiens	38-51
1634518-5	1992	Thus, we concluded that the disulfide-reduced state with partially folded variable conformation is involved in the reversible interconversion between the denatured reduced form and the native disulfide-bonded form of human serum albumin.	Disulfides	28-37	albumin	Homo sapiens	223-236
1634518-5	1992	Thus, we concluded that the disulfide-reduced state with partially folded variable conformation is involved in the reversible interconversion between the denatured reduced form and the native disulfide-bonded form of human serum albumin.	Disulfides	192-201	albumin	Homo sapiens	223-236
1634546-0	1992	Folding of human lysozyme in vivo by the formation of an alternative disulfide bond.	Disulfides	69-78	lysozyme	Homo sapiens	17-25
1628650-0	1992	The multimeric structure and disulfide-bonding pattern of bovine kappa-casein.	Disulfides	29-38	casein kappa	Bos taurus	65-77
1628650-1	1992	Bovine kappa-casein was analyzed by SDS/PAGE, MS and amino acid sequence analysis in order to determine its multimeric composition and disulfide-bonding pattern.	Disulfides	135-144	casein kappa	Bos taurus	7-19
1628650-3	1992	Three types of interchain disulfide linkage, Cys11-Cys11, Cys11-Cys88 and Cys88-Cys88, were all assigned in multimers purified from [14C]carboxymethylated and untreated bulk milk, as well as a milk sample from a kappa-casein-variant-B homozygote Co20.	Disulfides	26-35	casein kappa	Bos taurus	212-224
1379605-1	1992	Enhanced levels of disulfide-linked dimers of the neu oncogene product have been suggested to be associated with the transformed state [Weiner DB, Liu J, Cohen JA, Williams WV, Greene MI: Nature 338:230-231, (1989)].	Disulfides	19-28	erb-b2 receptor tyrosine kinase 2	Homo sapiens	50-53
1429498-0	1992	Amino acid sequence and disulfide-bridge location of canine haptoglobin.	Disulfides	24-33	haptoglobin	Canis lupus familiaris	60-71
1437708-0	1992	Bombyxin-II and its disulfide bond isomers: synthesis and activity.	Disulfides	20-29	bombyxin A-6	Bombyx mori	0-11
1429498-1	1992	The complete amino acid sequence and disulfide-bridge location of canine haptoglobin (Hp) were determined by analyzing various fragments produced chemically and/or enzymatically.	Disulfides	37-46	haptoglobin	Canis lupus familiaris	73-84
1437708-1	1992	Bombyxin-II, an insulin superfamily peptide of the silkmoth Bombyx mori, and its disulfide bond isomers have been synthesized by two ways of stepwise, semi-regioselective disulfide bond formation.	Disulfides	81-90	bombyxin A-6	Bombyx mori	0-11
1437708-1	1992	Bombyxin-II, an insulin superfamily peptide of the silkmoth Bombyx mori, and its disulfide bond isomers have been synthesized by two ways of stepwise, semi-regioselective disulfide bond formation.	Disulfides	171-180	bombyxin A-6	Bombyx mori	0-11
1534588-2	1992	Lipoprotein(a) (Lp[a]) can be defined as a lipoprotein particle having as a protein moiety apolipoprotein B-100 (the protein associated with low-density lipoprotein) disulfide-linked to apolipoprotein(a), the distinctive glycoprotein of Lp(a) that is homologous to plasminogen.	Disulfides	166-175	apolipoprotein B	Homo sapiens	91-111
1597472-5	1992	Under denaturing conditions the integrity of Gl-260 is maintained through the cross-linking of one monomer of the disulfide-linked TGF-beta 1 homodimer to Gl-85 and of the other monomer to the 100-kDa subunit of Gl-170.	Disulfides	114-123	transforming growth factor, beta 1	Rattus norvegicus	131-141
1606975-0	1992	Disulfide arrangement of human insulin-like growth factor I derived from yeast and plasma.	Disulfides	0-9	insulin like growth factor 1	Homo sapiens	31-59
1606975-1	1992	The disulfide arrangement of yeast derived human insulin-like growth factor I (yIGF-I) was determined using a combination of Staphylococcus aureus V8 protease mapping, fast-atom-bombardment mass spectrometry as well as amino acid sequence and composition analysis.	Disulfides	4-13	insulin like growth factor 1	Homo sapiens	49-77
1606975-3	1992	IGF-I isolated from human plasma (pIGF-I) was found to have an identical disulfide configuration.	Disulfides	73-82	insulin like growth factor 1	Homo sapiens	0-5
1606975-4	1992	A yeast-derived isomeric form of IGF-I (yisoIGF-I) exhibited an altered disulfide arrangement: Cys6-Cys47, Cys48-Cys52 and Cys18-Cys61.	Disulfides	72-81	insulin like growth factor 1	Homo sapiens	33-38
1606975-7	1992	The data demonstrate the importance of correct disulfide arrangement in IGF-I for full biological activity.	Disulfides	47-56	insulin like growth factor 1	Homo sapiens	72-77
1375939-9	1992	Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes.	Disulfides	76-85	fibroblast growth factor 1	Homo sapiens	96-101
1597148-15	1992	The decreased detectability associated with PRL transformation appears to involve the association of 23K PRL molecules into a 80 to greater than 100K disulfide-linked oligomer.	Disulfides	150-159	prolactin	Rattus norvegicus	44-47
1534287-1	1992	BACKGROUND: Lipoprotein(a) [Lp(a)] is a low density lipoprotein-like particle whose apolipoprotein B (apo B) moiety is disulfide-linked to apo(a), a plasminogen-like inhibitor of fibrinolysis in vitro.	Disulfides	119-128	apolipoprotein B	Homo sapiens	84-100
1618297-0	1992	A modified Kex2 enzyme retained in the endoplasmic reticulum prevents disulfide-linked dimerisation of recombinant human insulin-like growth factor-1 secreted from yeast.	Disulfides	70-79	insulin like growth factor 1	Homo sapiens	121-149
1618297-1	1992	The majority of the recombinant human insulin-like growth factor-1 (IGF1) molecules, secreted from yeast using the prepro sequence of the prepro-alpha-factor, are not active monomers but inactive, disulfide-linked dimers.	Disulfides	197-206	insulin like growth factor 1	Homo sapiens	38-66
1618297-1	1992	The majority of the recombinant human insulin-like growth factor-1 (IGF1) molecules, secreted from yeast using the prepro sequence of the prepro-alpha-factor, are not active monomers but inactive, disulfide-linked dimers.	Disulfides	197-206	insulin like growth factor 1	Homo sapiens	68-72
1618297-5	1992	We find that co-expression of a novel ER-retained Kex2p variant, soluble Kex2pHDEL, can prevent intermolecular disulfide bond formation between two IGF1 molecules, implying that the presence of the proregion during the folding of IGF1 in the ER could be a reason for disulfide-linked dimerisation.	Disulfides	111-120	insulin like growth factor 1	Homo sapiens	148-152
1597148-15	1992	The decreased detectability associated with PRL transformation appears to involve the association of 23K PRL molecules into a 80 to greater than 100K disulfide-linked oligomer.	Disulfides	150-159	prolactin	Rattus norvegicus	105-108
1597148-17	1992	DA appears to inhibit PRL transformation by preventing thiol-disulfide interchange.	Disulfides	61-70	prolactin	Rattus norvegicus	22-25
1428535-1	1992	The putative receptor-binding region of human transforming growth factor-alpha (TGF alpha) has been shown to be contributed by two fragments: an A-chain (residue 12-18) and a 17-residue carboxyl fragment (residue 34-50) that includes a disulfide-containing C-loop (residue 34-43).	Disulfides	236-245	tumor necrosis factor	Homo sapiens	46-78
1414126-5	1992	The purified human proinsulin-S-sulfonate was folded using a disulfide interchange method.	Disulfides	61-70	insulin	Homo sapiens	19-29
1316152-5	1992	Here we report several of its biochemical characteristics: A structural model for the native protein is proposed in which two disulfide-linked pairs of similar 18-kDa subunits (p18) associate to form a 72-kDa tetramer (p72).	Disulfides	126-135	DEAD-box helicase 17	Homo sapiens	219-222
1598575-4	1992	Constructs with thrombin cleavage sites were efficiently cleaved to soluble disulfide-linked heterodimers.	Disulfides	76-85	coagulation factor II	Rattus norvegicus	16-24
1559983-6	1992	Binding of 125I-labeled ovine PRL or human GH to membrane preparations from COS-7 cells transiently expressing the mutant receptors have defined a region within the first disulfide loop (residues Arg13, Asp16, Glu18) and the set of lactogen-specific sequences between the two pairs of cysteines as key determinants of PRL-binding specificity, which converge to form a patch on a two-dimensional model of the PRL receptor.	Disulfides	171-180	prolactin	Homo sapiens	30-33
1569180-10	1992	This bond is cleaved by cysteamine to form a new mixed disulfide, a pseudolysine that restores a thrombin cleavage site that is essential for procoagulant function.	Disulfides	55-64	coagulation factor II, thrombin	Homo sapiens	97-105
1565641-0	1992	Abnormal fibrinogens IJmuiden (B beta Arg14----Cys) and Nijmegen (B beta Arg44----Cys) form disulfide-linked fibrinogen-albumin complexes.	Disulfides	92-101	fibrinogen beta chain	Homo sapiens	9-19
1567819-0	1992	Complete primary structure of bovine beta 2-glycoprotein I: localization of the disulfide bridges.	Disulfides	80-89	apolipoprotein H	Bos taurus	37-58
1567819-2	1992	Bovine beta 2-glycoprotein I was purified from citrated plasma, and by sequencing selected peptides, the complete disulfide bridge patterns of the 11 disulfide bridges were established as well as the positions of the five asparagine-linked carbohydrate groups.	Disulfides	150-159	apolipoprotein H	Bos taurus	7-28
1567819-3	1992	Bovine beta 2-glycoprotein I comprises five mutually homologous domains or Short Consensus Repeats, each containing two disulfide bridges, except for the fifth most C-terminal domain which diverges from the Short Consensus Repeat consensus by containing an additional disulfide bridge.	Disulfides	120-129	apolipoprotein H	Bos taurus	7-28
1567819-3	1992	Bovine beta 2-glycoprotein I comprises five mutually homologous domains or Short Consensus Repeats, each containing two disulfide bridges, except for the fifth most C-terminal domain which diverges from the Short Consensus Repeat consensus by containing an additional disulfide bridge.	Disulfides	268-277	apolipoprotein H	Bos taurus	7-28
1544940-3	1992	LTBP plays an important role in the assembly and secretion of the latent TGF-beta 1 complex; if the TGF-beta 1 precursor fails to bind to LTBP, much of it remains inside the cells and may contain anomalous disulfide bond(s) between beta 1-LAP and the mature TGF-beta 1 molecule (Miyazono, K., Olofsson, A., Colosetti, P., and Heldin, C.-H. (1991) EMBO J.	Disulfides	206-215	transforming growth factor beta 1	Homo sapiens	73-83
1312714-4	1992	Several mutant forms of the EPO-R were analyzed; all constitutively active mutants form disulfide-linked homodimers, whereas EPO-responsive or inactive forms of the receptor do not.	Disulfides	88-97	erythropoietin	Homo sapiens	28-31
1312714-5	1992	Monomers and disulfide-linked dimers of the constitutive receptor are present on the plasma membrane and bind EPO with a single affinity.	Disulfides	13-22	erythropoietin	Homo sapiens	110-113
1544940-3	1992	LTBP plays an important role in the assembly and secretion of the latent TGF-beta 1 complex; if the TGF-beta 1 precursor fails to bind to LTBP, much of it remains inside the cells and may contain anomalous disulfide bond(s) between beta 1-LAP and the mature TGF-beta 1 molecule (Miyazono, K., Olofsson, A., Colosetti, P., and Heldin, C.-H. (1991) EMBO J.	Disulfides	206-215	transforming growth factor beta 1	Homo sapiens	100-110
1544940-3	1992	LTBP plays an important role in the assembly and secretion of the latent TGF-beta 1 complex; if the TGF-beta 1 precursor fails to bind to LTBP, much of it remains inside the cells and may contain anomalous disulfide bond(s) between beta 1-LAP and the mature TGF-beta 1 molecule (Miyazono, K., Olofsson, A., Colosetti, P., and Heldin, C.-H. (1991) EMBO J.	Disulfides	206-215	transforming growth factor beta 1	Homo sapiens	100-110
1733934-2	1992	Furthermore, thiol titration of bovine pituitary basic fibroblast growth factor (bFGF) indicates the presence of two free thiols, which is consistent with an intramolecular disulfide.	Disulfides	173-182	fibroblast growth factor 2	Bos taurus	49-79
1737028-0	1992	Disulfide exchange folding of insulin-like growth factor I.	Disulfides	0-9	insulin like growth factor 1	Homo sapiens	30-58
1737028-1	1992	The disulfide exchange folding properties of insulin-like growth factor I (IGF-I) have been analyzed in a redox buffer containing reduced (10 mM) and oxidized (1 mM) glutathione.	Disulfides	4-13	insulin like growth factor 1	Homo sapiens	45-73
1737028-1	1992	The disulfide exchange folding properties of insulin-like growth factor I (IGF-I) have been analyzed in a redox buffer containing reduced (10 mM) and oxidized (1 mM) glutathione.	Disulfides	4-13	insulin like growth factor 1	Homo sapiens	75-80
1737028-3	1992	Instead, five major forms of IGF-I were detected, and these components were concluded to be in equilibrium as their relative amounts were similar starting from either reduced, native, or a mismatched variant of IGF-I containing two non-native disulfides.	Disulfides	243-253	insulin like growth factor 1	Homo sapiens	29-34
1737028-10	1992	On the basis of the disulfide bond patterns of the different components in the equilibrium mixtures, we conclude that the disulfide between cysteines-47 and -52 in IGF-I is an unfavorable high-energy bond that may exist in the native molecule in a strained configuration.	Disulfides	20-29	insulin like growth factor 1	Homo sapiens	164-169
1737028-10	1992	On the basis of the disulfide bond patterns of the different components in the equilibrium mixtures, we conclude that the disulfide between cysteines-47 and -52 in IGF-I is an unfavorable high-energy bond that may exist in the native molecule in a strained configuration.	Disulfides	122-131	insulin like growth factor 1	Homo sapiens	164-169
1733934-0	1992	The disulfide structure of bovine pituitary basic fibroblast growth factor.	Disulfides	4-13	fibroblast growth factor 2	Bos taurus	44-74
1733934-1	1992	Basic fibroblast growth factor has 4 cysteine residues in its amino acid sequence, two of which are perfectly conserved within the fibroblast growth factor family of proteins suggesting a disulfide bond at this position.	Disulfides	188-197	fibroblast growth factor 2	Bos taurus	0-30
1562544-3	1992	It is known that oxidizing agents promote the formation of disulfide bonds in the glucocorticoid receptor, but it has not been determined what domains are involved in any disulfide bond formation that leads to inactivation of DNA-binding activity.	Disulfides	59-68	nuclear receptor subfamily 3, group C, member 1	Mus musculus	82-105
1737006-6	1992	Using oxidized and reduced glutathione, the equilibrium constants for forming the disulfide bonds at 25 degrees C and pH 7.0 are 0.018 M for Apa-1 and 0.033 M for Apa-2 and show little dependence on pH or temperature.	Disulfides	82-91	zinc finger protein 410	Homo sapiens	141-146
1733934-2	1992	Furthermore, thiol titration of bovine pituitary basic fibroblast growth factor (bFGF) indicates the presence of two free thiols, which is consistent with an intramolecular disulfide.	Disulfides	173-182	fibroblast growth factor 2	Bos taurus	81-85
1733936-8	1992	These results demonstrate that the protein is TGF-beta 2.3 heterodimer, consisting of one polypeptide chain each of TGF-beta 2 and TGF-beta 3 linked by one or more disulfide bonds.	Disulfides	164-173	transforming growth factor beta 2	Bos taurus	46-56
1730606-7	1992	Both proteins were shown by a number of analytical techniques to be of the inverted sequence, with insulin-like disulfide bonding.	Disulfides	112-121	insulin	Homo sapiens	99-106
1320041-1	1992	Insulin and IGF-I receptors are homologous disulfide linked alpha 2 beta 2 tetramers.	Disulfides	43-52	insulin	Homo sapiens	0-7
1320041-1	1992	Insulin and IGF-I receptors are homologous disulfide linked alpha 2 beta 2 tetramers.	Disulfides	43-52	insulin like growth factor 1	Homo sapiens	12-17
1515029-0	1992	Synthesis of bombyxin-IV, an insulin superfamily peptide from the silkworm, Bombyx mori, by stepwise and selective formation of three disulfide bridges.	Disulfides	134-143	bombyxin E-1	Bombyx mori	13-24
1515029-1	1992	We report the synthesis of bombyxin-IV, a disulfide-linked, heterodimeric, insulin superfamily peptide from the silkworm, Bombyx mori.	Disulfides	42-51	bombyxin E-1	Bombyx mori	27-38
1515030-0	1992	Determination of disulfide bond arrangement in bombyxin-IV, an insulin superfamily peptide from the silkworm, Bombyx mori, by combination of thermolysin digestion of natural peptide and selective synthesis of disulfide bond isomers.	Disulfides	17-26	bombyxin E-1	Bombyx mori	47-58
1515030-0	1992	Determination of disulfide bond arrangement in bombyxin-IV, an insulin superfamily peptide from the silkworm, Bombyx mori, by combination of thermolysin digestion of natural peptide and selective synthesis of disulfide bond isomers.	Disulfides	209-218	bombyxin E-1	Bombyx mori	47-58
1515030-1	1992	The mode of disulfide linkages in bombyxin-IV, an insulin superfamily peptide consisting of A- and B-chains, was determined as A6-A11, A7-B10, and A20-B22.	Disulfides	12-21	bombyxin E-1	Bombyx mori	34-45
1515030-3	1992	The mode of the remaining two bridges was determined by chemical and selective synthesis of three possible disulfide bond isomers of bombyxin-IV.	Disulfides	107-116	bombyxin E-1	Bombyx mori	133-144
1515031-9	1992	Similar gel patterns were observed in whole caseins and partially purified kappa-caseins, indicating that this size distribution is a natural disulfide-linked reporter for the distribution of kappa-casein in casein colloids (micelles).	Disulfides	142-151	casein kappa	Bos taurus	75-87
1570025-13	1992	It is concluded that a) a thioredoxin system in brain tissue reduces the interchain disulfide of two-chain tetanus toxin and botulinum neurotoxin A, b) tetanus toxin but not botulinum neurotoxin A consists of two electrophoretically distinct forms which differ by the thiol-disulfide status of their heavy chains, c) the disulfide loop within the heavy chain of tetanus toxin is resistant to the thioredoxin system.	Disulfides	274-283	thioredoxin 1	Rattus norvegicus	26-37
1570025-13	1992	It is concluded that a) a thioredoxin system in brain tissue reduces the interchain disulfide of two-chain tetanus toxin and botulinum neurotoxin A, b) tetanus toxin but not botulinum neurotoxin A consists of two electrophoretically distinct forms which differ by the thiol-disulfide status of their heavy chains, c) the disulfide loop within the heavy chain of tetanus toxin is resistant to the thioredoxin system.	Disulfides	274-283	thioredoxin 1	Rattus norvegicus	26-37
1632491-1	1992	Polylysine has been covalently bound to human transferrin in a 1:1 molar ratio over a disulfide bond that can be easily split by reducing agents such as dithiothreitol.	Disulfides	86-95	transferrin	Homo sapiens	46-57
1730484-9	1992	The specific toxicity of the neurotoxin, approximately 2 x 10(6) 50% lethal doses for mice per mg of protein injected, was not enhanced significantly by mild trypsinization, although the protease cleaved the neurotoxin within a disulfide loop that generated at least two primary fragments, approximately 47 and approximately 86 kDa, that remained linked by an interchain disulfide.	Disulfides	228-237	neurotoxin	Clostridium botulinum	29-39
1730484-9	1992	The specific toxicity of the neurotoxin, approximately 2 x 10(6) 50% lethal doses for mice per mg of protein injected, was not enhanced significantly by mild trypsinization, although the protease cleaved the neurotoxin within a disulfide loop that generated at least two primary fragments, approximately 47 and approximately 86 kDa, that remained linked by an interchain disulfide.	Disulfides	371-380	neurotoxin	Clostridium botulinum	29-39
1570025-13	1992	It is concluded that a) a thioredoxin system in brain tissue reduces the interchain disulfide of two-chain tetanus toxin and botulinum neurotoxin A, b) tetanus toxin but not botulinum neurotoxin A consists of two electrophoretically distinct forms which differ by the thiol-disulfide status of their heavy chains, c) the disulfide loop within the heavy chain of tetanus toxin is resistant to the thioredoxin system.	Disulfides	84-93	thioredoxin 1	Rattus norvegicus	26-37
1316357-1	1992	Insulin receptors are disulfide-linked oligotetramers composed of two heterodimers each containing a 130-kDa alpha subunit and a 90-kDa beta subunit.	Disulfides	22-31	insulin	Homo sapiens	0-7
1581029-0	1992	Stabilization of the structure of horse plasma vitamin D binding protein by disulfide bonds.	Disulfides	76-85	D-box binding PAR bZIP transcription factor	Equus caballus	55-72
1581029-6	1992	Circular dichroism and fluorescence studies revealed that the disulfide bonds of DBP contribute substantial structural stabilization to the molecule with respect to thermal denaturation.	Disulfides	62-71	D-box binding PAR bZIP transcription factor	Equus caballus	81-84
1721638-4	1991	We coupled [125I]tyrosine to 131I-alpha 2-macroglobulin or [131I] transferrin via a reducible disulfide linker.	Disulfides	94-103	transferrin	Homo sapiens	66-77
1403340-3	1992	After washing, biotinylated alpha-hANP was eluted from the polystyrene ball with HCI and was reacted with 2,4-dinitrophenyl-fluorescein-bovine serum albumin-disulfide-rabbit anti-alpha-hANP [6-28] IgG conjugate.	Disulfides	157-166	natriuretic peptide A	Homo sapiens	34-38
1751487-0	1991	Amino acid sequence and location of the disulfide bonds in bovine beta 2 glycoprotein I: the presence of five Sushi domains.	Disulfides	40-49	apolipoprotein H	Bos taurus	66-87
1751487-2	1991	The complete amino acid sequence and the location of all the disulfide bonds of bovine beta 2 glycoprotein I were determined.	Disulfides	61-70	apolipoprotein H	Bos taurus	87-108
1751487-5	1991	Eleven disulfide bonds in bovine beta 2 glycoprotein I constitute four characteristic domains, Sushi domains, and one modified form of a Sushi domain.	Disulfides	7-16	apolipoprotein H	Bos taurus	33-54
1751488-1	1991	Human zeta-thrombin, a catalytically competent serine proteinase, arises from a single chymotryptic cleavage at Trp-148 in alpha-thrombin to generate two nonconvalently associated polypeptide segments designated zeta 1-thrombin (the 36-residue A-chain disulfide linked to B-chain residues B1-148) and zeta 2-thrombin (B149-259).	Disulfides	252-261	coagulation factor II, thrombin	Homo sapiens	11-19
1530959-1	1992	CD3 zeta and CD3 eta form disulfide-linked homo- or heterodimers important in targeting partially assembled Ti alpha-beta/CD3 gamma delta epsilon T cell receptor (TCR) complexes to the cell surface and transducing stimulatory signals after antigen recognition.	Disulfides	26-35	CD247 antigen	Mus musculus	0-8
1530959-1	1992	CD3 zeta and CD3 eta form disulfide-linked homo- or heterodimers important in targeting partially assembled Ti alpha-beta/CD3 gamma delta epsilon T cell receptor (TCR) complexes to the cell surface and transducing stimulatory signals after antigen recognition.	Disulfides	26-35	CD247 antigen	Mus musculus	13-20
1744107-0	1991	Role of disulfide bonds in biologic activity of human interleukin-6.	Disulfides	8-17	interleukin 6	Homo sapiens	54-67
1748670-0	1991	The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase.	Disulfides	42-51	acetylcholinesterase (Cartwright blood group)	Homo sapiens	120-140
1756863-0	1991	A Lys27-to-Glu27 mutation in the human insulin-like growth factor-1 prevents disulfide linked dimerization and allows secretion of BiP when expressed in yeast.	Disulfides	77-86	insulin like growth factor 1	Homo sapiens	39-67
1756863-2	1991	A majority of the IGF1-like molecules are disulfide bonded dimers.	Disulfides	42-51	insulin like growth factor 1	Homo sapiens	18-22
1756863-5	1991	These results imply that by preventing ionic interactions between two IGF1 molecules, intermolecular disulfide bonds do not form in yeast, and that in the mutant there is a structural change which induces BiP, allowing its secretion.	Disulfides	101-110	insulin like growth factor 1	Homo sapiens	70-74
1744107-1	1991	We have examined the functional importance of the two disulfide bonds formed by the four conserved cysteines of human interleukin (IL-6).	Disulfides	54-63	interleukin 6	Homo sapiens	118-135
1744107-2	1991	Using a bacterial expression system, we have synthesized a series of recombinant IL-6 mutants in which the constituent cysteines of the first (Cys45-Cys51), second (Cys74-Cys84), or both disulfide bonds of recombinant human interleukin-6 were replaced by other amino acids.	Disulfides	187-196	interleukin 6	Homo sapiens	81-85
1744107-5	1991	These results indicate that the first disulfide bond of human interleukin-6 is not required for maintenance of normal biologic activity.	Disulfides	38-47	interleukin 6	Homo sapiens	62-75
1657953-9	1991	The mutation impairs several steps in the post-translational processing of the insulin receptor:dimerization of 190-kDa proreceptors into a disulfide linked species, proteolytic cleavage of the proreceptor into alpha- and beta-subunits, and terminal processing of the high mannose form of N-linked oligosaccharide into complex carbohydrate.	Disulfides	140-149	insulin	Homo sapiens	79-86
1761235-1	1991	Protein disulfide isomerase (PDI) is an enzyme involved in the catalysis of disulfide bond formation in secretory and cell-surface proteins.	Disulfides	8-17	protein disulfide isomerase family A member 2	Homo sapiens	29-32
1761059-0	1991	Disulfide-bonded dimerization of fibronectin in vitro.	Disulfides	0-9	fibronectin 1	Homo sapiens	33-44
1761059-4	1991	Low concentrations (less than 1 mM) of Fe3+ enhanced the redimerization of fibronectin, suggesting that metal ions may mediate oxidative reactions in the formation of the disulfides.	Disulfides	171-181	fibronectin 1	Homo sapiens	75-86
1761059-6	1991	Dimerization of fibronectin took place most effectively at pH greater than or equal to 8.8 but decreased strongly at lower pH, representing more unfavourable conditions for the action of the thiolate anion in the thiol/disulfide exchange reaction.	Disulfides	219-228	fibronectin 1	Homo sapiens	16-27
1761059-7	1991	Redimerized fibronectin, however, lost many of its binding properties to macromolecular ligands, suggesting that the disulfide bonding did not entirely regenerate the proper conformation of the protein.	Disulfides	117-126	fibronectin 1	Homo sapiens	12-23
1761059-9	1991	SDS/PAGE analysis of the dialyzed urea-denatured/reduced thrombin and plasmin digests of fibronectin revealed that the NH2-terminal 30-kDa fragment and other fragments that contained intrachain disulfides quantitatively regained their non-reduced electrophoretic mobility.	Disulfides	194-204	fibronectin 1	Homo sapiens	89-100
1761059-10	1991	The results show that the dimerization and formation of intrachain disulfides of fibronectin may occur, in part, spontaneously, based on the amino acid sequence information of the protein.	Disulfides	67-77	fibronectin 1	Homo sapiens	81-92
1837811-4	1991	Furthermore, the TcR-gamma combinatorial repertoire appears to be even more limited by the fact that particular V gamma genes are preferentially used in TcR-gamma 1 or TcR-gamma 2 derived receptors, i.e. in disulfide-linked or non-disulfide-linked TcR-gamma delta receptors.	Disulfides	207-216	tryptophanyl-tRNA synthetase 1	Homo sapiens	172-179
1657936-5	1991	The 90-100-kDa TGF-beta 1 binding proteins are components of a 190-kDa disulfide-linked complex.	Disulfides	71-80	transforming growth factor beta 1	Homo sapiens	15-25
1929422-1	1991	Meprin A and B are disulfide-linked, tetrameric metalloendopeptidases in renal brush border membranes.	Disulfides	19-28	meprin 1 beta	Mus musculus	0-14
1666024-2	1991	To modify the hormonal activity of hCG, hybrid molecules composed of hCG and other glycoproteins, either the A or B chain of lectin ricin (hCG-A and hCG-B) through disulfide bridges and horseradish peroxidase (hCG-HRP) through Schiff"s base, were synthesized.	Disulfides	164-173	chromogranin A	Homo sapiens	139-144
1719968-1	1991	Vascular permeability factor (VPF) is an approximately 40-kDa disulfide-linked dimeric glycoprotein that is active in increasing blood vessel permeability, endothelial cell growth and angiogenesis.	Disulfides	62-71	vascular endothelial growth factor A	Homo sapiens	0-28
1940793-0	1991	Reduction of disulfide bonds during antigen processing: evidence from a thiol-dependent insulin determinant.	Disulfides	13-22	insulin	Homo sapiens	88-95
1940793-9	1991	Our findings indicate that reduction of disulfide bonds is both necessary and sufficient for presentation of insulin to a major population of class II-restricted T cells.	Disulfides	40-49	insulin	Homo sapiens	109-116
1779968-8	1991	The structural organization of the chromogranin-A gene resembles that of the chromogranin-B gene in the exons corresponding to the signal peptide, N-terminal sequence, disulfide loop, and C-terminal sequence.	Disulfides	168-177	chromogranin A	Bos taurus	35-49
1779968-8	1991	The structural organization of the chromogranin-A gene resembles that of the chromogranin-B gene in the exons corresponding to the signal peptide, N-terminal sequence, disulfide loop, and C-terminal sequence.	Disulfides	168-177	chromogranin B	Bos taurus	77-91
1719968-1	1991	Vascular permeability factor (VPF) is an approximately 40-kDa disulfide-linked dimeric glycoprotein that is active in increasing blood vessel permeability, endothelial cell growth and angiogenesis.	Disulfides	62-71	vascular endothelial growth factor A	Homo sapiens	30-33
1834643-0	1991	Disulfide cross-linking of caldesmon to actin.	Disulfides	0-9	caldesmon 1	Homo sapiens	27-36
1953706-5	1991	These results suggest that the carboxyl-terminal sequence at residues 32-37 of big ET-1 is important for conversion, whereas the amino-terminal disulfide loop structure appears to interfere with access of ECE to big ET-1.	Disulfides	144-153	endothelin 1	Homo sapiens	216-220
1834643-1	1991	Treatment of a solution of actin and smooth muscle caldesmon with 5,5"-dithiobis(2-nitrobenzoic acid) results in the formation of a disulfide cross-link between the C-terminal penultimate residue Cys-374 of actin and Cys-580 in caldesmon"s C-terminal actin-binding region.	Disulfides	132-141	caldesmon 1	Homo sapiens	51-60
1834643-1	1991	Treatment of a solution of actin and smooth muscle caldesmon with 5,5"-dithiobis(2-nitrobenzoic acid) results in the formation of a disulfide cross-link between the C-terminal penultimate residue Cys-374 of actin and Cys-580 in caldesmon"s C-terminal actin-binding region.	Disulfides	132-141	caldesmon 1	Homo sapiens	228-237
1834643-6	1991	Reaction of 5,5"-dithiobis(2-nitrobenzoic acid)-modified actin with caldesmon leads to the same disulfide cross-linked product between actin and caldesmon Cys-580, enabling the specific labeling of the other caldesmon cysteine, residue 153, in the N-terminal part of caldesmon with a spectroscopic probe.	Disulfides	96-105	caldesmon 1	Homo sapiens	68-77
1939105-6	1991	The cystatin D sequence contains all regions of relevance for cysteine proteinase inhibitory activity and also the 4 cysteine residues that form disulfide bridges in the other members of cystatin Family 2.	Disulfides	145-154	cystatin D	Homo sapiens	4-14
1834643-6	1991	Reaction of 5,5"-dithiobis(2-nitrobenzoic acid)-modified actin with caldesmon leads to the same disulfide cross-linked product between actin and caldesmon Cys-580, enabling the specific labeling of the other caldesmon cysteine, residue 153, in the N-terminal part of caldesmon with a spectroscopic probe.	Disulfides	96-105	caldesmon 1	Homo sapiens	145-154
1834643-6	1991	Reaction of 5,5"-dithiobis(2-nitrobenzoic acid)-modified actin with caldesmon leads to the same disulfide cross-linked product between actin and caldesmon Cys-580, enabling the specific labeling of the other caldesmon cysteine, residue 153, in the N-terminal part of caldesmon with a spectroscopic probe.	Disulfides	96-105	caldesmon 1	Homo sapiens	145-154
1834643-6	1991	Reaction of 5,5"-dithiobis(2-nitrobenzoic acid)-modified actin with caldesmon leads to the same disulfide cross-linked product between actin and caldesmon Cys-580, enabling the specific labeling of the other caldesmon cysteine, residue 153, in the N-terminal part of caldesmon with a spectroscopic probe.	Disulfides	96-105	caldesmon 1	Homo sapiens	145-154
1761367-1	1991	The receptor-recognition site human transforming growth factor-alpha (TGF alpha), a 50-residue tricyclic peptide with three disulfide bonds, was mapped by a set of 46 peptide analogs consisting of linear, monocyclic, bicyclic, and tricyclic structures representing individual and overlapping subdomains of human TGF alpha.	Disulfides	124-133	tumor necrosis factor	Homo sapiens	36-68
1917966-5	1991	rCBP35 expressed in Escherichia coli forms disulfide-linked homodimers (Mr 67,000).	Disulfides	43-52	galectin 3	Rattus norvegicus	0-6
1654393-4	1991	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of partially reduced (alpha beta-heterodimer) receptors affinity-labeled with 125I-insulin indicated the presence of a disulfide-linked beta-subunit of approximately 95 kDa.	Disulfides	177-186	insulin	Homo sapiens	141-148
1898401-7	1991	These results suggest that the 47-Cys residue of GST-P may be located near the glutathione binding site, and modulation of this residue by thiol/disulfide exchange may play an important role in regulation of activity.	Disulfides	145-154	glutathione S-transferase pi 1	Rattus norvegicus	49-54
1716211-7	1991	Using an enzyme-linked immunosorbent sandwich assay for the measurement of the complex formation between protein S and C4BP, mAb against the central core and the disulfide-linked beta chain of C4BP were identified that inhibited the binding of protein S to C4BP.	Disulfides	162-171	complement component 4 binding protein alpha	Homo sapiens	119-123
1716211-7	1991	Using an enzyme-linked immunosorbent sandwich assay for the measurement of the complex formation between protein S and C4BP, mAb against the central core and the disulfide-linked beta chain of C4BP were identified that inhibited the binding of protein S to C4BP.	Disulfides	162-171	complement component 4 binding protein alpha	Homo sapiens	193-197
1716211-7	1991	Using an enzyme-linked immunosorbent sandwich assay for the measurement of the complex formation between protein S and C4BP, mAb against the central core and the disulfide-linked beta chain of C4BP were identified that inhibited the binding of protein S to C4BP.	Disulfides	162-171	complement component 4 binding protein alpha	Homo sapiens	193-197
1912563-8	1991	The duplicated Met resides within a disulfide bond loop proposed to be important in the function of the GPIb binding domain of vWF.	Disulfides	36-45	von Willebrand factor	Homo sapiens	127-130
1651718-0	1991	Connexon integrity is maintained by non-covalent bonds: intramolecular disulfide bonds link the extracellular domains in rat connexin-43.	Disulfides	71-80	gap junction protein, alpha 1	Rattus norvegicus	125-136
1845473-1	1991	Disulfide linkages were characterized for the first time in a fish growth hormone.	Disulfides	0-9	growth hormone 1	Homo sapiens	67-81
1651930-7	1991	Thus, the main erythropoietin-receptor complex in the plasma membrane of these cells consisted of a molecule of the cloned chain of the erythropoietin receptor noncovalently associated with one or two disulfide-bonded molecule(s) of the envelope protein of the defective virus.	Disulfides	201-210	erythropoietin	Homo sapiens	15-29
1837065-1	1991	Lipoprotein(a) [Lp(a)] is a low density lipoprotein which has apo(a) disulfide-linked to apoB100.	Disulfides	69-78	apolipoprotein B	Homo sapiens	89-96
1855480-9	1991	When reformation of disulfide bonds was inhibited by carbamidomethylation of 16K PRL the preparations were more potent.	Disulfides	20-29	prolactin	Rattus norvegicus	81-84
1906465-2	1991	The nascent transferrin receptor containing core-glycosylated asparagine-linked oligosaccharides does not possess complete intersubunit disulfide bonds, sediments predominantly as a monomer in sucrose density gradients, and shows reduced binding to transferrin-agarose.	Disulfides	136-145	transferrin	Homo sapiens	12-23
1864379-0	1991	Site-directed mutagenesis reveals the importance of disulfide bridges and aromatic residues for structure and proliferative activity of human interleukin-4.	Disulfides	52-61	interleukin 4	Homo sapiens	142-155
1856193-7	1991	The specific disulfide bridges, Cys-5 to Cys-59, Cys-15 to Cys-39, and Cys-33 to Cys-55, are analogous to those in the prototype Kunitz-type inhibitor, bovine pancreatic trypsin inhibitor (BPTI).	Disulfides	13-22	trophoblast Kunitz domain protein 1	Bos taurus	170-187
2054354-1	1991	Thrombospondin (TSP) is a 450-kDa glycoprotein that is comprised of three identical disulfide-bonded subunits (1152 amino acids) held together near the heparin-binding amino-terminal globular domains.	Disulfides	84-93	thrombospondin 1	Homo sapiens	0-14
2061339-1	1991	To evaluate potential catalytic mechanism for thioltransferase thiol-disulfide exchange reactions, seven pig liver mutants were constructed by site-directed mutagenesis.	Disulfides	69-78	glutaredoxin-1	Sus scrofa	46-62
2061339-7	1991	These data indicate that reduced thioltransferase reacts first with disulfide substrates, then with a thiol substrate, e.g. GSH.	Disulfides	68-77	glutaredoxin-1	Sus scrofa	33-49
2054354-1	1991	Thrombospondin (TSP) is a 450-kDa glycoprotein that is comprised of three identical disulfide-bonded subunits (1152 amino acids) held together near the heparin-binding amino-terminal globular domains.	Disulfides	84-93	thrombospondin 1	Homo sapiens	16-19
2054354-2	1991	TSP truncated at residue 277 (TSP-277) or 381 (TSP-381) consisted largely of disulfide-bonded trimers when expressed in COS cells or insect cells.	Disulfides	77-86	thrombospondin 1	Homo sapiens	0-3
2054354-2	1991	TSP truncated at residue 277 (TSP-277) or 381 (TSP-381) consisted largely of disulfide-bonded trimers when expressed in COS cells or insect cells.	Disulfides	77-86	thrombospondin 1	Homo sapiens	30-33
2054354-2	1991	TSP truncated at residue 277 (TSP-277) or 381 (TSP-381) consisted largely of disulfide-bonded trimers when expressed in COS cells or insect cells.	Disulfides	77-86	thrombospondin 1	Homo sapiens	30-33
2054354-6	1991	TSP-381 in which Cys-252 and Cys-256 were changed to glycine was secreted efficiently by COS cells but with only a minor portion of the protein in the form of disulfide-bonded trimers.	Disulfides	159-168	thrombospondin 1	Homo sapiens	0-3
2054354-8	1991	We suggest that assembly of TSP trimers involves formation of an alpha-helical coiled-coil structure which is stabilized by formation of disulfides.	Disulfides	137-147	thrombospondin 1	Homo sapiens	28-31
1777934-1	1991	Long-term exposure to natural sun-light (UVA, UVB) induced fluorescence and caused disulfide bond formation in bovine serum albumin (BSA).	Disulfides	83-92	albumin	Homo sapiens	118-131
1888034-6	1991	It was also observed that the digestion of insulin-like growth factor I with V8 protease normally yields two peptides V4(13-20) and V9(59-70) linked by a disulfide bridge.	Disulfides	154-163	insulin like growth factor 1	Homo sapiens	43-71
1710215-1	1991	Cultured fibroblasts bind soluble protomeric fibronectin and mediate its conversion to insoluble disulfide-bonded multimers.	Disulfides	97-106	fibronectin 1	Homo sapiens	45-56
2050696-0	1991	Identification of the disulfide-linked homodimer of apolipoprotein E3 in plasma.	Disulfides	22-31	superoxide dismutase 1	Homo sapiens	39-48
2050696-0	1991	Identification of the disulfide-linked homodimer of apolipoprotein E3 in plasma.	Disulfides	22-31	apolipoprotein E	Homo sapiens	52-69
2050696-2	1991	The nature of disulfide-linked structures of apolipoprotein (apo) E3 in the plasma of E3/3 subjects was examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis performed under nonreducing conditions followed by immunoblotting with apoE-specific antibodies.	Disulfides	14-23	apolipoprotein E	Homo sapiens	45-68
2050696-4	1991	This band and apoE3-A-II were both eliminated by disulfide reduction, which produced a corresponding increase in monomeric apoE3.	Disulfides	49-58	apolipoprotein E	Homo sapiens	14-19
2050696-4	1991	This band and apoE3-A-II were both eliminated by disulfide reduction, which produced a corresponding increase in monomeric apoE3.	Disulfides	49-58	apolipoprotein E	Homo sapiens	123-128
2050696-6	1991	In spite of its apparent molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the high molecular weight band was demonstrated to represent the disulfide-linked homodimer of apoE3.	Disulfides	169-178	superoxide dismutase 1	Homo sapiens	186-195
2050696-6	1991	In spite of its apparent molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the high molecular weight band was demonstrated to represent the disulfide-linked homodimer of apoE3.	Disulfides	169-178	apolipoprotein E	Homo sapiens	199-204
2050696-9	1991	Quantitation of the relative ratios of homodimer, apoE3-A-II, and monomer in the plasma of 22 normolipidemic E3/3 subjects by immunoblotting revealed that the disulfide-linked structures accounted for the majority (approximately 55%) of plasma apoE.	Disulfides	159-168	superoxide dismutase 1	Homo sapiens	39-48
2050696-9	1991	Quantitation of the relative ratios of homodimer, apoE3-A-II, and monomer in the plasma of 22 normolipidemic E3/3 subjects by immunoblotting revealed that the disulfide-linked structures accounted for the majority (approximately 55%) of plasma apoE.	Disulfides	159-168	apolipoprotein E	Homo sapiens	50-54
1664238-3	1991	Immunoblotting experiments with anti-Cek5 polyclonal antibodies indicated that Cek5 is a membrane-associated 120-kDa protein containing intramolecular (but not intermolecular) disulfide bonds.	Disulfides	176-185	EPH receptor B2	Gallus gallus	79-83
1647209-12	1991	Disulfide bridges were shown to connect Cys residues 1 and 99 as well as 29 and 139, respectively, as in IFN-alpha.	Disulfides	0-9	interferon alpha 1	Homo sapiens	105-114
2050146-5	1991	HPLC analysis of secreted IGFI revealed the presence of the correctly folded, genuine molecule as well as an isomeric byproduct of equal molecular mass but with two of the three disulfide bonds interchanged.	Disulfides	178-187	insulin like growth factor 1	Homo sapiens	26-30
2043761-9	1991	Other studies indicate that multimerin and vWF are the two largest platelet proteins and the only two platelet proteins exhibiting a complex, disulfide-linked multimeric composition with variability in multimer size.	Disulfides	142-151	von Willebrand factor	Homo sapiens	43-46
1917302-0	1991	Determination of the disulfide bond pairings in bovine transforming growth factor-alpha.	Disulfides	21-30	transforming growth factor alpha	Bos taurus	55-87
1710630-7	1991	IgE immunoblot studies demonstrated that the enzyme was allergenic and that its expression was dependent on the integrity of intrachain disulfide bonds.	Disulfides	136-145	immunoglobulin heavy constant epsilon	Homo sapiens	0-3
1709934-1	1991	Treatment of the transformed glucocorticoid receptor with hydrogen peroxide promotes the formation of disulfide bonds and inhibits the ability of the receptor to bind to DNA (Tienrungroj, W., Meshinchi, S., Sanchez, E. R., Pratt, S. E., Grippo, J. F., Holmgren, A., and Pratt, W. B.	Disulfides	102-111	nuclear receptor subfamily 3, group C, member 1	Mus musculus	29-52
2040307-1	1991	To investigate the mechanism of disulfide-bond-coupled de novo folding of human lysozyme, we have constructed 23 mutant enzymes in which cysteine residue(s) were replaced by alanine(s).	Disulfides	32-41	lysozyme	Homo sapiens	80-88
1917302-1	1991	A rapid method for determining the three disulfide bond pairings in bovine transforming growth factor-alpha (bTGF-alpha) was developed by digesting bTGF-alpha with thermolysin followed by separation of the generated peptides by reversed-phase HPLC.	Disulfides	41-50	transforming growth factor alpha	Bos taurus	75-107
2046401-3	1991	The protein is synthesized as a large precursor pro-vWF, which dimerizes in the endoplasmic reticulum through disulfide bonds located in the carboxyl-terminal portion of the subunit.	Disulfides	110-119	von Willebrand factor	Homo sapiens	52-55
2046401-8	1991	In the acidic environment of the trans-Golgi and post-Golgi compartments, pro-vWF dimers multimerize by a second set of interchain disulfide bonds.	Disulfides	131-140	von Willebrand factor	Homo sapiens	78-81
1903394-1	1991	The assembly of fibronectin into disulfide cross-linked extracellular matrices requires the interaction of mesenchymal cells with two distinct sites on fibronectin, the Arg-Gly-Asp cell adhesive site and an amino-terminal site contained within the first five type I homologous repeats (Quade, B. J., and McDonald, J.	Disulfides	33-42	fibronectin 1	Homo sapiens	16-27
1903394-1	1991	The assembly of fibronectin into disulfide cross-linked extracellular matrices requires the interaction of mesenchymal cells with two distinct sites on fibronectin, the Arg-Gly-Asp cell adhesive site and an amino-terminal site contained within the first five type I homologous repeats (Quade, B. J., and McDonald, J.	Disulfides	33-42	fibronectin 1	Homo sapiens	152-163
1851759-4	1991	The 150- and 180-kDa TGF-beta-binding proteins also are distinct from the recently described disulfide-linked TGF-beta 1-binding proteins which are present in rat glomeruli.	Disulfides	93-102	transforming growth factor beta 1	Homo sapiens	110-118
1897987-2	1991	These substrates were used to measure the rate of reduction (dethiolation) of protein mixed-disulfides by enzymes with properties similar to those of thioredoxin and glutaredoxin.	Disulfides	92-102	thioredoxin 1	Rattus norvegicus	150-161
2036372-7	1991	When the r-apo(a) plasmid was used to transfect a human hepatoma cell line, lipoprotein particles were secreted containing the disulfide-linked complex of apoB-100 and the r-apo(a).	Disulfides	127-136	apolipoprotein B	Homo sapiens	155-163
1897987-2	1991	These substrates were used to measure the rate of reduction (dethiolation) of protein mixed-disulfides by enzymes with properties similar to those of thioredoxin and glutaredoxin.	Disulfides	92-102	glutaredoxin	Rattus norvegicus	166-178
1897997-1	1991	We have reported recently that the disulfide groups in bovine serum albumin can be reduced by a radiolytic chain reaction which occurs in deoxygenated solutions containing formate ions.	Disulfides	35-44	albumin	Homo sapiens	62-75
1674604-1	1991	Cytotoxic lymphocyte maturation factor (CLMF) is a disulfide-bonded heterodimeric lymphokine that (i) acts as a growth factor for activated T cells independent of interleukin 2 and (ii) synergizes with suboptimal concentrations of interleukin 2 to induce lymphokine-activated killer cells.	Disulfides	51-60	interleukin 2	Homo sapiens	231-244
1826703-0	1991	Formation of intrachain disulfide bonds gives rise to two different forms of the murine IL-1 beta precursor.	Disulfides	24-33	interleukin 1 beta	Mus musculus	88-97
1747407-7	1991	A structural analysis of the N-terminal domain of mammalian prolactin revealed the important role of Pro-2 and Pro-4 residues at positions adjacent with and inside the disulfide moiety.	Disulfides	168-177	prolactin	Homo sapiens	60-69
1826703-11	1991	These data indicate that murine macrophages contain two populations of the IL-1 beta precursor, one of which can undergo a disulfide-mediated protein folding; they also suggest that oxidation of -SH groups may be critical for the proteolytic processing of the IL-1 beta precursor.	Disulfides	123-132	interleukin 1 beta	Mus musculus	75-84
1926582-0	1991	[Plasminogen activation by a tissue activator and effector properties of fibrinogen-N-terminal disulfide (N-DSK) fibrin complex].	Disulfides	95-104	fibrinogen beta chain	Homo sapiens	73-83
1870263-2	1991	vWF is composed of an identical subunit with a molecular weight (MW) of 270 kDa, which is held together by disulfide bonds.	Disulfides	107-116	von Willebrand factor	Homo sapiens	0-3
1707541-4	1991	mIgM is associated with the MB-1 protein, which is disulfide-linked to a protein designated Ig-beta.	Disulfides	51-60	CD79a molecule	Homo sapiens	28-32
2029525-2	1991	SDS-PAGE of haptoglobin (a tetramer composed of two glycosylated beta-chains each containing two sites for Asn-linked oligosaccharides connected by disulfide bonds with two nonglycosylated alpha-chains) clearly shows that the beta-chain of haptoglobin from diabetic rats is smaller than normal, with a molecular mass of 39 instead of 40 kDa.	Disulfides	148-157	haptoglobin	Rattus norvegicus	12-23
2007607-13	1991	We propose a model for the structure of loricrin in which (i) the unusual glycine-serine-rich sequences adopt a flexible loop conformation, indexed on the recurrent aliphatic residues; (ii) inter- or intramolecular isodipeptide and disulfide cross-links induce or stabilize folding of loricrin so as to form a more compact rosette-like structure; and (iii) the presence of the flexible glycine-rich loops necessarily will impact a flexible character to the cell envelope and entire epithelium.	Disulfides	232-241	loricrin cornified envelope precursor protein	Homo sapiens	40-48
2016320-4	1991	Structural characterization of CD6 revealed that it contained intrachain disulfide bonds, was N-glycosylated, and in activated cells was phosphorylated on serine.	Disulfides	73-82	CD6 molecule	Homo sapiens	31-34
1848998-4	1991	Air oxidation of P39 gave P78, a 78-residue covalent dimer having a disulfide bridge linking its C termini.	Disulfides	68-77	cyclin dependent kinase 5 regulatory subunit 2	Homo sapiens	17-20
1848998-7	1991	Its C-terminal disulfide bridge renders P78 significantly more stable than P39 to thermal denaturation or denaturation by urea.	Disulfides	15-24	cyclin dependent kinase 5 regulatory subunit 2	Homo sapiens	75-78
1897944-3	1991	Thus, inactivation of GST-P by H2O2 was indicated to involve concomitant formation of disulfide bonds between cysteinyl residues.	Disulfides	86-95	glutathione S-transferase pi 1	Rattus norvegicus	22-27
2007594-0	1991	Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme.	Disulfides	28-37	lysozyme	Homo sapiens	84-92
2007594-1	1991	Our previous results using the Saccharomyces cerevisiae secretion system suggest that intramolecular exchange of disulfide bonds occurs in the folding pathway of human lysozyme in vivo (Taniyama, Y., Yamamoto, Y., Kuroki, R., and Kikuchi, M. (1990) J. Biol.	Disulfides	113-122	lysozyme	Homo sapiens	168-176
2007594-14	1991	These results suggest that the introduction of Cys83 and Cys91 may act to suppress the process of native disulfide bond formation through disulfide bond interchange in the folding of human lysozyme.	Disulfides	105-114	lysozyme	Homo sapiens	189-197
2007594-14	1991	These results suggest that the introduction of Cys83 and Cys91 may act to suppress the process of native disulfide bond formation through disulfide bond interchange in the folding of human lysozyme.	Disulfides	138-147	lysozyme	Homo sapiens	189-197
1725450-7	1991	The disulfide bridge structure of alpha 1M was deduced from its sequence and showed extensive similarities with the experimentally determined structures of other alpha-macroglobulins, suggesting similar overall tertiary structures.	Disulfides	4-13	pregnancy-zone protein	Rattus norvegicus	34-42
2010538-13	1991	These findings suggest that vWD type IIB may be caused by relatively few distinct mutations, that these mutations may cluster within a specific region of one disulfide loop in vWF domain A1, and that this region can modulate the affinity of vWF for the platelet glycoprotein Ib-IX complex.	Disulfides	158-167	von Willebrand factor	Homo sapiens	176-179
2010538-13	1991	These findings suggest that vWD type IIB may be caused by relatively few distinct mutations, that these mutations may cluster within a specific region of one disulfide loop in vWF domain A1, and that this region can modulate the affinity of vWF for the platelet glycoprotein Ib-IX complex.	Disulfides	158-167	von Willebrand factor	Homo sapiens	241-244
2007122-0	1991	Identification of the disulfide bonds of human complement C1s.	Disulfides	22-31	complement C1s	Homo sapiens	58-61
1712069-0	1991	Covalent disulfide binding of human IL-1 beta to alpha 2-macroglobulin: inhibition by D-penicillamine.	Disulfides	9-18	interleukin 1 beta	Homo sapiens	36-45
1712069-4	1991	Thus, the possibility that IL-1 beta forms a disulfide bond with alpha 2M was investigated.	Disulfides	45-54	interleukin 1 beta	Homo sapiens	27-36
1712069-11	1991	Thus, disulfide bonds were formed between the free SH groups on [125I]rIL-1 beta and those resulting from the cleavage of the internal thioester bonds of alpha 2M.	Disulfides	6-15	interleukin 1 beta	Rattus norvegicus	70-80
2007122-2	1991	To determine the disulfide-bonding pattern, fragments of C1s were generated by cleavage with pepsin, thermolysin, or subtilisin.	Disulfides	17-26	complement C1s	Homo sapiens	57-60
2007122-5	1991	All of the disulfide bonds of the earlier described substructures of C1s, the EGF-homologous part, the two SCR units, and the two domains typical for C1s and C1r are localized within these domains.	Disulfides	11-20	complement C1s	Homo sapiens	69-72
2007122-5	1991	All of the disulfide bonds of the earlier described substructures of C1s, the EGF-homologous part, the two SCR units, and the two domains typical for C1s and C1r are localized within these domains.	Disulfides	11-20	complement C1s	Homo sapiens	150-153
2007122-5	1991	All of the disulfide bonds of the earlier described substructures of C1s, the EGF-homologous part, the two SCR units, and the two domains typical for C1s and C1r are localized within these domains.	Disulfides	11-20	complement C1r	Homo sapiens	158-161
1654774-12	1991	This results in the formation of intramolecular disulfide bridge(s) within the regulatory domain or catalytic domain leading to either reversible activation or inactivation of PKC, respectively.	Disulfides	48-57	proline rich transmembrane protein 2	Homo sapiens	176-179
2002060-10	1991	These changes are reversed by dithiothreitol and are consistent with a conformational change which transforms the inhibitory activity from a rapid, irreversible mode in native alpha 1-PI to a dissociable competitive mode in the mixed disulfide derivatives.	Disulfides	234-243	serpin family A member 1	Homo sapiens	176-186
1824944-1	1991	The high affinity receptor for immunoglobulin E (IgE) is a tetrameric structure (alpha beta gamma 2) consisting of non-covalently associated subunits: one IgE-binding alpha chain, one 4-fold membrane spanning beta chain, and two disulfide-linked gamma chains.	Disulfides	229-238	immunoglobulin heavy constant epsilon	Homo sapiens	31-47
1824944-1	1991	The high affinity receptor for immunoglobulin E (IgE) is a tetrameric structure (alpha beta gamma 2) consisting of non-covalently associated subunits: one IgE-binding alpha chain, one 4-fold membrane spanning beta chain, and two disulfide-linked gamma chains.	Disulfides	229-238	immunoglobulin heavy constant epsilon	Homo sapiens	49-52
1671533-6	1991	Stimulated neutrophils adhere to surfaces coated with the N-terminal disulfide knot fragment of fibrinogen or fibrinogen fragment E. Moreover, peptides containing the sequence Gly-Pro-Arg (which corresponds to amino acids 17-19 of the N-terminal region of the A alpha chain of fibrinogen), and monoclonal antibody LeuM5, block tumor necrosis factor-stimulated neutrophil adhesion to fibrinogen and to the N-terminal disulfide knot fragment of fibrinogen.	Disulfides	69-78	fibrinogen beta chain	Homo sapiens	96-106
1993171-0	1991	Disulfide assignments in recombinant mouse and human interleukin 4.	Disulfides	0-9	interleukin 4	Homo sapiens	53-66
1993171-1	1991	The disulfide pairings of mouse and human interleukin 4 (IL-4) proteins have been determined.	Disulfides	4-13	interleukin 4	Homo sapiens	42-55
1993171-1	1991	The disulfide pairings of mouse and human interleukin 4 (IL-4) proteins have been determined.	Disulfides	4-13	interleukin 4	Homo sapiens	57-61
1993171-8	1991	The disulfide bonds in human IL-4 are between the first and sixth, second and fourth, and third and fifth cysteines.	Disulfides	4-13	interleukin 4	Homo sapiens	29-33
1988154-5	1991	Pro-vWf, lacking the C-terminal region involved in interchain disulfide bonding, formed granules.	Disulfides	62-71	von Willebrand factor	Homo sapiens	4-7
1992463-6	1991	Monoclonal antibodies were used with Western blot analysis to localize the wild-type mouse peripherin/rds protein to isolated mouse rod outer segments and to show that it, like bovine peripherin, exists as two subunits linked by one or more disulfide bonds.	Disulfides	241-250	peripherin 2	Mus musculus	102-105
1703371-9	1991	Analysis of the fluorescent peptides generated by V8 protease cleavage of VP7 labeled with AEDANS in the absence of DTT (i.e., with any putative intramolecular disulfide bonds intact) suggested that the cysteine at position 154 was the only one accessible to AEDANS.	Disulfides	160-169	VP7	Bluetongue virus	74-77
1988044-4	1991	The structure of hCGRP-1 in this solvent comprises an amino-terminal disulfide-bonded loop (residues 2-7) leading into a well-defined alpha-helix between residues 8 and 18; thereafter, the structure is predominantly disordered, although there are indications of a preference for a turn-type conformation between residues 19 and 21.	Disulfides	69-78	calcitonin related polypeptide alpha	Homo sapiens	17-24
1839706-2	1991	Its unique immunochemical properties are caused by the Lp(a) polypeptide chain which is attached to apolipoprotein B (apoB) by a disulfide bridge.	Disulfides	129-138	apolipoprotein B	Homo sapiens	100-116
1839706-2	1991	Its unique immunochemical properties are caused by the Lp(a) polypeptide chain which is attached to apolipoprotein B (apoB) by a disulfide bridge.	Disulfides	129-138	apolipoprotein B	Homo sapiens	118-122
1987060-4	1991	The fragment of butyricum neurotoxin obtained by prolonged tryptic treatment was found to comprise the light chain and H-1 fragment linked together by a disulfide bond.	Disulfides	153-162	neurotoxin	Clostridium botulinum	26-36
1801725-0	1991	S-S bridges of cathepsin B and H from bovine spleen: a basis for cathepsin B model building and possible functional implications for discrimination between exo- and endopeptidase activities among cathepsins B, H and L. Bovine spleen cathepsin B contains 7 disulfide bridges.	Disulfides	256-265	cathepsin B	Bos taurus	15-26
2049799-0	1991	Activity of artificial mutant variants of human growth hormone deficient in a disulfide bond between Cys53 and Cys165.	Disulfides	78-87	growth hormone 1	Homo sapiens	48-62
1893830-0	1991	[The isolation of the NH2-terminal disulfide nodes of human fibrinogen and fibrin and of their constituent polypeptide chain fragments].	Disulfides	35-44	fibrinogen beta chain	Homo sapiens	60-70
1986917-9	1991	Human (but not bovine) chromogranin A displayed intermolecular disulfide crosslinks on SDS-PAGE gels and immunoblotting.	Disulfides	63-72	chromogranin A	Bos taurus	23-37
1786856-8	1991	Each subunit of CRP and SAP had one intrasubunit disulfide bond, determined by reduction and carboxymethylation.	Disulfides	49-58	amyloid P component, serum	Bos taurus	24-27
1846021-1	1991	Activin, a disulfide-linked polypeptide dimer first isolated from gonadal tissue extracts, has amino acid sequence and structural homology with transforming growth factor beta (TGF beta).	Disulfides	11-20	transforming growth factor, beta 1	Rattus norvegicus	177-185
1725423-4	1991	All ET-1 analogues had the proper intramolecular disulfide bonds.	Disulfides	49-58	endothelin 1	Rattus norvegicus	4-8
1985197-7	1991	Mutation of the putative disulfide bridge-forming Cys at residue 336 blocked gp160 cleavage and CD4 binding.	Disulfides	25-34	CD4 molecule	Homo sapiens	96-99
1840453-2	1991	Apolipoprotein(a) is bound to ApoB-100 by a disulfide bridge.	Disulfides	44-53	apolipoprotein B	Homo sapiens	30-38
1698670-9	1990	p75 displays a greater electrophoretic mobility under nonreducing conditions, indicating the presence of intramolecular disulfide bonds, a common characteristic of secreted proteins.	Disulfides	120-129	nerve growth factor receptor (TNFR superfamily, member 16)	Mus musculus	0-3
2253341-1	1990	Lipoprotein (a) [Lp(a)] represents a class of lipoprotein particles defined by the presence of apolipoprotein(a), a unique glycoprotein linked by a disulfide bond to apolipoprotein B-100 to form a single macromolecule.	Disulfides	148-157	apolipoprotein B	Homo sapiens	166-186
2126013-3	1990	Diferric-transferrin was conjugated to biotin via a cleavable disulfide bond and iodinated.	Disulfides	62-71	transferrin	Homo sapiens	9-20
2146276-13	1990	We found that scatter factor represents a 92,000 mol wt glycoprotein which, apparently, is converted by limited proteolysis into disulfide-linked 62,000 and 34/32,000 mol wt subunits.	Disulfides	129-138	hepatocyte growth factor	Canis lupus familiaris	14-28
1946344-6	1991	The mapping of three disulfide bridges in IL-4 provided additional constraints on possible tertiary structures.	Disulfides	21-30	interleukin 4	Homo sapiens	42-46
2090118-4	1990	Proinsulin with correct disulfide bonds, directly obtained from polymer--attached polypeptide, followed was converted into insulin.	Disulfides	24-33	insulin	Homo sapiens	0-10
2090118-4	1990	Proinsulin with correct disulfide bonds, directly obtained from polymer--attached polypeptide, followed was converted into insulin.	Disulfides	24-33	insulin	Homo sapiens	3-10
2220758-2	1990	Two-dimensional, nonreduced/reduced SDS gel electrophoresis of immunoprecipitated complexes revealed 1) endogenous disulfide linkages between Ii-Ii and Ii-p70 and 2) chemically crosslinked, nearest neighbors of alpha-beta, alpha-Ii, Ii-p70, and alpha-p80.	Disulfides	115-124	ubiquitin associated and SH3 domain containing B	Homo sapiens	155-158
2076464-13	1990	Finally, the three disulfide bonds were shown by tandem mass spectrometry to match those of insulin.	Disulfides	19-28	insulin	Homo sapiens	92-99
2212658-3	1990	Nucleotide sequence analysis of the DRA mRNA from HMy2.DRN revealed a 75 nucleotide deletion corresponding to the start of the alpha 2 domain and involving one of two cysteines that are involved in the formation of an intrachain disulfide bond.	Disulfides	229-238	solute carrier family 26 member 3	Homo sapiens	36-39
2171329-1	1990	From electrophoretic analysis, we identified in the saliva of an Ashkenazi Jew a disulfide-bonded major glycoprotein variant (Gl 8) that is a product of the proline-rich protein (PRP) locus PRB3.	Disulfides	81-90	complement component 4 binding protein alpha	Homo sapiens	157-177
2171329-1	1990	From electrophoretic analysis, we identified in the saliva of an Ashkenazi Jew a disulfide-bonded major glycoprotein variant (Gl 8) that is a product of the proline-rich protein (PRP) locus PRB3.	Disulfides	81-90	complement component 4 binding protein alpha	Homo sapiens	179-182
2171329-10	1990	It is interesting that products of different PRP genes, Gl 8 from PRB3 and Pa 1 from PRH1, are both disulfide bonded and probably modify salivary peroxidase (part of an important intraoral antibacterial system) through formation of disulfide-bonded heterodimers.	Disulfides	100-109	complement component 4 binding protein alpha	Homo sapiens	45-48
2171329-10	1990	It is interesting that products of different PRP genes, Gl 8 from PRB3 and Pa 1 from PRH1, are both disulfide bonded and probably modify salivary peroxidase (part of an important intraoral antibacterial system) through formation of disulfide-bonded heterodimers.	Disulfides	100-109	PAXIP1 associated glutamate rich protein 1	Homo sapiens	75-79
2171329-10	1990	It is interesting that products of different PRP genes, Gl 8 from PRB3 and Pa 1 from PRH1, are both disulfide bonded and probably modify salivary peroxidase (part of an important intraoral antibacterial system) through formation of disulfide-bonded heterodimers.	Disulfides	232-241	complement component 4 binding protein alpha	Homo sapiens	45-48
2171329-10	1990	It is interesting that products of different PRP genes, Gl 8 from PRB3 and Pa 1 from PRH1, are both disulfide bonded and probably modify salivary peroxidase (part of an important intraoral antibacterial system) through formation of disulfide-bonded heterodimers.	Disulfides	232-241	PAXIP1 associated glutamate rich protein 1	Homo sapiens	75-79
1975828-2	1990	The Ly-49 (A1, YE1/48) Ag is a disulfide-linked dimer with 44-kDa subunits, and is expressed on the cell surface of rare T cell tumors of C57BL/6 origin.	Disulfides	31-40	BCL2 related protein A1	Homo sapiens	4-13
2121685-4	1990	Purified elastase converted pro-uPA to an enzymatically inactive molecule composed of two polypeptide chains of Mr = 33,000 and 22,000 linked to each other by a disulfide bond.	Disulfides	161-170	plasminogen activator, urokinase	Homo sapiens	32-35
2398350-0	1990	Intra- and interchain disulfide bond generation in S100b protein.	Disulfides	22-31	S100 calcium binding protein B	Homo sapiens	51-56
2398350-1	1990	Disulfide-bridged S100b protein formation, aircatalyzed and induced by thiol/disulfide exchange, was studied under various ionic conditions.	Disulfides	0-9	S100 calcium binding protein B	Homo sapiens	18-23
2398350-1	1990	Disulfide-bridged S100b protein formation, aircatalyzed and induced by thiol/disulfide exchange, was studied under various ionic conditions.	Disulfides	77-86	S100 calcium binding protein B	Homo sapiens	18-23
2398350-2	1990	As native, physiological disulfide-bridged proteins are obtained easily from their reduced counterparts under appropriate redox conditions, this work was performed to determine whether this was the case for disulfide-bridged S100b proteins, reported to have neurite extension activity.	Disulfides	207-216	S100 calcium binding protein B	Homo sapiens	225-230
2398350-7	1990	Taken together, these data question the physiological relevance of these disulfide-bridged S100b protein species.	Disulfides	73-82	S100 calcium binding protein B	Homo sapiens	91-96
2117638-4	1990	The mu heavy chain and lambda 5 were disulfide-bonded with each other, while the VpreB protein was noncovalently associated.	Disulfides	37-46	pre-B lymphocyte gene 2	Mus musculus	23-31
2289632-11	1990	Following the signal sequence is a region of highly conserved amino acids that participate in disulfide bond formation critical for the maintenance of tertiary structure in mammalian fibrinogen.	Disulfides	94-103	fibrinogen beta chain	Homo sapiens	183-193
2201681-1	1990	Endothelins 1-3 are a family of 21-amino acid peptides whose structure consists of two rings formed by intra-chain disulfide bonds and a linear "COOH-terminal tail."	Disulfides	115-124	endothelin 1	Homo sapiens	0-15
2362273-1	1990	Cyclic analogues of angiotensin II (AII) were synthesized by connecting the side chains of residues 3 and 5 via a disulfide bridge.	Disulfides	114-123	angiotensinogen	Homo sapiens	20-34
2142945-7	1990	The observed heterogeneity of the soluble interferon gamma receptor under nonreducing electrophoretic conditions is probably due to different conformational forms resulting from the formation of non-native intramolecular disulfide bonds among the 8 cysteine residues present in the soluble interferon gamma receptor molecule.	Disulfides	221-230	interferon gamma	Homo sapiens	42-58
2217145-9	1990	These results demonstrated that the disulfide bond is not necessary for folding and activity, but are consistent with the analog having a looser, more flexible structure in solution than the native TNF-alpha.	Disulfides	36-45	tumor necrosis factor	Homo sapiens	198-207
2362273-1	1990	Cyclic analogues of angiotensin II (AII) were synthesized by connecting the side chains of residues 3 and 5 via a disulfide bridge.	Disulfides	114-123	angiotensinogen	Homo sapiens	36-39
2385828-2	1990	With purified GPIIb:IIIa as an antigen, we have produced monoclonal antibody CS-1, which immunoblotting demonstrates to be specific for native GPIIIa; disulfide bond reduction of GPIIIa resulted in loss of immunoreactivity.	Disulfides	151-160	integrin subunit beta 3	Homo sapiens	143-149
2385828-2	1990	With purified GPIIb:IIIa as an antigen, we have produced monoclonal antibody CS-1, which immunoblotting demonstrates to be specific for native GPIIIa; disulfide bond reduction of GPIIIa resulted in loss of immunoreactivity.	Disulfides	151-160	integrin subunit beta 3	Homo sapiens	179-185
2390214-0	1990	Disulfide bridges of bovine spleen cathepsin B.	Disulfides	0-9	cathepsin B	Bos taurus	35-46
2160974-8	1990	Glomerular TGF-beta 1-binding proteins are distinct from previously described TGF-beta-binding proteins in their specificity for TGF-beta 1 and their formation of disulfide-linked multimers.	Disulfides	163-172	transforming growth factor, beta 1	Rattus norvegicus	11-21
2390214-1	1990	Bovine spleen cathepsin B contains 7 disulfide bridges.	Disulfides	37-46	cathepsin B	Bos taurus	14-25
2161792-1	1990	Endothelins (ETs) are 21-amino acid peptides with two disulfide bonds that have powerful vasoactive properties.	Disulfides	54-63	endothelin 1	Homo sapiens	0-11
1699883-3	1990	The RCC-1 was shown to consist of 94,000 dalton disulfide-bonded dimers which were shown to be different from the transferrin receptor.	Disulfides	48-57	regulator of chromosome condensation 1	Homo sapiens	4-9
2142832-4	1990	Lp(a) is essentially an LDL-like lipoprotein particle to which the glycoprotein apo(a) is attached through a disulfide bridge with apo B-100.	Disulfides	109-118	apolipoprotein B	Homo sapiens	131-140
2337349-0	1990	Structural and ion-binding properties of an S100b protein mixed disulfide: comparison with the reappraised native S100b protein properties.	Disulfides	64-73	S100 calcium binding protein B	Homo sapiens	44-49
2337349-1	1990	S100b protein, chemically modified by thioethanol groups (linked via disulfide bonds to two out of four Cys per dimer) was largely similar to reduced native S100b protein in its overall structure and differed only by small modifications extending, however, to the whole protein structure.	Disulfides	69-78	S100 calcium binding protein B	Homo sapiens	0-5
1693524-0	1990	Denaturant-dependent folding of bovine pancreatic trypsin inhibitor mutants with two intact disulfide bonds.	Disulfides	92-101	trophoblast Kunitz domain protein 1	Bos taurus	50-67
2185224-2	1990	The di-chain neurotoxin generated in vitro is composed of an approximately 50-kDa light chain and an approximately 100-kDa heavy chain which are disulfide linked and is indistinguishable from the di-chain neurotoxin that forms in vivo and is routinely isolated (M.L.	Disulfides	145-154	neurotoxin	Clostridium botulinum	13-23
2163967-8	1990	The preS2-bound part of the human serum albumin could be removed from HBsAg by high-salt, such as CsCl centrifugation, but another part could only be removed by treatment with a disulfide cleaving reagent.	Disulfides	178-187	albumin	Homo sapiens	34-47
2354199-2	1990	Soluble protein kinase C was estimated to have 5-6 disulfide bonds which could potentially react with the mercury electrode.	Disulfides	51-60	proline rich transmembrane protein 2	Homo sapiens	8-24
2358073-3	1990	p24 (38,000 copies/platelet) has intramolecular disulfide bond(s) and, in SDS-PAGE, consists of major 24-kDa molecule and minor 26- to 31-kDa molecules.	Disulfides	48-57	transmembrane p24 trafficking protein 2	Homo sapiens	0-3
2393946-1	1990	The hexadodecapeptide corresponding to the entire amino acid sequence of porcine brain natriuretic peptide (pBNP) was synthesized by assembling four segments in solution, followed by HF deprotection and subsequent oxidation to establish an intramolecular disulfide bridge.	Disulfides	255-264	natriuretic peptide B	Rattus norvegicus	81-106
2180927-6	1990	Human growth hormone contains two disulfide bridges between residues 53-165 (large loop) and 182-189 (small loop).	Disulfides	34-43	growth hormone 1	Homo sapiens	6-20
2333290-3	1990	Human transferrin, as well as the chicken homologue conalbumin, has been covalently linked to the small DNA-binding protein protamine or to polylysines of various sizes through a disulfide linkage.	Disulfides	179-188	transferrin	Homo sapiens	6-17
2141278-1	1990	C1-s, one of the three subcomponents of C1-, the first component of complement, is a serine protease comprising two disulfide-linked chains, the B chain, containing the catalytic site, and the A chain, involved in Ca2+ binding and Ca2(+)-dependent interaction(s) with the other C1- subcomponents.	Disulfides	116-125	complement C1s	Homo sapiens	0-4
2141054-2	1990	The protein moiety of Lp[a], apoLp[a], consists of two apoproteins, apo[a] and apoB-100, linked by one or more disulfide bonds(s).	Disulfides	111-120	apolipoprotein B	Homo sapiens	79-87
2324203-6	1990	By using a combination of sedimentation velocity centrifugation and immunoprecipitation assays using polyclonal and conformation-specific monoclonal antibodies it was found that extracellular NAF consisted of a mixture of monomers, disulfide-linked dimers, and tetramers.	Disulfides	232-241	C-X-C motif chemokine ligand 8	Homo sapiens	192-195
2201313-1	1990	We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51-found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin.	Disulfides	66-75	insulin like growth factor 1	Homo sapiens	213-241
2201313-1	1990	We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51-found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin.	Disulfides	66-75	insulin like growth factor 1	Homo sapiens	243-248
2201313-1	1990	We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51-found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin.	Disulfides	66-75	insulin like growth factor 1	Homo sapiens	320-325
2315700-2	1990	The role of the pro-region in the biosynthesis of transforming growth factor--beta 1 (TGF-beta 1) and activin A, two structurally related disulfide-linked homodimers synthesized as large precursors, was studied.	Disulfides	138-147	transforming growth factor beta 1	Homo sapiens	50-84
2186807-3	1990	Recombinant renin contains carbohydrate covalently attached to asparagines at positions 5 and 75 (renin numbering) and disulfide linkages at Cys-51/Cys-58, Cys-217/Cys-221, and Cys-259/Cys-296.	Disulfides	119-128	renin	Homo sapiens	12-17
2315700-4	1990	The pro-regions of activin A and TGF-beta 1, therefore, aid the folding, disulfide bond formation, and export of their respective homodimers.	Disulfides	73-82	transforming growth factor beta 1	Homo sapiens	33-43
2158124-3	1990	The binding was highly specific for ET-1, because (1) none of the other various peptides or Ca2+-channel antagonists affected the binding, (2) the scission of disulfide bonds, the digestion of the C-terminal 6-amino acid residues, or nitrophenylsulfenylization of the C-terminal Trp21 of ET-1 markedly reduced the binding ability and, (3) ET-1 showed the highest affinity for the vascular receptor among three ET isopeptides.	Disulfides	159-168	endothelin 1	Homo sapiens	36-40
2322237-1	1990	Bovine transforming growth factor-alpha (bTGF-alpha) is a 50 amino acid polypeptide with three disulfide linkages.	Disulfides	95-104	transforming growth factor alpha	Bos taurus	7-39
2334711-0	1990	Disulfide bond reduction in fibrinogen: calcium protection and effect on clottability.	Disulfides	0-9	fibrinogen beta chain	Homo sapiens	28-38
2334711-1	1990	Fibrinogen contains 29 disulfide bonds.	Disulfides	23-32	fibrinogen beta chain	Homo sapiens	0-10
2334711-8	1990	The loss of thrombin clottability may have also come from gamma 326Cys-gamma 339Cys disulfide bond reduction since the structure supported by this bond may be important for the function of the C-terminal polymerization site.	Disulfides	84-93	coagulation factor II, thrombin	Homo sapiens	12-20
2404763-6	1990	These observations, plus structural considerations, suggest that Cys77 and Cys95 either remain uncrosslinked or the disulfide bond Cys77-Cys95, once formed, is opened during the final step in the folding of human lysozyme in vivo.	Disulfides	116-125	lysozyme	Homo sapiens	213-221
2137383-3	1990	In addition, Lp(a) contains the glycoprotein apolipoprotein(a) [apo(a)], which is disulfide-linked to apo B-100.	Disulfides	82-91	apolipoprotein B	Homo sapiens	102-111
2303061-2	1990	L-FABP-SSG, which was prepared in vitro through thiol-disulfide exchange reaction, showed more acidic pI (approximately 5.0) than the pI (approximately 7.0) of reduced L-FABP.	Disulfides	54-63	fatty acid binding protein 1	Rattus norvegicus	0-6
1968792-1	1990	The Lp(a) antigen resides in a polypeptide chain that is attached to apolipoprotein B (apoB) by a disulfide bridge.	Disulfides	98-107	apolipoprotein B	Homo sapiens	69-85
1968792-1	1990	The Lp(a) antigen resides in a polypeptide chain that is attached to apolipoprotein B (apoB) by a disulfide bridge.	Disulfides	98-107	apolipoprotein B	Homo sapiens	87-91
2194740-4	1990	All relaxins have the same two chain, disulfide-linked insulin-like structure and two arginine residues in the midregion of the B chain.	Disulfides	38-47	insulin	Homo sapiens	55-62
2297224-1	1990	The activity of the thiol-dependent enzyme glyceraldehyde-3-phosphate dehydrogenase (GPD), in vertebrate cells, was modulated by a change in the intracellular thiol:disulfide redox status.	Disulfides	165-174	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	43-83
2297224-1	1990	The activity of the thiol-dependent enzyme glyceraldehyde-3-phosphate dehydrogenase (GPD), in vertebrate cells, was modulated by a change in the intracellular thiol:disulfide redox status.	Disulfides	165-174	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	85-88
2294968-3	1990	The free cysteine residues of apolipoprotein B-100 on low-density lipoprotein are located at positions 3734 and 4190, either or both of which can potentially form a disulfide linkage with apolipoprotein(a) in lipoprotein(a).	Disulfides	165-174	apolipoprotein B	Homo sapiens	30-50
2104899-12	1990	TIA-1 was induced to form disulfide linked dimers, trimers, and tetramers of the basic 15-kDa unit.	Disulfides	26-35	TIA1 cytotoxic granule associated RNA binding protein	Homo sapiens	0-5
2112914-5	1990	These results support the previously held view that the disulfide bonds formed by insulin are influenced by its structure.	Disulfides	56-65	insulin	Homo sapiens	82-89
1701652-4	1990	Finally, formation of a disulfide bond between the two Cys residues conserved among all seven known members of the FGF family results in a virtually inactive product that can subsequently be reactivated by reduction.	Disulfides	24-33	fibroblast growth factor 1	Homo sapiens	115-118
1688410-1	1990	The rate-limiting event for combination of hCG alpha- and beta-subunits in JAR choriocarcinoma cells is the rate of disulfide bond formation in the beta-subunit.	Disulfides	116-125	chromogranin A	Homo sapiens	43-52
2298462-2	1990	The CD46 antigen is identified by the E4.3 monoclonal antibody (mAb) and exists at the surface of human peripheral blood lymphocytes (PBLs) as two acidic, non-disulfide bonded chains, alpha and beta, of Mr 66,000 and 56,000.	Disulfides	159-168	CD46 molecule	Homo sapiens	4-8
1701652-0	1990	Disulfide bonds are neither required, present, nor compatible with full activity of human recombinant acidic fibroblast growth factor.	Disulfides	0-9	fibroblast growth factor 1	Homo sapiens	102-133
2136886-2	1990	Sequence analysis of cDNA clones indicates that mouse Fc gamma RI is a transmembrane glycoprotein that is composed of three disulfide bonded extracellular Ig binding domains unlike Fc gamma RII of man and mouse.	Disulfides	124-133	Fc receptor, IgG, high affinity I	Mus musculus	54-65
2087556-4	1990	The neurotrophic activity is sensitive to reduction of disulfide bonds, and appears to be a disulfide dimer of S100 beta.	Disulfides	92-101	S100 calcium binding protein B	Homo sapiens	111-120
2188230-3	1990	Then they were coupled by stepwise removal of two different protecting groups at the cysteinyl thiols for semiselective formation of disulfide bridges to give bombyxin-IV in 8% yield.	Disulfides	133-142	bombyxin E-1	Bombyx mori	159-170
2188233-5	1990	Finally, its structure appears to contain two potential amphipathic helices joined by the single disulfide bridge present in all chromogranin A and B molecules.	Disulfides	97-106	chromogranin A	Homo sapiens	129-149
2296573-3	1990	We now report that at least some mouse p75 appears to exist as a disulfide-linked heterodimer with a subunit of Mr 22,000 (p22).	Disulfides	65-74	tumor necrosis factor receptor superfamily, member 1b	Mus musculus	39-42
2284959-2	1990	The corresponding disulfides (II1-7) were obtained by the oxidation of compounds I1-7 with hydrogen peroxide (1%) in weak alkali medium below 10 degrees C. In preliminary tests, some compounds showed inhibitory activity of ACE in vitro.	Disulfides	18-28	protein phosphatase 1 regulatory inhibitor subunit 1A	Homo sapiens	31-35
2296573-3	1990	We now report that at least some mouse p75 appears to exist as a disulfide-linked heterodimer with a subunit of Mr 22,000 (p22).	Disulfides	65-74	dynein cytoplasmic 1 heavy chain 1	Mus musculus	123-126
2284959-2	1990	The corresponding disulfides (II1-7) were obtained by the oxidation of compounds I1-7 with hydrogen peroxide (1%) in weak alkali medium below 10 degrees C. In preliminary tests, some compounds showed inhibitory activity of ACE in vitro.	Disulfides	18-28	angiotensin I converting enzyme	Homo sapiens	223-226
33816576-4	2021	The tail of angiotensinogen is restrained by a labile disulfide bond, with changes in its redox status affecting angiotensin release, as demonstrably so in the hypertensive complication of pregnancy, pre-eclampsia.	Disulfides	54-63	angiotensinogen	Homo sapiens	12-27
33808471-5	2021	Moreover, redox-regulated protein disulfide isomerase (PDI) chaperones have an essential role in catalyzing formation of disulfide bonds in viral proteins.	Disulfides	34-43	protein disulfide isomerase family A member 2	Homo sapiens	55-58
33797881-3	2021	Herein, we describe the use of two ligation manifolds, namely, diselenide-selenoester ligation and native chemical ligation, to assemble a 31.5 kDa phosphorylated insulin-like growth factor binding protein (IGFBP-2) that comprises 290 amino acid residues, a phosphoserine post-translational modification, and nine disulfide bonds.	Disulfides	314-323	insulin	Homo sapiens	163-170
33801906-5	2021	Furthermore, Env was stabilized on the VLP surface by introducing an interchain disulfide and proline substitution (SOSIP) mutations typically employed to stabilize soluble Env trimers.	Disulfides	80-89	melanoma antigen	Mus musculus	13-16
33800932-2	2021	The spike glycoprotein and envelope protein of SARS-CoV-2, containing disulfide bridges for stabilization, represent an attractive target as they are essential for binding to the ACE2 receptor in host cells present in the nasal mucosa.	Disulfides	70-79	envelope protein	Severe acute respiratory syndrome coronavirus 2	27-35
33800932-6	2021	Spike and envelope protein disulfide bonds were reduced by Acetylcysteine.	Disulfides	27-36	envelope protein	Severe acute respiratory syndrome coronavirus 2	10-18
33767592-7	2021	Physical interactions of AGR2 and FABP1 depended on the PDI motif in AGR2 and the formation of a disulfide bond between these two proteins.	Disulfides	97-106	anterior gradient 2	Mus musculus	25-29
34957576-0	2022	Biogenesis of secretory immunoglobulin M requires intermediate non-native disulfide bonds and engagement of the protein disulfide isomerase ERp44.	Disulfides	120-129	endoplasmic reticulum protein 44	Homo sapiens	140-145
33588457-3	2021	In the Golgi, VWFpp mediates the intermolecular disulfide linkages that generate high-molecular-weight VWF multimers.	Disulfides	48-57	von Willebrand factor	Homo sapiens	14-17
7688724-1	1993	Bovine seminal ribonuclease (BS-RNase), a homolog of bovine pancreatic ribonuclease (RNase A), is isolated as a dimer in which the subunits are cross-linked by two disulfide bonds.	Disulfides	164-173	ribonuclease pancreatic	Bos taurus	85-92
32796317-5	2021	Intra-articular injection of the toll-like receptor (TLR)4-activating, partially reduced disulfide, but not the fully reduced all-thiol, HMGB1 evoked mechanical hypersensitivity in both sexes.	Disulfides	89-98	toll-like receptor 4	Mus musculus	33-58
29261001-5	2018	Upon N-end rule interaction with the Nt-Arg of arginylated HSPA5 (R-HSPA5), SQSTM1 undergoes self-polymerization via disulfide bonds of Cys residues including Cys113, facilitating cargo collection.	Disulfides	117-126	heat shock protein family A (Hsp70) member 5	Homo sapiens	59-64
29261001-5	2018	Upon N-end rule interaction with the Nt-Arg of arginylated HSPA5 (R-HSPA5), SQSTM1 undergoes self-polymerization via disulfide bonds of Cys residues including Cys113, facilitating cargo collection.	Disulfides	117-126	heat shock protein family A (Hsp70) member 5	Homo sapiens	66-73
8535250-0	1995	Thrombin-binding affinities of different disulfide-bonded isomers of the fifth EGF-like domain of thrombomodulin.	Disulfides	41-50	coagulation factor II, thrombin	Homo sapiens	0-8
8535250-7	1995	In order to compare the thrombin-binding affinities of these isomers to the isomer with the EGF-like disulfide bonds, acetamidomethyl protection of the second and fourth cysteines was used to force the disulfide bonds into the EGF-like pattern.	Disulfides	202-211	coagulation factor II, thrombin	Homo sapiens	24-32
8535250-8	1995	Thrombin-binding affinity, measured as inhibition of fibrinogen clotting and as inhibition of protein C activation correlated inversely with the number of crossed disulfide bonds.	Disulfides	163-172	coagulation factor II, thrombin	Homo sapiens	0-8
7925354-3	1994	The del-helix II variant, shortened by 19 amino acids, is a basic, stefin-like mini-cystatin with one disulfide bridge.	Disulfides	102-111	cystatin C	Gallus gallus	84-92
34957576-6	2022	The rearrangement of the C-terminal tails into a native quaternary structure is guaranteed by the engagement of protein disulfide isomerase ERp44, which attacks the non-native C575 bonds.	Disulfides	120-129	endoplasmic reticulum protein 44	Homo sapiens	140-145
34970534-0	2021	Redox Potentials of Disulfide Bonds in LOXL2 Studied by Nonequilibrium Alchemical Simulation.	Disulfides	20-29	lysyl oxidase like 2	Homo sapiens	39-44
34674369-4	2022	Here we review recent evidence for production and function of multiple partially disulfide-bonded forms of plasma fibrinogen and platelet alphaIIbbeta3 integrin.	Disulfides	81-90	fibrinogen beta chain	Homo sapiens	114-124
34970534-3	2021	Disulfide bonds are important components in LOXL2, and they play a stabilizing role for protein structure or a functional role for regulating protein bioactivity.	Disulfides	0-9	lysyl oxidase like 2	Homo sapiens	44-49
34970534-5	2021	In this study, we have calculated the reduction potential of all the disulfide bonds in LOXL2 by non-equilibrium alchemical simulations.	Disulfides	69-78	lysyl oxidase like 2	Homo sapiens	88-93
34970534-10	2021	Our study provides an important insight for the classification of disulfide bonds in LOXL2 and can be utilized for the drug design that targets the cysteine residues in LOXL2.	Disulfides	66-75	lysyl oxidase like 2	Homo sapiens	85-90
34970534-10	2021	Our study provides an important insight for the classification of disulfide bonds in LOXL2 and can be utilized for the drug design that targets the cysteine residues in LOXL2.	Disulfides	66-75	lysyl oxidase like 2	Homo sapiens	169-174
34517052-2	2021	Nuclear magnetic resonance (NMR) and X-ray crystallography revealed the 3D structure of the globular domain of PrPC and the possibility of its dimerization via an interchain disulfide bridge that forms due to domain swap or by non-covalent association of two monomers.	Disulfides	174-183	prion protein	Homo sapiens	111-115
34846860-1	2021	Three disulfide bond-containing peptide amphiphiles (PA1-3) with different lengths of alkyl tails (PA1 for C6, PA2 for C12, and PA3 for C18) were synthesized by ring-opening polymerization of alpha-amino acid N-carboxyanhydride followed by post-polymerization modification.	Disulfides	6-15	PAXIP1 associated glutamate rich protein 1	Homo sapiens	53-56
34797669-2	2021	Here, we report the efficient synthesis of a novel disulfide dimer of human insulin tethered at the N-terminus of its B-chain through placement of a cysteine residue.	Disulfides	51-60	insulin	Homo sapiens	76-83
34418551-7	2021	Significantly, PARylation of UBC13 regulates K63-linked ubiquitination of PDIs, which may further promote their disulfide isomerase activities for correct protein folding and subsequent secretion.	Disulfides	112-121	ubiquitin-conjugating enzyme 13	Arabidopsis thaliana	29-34
34773863-1	2021	We have previously reported that gamma-interferon inducible lysosomal thiolreductase (GILT) functions as a host defense factor against retroviruses by digesting disulfide bonds on viral envelope proteins.	Disulfides	161-170	IFI30 lysosomal thiol reductase	Homo sapiens	33-84
34781108-8	2021	At the same time, this novel disulfide scrambled species structure-function relationship was found to be the molecular basis for reduced TNF-alpha binding and cell biological activities.	Disulfides	29-38	tumor necrosis factor	Homo sapiens	137-146
34781108-9	2021	In addition, incorrect disulfide bridging was found to be reversible under serum-like redox conditions, restoring TNF-alpha binding and cell biological activities to almost normal levels, all of which indicate that the variant is probably irrelevant to clinical efficacy once the drug enters the bloodstream.	Disulfides	23-32	tumor necrosis factor	Homo sapiens	114-123
34773863-1	2021	We have previously reported that gamma-interferon inducible lysosomal thiolreductase (GILT) functions as a host defense factor against retroviruses by digesting disulfide bonds on viral envelope proteins.	Disulfides	161-170	IFI30 lysosomal thiol reductase	Homo sapiens	86-90
34773863-6	2021	We have reported that human GILT suppresses HIV-1 particle production by digestion of disulfide bonds on CD63.	Disulfides	86-95	IFI30 lysosomal thiol reductase	Homo sapiens	28-32
34847145-2	2021	Gamma interferon inducible lysosomal thiol reductase (GILT) is a widespread superfamily which plays key role in processing and presentation of MHC class II restricted antigen by catalyzing disulfide bond reduction.	Disulfides	189-198	IFI30 lysosomal thiol reductase	Homo sapiens	54-58
34852234-3	2021	Our results show that CypA forms an intramolecular disulfide bond between Cys115 and Cys161 upon oxidative stress and the oxidized cysteines in CypA are recycled to a reduced state by peroxiredoxin-2 (PRDX2).	Disulfides	51-60	peroxiredoxin 2	Homo sapiens	184-199
34943005-6	2021	Using ELISA, we demonstrate that the disulfide bridge between the enzymatic cysteines is required to allow improved TLR4-dependent IL-8 secretion.	Disulfides	37-46	C-X-C motif chemokine ligand 8	Homo sapiens	131-135
34814838-0	2021	The thiol-disulfide exchange activity of AtPDI1 is involved in the response to abiotic stresses.	Disulfides	10-19	PDI-like 1-3	Arabidopsis thaliana	41-47
34838051-0	2021	The disulfide bond Cys2724-Cys2774 in the C-terminal cystine knot domain of von Willebrand factor is critical for its dimerization and secretion.	Disulfides	4-13	von Willebrand factor	Homo sapiens	76-97
34838051-7	2021	Therefore, all of the four intrachain disulfide bonds in CTCK monomer contribute to VWF dimerization and secretion.	Disulfides	38-47	von Willebrand factor	Homo sapiens	84-87
34792600-1	2021	EPPIN (epididymal protease inhibitor) is a mammalian conserved sperm-binding protein displaying an N-terminal WFDC (whey-acidic protein four-disulfide core) and a C-terminal Kunitz protease inhibitor domains.	Disulfides	141-150	epididymal peptidase inhibitor	Homo sapiens	0-5
34792600-1	2021	EPPIN (epididymal protease inhibitor) is a mammalian conserved sperm-binding protein displaying an N-terminal WFDC (whey-acidic protein four-disulfide core) and a C-terminal Kunitz protease inhibitor domains.	Disulfides	141-150	epididymal peptidase inhibitor	Homo sapiens	7-36
34814838-1	2021	BACKGROUND: Arabidopsis protein disulfide isomerase 1 (AtPDI1) has been demonstrated to have disulfide isomerase activity and to be involved in the stress response.	Disulfides	93-102	PDI-like 1-3	Arabidopsis thaliana	24-53
34814838-1	2021	BACKGROUND: Arabidopsis protein disulfide isomerase 1 (AtPDI1) has been demonstrated to have disulfide isomerase activity and to be involved in the stress response.	Disulfides	93-102	PDI-like 1-3	Arabidopsis thaliana	55-61
34814838-8	2021	CONCLUSION: Taken together, these results clearly suggest that the anti-stress function of AtPDI1 is directly related to the activity of disulfide isomerase.	Disulfides	137-146	PDI-like 1-3	Arabidopsis thaliana	91-97
34592574-0	2021	Difference in an intermolecular disulfide-bond between two highly homologous serum proteins Leg1a and Leg1b implicates their functional differentiation.	Disulfides	32-41	liver-enriched gene 1, tandem duplicate 1	Danio rerio	92-97
34802094-3	2021	Here, we report on epidermal growth factor receptor (EGFR)-targeted disulfide-crosslinked biodegradable chimaeric polymersomes (EGFR-CPs) to firmly load PEM and boost chemotherapy of MPM.	Disulfides	68-77	epidermal growth factor receptor	Homo sapiens	19-51
34802094-3	2021	Here, we report on epidermal growth factor receptor (EGFR)-targeted disulfide-crosslinked biodegradable chimaeric polymersomes (EGFR-CPs) to firmly load PEM and boost chemotherapy of MPM.	Disulfides	68-77	epidermal growth factor receptor	Homo sapiens	53-57
34802094-3	2021	Here, we report on epidermal growth factor receptor (EGFR)-targeted disulfide-crosslinked biodegradable chimaeric polymersomes (EGFR-CPs) to firmly load PEM and boost chemotherapy of MPM.	Disulfides	68-77	epidermal growth factor receptor	Homo sapiens	128-132
34592574-5	2021	We find that Leg1b forms an intermolecular disulfide bond through C358.	Disulfides	43-52	liver-enriched gene 1, tandem duplicate 2	Danio rerio	13-18
34592574-7	2021	We propose that the intermolecular disulfide bond in Leg1b might establish a rigid structure that makes it functionally different from Leg1a under certain oxidative conditions.	Disulfides	35-44	liver-enriched gene 1, tandem duplicate 2	Danio rerio	53-58
34592574-0	2021	Difference in an intermolecular disulfide-bond between two highly homologous serum proteins Leg1a and Leg1b implicates their functional differentiation.	Disulfides	32-41	liver-enriched gene 1, tandem duplicate 2	Danio rerio	102-107
34592574-7	2021	We propose that the intermolecular disulfide bond in Leg1b might establish a rigid structure that makes it functionally different from Leg1a under certain oxidative conditions.	Disulfides	35-44	liver-enriched gene 1, tandem duplicate 1	Danio rerio	135-140
34411303-7	2021	PIGR/FCAMR/FCMR are members of a larger superfamily including TREM, CD300, and NKp44, which we name the "double-disulfide Ig superfamily" (ddIgSF).	Disulfides	112-121	Fc alpha and mu receptor	Homo sapiens	5-10
34869967-3	2021	Using bovine pancreatic ribonuclease A (RNase A) as an exemplar, we review the regeneration (oxidative folding) of disulfide-bond-containing proteins from their fully reduced state to the biologically active form.	Disulfides	115-124	ribonuclease pancreatic	Bos taurus	40-47
34633020-4	2021	Supramolecular amphiphiles containing a dynamic covalent disulfide bond were prepared via the host-guest inclusion complexes between alkylated beta-cyclodextrin (beta-CD) hosts and adamantane terminated polyethylene glycol derivatives.	Disulfides	57-66	ACD shelterin complex subunit and telomerase recruitment factor	Homo sapiens	162-169
34832935-1	2021	In the present study we tested, using the microscale thermophoresis technique, a small library of thionocarbamates, thiolocarbamates, sulfide and disulfide as potential lead compounds for SARS-CoV-2 Mpro drug design.	Disulfides	146-155	NEWENTRY	Severe acute respiratory syndrome-related coronavirus	199-203
34752599-12	2022	ERp46 more strongly reduced disulfide bonds in the beta3 subunit than other PDIs, and in contrast to PDI generated thiols in beta3 independently of fibrinogen.	Disulfides	28-37	thioredoxin domain containing 5	Mus musculus	0-5
34752599-13	2022	ERp46 cleaved the Cys473-Cys503 disulfide bond in beta3 implicating a target for ERp46.	Disulfides	32-41	thioredoxin domain containing 5	Mus musculus	0-5
34752599-13	2022	ERp46 cleaved the Cys473-Cys503 disulfide bond in beta3 implicating a target for ERp46.	Disulfides	32-41	cholinergic receptor, nicotinic, alpha polypeptide 3	Mus musculus	50-55
34752599-14	2022	Finally, ERp46-deficient platelets have decreased thiols in beta3 implying that ERp46 cleaves disulfide bonds in platelets.	Disulfides	94-103	cholinergic receptor, nicotinic, alpha polypeptide 3	Mus musculus	60-65
34752599-14	2022	Finally, ERp46-deficient platelets have decreased thiols in beta3 implying that ERp46 cleaves disulfide bonds in platelets.	Disulfides	94-103	thioredoxin domain containing 5	Mus musculus	80-85
34752599-15	2022	In conclusion, ERp46 is critical for platelet function and thrombosis and facilitates alphaIIbbeta3 activation by targeting disulfide bonds.	Disulfides	124-133	thioredoxin domain containing 5	Mus musculus	15-20
34411303-7	2021	PIGR/FCAMR/FCMR are members of a larger superfamily including TREM, CD300, and NKp44, which we name the "double-disulfide Ig superfamily" (ddIgSF).	Disulfides	112-121	natural cytotoxicity triggering receptor 2	Homo sapiens	79-84
34077620-6	2021	Specifically, we demonstrate that the ZG16 cysteine thiols can be oxidized to a disulfide by QSOX1, which is a sulfhydryl oxidase present together with ZG16 in the Golgi apparatus and in mucus, as well as by protein disulfide isomerase.	Disulfides	80-89	zymogen granule protein 16	Homo sapiens	38-42
34077620-6	2021	Specifically, we demonstrate that the ZG16 cysteine thiols can be oxidized to a disulfide by QSOX1, which is a sulfhydryl oxidase present together with ZG16 in the Golgi apparatus and in mucus, as well as by protein disulfide isomerase.	Disulfides	80-89	zymogen granule protein 16	Homo sapiens	152-156
34673030-5	2021	By designing a covalent disulfide bridge between protomers to control homodimer strength and stability, we demonstrate the importance of dimer interface perturbations on the allosteric network bridging the two opposite glycan binding sites on GAL-7, resulting in control of induced apoptosis in Jurkat T cells.	Disulfides	24-33	galectin 7	Homo sapiens	243-248
34680573-5	2021	Moreover, we found two forms of NUP58 aggregates: oligomers and polymers stabilized by disulfide bonds.	Disulfides	87-96	nucleoporin 58	Homo sapiens	32-37
34428184-3	2021	We purified poly-IgA from the plasma of IgA nephrology patients and showed the complex being susceptible to reducing condition, suggesting intermolecular disulfide connections between IgA units.	Disulfides	154-163	CD79a molecule	Homo sapiens	17-20
34645844-6	2021	Finally, we evolve disulfide-containing trastuzumab antibody variants with improved binding to a Her2-like peptide and improved soluble expression.	Disulfides	19-28	erb-b2 receptor tyrosine kinase 2	Homo sapiens	97-101
34679944-4	2021	AGR2 is an endoplasmic reticulum-resident protein disulfide isomerase involved in the regulation of protein processing and also exists extracellularly via secretion to exert pro-oncogenic functions.	Disulfides	50-59	anterior gradient 2, protein disulphide isomerase family member	Canis lupus familiaris	0-4
34428184-3	2021	We purified poly-IgA from the plasma of IgA nephrology patients and showed the complex being susceptible to reducing condition, suggesting intermolecular disulfide connections between IgA units.	Disulfides	154-163	CD79a molecule	Homo sapiens	40-43
34428184-3	2021	We purified poly-IgA from the plasma of IgA nephrology patients and showed the complex being susceptible to reducing condition, suggesting intermolecular disulfide connections between IgA units.	Disulfides	154-163	CD79a molecule	Homo sapiens	184-187
34428184-6	2021	It is plausible that, with the absence of J-chain, the cysteine residue of mono-IgA1 might aberrantly form disulfide bond in poly-IgA formation.	Disulfides	107-116	CD79a molecule	Homo sapiens	130-133
34679713-5	2021	It is not clear, however, whether p53 also forms intermolecular disulfides with interacting proteins and whether these redox-dependent interactions contribute to the regulation of p53.	Disulfides	64-74	tumor protein p53	Homo sapiens	34-37
34679713-6	2021	In the present study, by combining (co-)immunoprecipitation, quantitative mass spectrometry and Western blot we found that p53 forms disulfide-dependent interactions with several proteins under oxidizing conditions.	Disulfides	133-142	tumor protein p53	Homo sapiens	123-126
34679713-7	2021	Cysteine 277 is required for most of the disulfide-dependent interactions of p53, including those with 14-3-3theta and 53BP1.	Disulfides	41-50	tumor protein p53	Homo sapiens	77-80
34564928-0	2021	Thiol/disulfide homeostasis and its relationship with insulin resistance in patients with rosacea.	Disulfides	6-15	insulin	Homo sapiens	54-61
34676214-3	2021	One of such genes could be ag1, which encodes secreted protein disulfide isomerase of the Agr family.	Disulfides	63-72	anterior gradient 1 L homeolog	Xenopus laevis	27-30
34174481-6	2021	MAJOR CONCLUSIONS: The dominant mutations in the INS gene typically affect the secondary structure of the insulin protein usually by disrupting the 3 disulfide bonds in mature insulin.	Disulfides	150-159	insulin	Homo sapiens	106-113
34174481-6	2021	MAJOR CONCLUSIONS: The dominant mutations in the INS gene typically affect the secondary structure of the insulin protein usually by disrupting the 3 disulfide bonds in mature insulin.	Disulfides	150-159	insulin	Homo sapiens	176-183
34252801-3	2021	Herein, we developed a pH- and glutathione (GSH)-responsive amphiphilic poly(disulfide acetal) (PCS) containing cinnamaldehyde (CA) and disulfide groups that amplify oxidative stress for anticancer drug delivery and simultaneously overcome drug resistance in cancer cells.	Disulfides	136-145	PCS	Homo sapiens	96-99
34424335-2	2021	One mechanism by which this modulation is achieved is via angiotensinogen"s Cys18 - Cys138 disulfide bond that acts as a redox switch.	Disulfides	91-100	angiotensinogen	Homo sapiens	58-73
34621751-6	2021	Additionally, we show that the effect of cross-linking in the mutant is due to the formation of the disulfide bond within the molecules of EAAT2.	Disulfides	100-109	solute carrier family 1 member 2	Homo sapiens	139-144
34464082-3	2021	Here, we report that conformation-restricted Abeta42 with an intramolecular disulfide bond at positions 17 and 28 (SS-Abeta42) formed stable Abeta oligomers in vitro.	Disulfides	76-85	amyloid beta precursor protein	Homo sapiens	141-146
34271044-3	2021	Here, we focus on smaller fragments of the highly amyloidogenic H-peptide comprising disulfide-bonded N-terminal sections of insulin"s A-chain (13 residues) and B-chain (11 residues).	Disulfides	85-94	insulin	Homo sapiens	125-132
34271044-6	2021	The self-assembling properties of ACC1-11 contrast with aggregation-resistant behavior of B1-11(7A) and its disulfide-linked homodimer, (B1-11)2 aggregating only at neutral pH.	Disulfides	108-117	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	137-144
34197967-4	2021	An antibacterial enzyme, lysozyme, was then conjugated on the surface of the nanocomposite by a cleavable disulfide linker, resulting in a redox-sensitive nanoplatform.	Disulfides	106-115	lysozyme	Homo sapiens	25-33
34324828-1	2021	Acetylcholinesterase (EC 3.1.1.7; AChE), a key acetylcholine-hydrolyzing enzyme in cholinergic neurotransmission, is present in a variety of states in situ, including monomers, C-terminally disulfide-linked homodimers, homotetramers, and up to three tetramers covalently attached to structural subunits.	Disulfides	190-199	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
34409609-5	2021	Molecular docking and experimental characterization results illustrated that the main reason of odor masking was due to the disulfide and thiocarbonyl groups of allicin being partially encapsulated by the cavity of alpha-CD.	Disulfides	124-133	ACD shelterin complex subunit and telomerase recruitment factor	Homo sapiens	215-223
34085839-7	2021	The Txnip-thioredoxin complex was detected in cells with overexpressing wild-type Txnip but not Txnip cysteine 247 to serine (C247S) mutant that disrupts the intermolecular disulfide bridge.	Disulfides	173-182	thioredoxin interacting protein	Mus musculus	4-9
34456199-1	2021	AIMS: Lipoprotein(a) (Lp(a)) is a plasma lipoprotein consisting of a low-density lipoprotein (LDL)-like particle with apolipoprotein (Apo)(a), attached via a disulfide bond to Apo B100.	Disulfides	158-167	apolipoprotein B	Homo sapiens	176-184
34532445-10	2021	The mutation truncated the gamma-peptide chain and destroyed the functional structure of fibrinogen, including the gamma352Cys-gamma365Cys disulfide bond.	Disulfides	139-148	fibrinogen beta chain	Homo sapiens	89-99
34544533-3	2021	Developed based on peptide BP10 with affinity to PROCR as a targeting element, constructing a peptide drug conjugate of BP10 covalently coupling doxorubicin with disulfide bonds.	Disulfides	162-171	BP10	Homo sapiens	27-31
34245311-1	2021	A precondition for efficient proinsulin export from the endoplasmic reticulum (ER) is that proinsulin meets ER quality control folding requirements, including formation of the Cys(B19)-Cys(A20) "interchain" disulfide bond, facilitating formation of the Cys(B7)-Cys(A7) bridge.	Disulfides	207-216	insulin	Homo sapiens	29-39
34245311-1	2021	A precondition for efficient proinsulin export from the endoplasmic reticulum (ER) is that proinsulin meets ER quality control folding requirements, including formation of the Cys(B19)-Cys(A20) "interchain" disulfide bond, facilitating formation of the Cys(B7)-Cys(A7) bridge.	Disulfides	207-216	insulin	Homo sapiens	91-101
34245311-3	2021	Nevertheless, an unpaired Cys(A11) can participate in disulfide mispairings, causing ER retention of proinsulin.	Disulfides	54-63	insulin	Homo sapiens	101-111
34245311-4	2021	Among the many missense mutations causing the syndrome of Mutant INS gene-induced Diabetes of Youth (MIDY), all seem to exhibit perturbed proinsulin disulfide bond formation.	Disulfides	149-158	insulin	Homo sapiens	138-148
34245311-6	2021	Three of these mutants, however, must disrupt the Cys(A6)-Cys(A11) pairing to expose a critical unpaired cysteine thiol perturbation of proinsulin folding and ER export, because when introduced into the proinsulin lose-A6/A11 background, these mutants exhibit native-like disulfide bonding and improved trafficking.	Disulfides	272-281	insulin	Homo sapiens	136-146
34544533-3	2021	Developed based on peptide BP10 with affinity to PROCR as a targeting element, constructing a peptide drug conjugate of BP10 covalently coupling doxorubicin with disulfide bonds.	Disulfides	162-171	BP10	Homo sapiens	120-124
34400904-3	2021	Interferon gamma-inducible protein 30 (IFI30) could catalyze the reduction of disulfide bonds and enhance major histocompatibility complex (MHC) class II-restricted antigen processing.	Disulfides	78-87	IFI30 lysosomal thiol reductase	Homo sapiens	0-37
34400904-3	2021	Interferon gamma-inducible protein 30 (IFI30) could catalyze the reduction of disulfide bonds and enhance major histocompatibility complex (MHC) class II-restricted antigen processing.	Disulfides	78-87	IFI30 lysosomal thiol reductase	Homo sapiens	39-44
34436011-8	2021	Network analysis showed significant difference in immune response and in disulfide bond formation, with EGR1/EGR2 and PDIA2 genes as regulators for immune response and disulfide bond formation, respectively.	Disulfides	73-82	protein disulfide isomerase family A member 2	Homo sapiens	118-123
34436011-8	2021	Network analysis showed significant difference in immune response and in disulfide bond formation, with EGR1/EGR2 and PDIA2 genes as regulators for immune response and disulfide bond formation, respectively.	Disulfides	168-177	protein disulfide isomerase family A member 2	Homo sapiens	118-123
34360542-6	2021	Cys-mutants of HspB6 and HspB8 containing a single-Cys residue in the central part of the beta7 strand in a position homologous to that of Cys137 in HspB1 can be crosslinked to the wild-type HspB7 through a disulfide bond.	Disulfides	207-216	heat shock protein family B (small) member 6	Homo sapiens	15-20
34232639-3	2021	Here, we demonstrate that extracellular TG2 activity is competitively controlled by the mutually exclusive binding of a high-affinity Ca2+ ion or the formation of a strained disulfide bond.	Disulfides	174-183	transglutaminase 2	Homo sapiens	40-43
34232639-5	2021	In contrast, disulfide bond formation competitively occludes the high-affinity Ca2+ site while resulting in complete TG2 inactivation.	Disulfides	13-22	transglutaminase 2	Homo sapiens	117-120
34360542-6	2021	Cys-mutants of HspB6 and HspB8 containing a single-Cys residue in the central part of the beta7 strand in a position homologous to that of Cys137 in HspB1 can be crosslinked to the wild-type HspB7 through a disulfide bond.	Disulfides	207-216	heat shock protein family B (small) member 8	Homo sapiens	25-30
34152716-5	2021	The engineered disulfide bond enhanced the conformational rigidity of the motif, resulting in a nanomolar affinity of MCNr-2c for Keap1.	Disulfides	15-24	kelch like ECH associated protein 1	Homo sapiens	130-135
34336854-8	2021	GPIHBP1 is an atypical member of the LU (Ly6/uPAR) domain protein superfamily, containing an intrinsically disordered and highly acidic N-terminal extension and a disulfide bond-rich three-fingered LU domain.	Disulfides	163-172	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	0-7
34138531-2	2021	hSOD1 is an enzyme that occurs as a stable dimeric protein with several post-translational modifications such as the formation of an intramolecular disulfide bond and the acquisition of metal cofactors that are essential for enzyme activity and further contribute to protein stability.	Disulfides	148-157	superoxide dismutase 1	Homo sapiens	0-5
34276694-9	2021	Hence, glycosylation and disulfide bonding as two posttranslational modifications influence IL-7 bioavailability in the human species: glycosylation protects against proteolysis, whereas internal cysteine bridging under physiological redox state keeps the IL-7 conformations as active proteoforms.	Disulfides	25-34	interleukin 7	Homo sapiens	92-96
34386337-8	2021	Moreover, disulfide bond-containing prodrug/albumin nanoaggregates exhibit long circulation time and superior antitumor efficacy in vivo.	Disulfides	10-19	albumin	Homo sapiens	44-51
34359447-1	2021	UV-B illumination facilitates aggregation of alpha-lactalbumin (alpha-LA) by intramolecular disulfide bond cleavage followed by intermolecular thiol-disulfide exchange reactions.	Disulfides	92-101	lactalbumin alpha	Homo sapiens	45-62
34359447-1	2021	UV-B illumination facilitates aggregation of alpha-lactalbumin (alpha-LA) by intramolecular disulfide bond cleavage followed by intermolecular thiol-disulfide exchange reactions.	Disulfides	149-158	lactalbumin alpha	Homo sapiens	45-62
34190687-6	2021	These results underscore a membrane fusion mechanism that could be triggered by ERp57, allowing a thiol/disulfide exchange reaction to occur and regulate isomerization of a critical CSD, which ultimately leads to the exposition of the fusion peptide.	Disulfides	104-113	protein disulfide isomerase family A member 3	Homo sapiens	80-85
34276694-9	2021	Hence, glycosylation and disulfide bonding as two posttranslational modifications influence IL-7 bioavailability in the human species: glycosylation protects against proteolysis, whereas internal cysteine bridging under physiological redox state keeps the IL-7 conformations as active proteoforms.	Disulfides	25-34	interleukin 7	Homo sapiens	256-260
34081441-0	2021	Targeting a Cryptic Pocket in a Protein-Protein Contact by Disulfide-Induced Rupture of a Homodimeric Interface.	Disulfides	59-68	cripto, FRL-1, cryptic family 1	Homo sapiens	12-19
34151236-4	2021	Mechanistically, KEAP1 inactivation in lung cancer cells induces constitutive activation of NRF2 transcription factor and aberrant expression of NRF2 target cystine transporter SLC7A11; under glucose limitation, high cystine uptake in KEAP1-inactivated lung cancer cells stimulates toxic intracellular disulfide buildup, NADPH depletion, and cell death, which can be rescued by genetic ablation of NRF2-SLC7A11 axis or treatments inhibiting disulfide accumulation.	Disulfides	441-450	kelch like ECH associated protein 1	Homo sapiens	17-22
34151236-4	2021	Mechanistically, KEAP1 inactivation in lung cancer cells induces constitutive activation of NRF2 transcription factor and aberrant expression of NRF2 target cystine transporter SLC7A11; under glucose limitation, high cystine uptake in KEAP1-inactivated lung cancer cells stimulates toxic intracellular disulfide buildup, NADPH depletion, and cell death, which can be rescued by genetic ablation of NRF2-SLC7A11 axis or treatments inhibiting disulfide accumulation.	Disulfides	302-311	kelch like ECH associated protein 1	Homo sapiens	17-22
34208101-7	2021	Moreover, disulfide-HMGB1 stimulation induced nuclear factor (NF)-kappaB activation and a significant release of interleukin-6, but not tumor necrosis factor alpha, into AP culture supernatants.	Disulfides	10-19	interleukin 6	Rattus norvegicus	113-126
34098868-8	2021	Mild oxidation forming a C23-C45 disulfide bond, while leaving C106 with a thiol group, was required for HMGB1 to induce phosphorylated NF-KB p65 subunit and TNF-alpha production.	Disulfides	33-42	tumor necrosis factor	Mus musculus	158-167
34458833-3	2021	We report the development of a novel antibody-drug conjugate (ADC) comprising the anti-LRG1 hinge-stabilised IgG4 monoclonal antibody Magacizumab coupled to the anti-mitotic payload monomethyl auristatin E (MMAE) via a cleavable dipeptide linker using the site-selective disulfide rebridging dibromopyridazinedione (diBrPD) scaffold.	Disulfides	271-280	leucine rich alpha-2-glycoprotein 1	Homo sapiens	87-91
34151236-4	2021	Mechanistically, KEAP1 inactivation in lung cancer cells induces constitutive activation of NRF2 transcription factor and aberrant expression of NRF2 target cystine transporter SLC7A11; under glucose limitation, high cystine uptake in KEAP1-inactivated lung cancer cells stimulates toxic intracellular disulfide buildup, NADPH depletion, and cell death, which can be rescued by genetic ablation of NRF2-SLC7A11 axis or treatments inhibiting disulfide accumulation.	Disulfides	302-311	NFE2 like bZIP transcription factor 2	Homo sapiens	145-149
34151236-4	2021	Mechanistically, KEAP1 inactivation in lung cancer cells induces constitutive activation of NRF2 transcription factor and aberrant expression of NRF2 target cystine transporter SLC7A11; under glucose limitation, high cystine uptake in KEAP1-inactivated lung cancer cells stimulates toxic intracellular disulfide buildup, NADPH depletion, and cell death, which can be rescued by genetic ablation of NRF2-SLC7A11 axis or treatments inhibiting disulfide accumulation.	Disulfides	302-311	kelch like ECH associated protein 1	Homo sapiens	235-240
34151236-4	2021	Mechanistically, KEAP1 inactivation in lung cancer cells induces constitutive activation of NRF2 transcription factor and aberrant expression of NRF2 target cystine transporter SLC7A11; under glucose limitation, high cystine uptake in KEAP1-inactivated lung cancer cells stimulates toxic intracellular disulfide buildup, NADPH depletion, and cell death, which can be rescued by genetic ablation of NRF2-SLC7A11 axis or treatments inhibiting disulfide accumulation.	Disulfides	441-450	NFE2 like bZIP transcription factor 2	Homo sapiens	145-149
34136078-2	2021	We have previously shown that disulfide trapping successfully yielded covalent stabilizers for the PPI of 14-3-3 with the estrogen receptor ERalpha.	Disulfides	30-39	estrogen receptor 1	Homo sapiens	140-147
34067304-8	2021	Exposure to DMDSe resulted in induction of the expression of the ER oxidoreductase Ero1p with concomitant reduction of its regulatory disulfide bonds.	Disulfides	134-143	ER oxidoreductin	Saccharomyces cerevisiae S288C	83-88
34064874-1	2021	ERp57, a member of the protein disulfide isomerase family, is a ubiquitous disulfide catalyst that functions in the oxidative folding of various clients in the mammalian endoplasmic reticulum (ER).	Disulfides	75-84	protein disulfide isomerase family A member 3	Homo sapiens	0-5
35618093-3	2022	Soy protein isolate (SPI) was mainly linked to wheat protein (WP) through non-covalent forces and disulfide bonds as determined by circular dichroism spectroscopy, disulfide bond, protein fraction extraction, interaction, and molecular modeling.	Disulfides	98-107	chromogranin A	Homo sapiens	21-24
35618093-3	2022	Soy protein isolate (SPI) was mainly linked to wheat protein (WP) through non-covalent forces and disulfide bonds as determined by circular dichroism spectroscopy, disulfide bond, protein fraction extraction, interaction, and molecular modeling.	Disulfides	164-173	chromogranin A	Homo sapiens	21-24
35617668-5	2022	These starting conformers generated through uniaxial compression of the native monomer in various spatial directions represent 6 distinct (out of 16 conceivable) two-dimensional (2D) topological classes varying in N-/C-terminal segments of insulin"s A- and B-chains being placed inside or outside of the central loop constituted by the middle sections of both chains and Cys7A-Cys7B/Cys19B-Cys20A disulfide bonds.	Disulfides	397-406	insulin	Homo sapiens	240-247
35427577-6	2022	Although in the CU 10 nm, a noticeable decrease in VDW energy interaction was demonstrated (-357.21Kj/mol) due to present of three disulfide bond which act as a node that limits the excessive opening of insulin and another reason is the decline of surface electron density with increasing Cu-NP size.	Disulfides	131-140	insulin	Homo sapiens	203-210
35617668-3	2022	Here, we conduct a multiscale MD study of the amyloidogenic self-assembly of insulin: a small protein with a complex topology defined by two polypeptide chains interlinked by three disulfide bonds.	Disulfides	181-190	insulin	Homo sapiens	77-84
35561106-3	2022	RESULTS: SPI was bound to SA through disulfide bonds, the zeta potential was reduced.	Disulfides	37-46	chromogranin A	Homo sapiens	9-12
35416493-3	2022	Defective transport of cystine into epithelial cells of renal tubules occurs because of mutations of the transport heterodimer, including protein b0,+AT (encoded by SLC7A9) and rBAT (encoded by SLC3A1) linked through a covalent disulfide bond.	Disulfides	228-237	solute carrier family 7 member 9	Rattus norvegicus	165-171
35587260-3	2022	To determine this, we created a mouse with a cysteine-to-serine mutation at position 129 in PTPN22 (C129S), a residue proposed to alter the redox regulatory properties of PTPN22 by forming a disulfide with the catalytic C227 residue.	Disulfides	191-200	protein tyrosine phosphatase, non-receptor type 22 (lymphoid)	Mus musculus	92-98
35587260-3	2022	To determine this, we created a mouse with a cysteine-to-serine mutation at position 129 in PTPN22 (C129S), a residue proposed to alter the redox regulatory properties of PTPN22 by forming a disulfide with the catalytic C227 residue.	Disulfides	191-200	protein tyrosine phosphatase, non-receptor type 22 (lymphoid)	Mus musculus	171-177
35587260-6	2022	We also observed that the disulfide of native PTPN22 can be directly reduced by the thioredoxin system, while the C129S mutant lacking this disulfide was less amenable to reductive reactivation.	Disulfides	26-35	protein tyrosine phosphatase, non-receptor type 22 (lymphoid)	Mus musculus	46-52
35587260-6	2022	We also observed that the disulfide of native PTPN22 can be directly reduced by the thioredoxin system, while the C129S mutant lacking this disulfide was less amenable to reductive reactivation.	Disulfides	140-149	protein tyrosine phosphatase, non-receptor type 22 (lymphoid)	Mus musculus	46-52
35247515-0	2022	Inhibitors of ERp44, PDIA1, and AGR2 induce disulfide-mediated oligomerization of Death Receptors 4 and 5 and cancer cell death.	Disulfides	44-53	endoplasmic reticulum protein 44	Homo sapiens	14-19
35247515-2	2022	Disulfide bond Disrupting Agents (DDAs) were previously identified as a novel class of anticancer compounds that selectively kill cancers that overexpress the Epidermal Growth Factor Receptor (EGFR) or its family member HER2.	Disulfides	0-9	epidermal growth factor receptor	Homo sapiens	159-191
35247515-2	2022	Disulfide bond Disrupting Agents (DDAs) were previously identified as a novel class of anticancer compounds that selectively kill cancers that overexpress the Epidermal Growth Factor Receptor (EGFR) or its family member HER2.	Disulfides	0-9	epidermal growth factor receptor	Homo sapiens	193-197
35247515-2	2022	Disulfide bond Disrupting Agents (DDAs) were previously identified as a novel class of anticancer compounds that selectively kill cancers that overexpress the Epidermal Growth Factor Receptor (EGFR) or its family member HER2.	Disulfides	0-9	erb-b2 receptor tyrosine kinase 2	Homo sapiens	220-224
35606511-2	2022	Using native mass spectrometry, we analyze the binding of peptides to an empty disulfide-stabilized HLA-A*02:01 molecule and, due to its unique stability, we determine binding affinities of complexes loaded with truncated or charge-reduced peptides.	Disulfides	79-88	major histocompatibility complex, class I, A	Homo sapiens	100-105
35460376-0	2022	Circulating protein disulfide isomerase family member 4 is associated with type 2 diabetes mellitus, insulin sensitivity, and obesity.	Disulfides	20-29	insulin	Homo sapiens	101-108
35532890-1	2022	Thioredoxin, encoded by Txn1, is a critical antioxidant that protects against oxidative damage by regulating the dithiol/disulfide balance of interacting proteins.	Disulfides	121-130	thioredoxin 1	Rattus norvegicus	0-11
35532890-1	2022	Thioredoxin, encoded by Txn1, is a critical antioxidant that protects against oxidative damage by regulating the dithiol/disulfide balance of interacting proteins.	Disulfides	121-130	thioredoxin 1	Rattus norvegicus	24-28
35247648-5	2022	There are four cysteine residues forming two disulfide linkage and 14 basic amino acid residues which result in a very basic property for the binding of IL-8 to heparan sulfate-proteoglycan.	Disulfides	45-54	C-X-C motif chemokine ligand 8	Homo sapiens	153-157
35606080-3	2022	The major structural difference between Lp(a) and LDL is that Lp(a) has a second large protein, apolipoprotein (a) (apo(a)), bound to the apolipoprotein B100 moiety of an LDL sized particle by a single disulfide bond.	Disulfides	202-211	apolipoprotein B	Homo sapiens	138-157
35491445-2	2022	C-terminal interchain-disulfide bonds in the cystine knot (CK) domain are essential for VWF dimerization.	Disulfides	22-31	von Willebrand factor	Homo sapiens	88-91
35176625-6	2022	The oligomerization of oxidized BAP1-UCH is attributed to inter-molecular disulfide bond formation.	Disulfides	74-83	BRCA1 associated protein 1	Homo sapiens	32-40
35306694-2	2022	Prx-2 is oxidized to a disulfide covalently-bound dimer by H2 O2 , and then reduced back by the NADPH-dependent thioredoxin-thioredoxin reductase system.	Disulfides	23-32	peroxiredoxin 2	Homo sapiens	0-5
35314356-6	2022	Such ambiguity in the metal quota and selectivity could be avoided when an intra-subunit disulfide bond in SOD1 was reduced before addition of the metal ions.	Disulfides	89-98	superoxide dismutase 1	Homo sapiens	107-111
35314356-7	2022	Apo-SOD1 in the disulfide-reduced state was monomeric and was found to bind only one zinc ion per monomer.	Disulfides	16-25	superoxide dismutase 1	Homo sapiens	4-8
35314356-8	2022	By binding a zinc ion, the disulfide-reduced SOD1 became conformationally compact and acquired the ability to dimerize.	Disulfides	27-36	superoxide dismutase 1	Homo sapiens	45-49
35051413-3	2022	The dimeric (d)-APOA1C-N mutant coupled the C-terminus of one APOA1 molecule to the N-terminus of a second with a short alanine linker, while the d-APOA1C-C and d-APOA1N-N mutants coupled the C-termini and the N-termini of two APOA1 molecules, respectively, using introduced cysteine residues to form disulfide linkages.	Disulfides	301-310	apolipoprotein A1	Homo sapiens	16-21
35189461-4	2022	This nanovaccine was constructed by linking bovine serum albumin (BSA) with the E7 antigen and then encapsulating the photosensitizer and adjuvant through disulfide bonds to form a highly biocompatible and stable structure.	Disulfides	155-164	albumin	Homo sapiens	51-64
35285615-5	2022	More detailed characterization of their glycosylation patterns is enabled by the recently introduced technique of cross-path reactive chromatography (XP-RC) with online MS detection, which combines chromatographic separation with in-line reduction of disulfide bonds to generate metastable haptoglobin subunits.	Disulfides	251-260	haptoglobin	Homo sapiens	290-301
35236515-4	2022	This behavior was ascribed to the fact that alpha-lactalbumin (alpha-La) and beta-lactoglobulin (beta-Lg) contained in WPI denatured after heating and engaged in disulfide bond formation with each other.	Disulfides	162-171	lactalbumin alpha	Homo sapiens	44-61
35299958-4	2022	In our first study (previous article in this issue), we described a one-disulfide peptide model of a proinsulin folding intermediate and its use to study such variants.	Disulfides	72-81	insulin	Homo sapiens	101-111
35299972-7	2022	Parent and variant peptides contain a single disulfide bridge (cystine B19-A20) to provide a model of proinsulin"s first oxidative folding intermediate.	Disulfides	45-54	insulin	Homo sapiens	102-112
35051413-3	2022	The dimeric (d)-APOA1C-N mutant coupled the C-terminus of one APOA1 molecule to the N-terminus of a second with a short alanine linker, while the d-APOA1C-C and d-APOA1N-N mutants coupled the C-termini and the N-termini of two APOA1 molecules, respectively, using introduced cysteine residues to form disulfide linkages.	Disulfides	301-310	apolipoprotein A1	Homo sapiens	62-67
35051413-3	2022	The dimeric (d)-APOA1C-N mutant coupled the C-terminus of one APOA1 molecule to the N-terminus of a second with a short alanine linker, while the d-APOA1C-C and d-APOA1N-N mutants coupled the C-termini and the N-termini of two APOA1 molecules, respectively, using introduced cysteine residues to form disulfide linkages.	Disulfides	301-310	apolipoprotein A1	Homo sapiens	148-153
35210360-5	2022	COA7 interacts transiently with the copper metallochaperones SCO1 and SCO2 and catalyzes the reduction of disulfide bonds within these proteins, which are crucial for copper relay to COX2.	Disulfides	106-115	synthesis of cytochrome C oxidase 1	Homo sapiens	61-65
35210360-5	2022	COA7 interacts transiently with the copper metallochaperones SCO1 and SCO2 and catalyzes the reduction of disulfide bonds within these proteins, which are crucial for copper relay to COX2.	Disulfides	106-115	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	183-187
2692565-0	1989	Human milk-fat globule membrane derived mucin is a disulfide-linked heteromer.	Disulfides	51-60	LOC100508689	Homo sapiens	40-45
35204825-9	2022	Redox sensitivity of p53 functions is supported by (i) thioredoxin-dependent reduction of p53 disulfides, (ii) inhibition of the thioredoxin-dependent deoxyribonucleotide synthesis by p53 binding to RRM2B and (iii) changed intracellular distribution of p53 through its oxidation by CHCHD4 in the mitochondrial intermembrane space.	Disulfides	94-104	tumor protein p53	Homo sapiens	21-24
35104142-2	2022	Insulin-Fc conjugates were synthesized using trifunctional linkers with one amino reactive group for reaction with a lysine residue of insulin and two thiol reactive groups used for re-bridging of a disulfide bond within the Fc molecule.	Disulfides	199-208	insulin	Homo sapiens	0-7
35015522-4	2022	The method yields disulfide-cyclized peptides, a format on which many important peptide drugs such as oxytocin, vasopressin, and octreotide are based.	Disulfides	18-27	arginine vasopressin	Homo sapiens	112-123
35054674-6	2022	Once implemented, the thiol-disulfide exchange allowed the hydrogel dots to successfully capture and release the protein bovine serum albumin (BSA).	Disulfides	28-37	albumin	Homo sapiens	128-141
35066065-8	2022	Also, the conformation of disulfide bonds in the folded proinsulin was confirmed by Raman spectroscopy.	Disulfides	26-35	insulin	Homo sapiens	56-66
35204825-9	2022	Redox sensitivity of p53 functions is supported by (i) thioredoxin-dependent reduction of p53 disulfides, (ii) inhibition of the thioredoxin-dependent deoxyribonucleotide synthesis by p53 binding to RRM2B and (iii) changed intracellular distribution of p53 through its oxidation by CHCHD4 in the mitochondrial intermembrane space.	Disulfides	94-104	tumor protein p53	Homo sapiens	90-93
35130104-5	2022	Although PDIs promote oxidative protein folding by catalyzing correct disulfide formation in the endoplasmic reticulum (ER), PDIA3/ERp57 adversely triggered the GP misfolding by targeting GP cysteine residues and activated the unfolded protein response (UPR).	Disulfides	70-79	protein disulfide isomerase family A member 3	Homo sapiens	125-130
35130104-5	2022	Although PDIs promote oxidative protein folding by catalyzing correct disulfide formation in the endoplasmic reticulum (ER), PDIA3/ERp57 adversely triggered the GP misfolding by targeting GP cysteine residues and activated the unfolded protein response (UPR).	Disulfides	70-79	protein disulfide isomerase family A member 3	Homo sapiens	131-136
34985274-0	2022	Deprotection of S-Acetamidomethyl and 1,3-Thiazolidine-4-Carbonyl Protecting Groups from Cysteine Side Chains in Peptides by trans-(PtX2(CN)4)2-: One-Pot Regioselective Synthesis of Disulfide Bonds.	Disulfides	182-191	paired like homeodomain 2	Homo sapiens	132-136
34609517-7	2022	Accordingly, the pdi9/10/11 triple mutant exhibited much stronger inhibition than pdi1/2/5/6 quadruple mutant under dithiothreitol treatment, which caused disruption of disulfide bonds in plant proteins.	Disulfides	169-178	PDI-like 1-3	Arabidopsis thaliana	82-92
35069438-6	2021	Although both mutants were retained in the cells, unlike C96Y, R46X did not induce ER stress or form abnormal disulfide-linked proinsulin complexes.	Disulfides	110-119	insulin	Homo sapiens	127-137
2692707-4	1989	It is concluded that native PZP molecules are dimers of disulfide-bridged 180-kDa subunits and that proteinase binding results in covalent 1:1 (tetrameric)PZP-enzyme complexes.	Disulfides	56-65	PZP alpha-2-macroglobulin like	Homo sapiens	28-31
2530243-3	1989	An analogous pattern of specific EGF or TGF-alpha growth inhibitory activity was obtained using a synthetic peptide analog encompassing the third disulfide loop region of TGF-alpha, but containing additional modifications designed for increased membrane affinity [( Ac-D-hArg(Et)2(31),Gly32,33]HuTGF-alpha(31-43)NH2).	Disulfides	146-155	transforming growth factor alpha	Homo sapiens	40-49
2819070-0	1989	Catalysis of thiol/disulfide exchange: single-turnover reduction of protein disulfide-isomerase by glutathione and catalysis of peptide disulfide reduction.	Disulfides	19-28	prolyl 4-hydroxylase subunit beta	Bos taurus	68-95
2675969-7	1989	Gel filtration of nondenatured CP4 on 4% agarose showed a high apparent molecular mass complex comprised of disulfide-bonded trimers of the 43-kDa subunits.	Disulfides	108-117	surfactant protein D	Rattus norvegicus	31-34
2477480-11	1989	ApoD was almost the only 4E11-antigen in LDL, and was in two states: the one free, the other an apoD-apoB mixed disulfide complex.	Disulfides	112-121	apolipoprotein D	Homo sapiens	0-4
2656672-2	1989	The ionization of at least three active site amino acid side chains can influence the spectra over the range of pH studied: the two nascent thiols (interchange thiol and electron transfer thiol) and the histidine residue which acts as the base catalyst in lipoamide dehydrogenase and the acid catalyst in glutathione reductase thiol-disulfide interchange reactions.	Disulfides	333-342	dihydrolipoamide dehydrogenase	Sus scrofa	256-279
2538505-2	1989	Reduction of disulfide bonds and alkylation in denaturing buffer (8 M urea) destroyed the inhibitory activity of sCD4, whereas reduction and alkylation in PBS had no effect.	Disulfides	13-22	stearoyl-CoA desaturase 5	Homo sapiens	113-117
2492959-5	1989	Proteolysis occurs near the amino- or carboxy-terminus of ZP2, producing a 23,000 Mr glycopeptide(s) that remains attached to ZP2 by intramolecular disulfide bonds.	Disulfides	148-157	zona pellucida glycoprotein 2	Mus musculus	58-61
2492959-5	1989	Proteolysis occurs near the amino- or carboxy-terminus of ZP2, producing a 23,000 Mr glycopeptide(s) that remains attached to ZP2 by intramolecular disulfide bonds.	Disulfides	148-157	zona pellucida glycoprotein 2	Mus musculus	126-129
2493820-1	1989	The follicle-stimulating hormone (FSH) receptor purified from calf bovine testis membranes appears to be an oligomeric glycoprotein, consisting of 4 disulfide-linked monomers of molecular weight about 60,000 each.	Disulfides	149-158	follicle stimulating hormone receptor	Bos taurus	4-47
2690069-5	1989	The sequences of the genes for amylin and the calcitonin gene-related peptides (CGRPs) show strong similarity, especially over their 5" coding regions, where both peptides have a conserved intramolecular disulfide bridge, and also over their 3" coding regions, where the presence of a glycine codon strongly suggests that the carboxyl-terminal residue of amylin, like that of CGRP, is amidated.	Disulfides	204-213	islet amyloid polypeptide	Homo sapiens	31-37
2478554-2	1989	Human transforming growth factor alpha (TGF alpha) is a 50-residue mitogenic peptide with a compact structure restrained by three disulfide bonds.	Disulfides	130-139	transforming growth factor alpha	Homo sapiens	40-49
2692565-4	1989	Immunoprecipitation of the mucin and analysis of the precipitated material using Western blots and identification of transferred material with monoclonal antibodies demonstrated that the MW 70,000 protein and the mucin were co-precipitated and linked by reducible disulfide bonds.	Disulfides	264-273	LOC100508689	Homo sapiens	213-218
2478557-2	1989	To study the function of the individual disulfide bonds in subunit assembly and secretion, site-directed mutagenesis was used to convert the 12 cysteine (Cys) residues in the beta subunit of hCG to either alanine or serine.	Disulfides	40-49	chorionic gonadotropin subunit beta 5	Homo sapiens	191-194
2478557-10	1989	Thus, interruption of any disulfide bond in the hCG beta subunit alters the structure sufficiently to block dimer formation and in some cases slow secretion, although the stability for most of the mutant hCG beta subunits is not greatly affected.	Disulfides	26-35	chorionic gonadotropin subunit beta 5	Homo sapiens	48-51
3203685-3	1988	Besides this Cys72, proteinase K has two disulfide bonds, Cys34--Cys123 and Cys178--Cys249, which contribute to the stability of the tertiary structure consisting of an extended central parallel beta-sheet decorated by six alpha-helices, three short antiparallel beta-sheets, 18 beta-turns and involving several internal, structurally important water molecules.	Disulfides	41-50	endogenous retrovirus group K member 7	Homo sapiens	20-30
2584229-5	1989	This amino acid sequence suggests that lamp-1 contains a hinge-like structure and could form disulfide bridges that are observed in the immunoglobulin superfamily.	Disulfides	93-102	lysosomal associated membrane protein 1	Homo sapiens	39-45
3219363-6	1988	Unlike SP-35, which consists of acidic isoforms assembled as disulfide-bonded dimers and multimers, CP4 was secreted as basic isoforms assembled as disulfide-bonded trimers.	Disulfides	148-157	surfactant protein D	Rattus norvegicus	100-103
2530005-1	1989	Lp(a) is a plasma lipoprotein particle consisting of a plasminogenlike protein [apo(a)] disulfide bonded to the apo B moiety of low-density lipoprotein (LDL).	Disulfides	88-97	lipoprotein(a)	Homo sapiens	0-5
2584229-7	1989	The results indicate that disulfide arrangement of lamp-1 is different from that of immunoglobulins.	Disulfides	26-35	lysosomal associated membrane protein 1	Homo sapiens	51-57
2790046-12	1989	The results suggest that the formation of an intramolecular disulfide bond results in only a small change in the secondary and tertiary structure of GLTP.	Disulfides	60-69	glycolipid transfer protein	Homo sapiens	149-153
2553722-7	1989	The 46-kDa and larger forms of unreduced plasma LACI are associated with apolipoprotein A-II (apoA-II) in mixed disulfide linkages.	Disulfides	112-121	tissue factor pathway inhibitor	Homo sapiens	48-52
2842945-8	1988	Furthermore, we have demonstrated the presence of high-molecular-weight complexes formed by disulfide bonding between gp150, gp105, and gp52.	Disulfides	92-101	alanyl aminopeptidase, membrane	Homo sapiens	118-123
2899082-1	1988	Atrial natriuretic peptide (ANP) contains a disulfide which is generally considered to be required for biological activity.	Disulfides	44-53	natriuretic peptides A	Oryctolagus cuniculus	0-26
2899082-1	1988	Atrial natriuretic peptide (ANP) contains a disulfide which is generally considered to be required for biological activity.	Disulfides	44-53	natriuretic peptides A	Oryctolagus cuniculus	28-31
2456242-7	1988	Two synthetic disulfide loop peptides from the hCG beta subunit beta 38-57 and beta 93-100 also block binding of hCG to its receptor.	Disulfides	14-23	chorionic gonadotropin subunit beta 5	Homo sapiens	47-50
2456242-7	1988	Two synthetic disulfide loop peptides from the hCG beta subunit beta 38-57 and beta 93-100 also block binding of hCG to its receptor.	Disulfides	14-23	chorionic gonadotropin subunit beta 5	Homo sapiens	113-116
2850475-4	1988	Synthetic peptides representing the N terminus, the C terminus, or the individual disulfide constrained rings of TGF-alpha did not exhibit receptor-binding or mitogenic activity.	Disulfides	82-91	transforming growth factor alpha	Homo sapiens	113-122
2576417-11	1989	This domain is resistant to proteolysis, even though it lacks any intrachain disulfides and, like the entire extracellular segment protein expressed in a baculovirus system, binds to its cellular ligand, LFA-3.	Disulfides	77-87	CD58 molecule	Homo sapiens	204-209
2813340-4	1989	Active human transforming growth factor-alpha (TGF-alpha), a 50 amino acid long protein with three disulfide bonds, has been synthesized and purified in multiple tens of mg amounts in less than 7 days.	Disulfides	99-108	transforming growth factor alpha	Homo sapiens	47-56
2790046-0	1989	Formation of an intramolecular disulfide bond of glycolipid transfer protein.	Disulfides	31-40	glycolipid transfer protein	Homo sapiens	49-76
2768241-9	1989	We have recently shown that approximately 10% of zeta is disulfide-linked to a chain which we have called eta.	Disulfides	57-66	endothelin receptor type A	Homo sapiens	50-53
3179268-0	1988	Disulfide-linked dimer of oncomodulin: comparison to calmodulin.	Disulfides	0-9	oncomodulin	Homo sapiens	26-37
3179268-4	1988	Evidence presented here shows that oncomodulin can dimerize by intermolecular disulfide formation via the Cys-18 thiol.	Disulfides	78-87	oncomodulin	Homo sapiens	35-46
2813340-5	1989	The purified human TGF-alpha migrated as a single band on SDS-polyacrylamide gels, ran as a single sharp major band at pI = 6.2 on isoelectric focusing gels, displayed an MW = 5546.2 (Th.5546.3) by mass spectrometry, contained three disulfide bonds and had EGF receptor binding, mitogenic and soft agar colony formation activities.	Disulfides	233-242	transforming growth factor alpha	Homo sapiens	19-28
3179268-6	1988	The disulfide-linked dimer of oncomodulin appears to be more similar to calmodulin than oncomodulin since the dimer displayed "calmodulin-like" affinity for the amphiphilic peptide melittin.	Disulfides	4-13	oncomodulin	Homo sapiens	30-41
2813340-6	1989	The locations of disulfide bonds were found to be analogous to those found in epidermal growth factor (EGF) and in human TGF-alpha expressed in bacteria.	Disulfides	17-26	transforming growth factor alpha	Homo sapiens	121-130
3220830-0	1988	Disulfide bond interchange in Escherichia coli-derived recombinant human interferon-beta 1 under denaturing conditions.	Disulfides	0-9	interferon beta 1	Homo sapiens	73-90
2506441-6	1989	Amino acid composition analysis of proteolytic fragments from TGF-alpha and the Lys-42 mutant indicated that these proteins contained the same disulfide bonds.	Disulfides	143-152	transforming growth factor alpha	Homo sapiens	62-71
2701945-2	1989	On thymocytes, CD1a forms noncovalent complexes with CD1b and CD1c, and a disulfide-linked heterodimer with CD8.	Disulfides	74-83	CD1a molecule	Homo sapiens	15-19
2697986-8	1989	The mature insulin receptor is inserted into the plasma membrane as an alpha 2-beta 2 disulfide-linked heterodimer.	Disulfides	86-95	insulin receptor	Homo sapiens	11-27
3220830-8	1988	These results indicate that disulfide bond interchange occurs in E. coli-derived recombinant human interferon-beta 1 under denaturing conditions in spite of the absence of a reducing agent.	Disulfides	28-37	interferon beta 1	Homo sapiens	99-116
2972066-1	1988	Lp(a) represents a genetically transmitted class of plasma LDL having apo B-100 linked by a disulfide bridge to a glycoprotein, apo(a).	Disulfides	92-101	lipoprotein(a)	Homo sapiens	0-5
2780565-2	1989	The protein, which we have designated complement cytolysis inhibitor (CLI), has a molecular mass of 70 kDa and consists of two nonidentical, disulfide-linked subunits of 35 kDa.	Disulfides	141-150	clusterin	Homo sapiens	38-68
2967296-1	1988	The T cell antigen receptor (TCR) consists of a disulfide-linked TCR-alpha/beta heterodimer that is both structurally and functionally associated with a set of four non-covalently linked membrane proteins termed CD3-gamma, -delta, -epsilon, and -zeta.	Disulfides	48-57	T cell receptor alpha constant	Homo sapiens	65-74
2745426-4	1989	Secretogranin II lacks the disulfide-bonded loop structure near the NH2 terminus which is conserved in chromogranin A and chromogranin B (secretogranin I), two other widespread constituents of neuroendocrine secretory granules, but like the latter two proteins contains (i) an -E-N/S-L-X-A/D-X-D/E-X-E-L- motif and (ii) multiple potential dibasic cleavage sites for the generation of smaller, perhaps biologically active peptides.	Disulfides	27-36	secretogranin II	Homo sapiens	0-16
2775757-1	1989	The amino acid sequence and disulfide bridges of bovine plasma derived angiogenin were determined by sequencer analysis of the intact protein and fragments derived by enzymatic and chemical digestion.	Disulfides	28-37	angiogenin	Homo sapiens	71-81
2780565-6	1989	As in SGP-2, proteolytic processing between residues 206 and 207 yields the two disulfide-linked subunits of plasma CLI.	Disulfides	80-89	clusterin	Homo sapiens	6-11
2501389-1	1989	The CD69 (Leu-23) activation Ag is a phosphorylated 28 to 32-kDa disulfide-linked homodimer that is rapidly induced after lymphocyte activation.	Disulfides	65-74	CD69 molecule	Homo sapiens	4-8
2775758-2	1989	Reduction of disulfide linkages released mucin subunits together with an associated protein(s) of approximately 140 kDa.	Disulfides	13-22	LOC100508689	Homo sapiens	41-46
3372526-1	1988	Human transferrin receptor is a disulfide-linked homodimer of 90-kDa glycoprotein subunits, capable of binding two transferrins.	Disulfides	32-41	transferrin receptor	Homo sapiens	6-26
2677670-6	1989	A significant fraction of these int-1 species formed disulfide-linked multimers.	Disulfides	53-62	wingless-type MMTV integration site family, member 1	Mus musculus	32-37
3382633-0	1988	Synthetic peptide models for the redox-active disulfide loop of glutaredoxin.	Disulfides	46-55	glutaredoxin	Homo sapiens	64-76
2963821-6	1988	Association of non-disulfide-linked TCR-alpha and -beta chains with CD3 was detected before that of disulfide-bridged TCR-alpha/beta heterodimers.	Disulfides	19-28	T cell receptor alpha constant	Homo sapiens	36-45
2963821-6	1988	Association of non-disulfide-linked TCR-alpha and -beta chains with CD3 was detected before that of disulfide-bridged TCR-alpha/beta heterodimers.	Disulfides	100-109	T cell receptor alpha constant	Homo sapiens	118-127
2963821-9	1988	Once the single TCR-alpha and -beta chains were associated with CD3, disulfide linkages were formed, and a 70-kDa form of the TCR was detected within the ER.	Disulfides	69-78	T cell receptor alpha constant	Homo sapiens	16-25
2547624-6	1989	Biochemical analysis revealed that all Ti gamma A+, BB3+ T cell clones expressed the disulfide-linked form of the receptor.	Disulfides	85-94	bombesin receptor subtype 3	Homo sapiens	52-55
2722851-8	1989	We conclude that disulfide formation by hemin provides a likely mechanism by which hemin prevents the activation and inhibits the activity of HRI.	Disulfides	17-26	eukaryotic translation initiation factor 2 alpha kinase 1	Homo sapiens	142-145
2499539-1	1989	Cysteines 265 and 287 of Pseudomonas aeruginosa exotoxin A (ETA) were substituted by serine, thereby eliminating a disulfide bridge within domain II, the putative membrane insertion-translocation domain.	Disulfides	115-124	endothelin receptor type A	Mus musculus	60-63
2785794-2	1989	EGF was bound to the liposomal surface by the disulfide bridge linkage using a heterobifunctional cross-linking reagent, N-hydroxysuccinimidyl-3-(2-pyridyl-dithio) propionate.	Disulfides	46-55	epidermal growth factor like 1	Rattus norvegicus	0-3
2925643-3	1989	The characteristic protein component of lipoprotein(a) is apolipoprotein(a) (apo(a)) which is disulfide-linked to apolipoprotein B-100.	Disulfides	94-103	apolipoprotein(a)	Macaca mulatta	58-75
2925643-3	1989	The characteristic protein component of lipoprotein(a) is apolipoprotein(a) (apo(a)) which is disulfide-linked to apolipoprotein B-100.	Disulfides	94-103	apolipoprotein(a)	Macaca mulatta	77-83
3067188-2	1988	Western blot analysis with anti human PDGF antibody of the PDGF-like factor synthesized and secreted by human blood monocytes (MDGF) on SDS gels indicates that it lacks interchain disulfide bridges and behaves as a 16-kd monomer under nonreducing conditions.	Disulfides	180-189	pro-platelet basic protein	Homo sapiens	127-131
3067188-4	1988	These data suggest that MDGF represents a unique form of PDGF which lacks interchain disulfide bridges and may represent a new member of the PDGF family of growth factors.	Disulfides	85-94	pro-platelet basic protein	Homo sapiens	24-28
3680245-1	1987	When the low density lipoprotein (LDL) receptor was solubilized from bovine adrenal cortex membranes and subjected to electrophoresis in the absence of reducing agents, a disulfide-bonded dimeric species was demonstrated.	Disulfides	171-180	low density lipoprotein receptor	Bos taurus	9-47
2471738-11	1989	The results obtained were consistent with a folding pattern for p75 that incorporates a disulfide bond between cysteines 161 and 194.	Disulfides	88-97	PC4 and SFRS1 interacting protein 1	Homo sapiens	64-67
3498943-2	1987	It is a disulfide-bonded heterodimer in which either the alpha or alpha" polypeptide chain encoded by Ly-2 is covalently linked to the beta polypeptide chain encoded by Ly-3.	Disulfides	8-17	CD8 antigen, alpha chain	Mus musculus	102-106
2568118-11	1989	Six posttranslational modifications of both PrP isoforms have been identified: (1) cleavage of an N-terminal signal peptide, (2) an intramolecular disulfide bond, (3) an N-linked oligosaccharide attached to Asn 181, (4) a second oligosaccharide attached to Asn 197, (5) cleavage of a C-terminal hydrophobic peptide, and (6) a phosphatidylinositol glycolipid attached to the C-terminus.	Disulfides	147-156	prion protein	Mus musculus	44-47
2588336-0	1989	[Kinetics of inhibition of aldehyde dehydrogenase isoenzymes of rat liver by fluorine-containing disulfides].	Disulfides	97-107	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	27-49
2494662-0	1989	Molecular heterogeneity of gamma delta T-cell antigen receptors expressed by CD4- CD8- T-cell clones from normal donors: both disulfide- and non-disulfide-linked receptors are delta TCS1+.	Disulfides	126-135	treacle ribosome biogenesis factor 1	Homo sapiens	182-186
2494662-8	1989	The anti-delta TCS1 monoclonal antibody stained and immunoprecipitated both disulfide- and non-disulfide-linked gamma delta TCRs from different T-cell clones from normal donors.	Disulfides	76-85	treacle ribosome biogenesis factor 1	Homo sapiens	15-19
2494662-8	1989	The anti-delta TCS1 monoclonal antibody stained and immunoprecipitated both disulfide- and non-disulfide-linked gamma delta TCRs from different T-cell clones from normal donors.	Disulfides	95-104	treacle ribosome biogenesis factor 1	Homo sapiens	15-19
3597378-2	1987	Treatment of the soluble insulin receptor from human placenta with 1.25 mM dithiothreitol and 75 mM Tris at pH 8.5 results in complete reduction of interhalf disulfide bonds (class 1 disulfides) and dissociation of the tetrameric receptor into the dimeric alpha beta form.	Disulfides	158-167	insulin receptor	Homo sapiens	25-41
3597378-2	1987	Treatment of the soluble insulin receptor from human placenta with 1.25 mM dithiothreitol and 75 mM Tris at pH 8.5 results in complete reduction of interhalf disulfide bonds (class 1 disulfides) and dissociation of the tetrameric receptor into the dimeric alpha beta form.	Disulfides	183-193	insulin receptor	Homo sapiens	25-41
2722851-2	1989	The results obtained from the analysis of sodium dodecyl sulfate-polyacrylamide gel electrophoresis of unphosphorylated and phosphorylated HRI under reducing and nonreducing conditions indicate that hemin promotes disulfide formation in HRI.	Disulfides	214-223	eukaryotic translation initiation factor 2 alpha kinase 1	Homo sapiens	139-142
3492556-4	1987	Anti-L24 antibody immunoprecipitates a molecule composed of two disulfide-linked monomers of 140 kd each.	Disulfides	64-73	immunoglobulin kappa variable 1D-8	Homo sapiens	5-8
2722851-2	1989	The results obtained from the analysis of sodium dodecyl sulfate-polyacrylamide gel electrophoresis of unphosphorylated and phosphorylated HRI under reducing and nonreducing conditions indicate that hemin promotes disulfide formation in HRI.	Disulfides	214-223	eukaryotic translation initiation factor 2 alpha kinase 1	Homo sapiens	237-240
2484680-7	1989	Tenascin is composed of disulfide-bonded subunits of approximate Mr between 200-280 kD.	Disulfides	24-33	tenascin C	Mus musculus	0-8
2722851-3	1989	Hemin-promoted disulfide formation in HRI occurs under quasi-physiological conditions, i.e. 30 degrees C, 10 min at hemin concentrations of 5-10 microM.	Disulfides	15-24	eukaryotic translation initiation factor 2 alpha kinase 1	Homo sapiens	38-41
3305626-5	1987	MG1 (greater than 10(3) kDa) contains 15% protein (several disulfide linked subunits), 78% carbohydrate (290 units of 4-16 residues), 7% sulfate, and small amounts of covalently linked fatty acids.	Disulfides	59-68	mucin 5B, oligomeric mucus/gel-forming	Homo sapiens	0-3
2722851-6	1989	In addition, hemin treatment of phosphorylated HRI results in the appearance of a disulfide-linked form of higher molecular mass when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under nonreducing conditions.	Disulfides	82-91	eukaryotic translation initiation factor 2 alpha kinase 1	Homo sapiens	47-50
2714400-9	1989	These results indicate that the disulfide-linked, multi-meric 80-kDa component is bovine IgM, which binds strongly to a cell-surface component of the microvilli, and is indirectly associated with the microfilament cores.	Disulfides	32-41	IgM	Bos taurus	89-92
2432067-7	1987	Native rat alpha 2M is a tetramer, but it separates in the gels as a disulfide-linked dimer with an Mr of approximately 360 kDa.	Disulfides	69-78	alpha-2-macroglobulin	Rattus norvegicus	11-19
2466936-7	1989	Evidence is presented that demonstrates that Blast-1 and LFA-3 possess a disulfide-bonded second domain.	Disulfides	73-82	CD58 molecule	Homo sapiens	57-62
2725510-5	1989	Exon 2 coded for a 42-amino-acid segment that was 100% identical with the corresponding segment of the mature PF4 sequence containing the amino-terminal and disulfide-bonded core regions.	Disulfides	157-166	platelet factor 4	Homo sapiens	110-113
2784209-1	1989	BB3 and delta-TCS1 monoclonal antibodies identify two distinct nonoverlapping populations of T-cell receptor (TcR) gamma/delta (TcR-1)-positive cells, which express a disulfide-linked and a nondisulfide-linked form of TcR, respectively.	Disulfides	167-176	bombesin receptor subtype 3	Homo sapiens	0-3
2719939-0	1989	A covalent angiogenin/ribonuclease hybrid with a fourth disulfide bond generated by regional mutagenesis.	Disulfides	56-65	angiogenin	Homo sapiens	11-21
2946796-2	1986	Rapid induction of a phosphorylated 28 kD/32 kD disulfide-linked early activation antigen (EA 1) by 12-o-tetradecanoyl phorbol-13-acetate, mitogens, and antigens.	Disulfides	48-57	CD69 molecule	Homo sapiens	91-95
2946796-3	1986	With human T cells activated by 12-o-tetradecanoyl phorbol-13-acetate (TPA) as immunogen, an IgG2a mAb, early activation antigen 1 (EA 1), was generated against a 60-kD protein with disulfide-linked 28-kD and 32-kD subunits.	Disulfides	182-191	CD69 molecule	Homo sapiens	104-136
3096745-11	1986	Lyt-2 is normally expressed on thymocytes and peripheral T cells as a heterodimer disulfide bonded to the Lyt-3 glycopeptide, yet Lyt-3 could not be detected on the cell membranes of our clones; Lyt-2 existed as stable homodimers without Lyt-3.	Disulfides	82-91	CD8 antigen, alpha chain	Mus musculus	0-5
2719939-3	1989	A striking structural difference between angiogenin and RNase is the virtual absence of sequence similarity within the region of RNase that contains the Cys-65--Cys-72 disulfide bond.	Disulfides	168-177	angiogenin	Homo sapiens	41-51
2719939-4	1989	Indeed, angiogenin lacks this disulfide linkage.	Disulfides	30-39	angiogenin	Homo sapiens	8-18
2719939-13	1989	The data indicate that introduction of a region of RNase A containing the Cys-65--Cys-72 disulfide bond into angiogenin dramatically increases RNase-like enzymatic activity while reducing its angiogenicity.	Disulfides	89-98	ribonuclease A family member 1, pancreatic	Homo sapiens	51-58
2719939-13	1989	The data indicate that introduction of a region of RNase A containing the Cys-65--Cys-72 disulfide bond into angiogenin dramatically increases RNase-like enzymatic activity while reducing its angiogenicity.	Disulfides	89-98	angiogenin	Homo sapiens	109-119
2704039-4	1989	Uteroglobin is a dimer of two independent polypeptide chains of 70 residues linked by two disulfide bridges and related by a pseudo binary axis.	Disulfides	90-99	uteroglobin	Oryctolagus cuniculus	0-11
2709339-2	1989	The intracellular thiol-disulfide ratio is also identical to that of mammalian tissues, due to the activity of glutathione reductase.	Disulfides	24-33	glutathione-disulfide reductase	Homo sapiens	111-132
3071185-4	1988	The protein isolated was identified as Met-(-1) angiogenin by amino acid analysis and tryptic peptide mapping; the latter demonstrated that all three disulfide bonds had formed correctly.	Disulfides	150-159	angiogenin	Homo sapiens	48-58
3531211-5	1986	The disulfide arrangement of the active TGF alpha was determined after digestion with thermolysin, and found to be analogous to the disulfide arrangement previously determined for EGF (Savage, C. R., Hash, J. H., and Cohen, S. (1973) J. Biol.	Disulfides	4-13	transforming growth factor alpha	Homo sapiens	40-49
3531211-5	1986	The disulfide arrangement of the active TGF alpha was determined after digestion with thermolysin, and found to be analogous to the disulfide arrangement previously determined for EGF (Savage, C. R., Hash, J. H., and Cohen, S. (1973) J. Biol.	Disulfides	132-141	transforming growth factor alpha	Homo sapiens	40-49
3489522-3	1986	Analysis of the purified polypeptide by gel electrophoresis indicates that TGF beta is composed of two polypeptide chains of Mr 12,500 cross-linked by disulfide bonds.	Disulfides	151-160	transforming growth factor, beta 1	Mus musculus	75-83
2499573-3	1989	Spirulina glutathione reductase was covalently bound to Thiopropyl-Sepharose 6B in the presence of 8M urea through thiol-disulfide exchange.	Disulfides	121-130	glutathione-disulfide reductase	Homo sapiens	10-31
3196347-4	1988	The high MW BNP consisted of 106 amino acid residues including one disulfide linkage and carried a BNP structure at its C-terminus.	Disulfides	67-76	natriuretic peptide B	Homo sapiens	12-15
2421778-7	1986	These data suggest that the stabilization of the subunit structure of the insulin receptor at physiological temperatures may take place via a disulfide interchange reaction catalyzed by glutathione-insulin transhydrogenase.	Disulfides	142-151	insulin receptor	Rattus norvegicus	74-90
2468359-9	1988	We suggest that the formation of the disulfide bridge between apo B and apo(a) in Lp(a) alters the system of disulfide bonds present in apo B and thereby modifies apo B structure.	Disulfides	37-46	lipoprotein(a)	Homo sapiens	82-87
2784209-6	1989	Thus, the disulfide-linked form of TcR-1 (BB3+ clones) was associated with the expression of J segments upstream to the C gamma 1 gene segment, whereas the nondisulfide-linked form (delta-TCS1+ clones) was associated with the expression of J segments upstream to C gamma 2. delta-TCS1+ clones, in most instances, exhibited a growth pattern different from that of BB3+ or conventional TcR alpha/beta+ clones as they adhered promptly to surfaces, spread, and emitted long filopodia ending with adhesion plaques.	Disulfides	10-19	bombesin receptor subtype 3	Homo sapiens	42-45
2468359-9	1988	We suggest that the formation of the disulfide bridge between apo B and apo(a) in Lp(a) alters the system of disulfide bonds present in apo B and thereby modifies apo B structure.	Disulfides	109-118	lipoprotein(a)	Homo sapiens	82-87
2469470-6	1989	The interchain disulfide bond present in the human alpha 2M carboxyl-terminal 20-kDa fragment was conserved in bovine alpha 2M and rat alpha 1I3, but not in rat alpha 1M.	Disulfides	15-24	alpha-1-inhibitor III	Rattus norvegicus	135-144
2845582-2	1988	The CD3-zeta chains are either disulfide-linked homodimers (CD3-zeta 2) or disulfide-linked heterodimers with eta (CD3-zeta eta).	Disulfides	31-40	endothelin receptor type A	Homo sapiens	9-12
2845582-2	1988	The CD3-zeta chains are either disulfide-linked homodimers (CD3-zeta 2) or disulfide-linked heterodimers with eta (CD3-zeta eta).	Disulfides	75-84	endothelin receptor type A	Homo sapiens	9-12
2937786-3	1986	Measurements of the rate of disulfide bond reduction by thioredoxin in intact protein S showed that the disulfide bonds are largely inaccessible to thioredoxin in the presence of Ca2+ ions, whereas in the presence of EDTA apparently all of the disulfide bonds are rapidly reduced.	Disulfides	104-113	thioredoxin	Bos taurus	56-67
2463905-7	1989	The transition of p beta 1 to uncombined p beta 2 involves the formation of at least one intramolecular disulfide bond coincident with the conformational shift of the p beta molecule.	Disulfides	104-113	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	43-49
2463905-9	1989	This peptide presumably contains one of the two crucial cysteine residues that participate in forming the disulfide bond that distinguishes p beta 1 from the p beta 2 forms.	Disulfides	106-115	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	160-166
3947091-4	1986	Thus, in 8-mercapto-FAD-glutathione reductase, the oxidation-reduction state of the active center disulfide can be monitored.	Disulfides	98-107	glutathione-disulfide reductase	Homo sapiens	24-45
2521314-9	1989	The BB3-reactive TCR molecules were represented by C gamma 1-encoded disulfide-linked heterodimers, whereas delta-TCS-1 reacted with C gamma 2-encoded nondisulfide-linked molecules.	Disulfides	69-78	bombesin receptor subtype 3	Homo sapiens	4-7
3492399-3	1986	Reduction-carboxymethylation and reduction-mercuration resulted in complete loss of Meg-CSF and Epo activities, suggesting that one of the essential chemical groups of Meg-CSF and Epo is a disulfide bond.	Disulfides	189-198	protein tyrosine phosphatase non-receptor type 4	Homo sapiens	84-87
3051005-4	1988	Whole amylin was synthesized by using solid-phase techniques, with formation of the disulfide linkage by oxidation in dilute aqueous solution and recovery of the peptide by lyophilization.	Disulfides	84-93	islet amyloid polypeptide	Homo sapiens	6-12
3936216-2	1985	FVIII/vWF was measured in six cases of atypical von Willebrand"s disease (type II), in gel-filtered fractions of normal cryoprecipitate and in the course of depolymerization of purified normal FVIII/vWF by disulfide reduction.	Disulfides	206-215	coagulation factor VIII	Homo sapiens	0-5
2537735-2	1989	CD28, a 44-kDa disulfide-linked homodimer, is present on the surface of the majority of TcR alpha/beta-bearing T lymphocytes.	Disulfides	15-24	CD28 molecule	Homo sapiens	0-4
3936216-3	1985	Small molecular forms of FVIII/vWF from normal and variant type II plasma, and those derived by disulfide reduction of high-molecular weight FVIII/vWF, showed remarkably decreased reactivity in ristocetin-, botrocetin- and latex-assay.	Disulfides	96-105	coagulation factor VIII	Homo sapiens	141-146
3160727-6	1985	These plasmin-cleaved "multimers" were composed of disulfide-linked fragments with no intact vWF subunits.	Disulfides	51-60	plasminogen	Homo sapiens	6-13
3160727-7	1985	Thus, many plasmin cleavages occur within disulfide loops.	Disulfides	42-51	plasminogen	Homo sapiens	11-18
3160727-10	1985	Analysis of plasmin-digested vWF allowed deduction of a model for the native vWF structure, including the approximate location of the interprotomer disulfide bond(s).	Disulfides	148-157	plasminogen	Homo sapiens	12-19
4030750-2	1985	A peptide bridged with a disulfide bond was reduced and cleaved with tributylphosphine, and then coupled with a thiol specific reagent, ammonium 7-fluorobenzo-2-oxa-1,3-diazole-4-sulfonate, under alkaline conditions.	Disulfides	25-34	OXA1L mitochondrial inner membrane protein	Homo sapiens	161-166
3261961-8	1988	This indicates that PPH consists of two subunits with Mr 100,000 each, which are held together by one or more disulfide bonds.	Disulfides	110-119	meprin A subunit alpha	Homo sapiens	20-23
3167026-5	1988	We have identified the active site peptide containing the redox-active disulfide, a peptide corresponding to the histidine-467 region of human erythrocyte glutathione reductase, as well as the flavin binding domain that is highly conserved in all disulfide-containing flavoprotein reductase enzymes.	Disulfides	71-80	glutathione-disulfide reductase	Homo sapiens	155-176
2837508-11	1988	After reduction the molecule was shown to be composed of two 55-kDa molecules with an isoelectric point of 5 to 6 indicating that the S152 Ag is a disulfide-linked homodimer.	Disulfides	147-156	CD27 antigen	Mus musculus	134-138
2537735-2	1989	CD28, a 44-kDa disulfide-linked homodimer, is present on the surface of the majority of TcR alpha/beta-bearing T lymphocytes.	Disulfides	15-24	T cell receptor alpha constant	Homo sapiens	88-97
3182746-1	1988	The effects of a disulfide reducing agent and sulfhydryl blocking agents on the biotinidase activity in human serum and on the purified biotinidase have been extensively studied by using a newly developed HPLC assay method.	Disulfides	17-26	biotinidase	Homo sapiens	80-91
3989305-3	1985	Plasmin degraded pro-HNP in vitro to HNP, which was also isolated from the urine of patients and which contained disulfide-linked polypeptides of beta 60, alpha 38, and alpha 26, and noncovalently bound polypeptide of beta 17.	Disulfides	113-122	plasminogen	Homo sapiens	0-7
2561638-0	1989	Selective inhibition of thrombin- and plasmin-induced platelet aggregation by a synthetic peptide disulfide.	Disulfides	98-107	plasminogen	Homo sapiens	38-45
2561638-2	1989	A synthetic peptide disulfide, Gln-Val-Val-Cys(NpyS)-Gly-NH2 (P1) inhibited thrombin and plasmin-induced platelet aggregation and cleavage of aggregin.	Disulfides	20-29	plasminogen	Homo sapiens	89-96
3277886-6	1988	MerA, mercuric ion reductase, is an FAD-containing and redox-active disulfide-containing enzyme with homology to glutathione reductase.	Disulfides	68-77	glutathione-disulfide reductase	Homo sapiens	113-134
2982409-2	1985	These reactives proved to dissociate the dimeric glycoprotein 5"-nucleotidase of Mr 160 000 into two subunits of apparent Mr 80 000, indicating that the subunits are held together by interchain disulfide bridges.	Disulfides	194-203	5'-nucleotidase ecto	Homo sapiens	62-77
3264302-7	1988	Diagonal gel electrophoresis showed that the major band of EA 1 was composed of a series of disulfide-linked homodimers with subunits of the same 24-kDa core protein that were differentially glycosylated.	Disulfides	92-101	CD69 molecule	Homo sapiens	59-63
2982566-0	1985	Enhancement of rat growth hormone binding by membrane disulfide reduction.	Disulfides	54-63	gonadotropin releasing hormone receptor	Rattus norvegicus	19-33
3144412-1	1988	Normally iodinated thyroglobulin (Tg) contains low molecular weight hormone-rich peptides associated to the bulk of the molecule by disulfide bridges.	Disulfides	132-141	thyroglobulin	Homo sapiens	19-32
3144412-1	1988	Normally iodinated thyroglobulin (Tg) contains low molecular weight hormone-rich peptides associated to the bulk of the molecule by disulfide bridges.	Disulfides	132-141	thyroglobulin	Homo sapiens	34-36
3243765-3	1988	All antibodies recognized the conformational structure of rat platelet phospholipase A2 supported by intramolecular disulfide bonds, since the reactivity between the antibodies and the enzyme was lost in the presence of 2-mercaptoethanol.	Disulfides	116-125	phospholipase A2 group IIA	Rattus norvegicus	62-87
3674885-6	1987	Reduction of disulfide bridges in MG1 increased the number of available hydrophobic binding sites.	Disulfides	13-22	mucin 5B, oligomeric mucus/gel-forming	Homo sapiens	34-37
3968434-3	1985	Monoclonals AB3 and CPG1, which recognize epitopes within 40,000 daltons of the carboxy terminus of intact fibronectin, and the cathepsin D-derived, disulfide-linked fragments that contain these epitopes each inhibited the opsonic function of 180K-opFnf.	Disulfides	149-158	cathepsin D	Homo sapiens	128-139
3968434-5	1985	The pretreatment of Er with 5 micrograms and 40 micrograms of the disulfide-linked, cathepsin D derivatives isolated from high and low affinity heparin fractions, respectively, inhibited the proportion of ingesting monocytes by 60%, but these types of fragments had little effect when concurrently incubated with the opsonic fragment and Er.	Disulfides	66-75	cathepsin D	Homo sapiens	84-95
3968434-9	1985	Thus, the inhibitory effects produced by monoclonals AB3 and CPG1 and by cathepsin D-derived, disulfide-linked fragments containing their corresponding epitopes demonstrated that the opsonic domain within 180K-opFnf is immunologically similar to regions within the carboxy terminus of intact plasma fibronectin.	Disulfides	94-103	cathepsin D	Homo sapiens	73-84
3139459-3	1988	Cleavage of disulfide bonds reveals that two 55 kDa polypeptides are linked together in native dimeric AChE.	Disulfides	12-21	Acetylcholine esterase	Drosophila melanogaster	103-107
2986534-3	1985	The predominant subunit configuration in the native insulin receptor is a disulfide-linked heterotetrameric structure containing two alpha and two beta subunits.	Disulfides	74-83	insulin receptor	Homo sapiens	52-68
3874157-6	1985	Their elevated concentration within this space may facilitate a low affinity binding interaction between Ly-2 and Ly-3 which is later stabilized by interchain disulfide bond formation.	Disulfides	159-168	CD8 antigen, alpha chain	Mus musculus	105-109
3297698-5	1987	We conclude that the dimeric structure of the RNase BS, which consists of two identical subunits cross-linked by interchain disulfide bridges, is probably responsible for the bundling activity and the accelerating effect on the polymerization of actin.	Disulfides	124-133	actin epsilon 1	Bos taurus	246-251
2972266-2	1988	Lipoprotein(a) (Lp[a]) represents a class of plasma lipoprotein particles that have overall characteristics similar to low-density lipoproteins but distinct from them by having apolipoprotein B100 linked to apolipoprotein(a) by disulfide bridge(s).	Disulfides	228-237	lipoprotein(a)	Homo sapiens	0-14
3607517-2	1987	Neurite extension factor (NEF) is a disulfide-bonded dimer of a protein closely related to S100 beta, a calcium-binding protein made by glial cells.	Disulfides	36-45	TNFAIP3 interacting protein 1	Mus musculus	0-24
3607517-2	1987	Neurite extension factor (NEF) is a disulfide-bonded dimer of a protein closely related to S100 beta, a calcium-binding protein made by glial cells.	Disulfides	36-45	TNFAIP3 interacting protein 1	Mus musculus	26-29
6152147-13	1984	The amidase was also inactivated by agents that reduce disulfide bridges.	Disulfides	55-64	AT695_RS13185	Staphylococcus aureus	4-11
6209286-1	1984	Fibroin is normally composed of one H chain (350 kd) and one L chain (25 kd) which are connected by disulfide bond(s).	Disulfides	100-109	fibroin light chain	Bombyx mori	0-7
3115821-6	1987	The IgM cells in PMG, where J chain is present in a disulfide-linked form, had no or few J+ nucleoli.	Disulfides	52-61	joining chain of multimeric IgA and IgM	Homo sapiens	28-35
2976021-1	1988	Coronary heart disease risk correlates directly with plasma concentrations of lipoprotein(a) (Lp(a)), a low-density lipoprotein-like particle distinguished by the presence of the glycoprotein apolipoprotein(a) (apo(a)), which is bound to apolipoprotein B-100 (apoB-100) by disulfide bridges.	Disulfides	273-282	lipoprotein(a)	Homo sapiens	78-92
3472206-1	1987	Apolipoprotein(a) [apo(a)] is a glycoprotein with Mr approximately equal to 280,000 that is disulfide linked to apolipoprotein B in lipoprotein(a) particles.	Disulfides	92-101	lipoprotein(a)	Homo sapiens	0-17
3472206-1	1987	Apolipoprotein(a) [apo(a)] is a glycoprotein with Mr approximately equal to 280,000 that is disulfide linked to apolipoprotein B in lipoprotein(a) particles.	Disulfides	92-101	lipoprotein(a)	Homo sapiens	19-25
6386810-1	1984	A limited reduction of the disulfide bonds of bovine enterokinase (enteropeptidase, EC 3.4.21.9) was accomplished with 50 mM dithioerythritol, at pH 9.0, and at 4 degrees C. The conditions separated the heavy and light subunits quantitatively with improved reliability when compared to the conditions used previously (Savithri, H. S., and Light, A.	Disulfides	27-36	transmembrane serine protease 15	Bos taurus	53-65
6386810-1	1984	A limited reduction of the disulfide bonds of bovine enterokinase (enteropeptidase, EC 3.4.21.9) was accomplished with 50 mM dithioerythritol, at pH 9.0, and at 4 degrees C. The conditions separated the heavy and light subunits quantitatively with improved reliability when compared to the conditions used previously (Savithri, H. S., and Light, A.	Disulfides	27-36	transmembrane serine protease 15	Bos taurus	67-82
2976021-1	1988	Coronary heart disease risk correlates directly with plasma concentrations of lipoprotein(a) (Lp(a)), a low-density lipoprotein-like particle distinguished by the presence of the glycoprotein apolipoprotein(a) (apo(a)), which is bound to apolipoprotein B-100 (apoB-100) by disulfide bridges.	Disulfides	273-282	lipoprotein(a)	Homo sapiens	94-99
6435677-7	1984	Interchain disulfide bonds result in the formation of dimers in glial fibrillary acidic protein.	Disulfides	11-20	glial fibrillary acidic protein	Bos taurus	64-95
3410046-4	1988	Two of the seven disulfide bonds were localized which apparently separate two distinct domains of mouse BM-40.	Disulfides	17-26	secreted acidic cysteine rich glycoprotein	Mus musculus	104-109
6381501-15	1984	In the native state, the insulin receptor consists of free alpha and beta subunits and several kinds of disulfide-linked oligomers of these subunits.	Disulfides	104-113	insulin receptor	Rattus norvegicus	25-41
3549299-8	1987	Trypanothione reductase, the parasite enzyme, and glutathione reductase, the host enzyme, exhibit mutually exclusive specificities for their respective disulfide substrates.	Disulfides	152-161	glutathione-disulfide reductase	Homo sapiens	50-71
2846046-3	1988	The disulfide pairings were established by enzymatic digestion and mass spectrometry and were found to be similar to those of EGF and TGF alpha.	Disulfides	4-13	transforming growth factor alpha	Homo sapiens	134-143
2952166-4	1987	Both the P44 and P46 fragments migrate slower in the presence of a reducing agent, indicating intrachain disulfide bonding, and do not have heparan sulfate side chains.	Disulfides	105-114	interferon induced protein 44	Homo sapiens	9-12
3290215-0	1988	Disulfide linkage of the zeta and eta chains of the T cell receptor.	Disulfides	0-9	endothelin receptor type A	Mus musculus	26-29
3580021-3	1987	It is concluded that the hepatic ALDH from rats posses in the active centre two SH-groups in close vicinity which can be oxidized slightly to the intramolecular disulfide and reduced again.	Disulfides	161-170	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	33-37
6438823-0	1984	Structure-function relationships of human factor VIII complex studied by thioredoxin dependent disulfide reduction.	Disulfides	95-104	cytochrome c oxidase subunit 8A	Homo sapiens	49-53
6438823-1	1984	A highly purified, multimeric factor VIII complex composed of VIII: vWF and some factor VIII: C contained about 100 disulfides per subunit of Mr 260,000.	Disulfides	116-126	cytochrome c oxidase subunit 8A	Homo sapiens	37-41
6438823-1	1984	A highly purified, multimeric factor VIII complex composed of VIII: vWF and some factor VIII: C contained about 100 disulfides per subunit of Mr 260,000.	Disulfides	116-126	cytochrome c oxidase subunit 8A	Homo sapiens	62-66
3048393-0	1988	Reoxidation of the class I disulfides of the rat adipocyte insulin receptor is dependent upon the presence of insulin: the class I disulfide of the insulin receptor is extracellular.	Disulfides	27-37	insulin receptor	Rattus norvegicus	59-75
6746628-1	1984	Disulfides (glutathione disulfide, cystine, cystamine) caused a first-order inactivation of rabbit-muscle fructose-1,6-bisphosphate aldolase at pH values of 7.4 and above.	Disulfides	0-10	fructose-bisphosphate aldolase B	Oryctolagus cuniculus	106-140
3768327-7	1986	Reduced and carboxymethylated prostatropin exhibits mitogenic activity, suggesting that disulfide bonds among cysteine residues 30, 61, and 97 are not functionally essential.	Disulfides	88-97	fibroblast growth factor 1	Bos taurus	30-42
3048393-0	1988	Reoxidation of the class I disulfides of the rat adipocyte insulin receptor is dependent upon the presence of insulin: the class I disulfide of the insulin receptor is extracellular.	Disulfides	27-37	insulin receptor	Rattus norvegicus	148-164
3019388-0	1986	Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor.	Disulfides	29-39	insulin receptor	Homo sapiens	43-59
3048393-0	1988	Reoxidation of the class I disulfides of the rat adipocyte insulin receptor is dependent upon the presence of insulin: the class I disulfide of the insulin receptor is extracellular.	Disulfides	27-36	insulin receptor	Rattus norvegicus	59-75
6610106-4	1984	The results show that the three disulfide-linked polypeptides of Lyt-2/3 molecules are all surface-expressed glycopeptides possessing hydrophobic regions residing within the lipid bilayer.	Disulfides	32-41	CD8 antigen, alpha chain	Mus musculus	65-72
3048393-0	1988	Reoxidation of the class I disulfides of the rat adipocyte insulin receptor is dependent upon the presence of insulin: the class I disulfide of the insulin receptor is extracellular.	Disulfides	27-36	insulin receptor	Rattus norvegicus	148-164
3341761-8	1988	These results show that NADP-MDH activation is dependent on the reduction of a critical disulfide bond.	Disulfides	88-97	malate dehydrogenase [NADP], chloroplastic	Zea mays	24-32
6373594-4	1984	The activated form of latent renin in crude brain extract was again inactivated by the disulfide compound sodium tetrathionate.	Disulfides	87-96	renin	Rattus norvegicus	29-34
3510133-2	1986	In contrast to a recent report, we found the erythrocyte insulin receptor to be similar in structure to that in classic target tissues for insulin, consisting of at least three species of molecular weight approximately 295,000, 265,000, and 245,000, containing disulfide-linked subunits of molecular weight approximately 130,000 and 95,000.	Disulfides	261-270	insulin receptor	Homo sapiens	57-73
2962926-3	1988	The Lp(a) lipoprotein is a complex particle composed of a low density lipoprotein (LDL)-like lipoprotein and the disulfide bonded Lp(a) glycoprotein.	Disulfides	113-122	lipoprotein(a)	Homo sapiens	4-8
3877646-15	1985	The data indicate that serum Meg-CSA is a 175,000-dalton protein (megakaryocyte colony-stimulating factor, Meg-CSF) in which higher order structure and disulfide bonding are necessary for biologic activity.	Disulfides	152-161	protein tyrosine phosphatase non-receptor type 4	Homo sapiens	29-32
3877646-15	1985	The data indicate that serum Meg-CSA is a 175,000-dalton protein (megakaryocyte colony-stimulating factor, Meg-CSF) in which higher order structure and disulfide bonding are necessary for biologic activity.	Disulfides	152-161	ERCC excision repair 8, CSA ubiquitin ligase complex subunit	Homo sapiens	33-36
3877646-15	1985	The data indicate that serum Meg-CSA is a 175,000-dalton protein (megakaryocyte colony-stimulating factor, Meg-CSF) in which higher order structure and disulfide bonding are necessary for biologic activity.	Disulfides	152-161	C-MPL ligand	Canis lupus familiaris	66-105
3877646-15	1985	The data indicate that serum Meg-CSA is a 175,000-dalton protein (megakaryocyte colony-stimulating factor, Meg-CSF) in which higher order structure and disulfide bonding are necessary for biologic activity.	Disulfides	152-161	protein tyrosine phosphatase non-receptor type 4	Homo sapiens	107-110
2999280-9	1985	These studies suggest that Lp(a) is, in essence, an LDL-particle to which the protein (a) is attached through disulfide bonds to apoB.	Disulfides	110-119	lipoprotein(a)	Homo sapiens	27-32
6319417-11	1984	These data suggest that 1) the hCG/luteinizing hormone receptor is an oligomeric complex linked by disulfide bonds and 2) that under reducing conditions, the oligomeric receptor dissociates into four nonidentical subunits.	Disulfides	99-108	chorionic gonadotropin subunit beta 5	Homo sapiens	31-34
6229271-5	1983	Treatment with plasmin proved to be the most reliable procedure for generating the active split product which could be readily separated from the inactive, disulfide-containing C-terminal fragment.	Disulfides	156-165	plasminogen	Homo sapiens	15-22
6417475-5	1983	In both PWM-stimulated (for 2 days) and unstimulated PBL, equal proportions of free and disulfide-linked J-chain were found.	Disulfides	88-97	joining chain of multimeric IgA and IgM	Homo sapiens	105-112
6417475-7	1983	In tissue culture fluids, J-chain was not secreted in a free form but was always disulfide-linked to polymeric Igs.	Disulfides	81-90	joining chain of multimeric IgA and IgM	Homo sapiens	26-33
6417475-8	1983	In lymphoblastoid cell lines, J-chain was present in a disulfide-linked form in IgM and IGA producers, but in IgG cells and in an IgM cell line (DAUDI) that did not secrete IgM but expressed it on the cell membrane, intracellular J-chain was present in free form.	Disulfides	55-64	joining chain of multimeric IgA and IgM	Homo sapiens	30-37
2931434-10	1985	In addition, firm evidence was found that upon activation by plasmin single-chain pro-urokinase is cleaved at the Lys-Ile bond between residues 158 and 159, resulting in the formation of a two-chain urokinase molecule held together by one disulfide linkage.	Disulfides	239-248	plasminogen	Homo sapiens	61-68
2962926-3	1988	The Lp(a) lipoprotein is a complex particle composed of a low density lipoprotein (LDL)-like lipoprotein and the disulfide bonded Lp(a) glycoprotein.	Disulfides	113-122	lipoprotein(a)	Homo sapiens	130-134
3121787-3	1988	We examined the polymeric structure of AChE forms by disulfide bridge reduction.	Disulfides	53-62	Acetylcholine esterase	Drosophila melanogaster	39-43
2866794-1	1985	The amino acid sequence and disulfide bond pairing of human tumor derived angiogenin, the first tumor angiogenesis factor to be isolated in pure form from human sources, have been determined by conventional sequencing techniques adapted and applied to nanomole and subnanomole levels of material.	Disulfides	28-37	angiogenin	Homo sapiens	74-84
6304715-8	1983	The predicted amino acid sequence of mature p34, as deduced from its gene structure, has 229 residues and reveals a single potential disulfide loop (between cysteine residues 107 and 163) as well as a 22-amino acid residue membrane integrated segment (residues 193-214).	Disulfides	133-142	alpha and gamma adaptin binding protein	Homo sapiens	44-47
6344921-0	1983	Insulin receptor: insulin-modulated interconversion between distinct molecular forms involving disulfide-sulfhydryl exchange.	Disulfides	95-104	insulin receptor	Homo sapiens	0-16
3320045-7	1987	Papilin forms oligomers linked by disulfide bridges, as shown by sodium dodecyl sulfate-agarose gel electrophoresis and electron microscopy.	Disulfides	34-43	Papilin	Drosophila melanogaster	0-7
6852243-1	1983	A mild cathepsin D digest of fibronectin only contained single-chain peptides of 200, 140 and 70 kDa and double-chain fragments of about 300 and 140 kDa containing the C-terminal disulfide link.	Disulfides	179-188	cathepsin D	Homo sapiens	7-18
7174672-1	1982	The structure of the CoA affinity analog-oxidized CoA disulfide (o-CoAS2) (Collier, G. E., and Nishimura, J. S. (1978) J. Biol.	Disulfides	54-63	peptidylprolyl isomerase A like 4E	Homo sapiens	67-72
7174672-4	1982	This deduction is based on several considerations among which are: the cleavage of o-CoAS2 by dithiothreitol under anaerobic conditions to equimolar amounts of CoASH and CoASO2H; the alkali-catalyzed dismutation of 3 mol of o-CoAS2 to 4 mol of CoASO2H and 1 mol of CoA disulfide; and comparison of the 13C-NMR spectra of CoA disulfide and o-CoAS2.	Disulfides	269-278	peptidylprolyl isomerase A like 4E	Homo sapiens	85-90
2991266-13	1985	The ABP seems to be a 40-kDa dimer in its native form without disulfide bonds between its monomers.	Disulfides	62-71	auxin-binding protein 4	Zea mays	4-7
6510521-1	1984	Cyanogen bromide digestion of hemopexin at its 6 methionine residues results in 7 fragments (CB1-CB7) partially connected by disulfide bridges.	Disulfides	125-134	hemopexin	Homo sapiens	30-39
3426230-10	1987	HCII differs from antithrombin III, which contains an essential disulfide bond for heparin-dependent thrombin inhibition (Longas, M. O., et al.	Disulfides	64-73	serpin family D member 1	Homo sapiens	0-4
6520117-4	1984	A substantial fraction of the fibroin L-chain synthesized was bound to the H-chain by disulfide bond.	Disulfides	86-95	fibroin light chain	Bombyx mori	30-45
7173207-0	1982	Synthesis of a new disulfide affinity adsorbent for purification of human uterine progesterone receptor.	Disulfides	19-28	progesterone receptor	Homo sapiens	82-103
2443495-14	1987	The data also support the previous suggestion that the NC-2 domain is involved in the formation of disulfide bond-stabilized type VII collagen dimers, and is subsequently removed by physiological proteolytic processing.	Disulfides	99-108	down-regulator of transcription 1	Homo sapiens	55-59
7096442-2	1982	Because cultured human umbilical vein endothelial cells synthesize and secrete a glycoprotein (GP-160) which is a disulfide-bonded multimer of 160 kdalton subunits, the possibility that GP-160 is thrombospondin was investigated.	Disulfides	114-123	glutamyl aminopeptidase	Homo sapiens	95-101
7076131-5	1982	After prolonged cathepsin D digestion another disulfide-linked fragment of Mr 90000 containing peptide chains of Mr 65000 and Mr 36000 was found.	Disulfides	46-55	cathepsin D	Homo sapiens	16-27
7076131-6	1982	The same fragment also formed during prolonged digestion of a previously described cathepsin D-derived heparin-binding piece of Mr 140000 which consisted of disulfide-linked chains of Mr 65000 and Mr 75000.	Disulfides	157-166	cathepsin D	Homo sapiens	83-94
6205252-0	1984	Monoclonal antibodies to hog thyroglobulin recognizing disulfide-dependent conformational structures.	Disulfides	55-64	thyroglobulin	Mus musculus	29-42
6205913-1	1984	125I-labeled insulin has been cross-linked to alpha 2-macroglobulin (alpha 2M) via a disulfide bond.	Disulfides	85-94	alpha-2-macroglobulin	Rattus norvegicus	46-67
6205913-1	1984	125I-labeled insulin has been cross-linked to alpha 2-macroglobulin (alpha 2M) via a disulfide bond.	Disulfides	85-94	alpha-2-macroglobulin	Rattus norvegicus	69-77
6233280-0	1984	Role of a disulfide bond in the gamma subunit in activation of the ATPase of chloroplast coupling factor 1.	Disulfides	10-19	dynein axonemal heavy chain 8	Homo sapiens	67-73
6233280-1	1984	The relationship between activation of the latent ATPase activity of isolated chloroplast coupling factor 1 (CF1) and reduction of a disulfide in the gamma subunit has been assessed.	Disulfides	133-142	dynein axonemal heavy chain 8	Homo sapiens	50-56
7060559-1	1982	Binding of added progesterone to native uteroglobin requires the reduction of the disulfide bonds that hold together the two polypeptide chains of the protein.	Disulfides	82-91	uteroglobin	Oryctolagus cuniculus	40-51
6795191-8	1981	The available data thus favor a model in which J chain is disulfide-bonded to both IgA monomer subunits in sIgA.	Disulfides	58-67	joining chain of multimeric IgA and IgM	Homo sapiens	47-54
3624271-9	1987	The pre-beta 1 form has a t1/2 of about 4 min and has a precursor-product relationship with a more completely disulfide-bonded form, termed pre-beta 2, which does combine with the alpha subunit to form a dimer.	Disulfides	110-119	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	144-150
7032915-20	1981	In view of the interchain disulfide bridge glutathione reductase should be regarded as a monomeric protein.	Disulfides	26-35	glutathione-disulfide reductase	Homo sapiens	43-64
6587385-6	1984	The disulfide bond arrangement in cathepsin D is probably similar to that of pepsin, because the positions of six half-cystine residues are conserved.	Disulfides	4-13	cathepsin D	Homo sapiens	34-45
6693383-3	1984	From two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence and presence of dithiothreitol, the purified insulin receptor was shown to be composed of heterogeneous disulfide-linked complexes of (alpha 2, 2 beta), (alpha 2, beta, beta 1), (alpha 2, 2 beta 1), (alpha 2), (alpha beta), and (alpha beta 1).	Disulfides	198-207	insulin receptor	Homo sapiens	139-155
2957697-3	1987	The gamma chains are expressed in the Lyt2-,L3T4- subsets of these T-cell populations as disulfide-linked heterodimers.	Disulfides	89-98	CD8 antigen, alpha chain	Mus musculus	38-42
6693383-4	1984	The largest disulfide-linked complex (alpha 2, 2 beta) appears to be the minimum unit of the intact insulin receptor whereas the other complexes appear to be generated from (alpha 2, 2 beta) by proteolytic degradation and/or reduction.	Disulfides	12-21	insulin receptor	Homo sapiens	100-116
6503714-0	1984	Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Homo sapiens	60-87
7025891-8	1981	These results indicate that the solubilized receptor binds significant amounts of detergents, that the insulin binding component of the receptor binds to other receptor components by hydrophobic interactions, and that one or more components of the insulin receptor contain intrachain disulfide bonds.	Disulfides	284-293	insulin receptor	Rattus norvegicus	248-264
7026550-5	1981	Not only HMW-UK but also LMW-UK was composed of two polypeptide chains linked by disulfide bond(s).	Disulfides	81-90	cilia and flagella associated protein 97	Homo sapiens	9-12
2823879-0	1987	Tac antigen forms disulfide-linked homodimers.	Disulfides	18-27	interleukin 2 receptor subunit alpha	Homo sapiens	0-11
6161173-9	1981	However unlike the human counterpart, the subunits of mouse C4-bp are not linked by disulfide bonds but are connected by non-covalent forces that can be disrupted by SDS.	Disulfides	84-93	complement component 4 binding protein	Mus musculus	60-65
6639070-5	1983	Sodium dodecyl sulfate-gel electrophoresis shows that hare uteroglobin is composed of two subunits of identical Mr (about 7000) held together by disulfide bridges.	Disulfides	145-154	uteroglobin	Oryctolagus cuniculus	59-70
2823879-4	1987	A variety of experimental approaches yield results indicating that the Tac antigen, which migrates as a single protein on NaDod-SO4/PAGE under reducing conditions, is also expressed as disulfide-linked homodimers and oligomers.	Disulfides	185-194	interleukin 2 receptor subunit alpha	Homo sapiens	71-82
2436691-3	1987	With trypsinized, labeled platelets, AK 1, SZ 1, and FMC 25 (epitope on GP IX) immunoprecipitated a membrane-bound proteolytic fragment of the GP Ib-IX complex consisting of GP IX and an congruent to 25,000 mol wt remnant of the alpha-chain of GP lb disulfide-linked to the beta-subunit.	Disulfides	250-259	DLG2 antisense RNA 1	Homo sapiens	43-47
6682760-12	1983	Digestion with plasmin yields the two-chain form with disulfide-bonded polypeptide chains, "A" and "B" (from the N-terminal and C-terminal parts, respectively).	Disulfides	54-63	plasminogen	Homo sapiens	15-22
7429030-1	1980	Three forms of disulfide-linked insulin receptor complexes are labeled by covalent cross-linking to receptor-bound 125I-insulin in native adipocyte or liver membranes.	Disulfides	15-24	insulin receptor	Homo sapiens	32-48
2436691-3	1987	With trypsinized, labeled platelets, AK 1, SZ 1, and FMC 25 (epitope on GP IX) immunoprecipitated a membrane-bound proteolytic fragment of the GP Ib-IX complex consisting of GP IX and an congruent to 25,000 mol wt remnant of the alpha-chain of GP lb disulfide-linked to the beta-subunit.	Disulfides	250-259	glycoprotein IX platelet	Homo sapiens	72-77
6997298-1	1980	The 28,000-dalton COOH-terminal cyanogen bromide peptide of complement factor B was isolated disulfide bonded to a second polypeptide of Mr = 3,500.	Disulfides	93-102	complement factor B	Homo sapiens	60-79
6880338-1	1983	A specific and sensitive radioimmunoassay for human choriogonadotropin (hCG) has been developed using rabbit antiserum to chemical analogs of beta subunit of human chorionic gonadotropin prepared by controlled reduction and S-alkylation of its disulfide linkages.	Disulfides	244-253	chorionic gonadotropin subunit beta 5	Homo sapiens	72-75
2436691-3	1987	With trypsinized, labeled platelets, AK 1, SZ 1, and FMC 25 (epitope on GP IX) immunoprecipitated a membrane-bound proteolytic fragment of the GP Ib-IX complex consisting of GP IX and an congruent to 25,000 mol wt remnant of the alpha-chain of GP lb disulfide-linked to the beta-subunit.	Disulfides	250-259	glycoprotein IX platelet	Homo sapiens	174-179
2949785-2	1987	The two chains (Mr approximately 33,000 and 22,000) were disulfide linked and resistant to subsequent activation by plasmin.	Disulfides	57-66	plasminogen	Homo sapiens	116-123
6402447-10	1983	Mutations that altered the amino acid sequence in the vicinity of the disulfide bond in the C1 domain had the greatest deleterious effects on Kb-controlled responsiveness to H-4.2.	Disulfides	70-79	histocompatibility 42	Mus musculus	174-179
6402447-12	1983	Therefore, the amino acid sequence in the vicinity of the disulfide bond in the C1 domain plays a prominent role in determining the H-4.2-specific immune response potential.	Disulfides	58-67	histocompatibility 42	Mus musculus	132-137
6992782-0	1980	Retention of enzymatic activity of bovine enterokinase after a limited reduction of disulfide bonds.	Disulfides	84-93	transmembrane serine protease 15	Bos taurus	42-54
3327411-1	1987	Ricin A chain, a potent ribosomal poison, was disulfide linked either to the iron transport protein, transferrin, or to anti-transferrin receptor antibodies to produce highly specific derivative toxins, Tf-A and TfR-A, respectively.	Disulfides	46-55	transferrin receptor	Homo sapiens	212-215
6248505-4	1980	These results suggest that Na+,K+-ATPase was inactivated by reduction of disulfide bond(s) embedded within the lipid bilayer in the presence of detergent, and that the subunits of the resulting enzyme were no longer bound to the membrane.	Disulfides	73-82	dynein axonemal heavy chain 8	Homo sapiens	34-40
6687224-2	1983	The native IAP was without effect, but its A-protomer, an active subunit, was effective after reduction of disulfide bonds in the peptide chain; it catalyzed ADP-ribosylation of the membrane Mr = 41,000 protein.	Disulfides	107-116	Cd47 molecule	Rattus norvegicus	11-14
6346428-3	1983	Our data and observations from other laboratories have led to the suggestion that the insulin receptor is a heterodimer of the 134,000 and 95,000 subunits and, in fact, has an immunoglobulin-like structure with heavy and light chains held together by disulfide bonds.	Disulfides	251-260	insulin receptor	Homo sapiens	86-102
6815213-5	1982	With progressive reduction of disulfide bonds by dithiothreitol (DTT), the electron microscopic size of FVIII/vWF decreased in parallel with increased electrophoretic mobility on SDS-agarose gels; between 0.1 and 0.5 mM DTT its structure changed from predominantly fibrillar species to large nodular forms.	Disulfides	30-39	coagulation factor VIII	Homo sapiens	104-109
6111625-6	1980	Reduction of disulfide bonds by DTE after diamide treatment restores the (Ca2+ + Mg2+)-ATPase activity but is unable to take the Mg2+-ATPase activity back to the original level.	Disulfides	13-22	dynein axonemal heavy chain 8	Homo sapiens	87-93
381308-7	1979	The proteinase B inhibitors of yeast, therefore, differ fundamentally from proteinase inhibitors of many other organisms, which generally contain a large number of disulfide bridges.	Disulfides	164-173	proteinase B	Saccharomyces cerevisiae S288C	4-16
3102228-1	1986	The human interleukin-2 (IL-2) receptor was quantitatively cleaved into two large disulfide-bonded fragments by either trypsin or endoproteinase lys-C (endo lys-C).	Disulfides	82-91	interleukin 2 receptor subunit beta	Homo sapiens	25-39
420716-4	1979	The amino acid composition of apparently homogeneous CTAP-III was determined, confirming the presence of two disulfide links and providing a calculated molecular weight of 11,633 daltons.	Disulfides	109-118	pro-platelet basic protein	Homo sapiens	53-61
6191201-4	1982	Monoclonal antibody to Lyt-2 or Lyt-3 (which are linked to one another by disulfide bonds) gave a uniform distribution of fluorescence and was mobile on the cell surface.	Disulfides	74-83	CD8 antigen, alpha chain	Mus musculus	23-28
3542030-2	1986	The SBP subunit consists of a 373-residue polypeptide chain containing two disulfide bonds and three oligosaccharide chains.	Disulfides	75-84	selenium binding protein 1	Homo sapiens	4-7
6291012-5	1982	Thiol reagents reduced the binding activity of the receptor, suggesting that an intrachain disulfide bond may form an important constituent of the binding site for TRH.	Disulfides	91-100	thyrotropin releasing hormone	Rattus norvegicus	164-167
83160-7	1978	Based on these data it is concluded that a major antigenic site of hCG resides in the region of residues 21-23 with a disulfide bond connecting cysteine-23 or -26 with the cysteines at positions 72 or 110.	Disulfides	118-127	chorionic gonadotropin subunit beta 5	Homo sapiens	67-70
3021744-10	1986	Both beta 1- and beta 2-receptors displayed this same shift in electrophoretic mobility observed in the presence as compared to the absence of disulfide bridge-reducing agents, as detected both by autoradiography of the radiolabeled receptors and by immunoblotting of native receptors.	Disulfides	143-152	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	17-23
30542-1	1978	Eight disulfides (I-VIII) and a thiolsulfonate (IX) were promising blocking agents of lymphocytes in graft-versus-host reactions (GvHR) without comensurate intracellular effects.	Disulfides	6-16	cytochrome c oxidase subunit 8A	Homo sapiens	20-24
7045094-0	1982	Role of disulfides in the subunit structure of the insulin receptor.	Disulfides	8-18	insulin receptor	Rattus norvegicus	51-67
7045094-2	1982	The native insulin receptor affinity-labeled by covalent cross-linking to 125I-insulin has been proposed to consist of two alpha receptor subunits and two beta-receptor subunits all disulfide-linked as a Mr = 350,000 (beta-S-S-alpha)-S-S-(alpha-S-S-beta) receptor complex (Massague, J., Pilch, P. F., and Czech, M. P. (1981) J. Biol.	Disulfides	182-191	insulin receptor	Rattus norvegicus	11-27
7045094-5	1982	We denote the disulfide bonds linking the two symmetrical (alpha-S-S-beta) receptor halves as class I insulin receptor disulfides, whereas the disulfide bonds linking one alpha receptor subunit to one beta receptor subunit are termed class II disulfides.	Disulfides	14-23	insulin receptor	Rattus norvegicus	102-118
7045094-7	1982	Reduction of class I insulin receptor disulfides did not prevent binding of insulin to the insulin receptor.	Disulfides	38-48	insulin receptor	Rattus norvegicus	21-37
7045094-11	1982	Class II insulin receptor disulfides were fully reduced by dithiothreitol only after denaturation of the insulin receptor by sodium dodecyl sulfate.	Disulfides	26-36	insulin receptor	Rattus norvegicus	9-25
7045094-12	1982	Class I insulin receptor disulfides were partially reoxidized by an incubation mixture consisting of reduced and oxidized glutathione.	Disulfides	25-35	insulin receptor	Rattus norvegicus	8-24
3463991-5	1986	Thioredoxin was most effective in reactivating inactive scrambled RNase, which contained mispaired disulfides, showing a t1/2 of 2 hr.	Disulfides	99-109	interleukin 1 receptor like 1	Homo sapiens	121-130
7045094-13	1982	When solubilized insulin receptor containing reduced class I disulfides was exposed to ethylene glycol bis(succinimidyl succinate), the receptor subunits were internally cross-linked and migrated like intact receptor complexes on nonreduced dodecyl sulfate gels.	Disulfides	61-71	insulin receptor	Rattus norvegicus	17-33
7076131-0	1982	Early and late cathepsin D-derived fragments of fibronectin containing the C-terminal interchain disulfide cross-link.	Disulfides	97-106	cathepsin D	Homo sapiens	15-26
6795191-2	1981	In view of the asymmetry in the disulfide bonding between SC and the IgA subunits, an arrangement which follows disulfide interchange, several models for the disulfide linkage of J chain and the bonds between IgA subunits were envisaged and investigated.	Disulfides	32-41	joining chain of multimeric IgA and IgM	Homo sapiens	179-186
568483-1	1978	Uteroglobin, a steroid-binding protein of the uterine secretion of the rabbit which is induced by progesterone, comprises two identical polypeptide chains of 70 amino acid residues linked by two disulfide bonds.	Disulfides	195-204	uteroglobin	Oryctolagus cuniculus	0-11
3015971-7	1986	Thus, disulfide bonding is important for the strong association of MAGP with elastic fibers.	Disulfides	6-15	microfibril associated protein 2	Bos taurus	67-71
952871-10	1976	According to this model hexosaminidase A is composed of two subunits alpha2 and beta2, in which the two polypeptide chains are linked by a disulfide bridge.	Disulfides	139-148	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	80-85
7251591-4	1981	Disulfide reducing agents reduce the viscosity of concentrated mucin solutions by dissociation of soluble mucin aggregates without affecting the insoluble aggregates.	Disulfides	0-9	LOC100508689	Homo sapiens	63-68
7251591-4	1981	Disulfide reducing agents reduce the viscosity of concentrated mucin solutions by dissociation of soluble mucin aggregates without affecting the insoluble aggregates.	Disulfides	0-9	LOC100508689	Homo sapiens	106-111
7251591-5	1981	Detailed chemical analyses of the mucins have been carried out and indicate that the reduction of interchain disulfides is accompanied, not only by a reduction in mucin viscosity, but by the liberation of two small proteins from the large mucin molecule.	Disulfides	109-119	LOC100508689	Homo sapiens	34-39
7251591-5	1981	Detailed chemical analyses of the mucins have been carried out and indicate that the reduction of interchain disulfides is accompanied, not only by a reduction in mucin viscosity, but by the liberation of two small proteins from the large mucin molecule.	Disulfides	109-119	LOC100508689	Homo sapiens	163-168
6457-1	1976	Reduction of the active center disulfide bond in the flavoprotein pig heart lipoamide dehydrogenase generates two sulfur moieties which are chemically inequivalent in the 2-electron reduced form of the enzyme.	Disulfides	31-40	dihydrolipoamide dehydrogenase	Sus scrofa	76-99
128454-3	1975	Sulfhydryl titrations of the heavy chain showed that the partial reduction involved primarily the cleavage of the sole interchain disulfide bridge of plasmin.	Disulfides	130-139	plasminogen	Homo sapiens	150-157
7240231-1	1981	The assignment of five disulfide bonds in the alpha subunit of human chorionic gonadotropin (hCG) using partial reduction and S-[14C]carboxymethylation has been reported earlier (Mise, T., and Bahl, O. P. (1980) J. Biol.	Disulfides	23-32	chorionic gonadotropin subunit beta 5	Homo sapiens	46-97
6269576-2	1981	Reduced RNase A was reoxidized, and the incorrectly formed disulfide bonds were reshuffled to the native ones by oxidized and reduced glutathiones, as described in the first paper of this series.	Disulfides	59-68	ribonuclease A family member 1, pancreatic	Homo sapiens	8-15
2944852-1	1986	The light chain of plasmin, prepared by selective reduction of the interchain disulfide bridges, can be separated from the heavy chain by affinity adsorption onto Kunitz inhibitor/Sepharose.	Disulfides	78-87	plasminogen	Homo sapiens	19-26
6974113-1	1980	As a model experiment for the preparation of cancer chemotherapeutic agents, a disulfide-linked conjugate of rabbit anti-mouse IgG (RaMIgG) and ricin A-cahin was synthesized.	Disulfides	79-88	immunoglobulin heavy variable V1-62	Mus musculus	127-130
809510-1	1975	After the cleavage of disulfide bonds of macroglobulin isolated from channel catfish (Ictalurus punctatus), an electrophoretically fast-moving polypeptide, which resembled human J chain, was released.	Disulfides	22-31	joining chain of multimeric IgA and IgM	Homo sapiens	178-185
1170876-1	1975	Kinetic studies have been made with glutathione-insulin transhydrogenase, an enzyme which degrades insulin by promoting cleavage of its disulfide bonds via sulfhydryl-disulfide interchange.	Disulfides	136-145	prolyl 4-hydroxylase subunit beta	Homo sapiens	36-72
2937786-3	1986	Measurements of the rate of disulfide bond reduction by thioredoxin in intact protein S showed that the disulfide bonds are largely inaccessible to thioredoxin in the presence of Ca2+ ions, whereas in the presence of EDTA apparently all of the disulfide bonds are rapidly reduced.	Disulfides	28-37	thioredoxin	Bos taurus	56-67
7391570-5	1980	Therefore, an altered form of C4b, C4b", consisting of four disulfide-linked polypeptide chains with the same m.w.	Disulfides	60-69	complement C4B (Chido blood group)	Homo sapiens	30-33
2937786-3	1986	Measurements of the rate of disulfide bond reduction by thioredoxin in intact protein S showed that the disulfide bonds are largely inaccessible to thioredoxin in the presence of Ca2+ ions, whereas in the presence of EDTA apparently all of the disulfide bonds are rapidly reduced.	Disulfides	104-113	thioredoxin	Bos taurus	56-67
4857118-0	1974	Direct spectrophotometric determination of mucin disulfide linkages.	Disulfides	49-58	LOC100508689	Homo sapiens	43-48
2417623-11	1985	Cathepsin D digestion produced an 83K heparin-binding, monoclonal antibody reactive fragment that contains the interchain disulfide bond(s) linking the two fibronectin chains at their C-termini.	Disulfides	122-131	cathepsin D	Homo sapiens	0-11
6106190-5	1980	In the course of this work it was found that the mixed disulfide between glutathione and gamma-glutamylcysteine is a good substrate of glutathione reductase.	Disulfides	55-64	glutathione-disulfide reductase	Homo sapiens	135-156
3902121-4	1985	Under reducing conditions, OKT16 reacted with an antigen of 40K daltons; however, under nonreducing conditions this antigen appeared as an 84K-dalton molecule, which suggests that the p40 antigen exists as a disulfide-linked dimer.	Disulfides	208-217	interleukin 9	Homo sapiens	184-187
6986378-9	1980	These data indicate that the labeled monomer with an apparent molecular weight of 125,00 represents a high affinity insulin receptor subunit which exists in the native adipocyte plasma membrane in a disulfide-linked complex.	Disulfides	199-208	insulin receptor	Homo sapiens	116-132
14323613-0	1965	THE REDUCTION AND REOXIDATION OF THE DISULFIDE BONDS OF SOY-BEAN TRYPSIN INHIBITOR.	Disulfides	37-46	cysteine rich secretory protein LCCL domain containing 2	Homo sapiens	65-82
2416352-2	1985	The results show that the insulin receptor exists under different free and disulfide-linked combinations of alpha and beta subunits.	Disulfides	75-84	insulin receptor	Homo sapiens	26-42
33660896-3	2021	The resulted chiral bulky Lewis trio (BLT) allows for the construction of chiral disulfides via direct disulfuration with beta-ketocarbonyls or alpha-branched aldehydes in a practical and highly stereocontrolled manner.	Disulfides	81-91	trio Rho guanine nucleotide exchange factor	Homo sapiens	32-36
3000460-1	1985	The insulin receptor appears as a tetrameric glycoprotein consisting of two Mr 130,000 subunits (alpha), and two Mr 95,000 subunits (beta) in a disulfide-linked complex.	Disulfides	144-153	insulin receptor	Homo sapiens	4-20
33107103-4	2021	Different isoforms of HMGB1 present with distinctive physiological functions in ECM-fully-reduced HMGB1 (all thiol) acts as the initial damage signal to recruit circulating myeloid cells, disulfide HMGB1 behaves as a cytokine to activate macrophages and neutrophils, and both signals are turned off when HMGB1 is terminally oxidized into the final sulfonate form.	Disulfides	188-197	high mobility group box 1	Homo sapiens	22-27
33107103-4	2021	Different isoforms of HMGB1 present with distinctive physiological functions in ECM-fully-reduced HMGB1 (all thiol) acts as the initial damage signal to recruit circulating myeloid cells, disulfide HMGB1 behaves as a cytokine to activate macrophages and neutrophils, and both signals are turned off when HMGB1 is terminally oxidized into the final sulfonate form.	Disulfides	188-197	high mobility group box 1	Homo sapiens	98-103
33107103-4	2021	Different isoforms of HMGB1 present with distinctive physiological functions in ECM-fully-reduced HMGB1 (all thiol) acts as the initial damage signal to recruit circulating myeloid cells, disulfide HMGB1 behaves as a cytokine to activate macrophages and neutrophils, and both signals are turned off when HMGB1 is terminally oxidized into the final sulfonate form.	Disulfides	188-197	high mobility group box 1	Homo sapiens	98-103
33107103-4	2021	Different isoforms of HMGB1 present with distinctive physiological functions in ECM-fully-reduced HMGB1 (all thiol) acts as the initial damage signal to recruit circulating myeloid cells, disulfide HMGB1 behaves as a cytokine to activate macrophages and neutrophils, and both signals are turned off when HMGB1 is terminally oxidized into the final sulfonate form.	Disulfides	188-197	high mobility group box 1	Homo sapiens	98-103
448074-4	1979	The three polypeptides, C3b alpha-60, C3b alpha-40, and C3 beta, are held together as a single unit by disulfide bonds.	Disulfides	103-112	endogenous retrovirus group K member 3	Homo sapiens	24-27
448074-4	1979	The three polypeptides, C3b alpha-60, C3b alpha-40, and C3 beta, are held together as a single unit by disulfide bonds.	Disulfides	103-112	endogenous retrovirus group K member 3	Homo sapiens	38-41
448074-4	1979	The three polypeptides, C3b alpha-60, C3b alpha-40, and C3 beta, are held together as a single unit by disulfide bonds.	Disulfides	103-112	endogenous retrovirus group K member 3	Homo sapiens	56-63
4079940-6	1985	The p26 molecule is not disulfide-linked to p24, and can be immunoprecipitated from a variety of 125I- or [35S]methionine-labeled cells.	Disulfides	24-33	transmembrane p24 trafficking protein 3	Homo sapiens	4-7
684756-7	1978	Thioltransferase, known to catalyze thiol-disulfide exchange reactions, increased the regain of glyceraldehyde-3-phosphate dehydrogenase activity to nearly the original value.	Disulfides	42-51	glutaredoxin	Homo sapiens	0-16
924986-1	1977	Disulfide-reduced RNase A, which could be reoxidized to give the native enzyme, was shown to have a CD spectrum quite different from that of the native enzyme or a random coil.	Disulfides	0-9	ribonuclease A family member 1, pancreatic	Homo sapiens	18-25
924986-2	1977	Disulfide-reduced and fully cysteine-S-carboxamidomethylated RNase A because the derivative was stable and gave a spectrum identical to that of reduced RNase A.	Disulfides	0-9	ribonuclease A family member 1, pancreatic	Homo sapiens	61-68
924986-2	1977	Disulfide-reduced and fully cysteine-S-carboxamidomethylated RNase A because the derivative was stable and gave a spectrum identical to that of reduced RNase A.	Disulfides	0-9	ribonuclease A family member 1, pancreatic	Homo sapiens	152-159
33522833-5	2021	MCU overexpression decreased SR Ca2+ leak in the ACi group and mitigated the elevated ryanodine receptor disulfide crosslinks in HF.	Disulfides	105-114	calcium uniporter protein, mitochondrial	Cavia porcellus	0-3
33837960-1	2021	Protein disulfide isomerase (PDI) is the prototypic member of the thiol isomerase family that catalyzes disulfide bond rearrangement.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
33731757-0	2021	Disulfide HMGB1 acts via TLR2/4 receptors to reduce the numbers of oligodendrocyte progenitor cells after traumatic injury in vitro.	Disulfides	0-9	high mobility group box 1	Homo sapiens	10-15
33855279-2	2021	Herein, we developed an in vitro system for directly monitoring PDI- or ERp46-catalyzed disulfide bond formation in ribosome-associated nascent chains of human serum albumin.	Disulfides	88-97	prolyl 4-hydroxylase subunit beta	Homo sapiens	64-67
33855279-4	2021	Single-molecule analysis by high-speed atomic force microscopy further revealed that PDI binds nascent chains persistently, forming a stable face-to-face homodimer, whereas ERp46 binds for a shorter time in monomeric form, indicating their different mechanisms for substrate recognition and disulfide bond introduction.	Disulfides	291-300	prolyl 4-hydroxylase subunit beta	Homo sapiens	85-88
3891757-9	1985	These studies demonstrate that the largest disulfide-linked complex (alpha 2 beta 2) is the predominant insulin receptor form purified from the human placenta with the other complexes being generated by proteolysis and by internal subunit dissociation.	Disulfides	43-52	insulin receptor	Homo sapiens	104-120
33855279-5	2021	Thus, ERp46 serves as a more potent disulfide introducer especially during the early stages of translation, whereas PDI can catalyze disulfide formation when longer nascent chains emerge out from ribosome.	Disulfides	133-142	prolyl 4-hydroxylase subunit beta	Homo sapiens	116-119
832762-1	1977	Of the eleven disulfide bonds of human chorionic gonadotropin (hCG), two were reduced with a 10-fold molar excess of dithiothreitol (DTT) relative to hormone.	Disulfides	14-23	chorionic gonadotropin subunit beta 5	Homo sapiens	39-67
2985702-9	1985	Disulfide bonding between chains was conserved in both PC-1 and the transferrin receptor in all species examined, but transferrin receptors from mouse cells had a significantly higher apparent m.w.	Disulfides	0-9	transferrin receptor	Mus musculus	68-88
942977-1	1976	Guinea pig eosinophil granules contain a protein, the major basic protein (MBP), which accounts for more than half of the total granule protein, has a high content of arginine, and displays a remarkable tendency to form disulfide-linked aggregates.	Disulfides	220-229	myelin basic protein	Homo sapiens	54-73
942977-1	1976	Guinea pig eosinophil granules contain a protein, the major basic protein (MBP), which accounts for more than half of the total granule protein, has a high content of arginine, and displays a remarkable tendency to form disulfide-linked aggregates.	Disulfides	220-229	myelin basic protein	Homo sapiens	75-78
942977-6	1976	The human MBP had a molecular weight of 9,200, contained less than 1% carbohydrate, was rich in arginine, and readily formed disulfide-bonded aggregates.	Disulfides	125-134	myelin basic protein	Homo sapiens	10-13
32426849-0	2021	Disulfide-HMGB1 Drives Ischemia-Reperfusion Injury in Human Liver Transplantation.	Disulfides	0-9	high mobility group box 1	Homo sapiens	10-15
32426849-4	2021	Portal blood immediately following allograft reperfusion (liver flush, LF) had increased total HMGB1, but only LF from patients with histopathological IRI had increased disulfide-HMGB1 and induced TLR4-dependent TNFalpha production by macrophages.	Disulfides	169-178	high mobility group box 1	Homo sapiens	179-184
32426849-5	2021	Disulfide HMGB1 levels increased concomitantly with IRI severity.	Disulfides	0-9	high mobility group box 1	Homo sapiens	10-15
32426849-6	2021	IRI+ pre-reperfusion biopsies contained macrophages with hyperacetylated, lysosomal disulfide-HMGB1 that increased post-reperfusion at sites of injury, paralleling increased histone acetyltransferase GTF3C4 and decreased histone deacetylase HDAC5 expression.	Disulfides	84-93	high mobility group box 1	Homo sapiens	94-99
3924595-4	1985	Prochymosin is a monomeric protein containing three disulfide bridges.	Disulfides	52-61	chymosin	Bos taurus	0-11
32426849-7	2021	Purified disulfide-HMGB1 or IRI+ blood stimulated further production of disulfide-HMGB1 and increased pro-inflammatory molecule and cytokine expression in macrophages via a positive feedback loop.	Disulfides	9-18	high mobility group box 1	Homo sapiens	19-24
32426849-7	2021	Purified disulfide-HMGB1 or IRI+ blood stimulated further production of disulfide-HMGB1 and increased pro-inflammatory molecule and cytokine expression in macrophages via a positive feedback loop.	Disulfides	9-18	high mobility group box 1	Homo sapiens	82-87
32426849-7	2021	Purified disulfide-HMGB1 or IRI+ blood stimulated further production of disulfide-HMGB1 and increased pro-inflammatory molecule and cytokine expression in macrophages via a positive feedback loop.	Disulfides	72-81	high mobility group box 1	Homo sapiens	19-24
32426849-7	2021	Purified disulfide-HMGB1 or IRI+ blood stimulated further production of disulfide-HMGB1 and increased pro-inflammatory molecule and cytokine expression in macrophages via a positive feedback loop.	Disulfides	72-81	high mobility group box 1	Homo sapiens	82-87
32426849-8	2021	CONCLUSIONS: These data identify disulfide-HMGB1 as a mechanistic biomarker of, and therapeutic target for, minimizing sterile inflammation during human liver IRI.	Disulfides	33-42	high mobility group box 1	Homo sapiens	43-48
125109-2	1975	Molecular model of the plasmin-resistant disulfide knot in monomeric fragment D. A mixture of fragments D, derived from fibrinogen by plasmic degradation, was S-reduced and carboxymethylated.	Disulfides	41-50	plasminogen	Homo sapiens	23-30
1169964-1	1975	The insertion of a second disulfide bridge into native pig heart lipoamide dehydrogenase, requires two Cu-2+ ions for each catalytic center inactivated under anaerobic conditions.	Disulfides	26-35	dihydrolipoamide dehydrogenase	Sus scrofa	65-88
3924595-9	1985	The presence of intermolecular disulfides probably contributes to the difficulty of solubilizing recombinant prochymosin during its purification from E. coli.	Disulfides	31-41	chymosin	Bos taurus	109-120
4019439-6	1985	The purified enzyme utilized some disulfides including S-sulfocysteine, alpha-chymotrypsin, trypsin, bovine serum albumin, and insulin as substrates in the presence of GSH.	Disulfides	34-44	insulin	Oryctolagus cuniculus	127-134
1126937-8	1975	These results suggest that J chain is disulfide-bonded to only two of the subunits of polymeric IgA and that the remaining subunits in the higher polymers are disulfide-bonded one to the other.	Disulfides	38-47	joining chain of multimeric IgA and IgM	Homo sapiens	27-34
123195-1	1975	The biologically active component of plasmin digested human growth hormone consisted of residues 1-134 attached to residues 141-191 by the disulfide bond between residues 53 and 165.	Disulfides	139-148	plasminogen	Homo sapiens	37-44
4422288-0	1974	Absence of interchain disulfide bridges in rabbit haptoglobin molecule.	Disulfides	22-31	haptoglobin	Oryctolagus cuniculus	50-61
33259849-5	2021	Moreover, the disulfide bond of CyD assisted nanoparticles with a drug by minimizing the interaction between the NIR dye and drug, and also by releasing the drug in a redox environment.	Disulfides	14-23	cytochrome b-245, beta polypeptide	Mus musculus	32-35
33447253-0	2020	The Arabidopsis Protein Disulfide Isomerase Subfamily M Isoform, PDI9, Localizes to the Endoplasmic Reticulum and Influences Pollen Viability and Proper Formation of the Pollen Exine During Heat Stress.	Disulfides	24-33	PDI-like 2-3	Arabidopsis thaliana	65-69
33375389-7	2020	In most cases, HMW-GSs with additional or less cysteines are related to the formation of relatively more or less interchain disulfide bonds and HMW-GSs also affect the gluten secondary structures, which in turn impact the end use qualities of dough.	Disulfides	124-133	cilia and flagella associated protein 97	Homo sapiens	15-18
3855550-2	1985	Human hemopexin (Mr approximately equal to 63,000) consists of a single polypeptide chain containing 439 amino acid residues with six intrachain disulfide bridges.	Disulfides	145-154	hemopexin	Homo sapiens	6-15
33297586-3	2020	Here, we introduced synonymous codon substitutions in the N-terminal region encoding sequence of hFGF19 and co-expressed disulfide bond isomerase (DeltassDsbC) to functionally express hFGF19 without any fusion protein.	Disulfides	121-130	fibroblast growth factor 19	Homo sapiens	184-190
4202845-2	1973	Under these conditions, which selectively cleave intersubunit disulfides, J chain was released.	Disulfides	62-72	joining chain of multimeric IgA and IgM	Homo sapiens	74-81
6525342-8	1984	Mild tryptic digestion of disulfide-cross-linked long S2, under conditions that resulted in partial production of short S2 from un-cross-linked LS2, produced peptides T1a and T1b (residues 1 to approximately 360), with one and two disulfide cross-links, respectively.	Disulfides	26-35	serpin family D member 1	Homo sapiens	144-147
4113888-5	1972	Treatment of the virus with beta-mercaptoethanol and iodination experiments suggest that VP1 and VP2 might exist as compact structures cross-linked with disulfide bonds, perhaps forming the capsid.	Disulfides	153-162	hypothetical protein	Macaca mulatta polyomavirus 1	97-100
32878739-15	2020	These results indicate that PDIa4 affects the production of monoclonal antibodies by catalyzing disulfide bond formation in these antibodies in CHO cells.	Disulfides	96-105	protein disulfide-isomerase A4	Cricetulus griseus	28-33
6438823-1	1984	A highly purified, multimeric factor VIII complex composed of VIII: vWF and some factor VIII: C contained about 100 disulfides per subunit of Mr 260,000.	Disulfides	116-126	cytochrome c oxidase subunit 8A	Homo sapiens	62-66
33933962-6	2021	UPA further inhibited the formation of disulfide bonds of myosin head and increased gel firmness.	Disulfides	39-48	myosin, heavy chain 7B, cardiac muscle, beta	Gallus gallus	58-64
6438823-2	1984	Limited reduction of disulfide bonds in this complex by NADPH, thioredoxin reductase and thioredoxin leads to partial disaggregation of the multimeric VIII:vWF with concomitant loss of its platelet agglutinating activity in the presence of ristocetin, and with dissociation of factor VIII:C from the complex.	Disulfides	21-30	cytochrome c oxidase subunit 8A	Homo sapiens	151-155
6438823-2	1984	Limited reduction of disulfide bonds in this complex by NADPH, thioredoxin reductase and thioredoxin leads to partial disaggregation of the multimeric VIII:vWF with concomitant loss of its platelet agglutinating activity in the presence of ristocetin, and with dissociation of factor VIII:C from the complex.	Disulfides	21-30	cytochrome c oxidase subunit 8A	Homo sapiens	284-288
33037145-0	2020	M-type Thioredoxins Regulate the PGR5/PGRL1-dependent Pathway by Forming a Disulfide-linked Complex with PGRL1.	Disulfides	75-84	proton gradient regulation 5	Arabidopsis thaliana	33-37
6725264-1	1984	Rabbit haptoglobin is a tetrameric protein consisting of two nonglycosylated alpha and two glycosylated beta chains, the latter being joined to the former and the former to each other by disulfide linkages.	Disulfides	187-196	haptoglobin	Oryctolagus cuniculus	7-18
32848019-6	2020	The in vitro studies using recombinant proteins from Arabidopsis thaliana showed that a specific PGDH isoform, PGDH1, forms the intramolecular disulfide bond under non-reducing conditions, which lowers PGDH enzyme activity.	Disulfides	143-152	D-3-phosphoglycerate dehydrogenase	Arabidopsis thaliana	111-116
33601276-10	2021	Moreover, Alb reacted with GSH/GSSG via thiol-disulfide exchange and reciprocally regulated the availability of -SH groups.	Disulfides	46-55	albumin	Mus musculus	10-13
6324613-2	1984	The free thiol is a mucolytic compound which acts via the reduction of disulfide bonds of mucin molecules.	Disulfides	71-80	LOC100508689	Homo sapiens	90-95
33891658-2	2021	The membrane (glyco)proteins GP5 and M form a disulfide-linked dimer, which is a major component of virions.	Disulfides	46-55	glycoprotein V platelet	Sus scrofa	29-32
32848019-7	2020	Mass spectrometry and site-directed mutagenesis analyses allowed us to identify the redox-active Cys pair that is mainly involved in disulfide bond formation in PGDH1; this Cys pair is uniquely found in land plant PGDH.	Disulfides	133-142	D-3-phosphoglycerate dehydrogenase	Arabidopsis thaliana	161-166
6194153-6	1983	The half-time of disappearance of disulfide linked insulin-receptor complexes (I-(S-S)-R) was rapid (4.5 min), consistent with their hypothesized role.	Disulfides	34-43	insulin receptor	Homo sapiens	51-67
33103597-6	2022	We show that the Cys33-Cys33 intermolecular disulfide bridge that stabilizes the Hp1:Hp1 complex is replaced by the Phe33, Pro34, and Phe48 hydrophobic core in the Hpr:Hpr dimer.	Disulfides	44-53	haptoglobin-related protein	Homo sapiens	164-167
33103597-6	2022	We show that the Cys33-Cys33 intermolecular disulfide bridge that stabilizes the Hp1:Hp1 complex is replaced by the Phe33, Pro34, and Phe48 hydrophobic core in the Hpr:Hpr dimer.	Disulfides	44-53	haptoglobin-related protein	Homo sapiens	168-171
33903070-7	2021	NME1 is also found covalently modified by CoA (CoAlation) at Cys109 in the CoAlome analysis of HEK293/Pank1beta cells treated with the disulfide-stress inducer, diamide.	Disulfides	135-144	NME/NM23 nucleoside diphosphate kinase 1	Homo sapiens	0-4
6219896-8	1983	Apo B and Lp(a)-protein seem to be linked by disulfide bonds in the native lipoprotein.	Disulfides	45-54	lipoprotein(a)	Homo sapiens	10-15
32815200-5	2020	We show that AK2 is a substrate of the mitochondrial disulfide relay, thus lacking an N-terminal mitochondrial targeting sequence and undergoing comparatively slow import.	Disulfides	53-62	adenylate kinase 2	Homo sapiens	13-16
6296105-5	1983	Intoxication by TRH-CRM45 was prevented by excess TRH, preincubation with diphtheria antitoxin, or reduction of the disulfide cross-link.	Disulfides	116-125	thyrotropin releasing hormone	Rattus norvegicus	16-19
32737467-5	2020	Here we have designed mutations in S that allow the production of thermostable, disulfide-bonded S-protein trimers that are trapped in the closed, prefusion state.	Disulfides	80-89	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	35-36
32737467-6	2020	Structures of the disulfide-stabilized and non-disulfide-stabilized proteins reveal distinct closed and locked conformations of the S trimer.	Disulfides	18-27	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	0-1
33607928-0	2021	Salmonella enterica BcfH is a trimeric thioredoxin-like bifunctional enzyme with both thiol oxidase and disulfide isomerase activities.	Disulfides	104-113	thioredoxin	Bos taurus	39-50
33607928-3	2021	In bacteria, the thioredoxin-like disulfide bond (Dsb) family mediates the oxidative folding of multiple proteins required for fitness and pathogenic potential.	Disulfides	34-43	thioredoxin	Bos taurus	17-28
33607928-5	2021	This contrasts with the eukaryotic disulfide forming machinery where the modular thioredoxin protein PDI mediates thiol oxidation and disulfide reshuffling.	Disulfides	35-44	thioredoxin	Bos taurus	81-92
33607928-5	2021	This contrasts with the eukaryotic disulfide forming machinery where the modular thioredoxin protein PDI mediates thiol oxidation and disulfide reshuffling.	Disulfides	134-143	thioredoxin	Bos taurus	81-92
32979223-9	2021	These findings led us to propose that ROS levels modulate RAGE and/or TLR4-mediated inflammatory allodynia by regulating the concentrations of disulfide HMGB1 or all-thiol HMGB1.	Disulfides	143-152	high mobility group box 1	Mus musculus	153-158
33620491-3	2021	Two conserved cysteines forming intra- or intermolecular disulfide bonds in the lumenal domain of STN7 are essential for the kinase activity although it is still unknown how activation of the kinase is regulated.	Disulfides	57-66	Serine/Threonine kinase domain protein	Arabidopsis thaliana	98-102
33620491-5	2021	LTO1 contains thioredoxin (TRX)-like and VKOR domains which are related to the disulfide-bond-formation (Dsb) system in bacteria.	Disulfides	79-88	thioredoxin H-type 1	Arabidopsis thaliana	14-25
33620491-5	2021	LTO1 contains thioredoxin (TRX)-like and VKOR domains which are related to the disulfide-bond-formation (Dsb) system in bacteria.	Disulfides	79-88	thioredoxin H-type 1	Arabidopsis thaliana	27-30
33539422-13	2021	An up-shift in the HIF-1alpha band by the overexpression of PDI was detected, suggesting that PDI formed disulfide bond in HIF-1alpha.	Disulfides	105-114	prolyl 4-hydroxylase subunit beta	Homo sapiens	60-63
33539422-13	2021	An up-shift in the HIF-1alpha band by the overexpression of PDI was detected, suggesting that PDI formed disulfide bond in HIF-1alpha.	Disulfides	105-114	prolyl 4-hydroxylase subunit beta	Homo sapiens	94-97
33539422-14	2021	HIF-1alpha oxidized by PDI was not degraded in HSC70-knockdown cells, indicating that the formation of disulfide bond in HIF-1alpha was important for decreases in HIF-1alpha expression.	Disulfides	103-112	prolyl 4-hydroxylase subunit beta	Homo sapiens	23-26
33539422-16	2021	We also demonstrated that PDI formed disulfide bonds in HIF-1alpha 1-245 aa and decreased its expression.	Disulfides	37-46	prolyl 4-hydroxylase subunit beta	Homo sapiens	26-29
32737467-6	2020	Structures of the disulfide-stabilized and non-disulfide-stabilized proteins reveal distinct closed and locked conformations of the S trimer.	Disulfides	47-56	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	0-1
32830969-1	2020	Disulfide bond formation is a critical post-translational modification of newly synthesized polypeptides in the oxidizing environment of the endoplasmic reticulum and is mediated by protein disulfide isomerase (PDIA1).	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	182-209
32830969-1	2020	Disulfide bond formation is a critical post-translational modification of newly synthesized polypeptides in the oxidizing environment of the endoplasmic reticulum and is mediated by protein disulfide isomerase (PDIA1).	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	211-216
32971737-1	2020	P2 x 4R is allosterically modulated by Zn(II), and despite the efforts to understand the mechanism, there is not a consensus proposal; C132 is a critical amino acid for the Zn(II) modulation, and this residue is located in the receptor head domain, forming disulfide SS3.	Disulfides	257-266	purinergic receptor P2X 4	Homo sapiens	0-7
32848143-3	2020	Here we show that an ER protein disulfide isomerase, thioredoxin domain containing 5 (TXNDC5), is highly upregulated in the lung tissues from both patients with idiopathic pulmonary fibrosis and a mouse model of bleomycin (BLM)-induced PF.	Disulfides	32-41	epiregulin	Homo sapiens	21-23
6810885-0	1982	Copper inhibition of glutathione reductase and its reversal with gold thiolates, thiol, and disulfide compounds.	Disulfides	92-101	glutathione-disulfide reductase	Homo sapiens	21-42
32824977-5	2020	The in silico structural model predicted five beta-strands stabilized by four intramolecular disulfide bonds in PAFC.	Disulfides	93-102	PAFC	Homo sapiens	112-116
33314217-3	2021	Under stress conditions, TFEB-C212 undergoes oxidation, allowing the formation of intermolecular disulfide bonds that result in TFEB oligomerization.	Disulfides	97-106	transcription factor EB	Homo sapiens	25-29
33314217-3	2021	Under stress conditions, TFEB-C212 undergoes oxidation, allowing the formation of intermolecular disulfide bonds that result in TFEB oligomerization.	Disulfides	97-106	transcription factor EB	Homo sapiens	128-132
33161042-4	2021	We showed that GC1 activity is modulated via mixed-disulfide bond by protein disulfide isomerase and thioredoxin 1.	Disulfides	51-60	prolyl 4-hydroxylase subunit beta	Homo sapiens	69-96
6980121-5	1982	Hydrolysis of labeled C3b (Mr = 175000) by solubilized human erythrocyte membranes led to the formation of a split product of Mr = 35000 consisting of two disulfide-linked polypeptide chains of Mr = 17000.	Disulfides	155-164	endogenous retrovirus group K member 3	Homo sapiens	22-25
33409271-3	2020	The receptor-binding domain (RBD) of the 2019-nCoV spike (S) protein contains disulfide bonds and N-linked glycosylations, therefore, it is typically produced by secretion.	Disulfides	78-87	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	51-56
32453609-3	2020	Lp(a) is a low-density lipoprotein with an added apolipoprotein(a) attached to the apolipoprotein B component via a disulfide bond.	Disulfides	116-125	lipoprotein(a)	Homo sapiens	0-5
32453609-3	2020	Lp(a) is a low-density lipoprotein with an added apolipoprotein(a) attached to the apolipoprotein B component via a disulfide bond.	Disulfides	116-125	lipoprotein(a)	Homo sapiens	49-66
6276531-6	1982	When incubated with whole sputum or with purified mucin solutions in vitro, MDP decreased the viscosity of these solutions by reduction of the accessible disulfide bonds of the mucin molecule and was subsequently found in mixed disulfide association with the mucin molecule.	Disulfides	154-163	LOC100508689	Homo sapiens	50-55
33397549-0	2020	Enhanced Suppression of Disulfide Cross-Linking Micelles Nanocarriers Loaded miR-145 Delivering System via Down-Regulation of MYC and FSCN1 in Colon Cancer Cells.	Disulfides	24-33	fascin actin-bundling protein 1	Homo sapiens	134-139
33409271-3	2020	The receptor-binding domain (RBD) of the 2019-nCoV spike (S) protein contains disulfide bonds and N-linked glycosylations, therefore, it is typically produced by secretion.	Disulfides	78-87	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	58-59
32810779-7	2020	In particular, the dynamical study reveals that the redox reaction between oxidized AtGPX3 and reduced AtTRXh9 is realized through the forming and breaking of disulfide bonds via the active sites of Cys4 and Cys57 in AtTRXh9.	Disulfides	159-168	glutathione peroxidase 3	Arabidopsis thaliana	84-90
32681182-3	2020	Protein disulfide isomerase (PDI) is a member of the thioredoxin (Trx) superfamily, is capable of catalyzing the formation and heterogeneity of protein disulfide bonds and inhibiting the aggregation of misfolded proteins.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
6276531-6	1982	When incubated with whole sputum or with purified mucin solutions in vitro, MDP decreased the viscosity of these solutions by reduction of the accessible disulfide bonds of the mucin molecule and was subsequently found in mixed disulfide association with the mucin molecule.	Disulfides	154-163	LOC100508689	Homo sapiens	177-182
32810779-7	2020	In particular, the dynamical study reveals that the redox reaction between oxidized AtGPX3 and reduced AtTRXh9 is realized through the forming and breaking of disulfide bonds via the active sites of Cys4 and Cys57 in AtTRXh9.	Disulfides	159-168	thioredoxin H-type 9	Arabidopsis thaliana	103-110
32810779-7	2020	In particular, the dynamical study reveals that the redox reaction between oxidized AtGPX3 and reduced AtTRXh9 is realized through the forming and breaking of disulfide bonds via the active sites of Cys4 and Cys57 in AtTRXh9.	Disulfides	159-168	Cystatin/monellin superfamily protein	Arabidopsis thaliana	199-203
32810779-7	2020	In particular, the dynamical study reveals that the redox reaction between oxidized AtGPX3 and reduced AtTRXh9 is realized through the forming and breaking of disulfide bonds via the active sites of Cys4 and Cys57 in AtTRXh9.	Disulfides	159-168	thioredoxin H-type 9	Arabidopsis thaliana	217-224
32602810-5	2021	rBAT (heavy subunit; SLC3A1) and catalytic b0,+AT (light subunit; SLC7A9), linked by single disulfide bond, mediate renal reabsorption of cystine and dibasic amino acids in Na+ independent manner.	Disulfides	92-101	solute carrier family 3 member 1	Homo sapiens	21-27
6276531-6	1982	When incubated with whole sputum or with purified mucin solutions in vitro, MDP decreased the viscosity of these solutions by reduction of the accessible disulfide bonds of the mucin molecule and was subsequently found in mixed disulfide association with the mucin molecule.	Disulfides	154-163	LOC100508689	Homo sapiens	177-182
33230296-5	2020	UCP2-silenced KRASmut cell lines display decreased glutaminolysis, lower NADPH/NADP+ and glutathione/glutathione disulfide ratios and higher reactive oxygen species levels compared to wild-type counterparts.	Disulfides	113-122	uncoupling protein 2	Homo sapiens	0-4
7051704-7	1982	The evidence suggests that the inhibitory mechanism is based on an active sulfhydryl group of the inhibitor which may interact with the disulfide bridge of the inhibited proteinase.	Disulfides	136-145	endogenous retrovirus group K member 21, envelope	Homo sapiens	170-180
32768572-5	2020	Reduced recombinant human PDI (hPDI) reacted quickly with S-nitrosocompounds, with an observed increase in the expected S-nitrosylated species and the appearance of the disulfide state of the active sites.	Disulfides	169-178	prolyl 4-hydroxylase subunit beta	Homo sapiens	26-29
32670896-1	2020	Quiescin sulfhydryl oxidase (QSOX), present in a wide variety of eukaryotic species, catalyzes the insertion of disulfide bonds into unfolded, reduced proteins.	Disulfides	112-121	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	29-33
32630599-6	2020	Within recent years, the formation of disulfide-linked heterodimers was documented for TFF1 and TFF3, e.g., with gastrokine-2 and IgG Fc binding protein (FCGBP).	Disulfides	38-47	gastrokine 2	Mus musculus	113-125
6174078-0	1982	Human complex-forming glycoprotein, heterogeneous in charge: the primary structure around the cysteine residues and characterization of a disulfide bridge.	Disulfides	138-147	alpha-1-microglobulin/bikunin precursor	Homo sapiens	6-59
32587593-5	2020	We currently investigated that peroxiredoxins I and II (PrxI/II) induce the intramolecular disulfide bond formation of HMGB1 in the nucleus.	Disulfides	91-100	high mobility group box 1	Homo sapiens	119-124
32587593-6	2020	Disulfide HMGB1 is preferentially transported out of the nucleus by binding to the nuclear exportin chromosome-region maintenance 1 (CRM1).	Disulfides	0-9	high mobility group box 1	Homo sapiens	10-15
32587593-7	2020	We determined the kinetics of HMGB1 oxidation in bone marrow-derived macrophage as early as a few minutes after lipopolysaccharide treatment, peaking at 4 h while disulfide HMGB1 accumulation was observed within the cells, starting to secrete in the late time point.	Disulfides	163-172	high mobility group box 1	Homo sapiens	173-178
33544473-9	2021	Finally, the critical amino acids on CD25 were targeted by a de novo designed peptide with disulfide bond.	Disulfides	91-100	interleukin 2 receptor subunit alpha	Homo sapiens	37-41
6950391-1	1981	Thioredoxin and glutaredoxin may be important in regulating cell metabolism by mediating interchanges between sulfhydryl and disulfide groups.	Disulfides	125-134	glutaredoxin	Homo sapiens	16-28
32059843-6	2020	NTE trapping preserves OCP photocycling within the compact protein structure but precludes functional interaction with PBs and especially FRP, which is completely restored upon reduction of the disulfide bridge.	Disulfides	194-203	secreted frizzled related protein 1	Homo sapiens	138-141
33146213-5	2020	Meanwhile, changes in SDS-PAGE, FT-IR, and sulfhydryl contents showed that TGase increased the disulfide bond contents, whereas it decreased after EGCG was added, suggesting that EGCG could react with MP via non-covalent and covalent interactions.	Disulfides	95-104	transglutaminase 1	Homo sapiens	75-80
7217104-4	1981	Analyses of the mechanism of polymerization suggested that polymerizing enzyme is a sulfhydryl oxidase; it was found to be inactivated by chelating agents and to resemble Cu2+ in catalyzing the formation of IgM intersubunit disulfide bonds.	Disulfides	224-233	immunoglobulin kappa variable 1-35	Mus musculus	171-174
32201313-2	2020	Over 30% of proteins require the chaperone PDI to promote disulfide bond formation.	Disulfides	58-67	prolyl 4-hydroxylase subunit beta	Homo sapiens	43-46
32201313-3	2020	PDI oxidizes cysteines in nascent polypeptides to form disulfide bonds and can also reduce and isomerize disulfide bonds.	Disulfides	55-64	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
32201313-3	2020	PDI oxidizes cysteines in nascent polypeptides to form disulfide bonds and can also reduce and isomerize disulfide bonds.	Disulfides	105-114	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
33208461-2	2021	The coinherited Pattern D GAS-secreted streptokinase (SK2b) then accelerates cleavage of hPg at the R561-V562 peptide bond, resulting in the disulfide-linked two-chain protease, plasmin (hPm).	Disulfides	141-150	plasminogen	Homo sapiens	178-185
6893275-6	1980	The sign reversal is also present in a closely related disulfide enzyme, glutathione reductase, but absent in glucose oxidase.	Disulfides	55-64	glutathione-disulfide reductase	Homo sapiens	73-94
32297376-5	2020	Despite sharing this conserved ligand-binding module, IR and EGFR family members are considered mechanistically distinct-in part because IR is a disulfide-linked (alphabeta)2 dimer regardless of ligand binding, whereas EGFR is a monomer that undergoes ligand-induced dimerization.	Disulfides	145-154	insulin receptor	Homo sapiens	137-139
6998236-0	1980	A possible role of cytoplasmic thioltransferase in the intracellular degradation of disulfide-containing proteins.	Disulfides	84-93	glutaredoxin	Homo sapiens	31-47
33093204-0	2020	Amyloid formation of fish beta-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers.	Disulfides	84-93	oncomodulin	Homo sapiens	26-42
33093204-4	2020	We performed biophysical experiments in combination with mathematical modeling of aggregation kinetics and discovered that the aggregation of beta-parvalbumin is initiated by the formation of dimers stabilized by disulfide bonds and then proceeds via primary nucleation and fibril elongation processes.	Disulfides	213-222	oncomodulin	Homo sapiens	142-158
291908-8	1979	These results indicate that the insulin receptor of both liver and placenta has a subunit of molecular weight 135,000 that binds insulin and that the receptor may be composed of at least two different subunits that are linked together or greatly stabilized by disulfide bonds.	Disulfides	260-269	insulin receptor	Rattus norvegicus	32-48
32997203-7	2020	In concert, these proteins mediate disulfide transfer from H2O2 to target proteins via PDI-Gpx7 fusions.	Disulfides	35-44	glutathione peroxidase 7	Homo sapiens	91-95
32997205-5	2020	Analysis during production cell culture showed that increased GAPDH gene and protein expression correlated to disulfide reduction risk in HCCF in every case examined.	Disulfides	110-119	glyceraldehyde-3-phosphate dehydrogenase	Cricetulus griseus	62-67
31981247-1	2020	A distinguishing feature of camel (Camelus dromedarius) VHH domains are noncanonical disulfide bonds between CDR1 and CDR3.	Disulfides	85-94	LOW QUALITY PROTEIN: cerebellar degeneration-related antigen 1	Camelus dromedarius	109-113
32226330-3	2020	Cys401K10 formed a disulfide-linkage with Cys401 from another K1/10 heterodimer, creating an "X-shaped" structure and a loose crystal packing arrangement.	Disulfides	19-28	keratin 1	Homo sapiens	62-67
32226330-8	2020	We postulated that elimination of the disulfide linkage in the K1/K10(Cys401Ala) 2B structure could allow for the 2B heterodimers to bind/pack in the A22 tetramer configuration associated with mature keratin intermediate filament assembly.	Disulfides	38-47	keratin 1	Homo sapiens	63-69
32265930-5	2020	Disulfide HMGB1 activates the TLR4 complex by binding to MD-2.	Disulfides	0-9	high mobility group box 1	Homo sapiens	10-15
32871222-6	2020	There was convergence between nonhomologous eutherian supercluster IF1 and supercluster IF2 protein primary structures including common cysteine amino acid residues implicated in disulfide bonding.	Disulfides	179-188	eukaryotic translation initiation factor 5B	Homo sapiens	88-91
24408196-12	1978	L-2 posesses a total of 8 cysteine molecules with only one disulfide bond.	Disulfides	59-68	seed linoleate 9S-lipoxygenase-2	Glycine max	0-3
33077910-6	2020	Cell surface Cnx-ERp57 complexes reduce these extracellular disulfide bonds and are essential for ECM degradation.	Disulfides	60-69	calnexin	Homo sapiens	13-16
33066432-9	2020	In fact, cleaving NMDAR disulfide bonds in neurons reversed the HCY-induced Ca2+ accumulation, making it dependent on GluN2B- rather than GluN2A-containing NMDARs.	Disulfides	24-33	glutamate ionotropic receptor NMDA type subunit 2B	Homo sapiens	118-124
32110281-1	2020	The sequence asparagine-glycine arginine (NGR), flanked by Cysteine (Cys) residues so as to form a disulfide-bridge (CNGRC), has previously been found to target and bind specifically to aminopeptidase N (APN), which is highly expressed on the surface of tumor cells.	Disulfides	99-108	alanyl aminopeptidase, membrane	Homo sapiens	186-202
32110281-1	2020	The sequence asparagine-glycine arginine (NGR), flanked by Cysteine (Cys) residues so as to form a disulfide-bridge (CNGRC), has previously been found to target and bind specifically to aminopeptidase N (APN), which is highly expressed on the surface of tumor cells.	Disulfides	99-108	alanyl aminopeptidase, membrane	Homo sapiens	204-207
863928-2	1977	A mixed disulfide reagent for photolabeling is described which reacts stoichiometrically with a cysteine sulfhydryl group of rabbit muscle creatine kinase to form a new mixed disulfide between enzyme and 2-thiobenzyl[14C]diazoacetate.	Disulfides	8-17	creatine kinase M-type	Oryctolagus cuniculus	132-154
31939472-2	2020	In addition, the ground and excited state absorption spectra of bis(2-naphthyl)disulfide with or without NEt3 suggested the Lewis acidity of bis(2-naphthyl)disulfide upon photo-irradiation.	Disulfides	141-165	tetraspanin 2	Homo sapiens	105-109
32038043-3	2020	Here, the crystal structure of the thrombospondin module 1 (TSP1) domain of CCN3 (previously known as Nov) is presented, which shares a similar three-stranded fold with the thrombospondin type 1 repeats of thrombospondin-1 and spondin-1, but with variations in the disulfide connectivity.	Disulfides	265-274	spondin 1	Homo sapiens	213-222
32993041-3	2020	The human HAT 4F2hc-LAT2 is composed of the type-II membrane N-glycoprotein 4F2hc (SCL3A2) and the L-type amino acid transporter LAT2 (SLC7A8), which are covalently linked to each other by a conserved disulfide bridge.	Disulfides	201-210	linker for activation of T cells family member 2	Homo sapiens	20-24
32993041-3	2020	The human HAT 4F2hc-LAT2 is composed of the type-II membrane N-glycoprotein 4F2hc (SCL3A2) and the L-type amino acid transporter LAT2 (SLC7A8), which are covalently linked to each other by a conserved disulfide bridge.	Disulfides	201-210	linker for activation of T cells family member 2	Homo sapiens	129-133
863928-2	1977	A mixed disulfide reagent for photolabeling is described which reacts stoichiometrically with a cysteine sulfhydryl group of rabbit muscle creatine kinase to form a new mixed disulfide between enzyme and 2-thiobenzyl[14C]diazoacetate.	Disulfides	175-184	creatine kinase M-type	Oryctolagus cuniculus	132-154
137901-5	1977	The data presented in this paper reveal that initially an internal peptide bond of plasminogen (in the complex) is cleaved to yield a two-chain, disulfide-linked plasmin molecule.	Disulfides	145-154	plasminogen	Homo sapiens	83-90
32686399-4	2020	Herein, we use a peptide ligase, butelase 1, to label the human transferrin receptor 1 (TfR1) in established human cell lines with a designer disulfide FRET probe.	Disulfides	142-151	transferrin receptor	Homo sapiens	64-86
32686399-4	2020	Herein, we use a peptide ligase, butelase 1, to label the human transferrin receptor 1 (TfR1) in established human cell lines with a designer disulfide FRET probe.	Disulfides	142-151	transferrin receptor	Homo sapiens	88-92
32004955-2	2020	Ahp1 assembles into a homodimer that detoxifies peroxides via forming intersubunit disulfides between peroxidatic and resolving cysteines that are subsequently reduced by the thioredoxin system.	Disulfides	83-93	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	0-4
839859-5	1977	The calculations indicate that (i) under denaturing conditions, reduced trypsin inhibitor when oxidized should form initially 14 of the 15 possible single disulfide bridge intermediates in roughly equal proportions, and (ii) under renaturing conditions (pH 8.7, room temperature, aqueous solution) the single disulfide bridge intermediate with cys 30 and cys 51 connected is present in higher concentration than that with cys 30 and cys 55 linked.	Disulfides	155-164	cysteine rich secretory protein LCCL domain containing 2	Homo sapiens	72-89
31590044-9	2020	Addition of NADPH after BQ pre-treatment could resolve the disulfide-linked crosslinking.	Disulfides	59-68	2,4-dienoyl CoA reductase 1, mitochondrial	Mus musculus	12-17
32771683-6	2020	High Mobility Group Box 1 (HMGB1) is a mediator of lethality in trauma and sepsis and our mechanistic studies revealed that disulfide and oxidized forms of HMGB1 bind to the gp91phox subunit of NOX2, and thus decrease the neutrophil respiratory burst and bacterial killing.	Disulfides	124-133	high mobility group box 1	Homo sapiens	0-25
32771683-6	2020	High Mobility Group Box 1 (HMGB1) is a mediator of lethality in trauma and sepsis and our mechanistic studies revealed that disulfide and oxidized forms of HMGB1 bind to the gp91phox subunit of NOX2, and thus decrease the neutrophil respiratory burst and bacterial killing.	Disulfides	124-133	high mobility group box 1	Homo sapiens	27-32
31891077-4	2019	These residues are also responsible for connecting the two beta-sheets together, by being part of beta2 and beta4, respectively, and together with disulfide bridges, they create CBM14"s characteristic "hevein-like" fold.	Disulfides	147-156	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	98-103
839859-5	1977	The calculations indicate that (i) under denaturing conditions, reduced trypsin inhibitor when oxidized should form initially 14 of the 15 possible single disulfide bridge intermediates in roughly equal proportions, and (ii) under renaturing conditions (pH 8.7, room temperature, aqueous solution) the single disulfide bridge intermediate with cys 30 and cys 51 connected is present in higher concentration than that with cys 30 and cys 55 linked.	Disulfides	309-318	cysteine rich secretory protein LCCL domain containing 2	Homo sapiens	72-89
31891077-4	2019	These residues are also responsible for connecting the two beta-sheets together, by being part of beta2 and beta4, respectively, and together with disulfide bridges, they create CBM14"s characteristic "hevein-like" fold.	Disulfides	147-156	tubulin beta 3 class III	Homo sapiens	108-113
841616-0	1977	Synthesis of a disulfide affinity adsorbent for purification of estrogen receptor.	Disulfides	15-24	estrogen receptor 1	Bos taurus	64-81
31651920-0	2019	A rational approach to form disulfide linked mucin hydrogels.	Disulfides	28-37	LOC100508689	Homo sapiens	45-50
31651920-2	2019	By using a cross-linking reagent capable of forming hydrogen bonds and disulfide linkages within the gel network, we were able to produce mucin-based hydrogels with viscoelastic properties similar to natural mucus as measured by bulk rheology.	Disulfides	71-80	LOC100508689	Homo sapiens	138-143
31651920-3	2019	We confirmed disulfide cross-links strongly contribute to gel formation in our system using chemical treatments to block and reduce cysteines where we found mucin hydrogel network formation was inhibited and disrupted, respectively.	Disulfides	13-22	LOC100508689	Homo sapiens	157-162
32629276-2	2020	Because of structural similarity to the potent antimitotic natural product combretastatin A-4 (CA-4), the compounds were examined for inhibition of tubulin polymerization, and the thiosulfonates were more active than the disulfides.	Disulfides	221-231	carbonic anhydrase 4	Homo sapiens	95-99
32327487-10	2020	Moreover, in cells, MANF bound to a model ER protein exhibiting improper disulfide bond formation during reductive ER stress, but did not bind to this protein during non-reductive ER stress.	Disulfides	73-82	mesencephalic astrocyte-derived neurotrophic factor	Rattus norvegicus	20-24
186316-0	1976	Importance of interpeptide disulfide bond in a viral glycoprotein with hemagglutination and neuraminidase activities.	Disulfides	27-36	neuraminidase 1	Homo sapiens	92-105
32385162-3	2020	We determined the crystal structure of PEDF in complex with a disulfide cross-linked heterotrimeric collagen peptide, in which the alpha(I) chain segments-each containing the respective PEDF-binding region (residues 930 to 938)-are assembled with an alpha2alpha1alpha1 staggered configuration.	Disulfides	62-71	serpin family F member 1	Homo sapiens	39-43
30477399-0	2019	Rectification ratio based determination of disulfide bonds of beta2 extracellular loop of BK channel.	Disulfides	43-52	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	62-67
30477399-5	2019	To address this, based on the fact that the rectification and association of BK alpha to beta2 subunits are highly sensitive to disruption of the disulfide bonds in the extracellular loop of beta2, we developed a rectification ratio based assay by combining the site-directed mutagenesis, electrophysiology and enzymatic cleavage.	Disulfides	146-155	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	89-94
30477399-5	2019	To address this, based on the fact that the rectification and association of BK alpha to beta2 subunits are highly sensitive to disruption of the disulfide bonds in the extracellular loop of beta2, we developed a rectification ratio based assay by combining the site-directed mutagenesis, electrophysiology and enzymatic cleavage.	Disulfides	146-155	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	191-196
30477399-6	2019	Three disulfide bonds: C1(C84)-C5(C113), C3(C101)-C7(C148) and C6(C142)-C8C(174) are successfully deduced in beta2 subunit in complex with a BK alpha subunit, which are helpful to predict structural model of beta2 subunits through computational simulation and to understand the interface between the extracellular domain of the beta subunits and the pore-forming alpha subunit.	Disulfides	6-15	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	109-114
30477399-6	2019	Three disulfide bonds: C1(C84)-C5(C113), C3(C101)-C7(C148) and C6(C142)-C8C(174) are successfully deduced in beta2 subunit in complex with a BK alpha subunit, which are helpful to predict structural model of beta2 subunits through computational simulation and to understand the interface between the extracellular domain of the beta subunits and the pore-forming alpha subunit.	Disulfides	6-15	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	208-213
10309-7	1976	Evidence is presented which indicates that PTP is assembled as a tube within the spore; that the ejected tube has plasticity during sporoplasm passage; and, finally, that the subunits within the tube polymer are bound together, in part, by interprotein disulfide linkages.	Disulfides	253-262	protein tyrosine phosphatase receptor type U	Homo sapiens	43-46
31419547-8	2019	Furthermore, tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) fusion with the third disulfide loop of TGF-alpha (TGF3L-TRAIL) fused with the NCTR25-tag retained the stability and superactivity of His-TGF3L-TRAIL.	Disulfides	105-114	transforming growth factor alpha	Homo sapiens	123-132
32039168-4	2019	Co-expression of a Hsp70 family molecular chaperone Kar2p and/or protein-disulfide isomerase (Pdi1p) significantly improved efficiency of functional display (defined as the ratio of cells displaying functional Fab over cells displaying assembled Fab).	Disulfides	73-82	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	94-99
32184018-2	2020	Previous study suggested that protein disulfide isomerase (PDI), an enzyme which catalyzes the formation and breakage of disulfide bonds in proteins, regulates AB5 toxin such as cholera toxin by unfolding of A subunit, leading to its translocation into cytosol to induce disease.	Disulfides	38-47	prolyl 4-hydroxylase subunit beta	Homo sapiens	59-62
32369015-0	2020	Keratin 14-dependent disulfides regulate epidermal homeostasis and barrier function via 14-3-3sigma and YAP1.	Disulfides	21-31	yes-associated protein 1	Mus musculus	104-108
1270440-10	1976	It is likely, but as yet unproven, that formation of disulfide I-VIII completes the cross-linking of lysozyme.	Disulfides	53-62	cytochrome c oxidase subunit 8A	Homo sapiens	65-69
32231310-5	2020	Limiting glucose supply to SLC7A11high cancer cells results in marked accumulation of intracellular cystine, redox system collapse and rapid cell death, which can be rescued by treatments that prevent disulfide accumulation.	Disulfides	201-210	solute carrier family 7 (cationic amino acid transporter, y+ system), member 11	Mus musculus	27-34
31570526-6	2019	Using immunoblotting with CLCA1-specific antibodies and recombinant proteins, we observed that the CLCA1 C-terminal self-cleavage product forms a disulfide-linked dimer that noncovalently interacts with the N-terminal part of CLCA1, which further interacts to form oligomers.	Disulfides	146-155	chloride channel accessory 1	Homo sapiens	26-31
31570526-6	2019	Using immunoblotting with CLCA1-specific antibodies and recombinant proteins, we observed that the CLCA1 C-terminal self-cleavage product forms a disulfide-linked dimer that noncovalently interacts with the N-terminal part of CLCA1, which further interacts to form oligomers.	Disulfides	146-155	chloride channel accessory 1	Homo sapiens	99-104
31570526-6	2019	Using immunoblotting with CLCA1-specific antibodies and recombinant proteins, we observed that the CLCA1 C-terminal self-cleavage product forms a disulfide-linked dimer that noncovalently interacts with the N-terminal part of CLCA1, which further interacts to form oligomers.	Disulfides	146-155	chloride channel accessory 1	Homo sapiens	99-104
815121-5	1976	These results indicate that the sequential degradative pathway is operative, both at low and high concentrations of insulin, in isolated liver cells, i.e., the insulin is first split at the disulfide bonds by glutathione-insulin transhydrogenase (GIT) into A and B chains, followed by proteolysis of the resultant polypeptides, and that this system might be used for well-defined studies of factors controlling insulin metabolism.	Disulfides	190-199	prolyl 4-hydroxylase subunit beta	Homo sapiens	209-245
31755157-8	2020	We then isolated recombinant BSD2 (rBSD2) from E. coli and found that rBSD2 reduces disulfide bonds using reductants present in vivo, e.g. glutathione, and that rBSD2 has the ability to reactivate Rubisco that has been inactivated by oxidants.	Disulfides	84-93	bundle sheath defective 2	Zea mays	29-33
32156734-2	2020	Its signaling cascade results in the formation of disulfide bond-dependent amyloid-like polymers of mixed lineage kinase domain-like protein (MLKL), which mediate proinflammatory cell membrane disruption.	Disulfides	50-59	mixed lineage kinase domain like pseudokinase	Homo sapiens	100-140
32156734-2	2020	Its signaling cascade results in the formation of disulfide bond-dependent amyloid-like polymers of mixed lineage kinase domain-like protein (MLKL), which mediate proinflammatory cell membrane disruption.	Disulfides	50-59	mixed lineage kinase domain like pseudokinase	Homo sapiens	142-146
30973786-10	2019	Normally, IL-33 is quickly inactivated by a post-translational disulfide bond formation.	Disulfides	63-72	interleukin 33	Homo sapiens	10-15
31448842-4	2019	In addition, mouse SVS contributes to the existence of sulfhydryl oxidase (Sox), which mediates the disulfide bond formation between cysteine residues.	Disulfides	100-109	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	55-73
31448842-4	2019	In addition, mouse SVS contributes to the existence of sulfhydryl oxidase (Sox), which mediates the disulfide bond formation between cysteine residues.	Disulfides	100-109	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	75-78
815121-5	1976	These results indicate that the sequential degradative pathway is operative, both at low and high concentrations of insulin, in isolated liver cells, i.e., the insulin is first split at the disulfide bonds by glutathione-insulin transhydrogenase (GIT) into A and B chains, followed by proteolysis of the resultant polypeptides, and that this system might be used for well-defined studies of factors controlling insulin metabolism.	Disulfides	190-199	prolyl 4-hydroxylase subunit beta	Homo sapiens	247-250
187878-7	1976	These results are discussed in terms of reported cycles and activations of glutathione reductase (GR) in cells and reports that mixed disulfides of glutathione and proteins can act as substrates for GR.	Disulfides	134-144	glutathione reductase	Mus musculus	199-201
31720508-9	2019	Density functional theory calculations highlighted the formation of the type-II" beta-turn on the four central residues of cFEE (i.e., -Ser2-Phe3-Glu4-Glu5-) either with a left- or with a right-handed disulfide.	Disulfides	201-210	jagged canonical Notch ligand 2	Homo sapiens	136-140
31720508-9	2019	Density functional theory calculations highlighted the formation of the type-II" beta-turn on the four central residues of cFEE (i.e., -Ser2-Phe3-Glu4-Glu5-) either with a left- or with a right-handed disulfide.	Disulfides	201-210	dihydrolipoamide dehydrogenase	Homo sapiens	141-145
31734460-1	2020	BACKGROUND: Extracellular surface protein disulfide isomerase-A1 (PDI) is involved in platelet aggregation, thrombus formation and vascular remodeling.	Disulfides	42-51	prolyl 4-hydroxylase subunit beta	Homo sapiens	66-69
4148072-0	1973	Cleavage of lens protein-GSH mixed disulfide by glutathione reductase.	Disulfides	35-44	glutathione-disulfide reductase	Homo sapiens	48-69
32564733-7	2020	We found that formation of the disulfide bond between Cys12 and Cys20 residues as a result of XRCC1 oxidation (previously shown to modulate the protein affinity for Polbeta), affects the yield of the final product of SP BER and of non-ligated DNA intermediates (substrates of long-patch BER).	Disulfides	31-40	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	165-172
31302867-6	2019	The CRM plays a critical role in the conformational change and self-interaction of NYE1 via the formation of inter- and intra-molecular disulfide bonds.	Disulfides	136-145	non-yellowing 1	Arabidopsis thaliana	83-87
33827045-6	2021	Thioredoxin reductase and glutathione reductase create new inter disulfide bonds.	Disulfides	65-74	glutathione-disulfide reductase	Homo sapiens	26-47
31228548-6	2019	Using an in vitro model system, we demonstrate that DHA causes disulfide bond formation within the active site of recombinant human glutaredoxin (Grx-1).	Disulfides	63-72	glutaredoxin	Homo sapiens	132-144
31228548-6	2019	Using an in vitro model system, we demonstrate that DHA causes disulfide bond formation within the active site of recombinant human glutaredoxin (Grx-1).	Disulfides	63-72	glutaredoxin	Homo sapiens	146-151
31899610-3	2020	These disulfide bonds are typically formed within the ER by a variety of oxidoreductases, including members of the protein disulfide isomerase (PDI) family.	Disulfides	6-15	prolyl 4-hydroxylase subunit beta	Homo sapiens	115-142
31899610-3	2020	These disulfide bonds are typically formed within the ER by a variety of oxidoreductases, including members of the protein disulfide isomerase (PDI) family.	Disulfides	6-15	prolyl 4-hydroxylase subunit beta	Homo sapiens	144-147
33157095-1	2021	Whey acidic protein Four-Disulfide Core (WFDC) proteins, such as PI3 and SLPI, inhibit proteases in the epidermis and other tissues.	Disulfides	25-34	peptidase inhibitor 3	Homo sapiens	65-68
32065582-0	2020	EDEM2 stably disulfide-bonded to TXNDC11 catalyzes the first mannose trimming step in mammalian glycoprotein ERAD.	Disulfides	13-22	ER degradation enhancing alpha-mannosidase like protein 2	Homo sapiens	0-5
32065582-4	2020	Here, we found that EDEM2 was stably disulfide-bonded to TXNDC11, an endoplasmic reticulum protein containing five thioredoxin (Trx)-like domains.	Disulfides	37-46	ER degradation enhancing alpha-mannosidase like protein 2	Homo sapiens	20-25
30238832-5	2019	From our findings, we hypothesize that disulfide A-box fragment binds as an anchor toward the TLR4-MD-2 but does not facilitate the TLR4 dimer formation, thereby competing with the HMGb1-binding site and preventing HMGb1-induced signaling and downstream inflammation, whereas the pro-inflammatory B-box fragment retains the MD-2 active conformation and binds to both TLR4 proteins in the complex to aid TLR4 dimer formation, which activates the intracellular signaling for downstream inflammatory pathways and cytokine release.	Disulfides	39-48	high mobility group box 1	Homo sapiens	181-186
30238832-5	2019	From our findings, we hypothesize that disulfide A-box fragment binds as an anchor toward the TLR4-MD-2 but does not facilitate the TLR4 dimer formation, thereby competing with the HMGb1-binding site and preventing HMGb1-induced signaling and downstream inflammation, whereas the pro-inflammatory B-box fragment retains the MD-2 active conformation and binds to both TLR4 proteins in the complex to aid TLR4 dimer formation, which activates the intracellular signaling for downstream inflammatory pathways and cytokine release.	Disulfides	39-48	high mobility group box 1	Homo sapiens	215-220
33906974-9	2021	Our data suggest that the oxidation of Cys206 prevented hyperactivation of STING by causing a conformational change associated with the formation of inactive polymers containing intermolecular disulfide bonds.	Disulfides	193-202	stimulator of interferon response cGAMP interactor 1	Homo sapiens	75-80
31284117-9	2019	Importantly, the disulfide-bond Cys58-Cys147 which is critical for the structural and functional integrity of ySOD1 was detected as being oxidized at Cys147.	Disulfides	17-26	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	110-115
31874828-1	2020	Protein disulfide isomerase (PDI), a chaperone protein mostly in endoplasmic reticulum, catalyzes disulfide bond breakage, formation, and rearrangement to promote protein folding.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
33721668-2	2021	Cetuximab conjugates consisting of CA4 derivatives were site-specially prepared by disulfide re-bridging approach using cleavable and non-cleavable linkers.	Disulfides	83-92	carbonic anhydrase 4	Homo sapiens	35-38
31995732-4	2020	The CLCA1 VWA contains a disulfide bond between alpha3 and alpha4 in close proximity to the MIDAS that is invariant in the CLCA family and unique in VWA structures.	Disulfides	25-34	chloride channel accessory 1	Homo sapiens	4-9
33463200-3	2020	Herein, we report branched modified nona-arginine (B-mR9) composed of redox-cleavable disulfide bonds to form stable complexes with methotrexate (MTX) as an anticancer agent, which is further coated with hyaluronic acid (HA).	Disulfides	86-95	eosinophil-associated, ribonuclease A family, member 9	Mus musculus	53-56
31266802-6	2019	Thioredoxin (Trx) and glutaredoxin (Grx) systems have been implicated as electron donors for the RNR disulfide reduction via the swinging arm.	Disulfides	101-110	glutaredoxin	Homo sapiens	22-34
31266802-6	2019	Thioredoxin (Trx) and glutaredoxin (Grx) systems have been implicated as electron donors for the RNR disulfide reduction via the swinging arm.	Disulfides	101-110	glutaredoxin	Homo sapiens	36-39
31387209-0	2019	SUSD2 Proteolytic Cleavage Requires the GDPH Sequence and Inter-Fragment Disulfide Bonds for Surface Presentation of Galectin-1 on Breast Cancer Cells.	Disulfides	73-82	sushi domain containing 2	Homo sapiens	0-5
33857433-6	2021	Disassembly of P5 to monomers compromised its ability to inactivate IRE1alpha via intermolecular disulfide bond reduction and its Ca2+-dependent regulation of chaperone function in vitro.	Disulfides	97-106	endoplasmic reticulum to nucleus signaling 1	Homo sapiens	68-77
31063765-2	2019	CACT transport activity, which was strongly impaired after oxidation by atmospheric O2 or H2O2, due to the formation of a disulfide bridge between cysteines 136 and 155, was restored by externally added polyphenols.	Disulfides	122-131	solute carrier family 25 member 20	Homo sapiens	0-4
31924219-15	2020	When the autophagy inducer, rapamycin, is used to facilitate the mitophagy flux, this treatment results in attenuated NF-kappaB activation and reduced PIC release in exogenous disulfide HMGB1 (ds-HMGB1)-stimulated microglia.	Disulfides	176-185	high mobility group box 1	Mus musculus	186-191
33755428-4	2021	The CD138 antibody-decorated herringbone chip with a disulfide linker was designed to enhance the collision probability between blood cells and capture antibodies, leading to high capture efficiency of CMCs.	Disulfides	53-62	syndecan 1	Homo sapiens	4-9
31892265-2	2019	Also, GILT catalyzes the reduction of disulfide bonds, which plays an important role in cellular immunity.	Disulfides	38-47	Gamma interferon responsive lysosomal thiol (GILT) reductase family protein	Arabidopsis thaliana	6-10
31080061-3	2019	The Mxra8 ectodomain contains two strand-swapped Ig-like domains oriented in a unique disulfide-linked head-to-head arrangement.	Disulfides	86-95	matrix remodeling associated 8	Homo sapiens	4-9
33718141-0	2021	Fermentation, Purification, and Tumor Inhibition of a Disulfide-Stabilized Diabody Against Fibroblast Growth Factor-2.	Disulfides	54-63	fibroblast growth factor 2	Mus musculus	91-117
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	90-99	glutaredoxin	Homo sapiens	59-71
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	90-99	glutaredoxin	Homo sapiens	73-76
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	171-180	glutaredoxin	Homo sapiens	59-71
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	171-180	glutaredoxin	Homo sapiens	73-76
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	171-180	glutaredoxin	Homo sapiens	59-71
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	171-180	glutaredoxin	Homo sapiens	73-76
31604106-1	2019	Human chorionic gonadotropin (hCG) is a glycoprotein hormone that exists as a heterodimer comprised of an alpha subunit and beta subunit linked with disulfide bridges.	Disulfides	149-158	glycoprotein hormones, alpha polypeptide	Homo sapiens	30-33
33718141-4	2021	A disulfide-stabilized diabody (ds-Diabody) against FGF-2 was produced in Pichia pastoris (GS115) by fermentation and the anti-tumor activity was analyzed.	Disulfides	2-11	fibroblast growth factor 2	Mus musculus	52-57
31839995-5	2019	At the protein level, DDAs alter DR5 disulfide bonding to increase steady-state DR5 levels and oligomerization, leading to downstream caspase 8 and 3 activation.	Disulfides	37-46	caspase 8	Homo sapiens	134-143
32773600-0	2021	Sex-dependent role of microglia in disulfide HMGB1-mediated mechanical hypersensitivity.	Disulfides	35-44	high mobility group box 1	Mus musculus	45-50
31418171-2	2019	HMGB1 has several redox states: reduced HMGB1 recruits inflammatory cells to injured tissues forming a heterocomplex with CXCL12 and signaling via its receptor CXCR4; disulfide-containing HMGB1 binds to TLR4 and promotes inflammatory responses.	Disulfides	167-176	high mobility group box 1	Homo sapiens	0-5
30658057-5	2019	The crystal structures of G23A-HNP4 and T27A-HNP4 were determined, both exhibiting a disulfide-stabilized canonical alpha-defensin dimer identical to wild-type HNP4.	Disulfides	85-94	defensin alpha 4	Homo sapiens	31-35
30544224-5	2019	Mutations in NCSTN are predicted to cause loss of function, to result in loss of transmembrane (TM) domain, to affect NCSTN substrate recruitment sites, to cause loss or creation of new ligand binging sites and to alter post-translational modifications and disulfide bonds.	Disulfides	257-266	nicastrin	Homo sapiens	13-18
32773600-4	2021	We found disulfide HMGB1 to equally increase microglial Iba-1 immunoreactivity in lumbar spinal dorsal horn in male and female mice, but evoke higher cytokine and chemokine expression in primary microglial culture derived from males compared to females.	Disulfides	9-18	high mobility group box 1	Mus musculus	19-24
32773600-6	2021	Spinal administration of the glial inhibitor, minocycline, with disulfide HMGB1 also prevented pain-like behavior in male mice.	Disulfides	64-73	high mobility group box 1	Mus musculus	74-79
30700553-0	2019	Disulfide engineering of human Kunitz-type serine protease inhibitors enhances proteolytic stability and target affinity toward mesotrypsin.	Disulfides	0-9	serine protease 3	Homo sapiens	128-139
30700553-5	2019	Substitution within the Kunitz inhibitor domain of the amyloid precursor protein (APPI) that incorporated a new disulfide bond between residues 17 and 34 reduced proteolysis by mesotrypsin 74-fold.	Disulfides	112-121	serine protease 3	Homo sapiens	177-188
33361333-5	2021	A covalent disulfide-linked dimer is formed through an N-terminal sequence specific to SARS-CoV-2, while a separate noncovalent interface is formed by another SARS-CoV-2-specific sequence, 73YIDI76 Together, the presence of these interfaces shows how SARS-CoV-2 ORF8 can form unique large-scale assemblies not possible for SARS-CoV, potentially mediating unique immune suppression and evasion activities.	Disulfides	11-20	ORF8 protein	Severe acute respiratory syndrome coronavirus 2	262-266
30700553-7	2019	Crystal structures of disulfide-engineered APPI and KD1TFPI1 variants in a complex with mesotrypsin at 1.5 and 2.0 A resolution, respectively, confirmed the formation of well-ordered disulfide bonds positioned to stabilize the binding loop.	Disulfides	22-31	serine protease 3	Homo sapiens	88-99
30700553-7	2019	Crystal structures of disulfide-engineered APPI and KD1TFPI1 variants in a complex with mesotrypsin at 1.5 and 2.0 A resolution, respectively, confirmed the formation of well-ordered disulfide bonds positioned to stabilize the binding loop.	Disulfides	183-192	serine protease 3	Homo sapiens	88-99
30700553-8	2019	Long all-atom molecular dynamics simulations of disulfide-engineered Kunitz domains and their complexes with mesotrypsin revealed conformational stabilization of the primed side of the inhibitor-binding loop by the engineered disulfide, along with global suppression of conformational dynamics in the Kunitz domain.	Disulfides	48-57	serine protease 3	Homo sapiens	109-120
30700553-8	2019	Long all-atom molecular dynamics simulations of disulfide-engineered Kunitz domains and their complexes with mesotrypsin revealed conformational stabilization of the primed side of the inhibitor-binding loop by the engineered disulfide, along with global suppression of conformational dynamics in the Kunitz domain.	Disulfides	226-235	serine protease 3	Homo sapiens	109-120
30893592-6	2019	Using pharmacological inhibition, we further show that PDI function is required in human cells for Wnt3a secretion, revealing a conserved role for disulfide isomerases.	Disulfides	147-156	prolyl 4-hydroxylase subunit beta	Homo sapiens	55-58
30893592-6	2019	Using pharmacological inhibition, we further show that PDI function is required in human cells for Wnt3a secretion, revealing a conserved role for disulfide isomerases.	Disulfides	147-156	Wnt family member 3A	Homo sapiens	99-104
31085544-8	2019	Collectively, these in vitro experiments demonstrate that TRX as well as GRX can catalyze the cleavage of disulfide bonds in both small molecules and linkers of ADCs.	Disulfides	106-115	glutaredoxin	Homo sapiens	73-76
31417095-5	2019	Unlike previously reported semaphorin structures, Sema1a, Sema2a and Sema2b show stabilisation of sema domain dimer formation via a disulfide bond.	Disulfides	132-141	Semaphorin 2a	Drosophila melanogaster	58-64
31417095-5	2019	Unlike previously reported semaphorin structures, Sema1a, Sema2a and Sema2b show stabilisation of sema domain dimer formation via a disulfide bond.	Disulfides	132-141	Semaphorin 2b	Drosophila melanogaster	69-75
31292775-8	2019	Only complete Sod1 activation (i.e. active site copper delivery and intra-subunit disulfide bond formation) breaks the Sod1 Ccs Ctr1c complex.	Disulfides	82-91	copper chaperone for superoxide dismutase	Homo sapiens	124-127
31417599-12	2019	The activity of oxidized AtAMY3 was completely restored by simultaneous reduction by both glutaredoxin (specific for the removal of glutathione-mixed disulfide) and thioredoxin (specific for the reduction of protein disulfide), supporting a possible liaison between both redox modifications.	Disulfides	216-225	thioredoxin H-type 1	Arabidopsis thaliana	165-176
31230712-3	2019	Disease-causing hyperactive STING mutations either flank C148 and depend on disulfide formation or reside in the C-terminal tail binding site and cause constitutive C-terminal tail release and polymerization.	Disulfides	76-85	stimulator of interferon response cGAMP interactor 1	Homo sapiens	28-33
30586735-3	2019	Here, we established the role of platelet-derived protein disulfide isomerase (PDI) in reducing the allosteric disulfide bonds in GPIbalpha and enhancing the ligand-binding activity under thromboinflammatory conditions.	Disulfides	58-67	glycoprotein 1b, alpha polypeptide	Mus musculus	130-139
30586735-4	2019	METHODS: Bioinformatic analysis identified 2 potential allosteric disulfide bonds in GPIbalpha.	Disulfides	66-75	glycoprotein 1b, alpha polypeptide	Mus musculus	85-94
33431842-3	2021	To support ongoing vaccine development efforts, we report the structure-based design of soluble S trimers with increased yields and stabilities, based on introduction of single point mutations and disulfide-bridges.	Disulfides	197-206	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	96-97
30586735-9	2019	PDI directly bound to the extracellular domain of GPIbalpha on the platelet surface and reduced the Cys4-Cys17 and Cys209-Cys248 disulfide bonds.	Disulfides	129-138	glycoprotein 1b, alpha polypeptide	Mus musculus	50-59
30586735-12	2019	CONCLUSIONS: Our results demonstrate that PDI-facilitated cleavage of the allosteric disulfide bonds tightly regulates GPIbalpha function, promoting platelet-neutrophil interactions, vascular occlusion, and tissue damage under thromboinflammatory conditions.	Disulfides	85-94	glycoprotein 1b, alpha polypeptide	Mus musculus	119-128
31151791-3	2019	We herein present the stereospecific synthesis of covalently binding disulfide ligands based on the pharmacophores of adrenergic beta1- and beta2 receptor antagonists.	Disulfides	69-78	adrenoceptor beta 1	Homo sapiens	118-154
33431872-3	2021	Biophysical properties of mucus are controlled by mucin glycoproteins that polymerize covalently via disulfide bonds.	Disulfides	101-110	LOC100508689	Homo sapiens	50-55
33431872-5	2021	Here we show that reducing mucin disulfide bonds disrupts mucus in human asthmatics and reverses pathological effects of mucus hypersecretion in a mouse allergic asthma model.	Disulfides	33-42	LOC100508689	Homo sapiens	27-32
30782819-9	2019	We achieved complete durable remissions when treating mice with H929-GFP-luc cells with anti-BCMA RITs both leptomycin B-75 (LMB-75) [anti-BCMA-disulfide-stabilized (ds)-Fv-PE24] (where PE represents Pseudomonas exotoxin A) or LMB-70 (anti-BCMA-Fab-PE24) given every other day for 5-d (QODx5) doses beginning on day 4 or day 8.	Disulfides	144-153	tumor necrosis factor receptor superfamily, member 17	Mus musculus	93-97
30744866-6	2019	MW enhanced intermolecular forces by engendering more disulfide bonds, which hindered the catalysis by TGase.	Disulfides	54-63	transglutaminase 1	Homo sapiens	103-108
30782819-9	2019	We achieved complete durable remissions when treating mice with H929-GFP-luc cells with anti-BCMA RITs both leptomycin B-75 (LMB-75) [anti-BCMA-disulfide-stabilized (ds)-Fv-PE24] (where PE represents Pseudomonas exotoxin A) or LMB-70 (anti-BCMA-Fab-PE24) given every other day for 5-d (QODx5) doses beginning on day 4 or day 8.	Disulfides	144-153	tumor necrosis factor receptor superfamily, member 17	Mus musculus	139-143
33326798-4	2020	The disulfide-bonded ACE2 microbody protein inhibits entry of SARS-CoV-2 spike protein pseudotyped virus and replication of live SARS-CoV-2 in vitro and in a mouse model.	Disulfides	4-13	angiotensin converting enzyme 2	Homo sapiens	21-25
30782819-9	2019	We achieved complete durable remissions when treating mice with H929-GFP-luc cells with anti-BCMA RITs both leptomycin B-75 (LMB-75) [anti-BCMA-disulfide-stabilized (ds)-Fv-PE24] (where PE represents Pseudomonas exotoxin A) or LMB-70 (anti-BCMA-Fab-PE24) given every other day for 5-d (QODx5) doses beginning on day 4 or day 8.	Disulfides	144-153	tumor necrosis factor receptor superfamily, member 17	Mus musculus	139-143
30503285-3	2019	The latter plasmid encodes human polypeptide N-acetylgalactosaminyl transferase as well as a beta1,3-galactosyl transferase and UDP-Glc(NAc)-4-epimerase, both from Campylobacter jejuni, and a disulfide bond isomerase of bacterial or human origin.	Disulfides	192-201	UDP-galactose-4-epimerase	Homo sapiens	128-152
33326798-4	2020	The disulfide-bonded ACE2 microbody protein inhibits entry of SARS-CoV-2 spike protein pseudotyped virus and replication of live SARS-CoV-2 in vitro and in a mouse model.	Disulfides	4-13	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	73-78
31333815-4	2019	Here, we used multi-microsecond molecular dynamics (MD) simulations to elucidate the effect of the disulfide bond on the structure and dynamics of HMGB1.	Disulfides	99-108	high mobility group box 1	Homo sapiens	147-152
31333815-5	2019	The results of the MD simulations show that the presence or lack of the disulfide bond between Cys23 and Cys45 modulates the conformational space explored by HMGB1, making the reduced protein more suitable to form a complex with CXCL12.	Disulfides	72-81	high mobility group box 1	Homo sapiens	158-163
31333815-5	2019	The results of the MD simulations show that the presence or lack of the disulfide bond between Cys23 and Cys45 modulates the conformational space explored by HMGB1, making the reduced protein more suitable to form a complex with CXCL12.	Disulfides	72-81	C-X-C motif chemokine ligand 12	Homo sapiens	229-235
30991141-7	2019	In addition, PDT promoted intramolecular disulfide formation and inactivation of tumor suppressor PTEN, thereby favoring Akt and p300 activation leading to iNOS upregulation.	Disulfides	41-50	E1A binding protein p300	Homo sapiens	129-133
30781856-7	2019	Protein disulfide isomerase (PDI), which is an enzyme that had a high-ranking fold change and that catalyzes the formation, breakage, and rearrangement of disulfide bonds within a protein molecule, was selected for further study.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
33196173-7	2020	Using the DNA-binding domain of the nuclear receptor Estrogen Related Receptor gamma (ERRgamma), we target a native cysteine positioned at the 14-3-3 PPI interface and identify several fragments that form a disulfide bond to ERRgamma and stabilize the complex up to 5-fold.	Disulfides	207-216	estrogen related receptor gamma	Homo sapiens	86-94
30221761-3	2019	In the cytosol, two NADPH-dependent enzymes, glutathione reductase and thioredoxin reductase, as well as a recently identified NADPH-independent system that uses catabolism of methionine to maintain pools of reduced glutathione, supply disulfide reducing power.	Disulfides	236-245	glutathione-disulfide reductase	Homo sapiens	45-66
31026770-0	2019	Peroxiredoxin-mediated disulfide bond formation is required for nucleocytoplasmic translocation and secretion of HMGB1 in response to inflammatory stimuli.	Disulfides	23-32	high mobility group box 1	Mus musculus	113-118
31026770-3	2019	Here we show that H2O2-induced oxidation of HMGB1, which results in the formation of an intramolecular disulfide bond between Cys23 and Cys45, is necessary and sufficient for its nucleocytoplasmic translocation and secretion.	Disulfides	103-112	high mobility group box 1	Mus musculus	44-49
31026770-4	2019	The oxidation is catalyzed by peroxiredoxin I (PrxI) and PrxII, which are first oxidized by H2O2 and then transfer their disulfide oxidation state to HMGB1.	Disulfides	121-130	peroxiredoxin 2	Mus musculus	57-62
31026770-4	2019	The oxidation is catalyzed by peroxiredoxin I (PrxI) and PrxII, which are first oxidized by H2O2 and then transfer their disulfide oxidation state to HMGB1.	Disulfides	121-130	high mobility group box 1	Mus musculus	150-155
31026770-5	2019	The disulfide form of HMGB1 showed higher affinity for nuclear exportin CRM1 compared with the reduced form.	Disulfides	4-13	high mobility group box 1	Mus musculus	22-27
30537892-2	2019	After characterization of the chemical structure of TG-DPU using proton nuclear magnetic resonance spectroscopy, bone morphogenetic protein (BMP-2) was loaded in the TG-DPU under oxidative conditions to form disulfides between the free thiol of TG-DPU and BMP-2.	Disulfides	208-218	bone morphogenetic protein 2	Homo sapiens	141-146
33196173-7	2020	Using the DNA-binding domain of the nuclear receptor Estrogen Related Receptor gamma (ERRgamma), we target a native cysteine positioned at the 14-3-3 PPI interface and identify several fragments that form a disulfide bond to ERRgamma and stabilize the complex up to 5-fold.	Disulfides	207-216	estrogen related receptor gamma	Homo sapiens	225-233
30537892-3	2019	The interaction between TG-DPU and BMP-2, so-called bioconjugates, was investigated using X-ray photoelectron spectroscopy analysis; the appearance of disulfide (S-S) linkage indicated the formation of a polymer/growth factor conjugate system.	Disulfides	151-160	bone morphogenetic protein 2	Homo sapiens	35-40
33066406-4	2020	The heavy (i.e., 4F2hc) and light (i.e., LAT1 and LAT2) chains belong to the solute carrier (SLC) families SLC3 and SLC7, and are covalently linked by a conserved disulfide bridge.	Disulfides	163-172	linker for activation of T cells family member 2	Homo sapiens	50-54
30429345-1	2019	Binding to the receptor CD4 triggers entry-related conformational changes in the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer, (gp120/gp41)3 Soluble versions of HIV-1 Env trimers (sgp140 SOSIP.664) stabilized by a gp120-gp41 disulfide bond and a change (I559P) in gp41 have been structurally characterized.	Disulfides	259-268	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	125-146
30429345-1	2019	Binding to the receptor CD4 triggers entry-related conformational changes in the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer, (gp120/gp41)3 Soluble versions of HIV-1 Env trimers (sgp140 SOSIP.664) stabilized by a gp120-gp41 disulfide bond and a change (I559P) in gp41 have been structurally characterized.	Disulfides	259-268	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	148-151
30429345-1	2019	Binding to the receptor CD4 triggers entry-related conformational changes in the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) trimer, (gp120/gp41)3 Soluble versions of HIV-1 Env trimers (sgp140 SOSIP.664) stabilized by a gp120-gp41 disulfide bond and a change (I559P) in gp41 have been structurally characterized.	Disulfides	259-268	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	162-167
31034891-7	2019	Here, we show that formation of a single disulfide bond is an evolutionary conserved trait, which determines secretion-competency of IL-27alpha.	Disulfides	41-50	interleukin 27	Homo sapiens	133-143
31880198-5	2020	We also determined that Cys292 and Cys361 are essential sites of ATG4B to form reversible intramolecular disulfide bonds that respond to oxidative stress.	Disulfides	105-114	autophagy related 4B cysteine peptidase	Homo sapiens	65-70
31121865-10	2019	We also found that untreated cells contained Prx6 multimers bound through disulfide bonds.	Disulfides	74-83	peroxiredoxin 6	Homo sapiens	45-49
30448513-6	2019	Here we show that Sac1undergoes reversible inactivation in mammalian cells when its catalytic Cys389 residue is oxidized by exogenous H2O2 to form an intramolecular disulfide with Cys392.	Disulfides	165-174	SAC1 like phosphatidylinositide phosphatase	Homo sapiens	18-22
31880198-6	2020	Interestingly, we unraveled a new phenomenon that ATG4B concurrently formed disulfide-linked oligomers at Cys292 and Cys361, and that both sites underwent redox modifications thereby modulating ATG4B activity.	Disulfides	76-85	autophagy related 4B cysteine peptidase	Homo sapiens	50-55
32929035-2	2020	In vitro studies have shown that S-glutathionylation and disulfide bonding of titin fragments could alter the elastic properties of titin; however, whether and where titin becomes oxidized in vivo is less certain.	Disulfides	57-66	titin	Homo sapiens	78-83
30584462-7	2018	Second, we utilized the active site mutant Cys208Ser of Nrx, which stabilizes a mixed disulfide intermediate with its substrates and therefore trapped interacting proteins from the mouse brain (identifying 1710 proteins) and neuronal cell culture extracts (identifying 609 proteins).	Disulfides	86-95	nucleoredoxin	Homo sapiens	56-59
30584462-9	2018	These results characterize Nrx as a cellular oxidase that itself may be oxidized by the formation of disulfide relays with peroxiredoxins.	Disulfides	101-110	nucleoredoxin	Homo sapiens	27-30
30765605-3	2019	The immunoglobulin domain of beta2 interacts with the shoulder of the pore domain through a disulfide bond.	Disulfides	92-101	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	29-34
30659052-4	2019	We hypothesized that a mechanism of T-cell-intrinsic energy consumption was the process of oxidative protein folding and disulfide bond formation that takes place in the endoplasmic reticulum (ER) guided by protein kinase R-like endoplasmic reticulum kinase (PERK) and downstream PERK axis target ER oxidoreductase 1 (ERO1alpha).	Disulfides	121-130	endoplasmic reticulum oxidoreductase 1 alpha	Mus musculus	318-327
30464464-0	2018	A novel disulfide bond-mediated cleavable RGD-modified PAMAM nanocomplex containing nuclear localization signal HMGB1 for enhancing gene transfection efficiency.	Disulfides	8-17	high mobility group box 1	Homo sapiens	112-117
30464464-10	2018	Intracellular trafficking and in vitro expression study indicated that the DHP nanocomplex escaped from lysosomes and the disulfide bonds between PAMAM and PEG cleaved due to the high concentration of GSH in the cytoplasm, pDNA consequently became exclusively located in the nucleus under the guidance of HMGB1, thereby promoting the red fluorescence protein (RFP) expression.	Disulfides	122-131	high mobility group box 1	Homo sapiens	305-310
30593501-6	2019	We observed that Grx1 reduces GSH-containing disulfides (including oxidized trypanothione) in very fast reactions (k &gt; 5 x 105 m-1 s-1).	Disulfides	45-55	glutaredoxin	Homo sapiens	17-21
30388869-8	2018	The activated HGFAC cleaves proHGF at Arg494-Val495, resulting in the formation of the active disulfide-linked heterodimer HGF.	Disulfides	94-103	hepatocyte growth factor	Homo sapiens	14-17
32929035-2	2020	In vitro studies have shown that S-glutathionylation and disulfide bonding of titin fragments could alter the elastic properties of titin; however, whether and where titin becomes oxidized in vivo is less certain.	Disulfides	57-66	titin	Homo sapiens	132-137
30593501-9	2019	This kinetic selectivity in the reduction step of the catalytic cycle suggests that Grx1 uses preferentially a dithiol mechanism, forming a disulfide on the active site during the oxidative half of the catalytic cycle and then being rapidly reduced by T(SH)2 in the reductive half.	Disulfides	140-149	glutaredoxin	Homo sapiens	84-88
32929035-2	2020	In vitro studies have shown that S-glutathionylation and disulfide bonding of titin fragments could alter the elastic properties of titin; however, whether and where titin becomes oxidized in vivo is less certain.	Disulfides	57-66	titin	Homo sapiens	132-137
33195401-2	2020	The accessory Cys-rich proteins expressed in SARS-CoV-2 by genes ORF7a and ORF8 are likely involved in zinc binding and in interactions with cellular antigens activated by extensive disulfide bonds.	Disulfides	182-191	ORF7a protein	Severe acute respiratory syndrome coronavirus 2	65-70
31037139-11	2019	H2Se could interrupt the disulfide bond in HMGB1 and promote its secretion.	Disulfides	25-34	high mobility group box 1	Homo sapiens	43-48
30011082-0	2018	Binding of p67phox to Nox2 is stabilized by disulfide bonds between cysteines in the 369 Cys-Gly-Cys371 triad in Nox2 and in p67phox.	Disulfides	44-53	neutrophil cytosolic factor 2	Homo sapiens	11-18
30011082-0	2018	Binding of p67phox to Nox2 is stabilized by disulfide bonds between cysteines in the 369 Cys-Gly-Cys371 triad in Nox2 and in p67phox.	Disulfides	44-53	neutrophil cytosolic factor 2	Homo sapiens	125-132
30011082-6	2018	Results show that the primary interaction of p67phox with Nox2 is followed by a stabilizing step, based on the establishment of disulfide bonds between cysteine(s) in the 369 Cys-Gly-Cys371 triad and cysteine(s) in p67phox .	Disulfides	128-137	neutrophil cytosolic factor 2	Homo sapiens	45-52
33195401-2	2020	The accessory Cys-rich proteins expressed in SARS-CoV-2 by genes ORF7a and ORF8 are likely involved in zinc binding and in interactions with cellular antigens activated by extensive disulfide bonds.	Disulfides	182-191	ORF8 protein	Severe acute respiratory syndrome coronavirus 2	75-79
32601061-8	2020	Subsequent MS analysis indicated corresponding disulfide formation of the substrates, suggesting that the presence of the substrate could reactivate ADO to defend against oxidative stress.	Disulfides	47-56	2-aminoethanethiol (cysteamine) dioxygenase	Mus musculus	149-152
30591932-3	2018	As a critical member of the PDI family, thioredoxin domain containing protein 5 (TXNDC5) assists the folding of newly synthesized peptides to their mature form through series of disulfide bond exchange reactions.	Disulfides	178-187	prolyl 4-hydroxylase subunit beta	Homo sapiens	28-31
30237412-8	2018	Opening of adherens junctions leads to substantial alterations of cellular mechanics such as reduced overall stiffness, but these changes turned out to be reversible after re-establishing disulfide bridges in E-cadherin by removal of DTT.	Disulfides	188-197	cadherin 1	Canis lupus familiaris	209-219
30530491-3	2019	CCS1, the budding yeast (S. cerevisiae) Cu chaperone for Cu-zinc (Zn) superoxide dismutase (SOD1) activates by directly promoting both Cu delivery and disulfide formation in SOD1.	Disulfides	151-160	copper chaperone CCS1	Saccharomyces cerevisiae S288C	0-4
30530491-3	2019	CCS1, the budding yeast (S. cerevisiae) Cu chaperone for Cu-zinc (Zn) superoxide dismutase (SOD1) activates by directly promoting both Cu delivery and disulfide formation in SOD1.	Disulfides	151-160	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	92-96
30580571-0	2019	Redox Activation of Nox1 (NADPH Oxidase 1) Involves an Intermolecular Disulfide Bond Between Protein Disulfide Isomerase and p47phox in Vascular Smooth Muscle Cells.	Disulfides	70-79	NADPH oxidase 1	Homo sapiens	20-24
32677157-4	2020	In addition, glutathione (GSH) depletion through disulfide-thiol exchange leads to the inactivation of glutathione peroxide 4 (GPX4), which results in a further increase in LPO content.	Disulfides	49-58	lactoperoxidase	Mus musculus	173-176
30580571-0	2019	Redox Activation of Nox1 (NADPH Oxidase 1) Involves an Intermolecular Disulfide Bond Between Protein Disulfide Isomerase and p47phox in Vascular Smooth Muscle Cells.	Disulfides	70-79	NADPH oxidase 1	Homo sapiens	26-41
30580571-0	2019	Redox Activation of Nox1 (NADPH Oxidase 1) Involves an Intermolecular Disulfide Bond Between Protein Disulfide Isomerase and p47phox in Vascular Smooth Muscle Cells.	Disulfides	70-79	prolyl 4-hydroxylase subunit beta	Homo sapiens	93-120
30580571-4	2019	Mass spectrometry of crosslinked peptides confirmed redox-dependent disulfide bonds between cysteines of p47phox and PDI and an intramolecular bond between Cys 196 and 378 in p47phox.	Disulfides	68-77	prolyl 4-hydroxylase subunit beta	Homo sapiens	117-120
30600428-2	2019	Through cleavage of disulfide bonds, FXI becomes reduced (rFXI), accelerating intrinsic coagulation cascade activation.	Disulfides	20-29	coagulation factor XI	Homo sapiens	37-40
30059675-2	2018	The third disulfide loop of TGF-alpha (TGF3L peptide) with a very low affinity for EGFR has been reported to enhance the activity of fused antigens or cytokines.	Disulfides	10-19	transforming growth factor alpha	Homo sapiens	28-37
32694171-6	2020	We further showed that covalent disulfide adducts of this residue promote autophosphorylation of the Aurora A kinase domain.	Disulfides	32-41	aurora kinase A	Homo sapiens	101-109
29934306-3	2018	Previously, we reported that the region between the first and the second alpha-helix (H1~H2) of PrPC might cooperate with the more C-terminal side region for efficient interactions with PrPSc From this starting point, we created a series of PrP variants with two cysteine substitutions (C;C-PrP) forming a disulfide-crosslink between H1~H2 and the distal region of the third helix (Ctrm).	Disulfides	306-315	prion protein	Mus musculus	96-99
30552876-0	2019	Molecular Mechanisms of Glutaredoxin Enzymes: Versatile Hubs for Thiol-Disulfide Exchange between Protein Thiols and Glutathione.	Disulfides	71-80	glutaredoxin	Homo sapiens	24-36
32765524-2	2020	CD28 is expressed at the cell surface as a disulfide linked homodimer that is thought to bind ligand monovalently.	Disulfides	43-52	CD28 molecule	Homo sapiens	0-4
30244311-6	2019	Using high-resolution mass spectrometry, 39 endogenous Ng peptides were identified while full-length Ng was found to be modified including disulfide bridges or glutathione.	Disulfides	139-148	neurogranin	Homo sapiens	101-103
31787719-6	2019	The X-ray crystal structures revealed that RNase He1 and RNase Po1 are almost identical in their catalytic sites and in the cysteine residues involved in disulfide bonds that increase their stability.	Disulfides	154-163	NPC intracellular cholesterol transporter 2	Homo sapiens	49-52
29980609-5	2018	Cys87 residing within the C-type lectin-like domain not only ensures stable homodimerization of AICL glycoproteins by disulfide bonding, but Cys87 is also required for efficient cell surface expression of AICL homodimers and essential for AICL-NKp80 interaction.	Disulfides	118-127	C-type lectin domain family 2 member B	Homo sapiens	96-100
30147916-2	2018	This mutation may cause the loss of the disulfide bond between Cys 1393 and Cys 1378 residues of fibrillin-2.	Disulfides	40-49	fibrillin 2	Homo sapiens	97-108
29915197-3	2018	In this study, we engineer disulfide crosslinks in the coiled-coils of the archaeal proteasomal ATPase (PAN) and report that its three identical coiled-coil domains can adopt three different conformations: (1) in-register and zipped, (2) in-register and partially unzipped, and (3) out-of-register.	Disulfides	27-36	dynein axonemal heavy chain 8	Homo sapiens	96-102
29915197-3	2018	In this study, we engineer disulfide crosslinks in the coiled-coils of the archaeal proteasomal ATPase (PAN) and report that its three identical coiled-coil domains can adopt three different conformations: (1) in-register and zipped, (2) in-register and partially unzipped, and (3) out-of-register.	Disulfides	27-36	adenosine deaminase 2	Homo sapiens	104-107
32656452-6	2020	In this study, the role of thiol-disulfide balance on the interactions between SARS-CoV/CoV-2 spike proteins and ACE2 was investigated using molecular dynamics simulations.	Disulfides	33-42	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	94-99
29196860-1	2018	High mobility group box 1 (HMGB1), a nuclear protein, once released into the extracellular space under pathological conditions, plays a pronociceptive role in redox-dependent distinct active forms, all-thiol HMGB1 (at-HMGB1) and disulfide HMGB1 (ds-HMGB1), that accelerate nociception through the receptor for advanced glycation endproducts (RAGE) and Toll-like receptor 4 (TLR4), respectively.	Disulfides	229-238	high mobility group box 1	Mus musculus	0-25
29196860-1	2018	High mobility group box 1 (HMGB1), a nuclear protein, once released into the extracellular space under pathological conditions, plays a pronociceptive role in redox-dependent distinct active forms, all-thiol HMGB1 (at-HMGB1) and disulfide HMGB1 (ds-HMGB1), that accelerate nociception through the receptor for advanced glycation endproducts (RAGE) and Toll-like receptor 4 (TLR4), respectively.	Disulfides	229-238	high mobility group box 1	Mus musculus	27-32
29725115-7	2019	We show that MICU3 forms a disulfide bond-mediated dimer with MICU1, but not with MICU2, and it acts as enhancer of MCU-dependent mitochondrial Ca2+ uptake.	Disulfides	27-36	mitochondrial calcium uptake family member 3	Homo sapiens	13-18
29725115-7	2019	We show that MICU3 forms a disulfide bond-mediated dimer with MICU1, but not with MICU2, and it acts as enhancer of MCU-dependent mitochondrial Ca2+ uptake.	Disulfides	27-36	mitochondrial calcium uptake 1	Homo sapiens	62-67
30251679-3	2018	Here we determined which Cys residues are involved in disulfide-mediated crosslinking of recombinant human gammaD-crystallin (hgammaD).	Disulfides	54-63	crystallin gamma D	Homo sapiens	107-134
32656452-6	2020	In this study, the role of thiol-disulfide balance on the interactions between SARS-CoV/CoV-2 spike proteins and ACE2 was investigated using molecular dynamics simulations.	Disulfides	33-42	angiotensin converting enzyme 2	Homo sapiens	113-117
29542339-1	2018	INTRODUCTION: The protein disulfide isomerase (PDI) family of thiol isomerases are intracellular enzymes known to catalyze the oxidation, reduction and isomerization of disulfide bonds during protein synthesis in the endoplasmic reticulum.	Disulfides	26-35	prolyl 4-hydroxylase subunit beta	Homo sapiens	47-50
32656452-7	2020	The study revealed that the binding affinity was significantly impaired when all of the disulfide bonds of both ACE2 and SARS-CoV/CoV-2 spike proteins were reduced to thiol groups.	Disulfides	88-97	angiotensin converting enzyme 2	Homo sapiens	112-116
32656452-7	2020	The study revealed that the binding affinity was significantly impaired when all of the disulfide bonds of both ACE2 and SARS-CoV/CoV-2 spike proteins were reduced to thiol groups.	Disulfides	88-97	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	136-141
32044416-4	2020	However, purification of wild-type serpin B1 in the absence of a reducing agent resulted in the specific loss of elastase - but not chymotrypsin - inhibition, concomitant with the formation of two higher molecular weight forms of the protein - a modified monomer and a dimer created via an intermolecular disulfide bond formed between C344 in respective serpin B1 monomers.	Disulfides	305-314	serpin family B member 1	Homo sapiens	35-44
29447008-7	2018	Expert opinion: Blocking excessive amounts of extracellular HMGB1, particularly the disulfide isoform, offers an attractive clinical opportunity to ameliorate systemic inflammatory diseases.	Disulfides	84-93	high mobility group box 1	Homo sapiens	60-65
30252897-7	2018	Treatments leading to the formation of a disulfide bond between ADH and glutathione (protein S-glutathionylation) had no negative effect on the enzyme activity.	Disulfides	41-50	alcohol dehydrogenase 1	Arabidopsis thaliana	64-67
30250028-4	2018	Complemented by disulfide trapping and chemical crosslinking, structural analysis in solution reveals the topology of metastable complexes of OCP and the FRP scaffold with different stoichiometries.	Disulfides	16-25	secreted frizzled related protein 1	Homo sapiens	154-157
32087195-6	2020	Removal of the disulfide bridge in the C-terminal EF-hand2 of SPARC, which is known to enhance Col(IV) binding, did not lead to larval lethality; however, a less intense fat body phenotype was observed.	Disulfides	15-24	Secreted protein, acidic, cysteine-rich	Drosophila melanogaster	62-67
30283452-2	2018	The alarmin HMGB1, in its reduced form, can complex with CXCL12 enhancing its activity on monocytes via the chemokine receptor CXCR4, while the form containing a disulfide bond, by binding to TLR2 or TLR4, initiates a cascade of events leading to production of cytokines and chemokines.	Disulfides	162-171	high mobility group box 1	Homo sapiens	12-17
29293453-8	2018	Our data suggest that upon activation of integrins, PDI is released from endothelial cells and forms a disulfide bond complex with alphaVbeta3 integrin.	Disulfides	103-112	prolyl 4-hydroxylase subunit beta	Homo sapiens	52-55
32087195-6	2020	Removal of the disulfide bridge in the C-terminal EF-hand2 of SPARC, which is known to enhance Col(IV) binding, did not lead to larval lethality; however, a less intense fat body phenotype was observed.	Disulfides	15-24	Collagen type IV alpha 1	Drosophila melanogaster	95-102
29721409-3	2018	Here, glutathione (GSH)-activated light-up peptide-polysaccharide-inter-polyelectrolyte nanocomplexes are established through self-assembly of carboxymethyl dextran with disulfide-bridged ("S-S") oligoarginine peptide (S-Arg4), in which microRNA-34a (miR-34a) and indocyanine green (ICG) are simultaneously embedded and the nanocomplexes are subsequently stabilized by intermolecular cross-linking.	Disulfides	170-179	microRNA 34a	Homo sapiens	237-249
32380958-4	2020	Disulfide-HMGB1 triggers TLR4 receptors generating pro-inflammatory cytokine release.	Disulfides	0-9	high mobility group box 1	Homo sapiens	10-15
29721409-3	2018	Here, glutathione (GSH)-activated light-up peptide-polysaccharide-inter-polyelectrolyte nanocomplexes are established through self-assembly of carboxymethyl dextran with disulfide-bridged ("S-S") oligoarginine peptide (S-Arg4), in which microRNA-34a (miR-34a) and indocyanine green (ICG) are simultaneously embedded and the nanocomplexes are subsequently stabilized by intermolecular cross-linking.	Disulfides	170-179	microRNA 34a	Homo sapiens	251-258
29721409-5	2018	However, after intracellular delivery, the disulfide bond in S-Arg4 can be cleaved by intracellular GSH, which leads to the dissociation of nanocomplexes and triggers the simultaneous release of miR-34a and ICG.	Disulfides	43-52	microRNA 34a	Homo sapiens	195-202
29930975-10	2018	Proteomic data and molecular dynamic simulations of Carboxyl ester lipase (Cel), a unique serine hydrolase active within ER, showed an uncoupled disulfide bond involving Cel Cys266, Cel dimerization, ER retention, and complex formation in ethanol-fed, XBP1-deficient mice.	Disulfides	145-154	carboxyl ester lipase	Mus musculus	52-73
29930975-10	2018	Proteomic data and molecular dynamic simulations of Carboxyl ester lipase (Cel), a unique serine hydrolase active within ER, showed an uncoupled disulfide bond involving Cel Cys266, Cel dimerization, ER retention, and complex formation in ethanol-fed, XBP1-deficient mice.	Disulfides	145-154	carboxyl ester lipase	Mus musculus	75-78
29930975-10	2018	Proteomic data and molecular dynamic simulations of Carboxyl ester lipase (Cel), a unique serine hydrolase active within ER, showed an uncoupled disulfide bond involving Cel Cys266, Cel dimerization, ER retention, and complex formation in ethanol-fed, XBP1-deficient mice.	Disulfides	145-154	carboxyl ester lipase	Mus musculus	170-173
29930975-10	2018	Proteomic data and molecular dynamic simulations of Carboxyl ester lipase (Cel), a unique serine hydrolase active within ER, showed an uncoupled disulfide bond involving Cel Cys266, Cel dimerization, ER retention, and complex formation in ethanol-fed, XBP1-deficient mice.	Disulfides	145-154	carboxyl ester lipase	Mus musculus	170-173
29203538-4	2018	Here we report that fully reduced HMGB1 orchestrates muscle and liver regeneration via CXCR4, whereas disulfide HMGB1 and its receptors TLR4/MD-2 and RAGE (receptor for advanced glycation end products) are not involved.	Disulfides	102-111	high mobility group box 1	Homo sapiens	112-117
29925506-10	2018	CTGF and latent TGFbeta migrated as a single high molecular weight band under non-reducing conditions, suggesting that they were in a covalent (disulfide) complex.	Disulfides	144-153	cellular communication network factor 2	Mus musculus	0-4
29925506-10	2018	CTGF and latent TGFbeta migrated as a single high molecular weight band under non-reducing conditions, suggesting that they were in a covalent (disulfide) complex.	Disulfides	144-153	transforming growth factor, beta 1	Mus musculus	16-23
29888867-3	2018	We recently identified a disulfide-bridged nonapeptide, named PTPRJ-19 (H-[Cys-His-His-Asn-Leu-Thr-His-Ala-Cys]-OH), which activates PTPRJ, thereby causing cell growth inhibition and apoptosis of both cancer and endothelial cells.	Disulfides	25-34	protein tyrosine phosphatase receptor type J	Homo sapiens	62-67
29888867-3	2018	We recently identified a disulfide-bridged nonapeptide, named PTPRJ-19 (H-[Cys-His-His-Asn-Leu-Thr-His-Ala-Cys]-OH), which activates PTPRJ, thereby causing cell growth inhibition and apoptosis of both cancer and endothelial cells.	Disulfides	25-34	protein tyrosine phosphatase receptor type J	Homo sapiens	133-138
30091702-3	2018	Disulfide crosslinks between cysteine-modified H2A.Z and/or H2A histones within nucleosomes were induced using a membrane-permeable oxidant.	Disulfides	0-9	H2A clustered histone 18	Homo sapiens	47-50
32152224-2	2020	The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme.	Disulfides	108-117	heme oxygenase 2	Homo sapiens	36-52
29031614-8	2018	Interfering with disulfide HMGB1-activated cell signaling mediates significant therapeutic effects in epilepsy models.	Disulfides	17-26	high mobility group box 1	Homo sapiens	27-32
29216561-5	2018	The compound consists of the myelin basic protein (MBP) 85-99 immunodominant epitope (MBP85-99) coupled to an anthraquinone type molecule (AQ) via a disulfide (S-S) and 6 amino hexanoic acid (Ahx) residues (AQ-S-S-(Ahx)6MBP85-99).	Disulfides	149-158	myelin basic protein	Homo sapiens	29-49
29216561-5	2018	The compound consists of the myelin basic protein (MBP) 85-99 immunodominant epitope (MBP85-99) coupled to an anthraquinone type molecule (AQ) via a disulfide (S-S) and 6 amino hexanoic acid (Ahx) residues (AQ-S-S-(Ahx)6MBP85-99).	Disulfides	149-158	myelin basic protein	Homo sapiens	51-54
32152224-2	2020	The C-terminal tail region of human heme oxygenase-2 (HO2) contains two HRMs whose cysteine residues form a disulfide bond; when reduced, these cysteines are available to bind Fe3+-heme.	Disulfides	108-117	heme oxygenase 2	Homo sapiens	54-57
31879955-3	2020	We show that SMIM1 dimerization is mediated both by an extracellular Cys77-dependent, homomeric disulfide linkage and via a GxxxG helix-helix interaction motif in the transmembrane domain.	Disulfides	96-105	small integral membrane protein 1 (Vel blood group)	Homo sapiens	13-18
30101863-7	2018	Consequently, abnormal aggregates of orexin and/or its precursor that possess two intra-molecular disulfide bonds accumulate within orexin neurons.	Disulfides	98-107	hypocretin neuropeptide precursor	Homo sapiens	37-43
30101863-7	2018	Consequently, abnormal aggregates of orexin and/or its precursor that possess two intra-molecular disulfide bonds accumulate within orexin neurons.	Disulfides	98-107	hypocretin neuropeptide precursor	Homo sapiens	132-138
29682907-1	2018	Analogs of the cationic C-terminal segments of human-beta-defensins HBD1-3, Phd1-3 with a single disulfide bond, exhibited comparable antimicrobial activity that was salt sensitive.	Disulfides	97-106	egl-9 family hypoxia inducible factor 2	Homo sapiens	76-80
31996435-5	2020	Here, we show that Can GPC aggregates in the ER of infected cells, forming incorrect cross-chain disulfide bonds, which results in impaired GPC processing into G1 and G2.	Disulfides	97-106	glycoprotein precursor	Argentinian mammarenavirus	23-26
30256204-3	2018	The aim of this prospective study was to evaluate the role of oxidative stress, using native thiol/disulfide (SH/SS) homeostasis as a novel indicator, in the etiology of BPPV.	Disulfides	99-108	benign paroxysmal positional vertigo	Homo sapiens	170-174
29845893-7	2018	This study investigated the involvement of cysteine residues conserved in DUOX1 toward the formation of disulfide bridges, which could be important for the function of the DUOX1DUOXA1 complex.	Disulfides	104-113	dual oxidase 1	Homo sapiens	74-79
28981703-3	2017	However, while JunD is competent to bind DNA, the FosB bZIP domain must undergo a large conformational rearrangement that is controlled by a "redox switch" centered on an inter-molecular disulfide bond.	Disulfides	187-196	FosB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	50-54
31996435-5	2020	Here, we show that Can GPC aggregates in the ER of infected cells, forming incorrect cross-chain disulfide bonds, which results in impaired GPC processing into G1 and G2.	Disulfides	97-106	glycoprotein precursor	Argentinian mammarenavirus	140-143
32098132-7	2020	In human VDAC2 and 3 isoforms the permanently reduced state of a cluster of close cysteines indicates the possibility that disulfide bridges are formed in the proteins.	Disulfides	123-132	voltage dependent anion channel 2	Homo sapiens	9-20
28844745-1	2017	Protein disulfide isomerase (PDI) has diverse functions in the endoplasmic reticulum as catalyst of redox transfer, disulfide isomerization and oxidative protein folding, as molecular chaperone and in multi-subunit complexes.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
30031898-8	2018	In silico and Inductively Coupled Plasma Mass Spectrometry studies revealed the interaction of Arsenic to the Cx43 preferably occurs through surface exposed cysteines, thereby capping the thiol groups that form disulfide bonds in the tertiary structure.	Disulfides	211-220	gap junction protein alpha 1	Homo sapiens	110-114
29878755-9	2018	Applying this workflow, we successfully mapped the complex disulfide bonds of tertiapin and the epidermal growth factor (EGF) family members transforming growth factor alpha (TGFalpha) and EGF.	Disulfides	59-68	transforming growth factor alpha	Homo sapiens	175-183
28875601-0	2017	Can the Thiol/Disulfide Imbalance Be a Predictor of Colchicine Resistance in Familial Mediterranean Fever?	Disulfides	14-23	MEFV innate immuity regulator, pyrin	Homo sapiens	77-105
28875601-4	2017	The aim of this study was to investigate the relationship between thiol-disulfide balance and colchicine resistance in FMF patients during an attack or attack-free period.	Disulfides	72-81	MEFV innate immuity regulator, pyrin	Homo sapiens	119-122
28849192-1	2017	High molecular weight (HMW) adiponectin (APN) is closely correlated with the development of fatty liver and is modulated by the Akt/forkhead box protein O1 (FOXO1) pathway through disulfide-bond A oxidoreductase-like protein (DsbA-L).	Disulfides	180-189	forkhead box O1	Rattus norvegicus	132-155
28849192-1	2017	High molecular weight (HMW) adiponectin (APN) is closely correlated with the development of fatty liver and is modulated by the Akt/forkhead box protein O1 (FOXO1) pathway through disulfide-bond A oxidoreductase-like protein (DsbA-L).	Disulfides	180-189	forkhead box O1	Rattus norvegicus	157-162
32075046-5	2020	The three-dimensional structure of the NKG2D monomeric protein contains two alpha-helices, two beta-lamellae, and four disulfide bonds, and its" signal of activation is transmitted mainly by the adaptor protein (DAP).	Disulfides	119-128	killer cell lectin like receptor K1	Homo sapiens	39-44
28954633-1	2017	BACKGROUND: Secreted clusterin (sCLU), a 75-80 kDa disulfide-linked heterodimeric protein, plays crucial roles in various pathophysiological processes, including lipid transport, tissue remodeling, cell apoptosis and reproduction.	Disulfides	51-60	clusterin	Homo sapiens	21-30
29194485-6	2018	Moreover, MS analyses and comparison of crystal structures between the reduced and H2O2-treated cytMDH1 further show that thioredoxin-reversible homodimerization of cytMDH1 through Cys330 disulfide formation protects the protein from overoxidation.	Disulfides	188-197	thioredoxin H-type 1	Arabidopsis thaliana	122-133
32064042-3	2020	Specifically, the disulfide bond-forming activity of the enzyme Quiescin sulfhydryl oxidase 1 (QSOX1) is required by fibroblasts to assemble ECM components for adhesion and migration of cancer cells.	Disulfides	18-27	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	64-93
29796570-4	2018	Moreover, SNO+ encapsulation also prevents its decomposition yielding disulfide and nitric oxide.	Disulfides	70-79	strawberry notch homolog 1	Homo sapiens	10-13
32064042-3	2020	Specifically, the disulfide bond-forming activity of the enzyme Quiescin sulfhydryl oxidase 1 (QSOX1) is required by fibroblasts to assemble ECM components for adhesion and migration of cancer cells.	Disulfides	18-27	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	95-100
28827318-10	2017	These results demonstrate that disulfide bond-dependent, amyloid-like MLKL polymers are necessary and sufficient to induce necroptosis.	Disulfides	31-40	mixed lineage kinase domain like pseudokinase	Homo sapiens	70-74
31919279-7	2020	PD-1H exhibits a noncanonical IgV-like topology including an extra "H" beta-strand and "clamping" disulfide, absent in known IgV-like structures, that likely restricts its orientation on the cell surface differently from other IgV-like domains.	Disulfides	98-107	V-set immunoregulatory receptor	Homo sapiens	0-5
30362439-1	2018	Lipoprotein(a) [Lp(a)] consists of an LDL-like particle in which the apolipoprotein B100 is covalently bound to apolipoprotein(a) by a single disulfide bond.	Disulfides	142-151	lipoprotein(a)	Homo sapiens	0-14
30362439-1	2018	Lipoprotein(a) [Lp(a)] consists of an LDL-like particle in which the apolipoprotein B100 is covalently bound to apolipoprotein(a) by a single disulfide bond.	Disulfides	142-151	lipoprotein(a)	Homo sapiens	16-21
29697253-10	2018	Removal of the disulfide weakens the ability of hIAPP to induce leakage of vesicles consisting of POPS and POPC.	Disulfides	15-24	islet amyloid polypeptide	Homo sapiens	48-53
33250972-4	2020	Our analysis of retrieved amino acid sequences deposited in data bases shows that S-proteins and ACE2 are rich in cysteine (Cys) residues, many of which are conserved in various SARS-related coronaviruses and participate in intra-molecular disulfide bonds.	Disulfides	240-249	angiotensin converting enzyme 2	Homo sapiens	97-101
28629706-0	2017	Disulfide-linked dimerization of the FcRgamma chain is required for positive and negative regulation of mast cell activation via FcepsilonRI.	Disulfides	0-9	Fc epsilon receptor Ig	Homo sapiens	37-45
28629706-0	2017	Disulfide-linked dimerization of the FcRgamma chain is required for positive and negative regulation of mast cell activation via FcepsilonRI.	Disulfides	0-9	Fc epsilon receptor Ia	Homo sapiens	129-140
33250972-5	2020	High-resolution protein structures of S-proteins and ACE2 receptors highlighted the probability that two of these disulfide bonds are potentially redox-active, facilitating the primal interaction between the receptor and the spike protein.	Disulfides	114-123	angiotensin converting enzyme 2	Homo sapiens	53-57
28692254-0	2017	Dissecting the Disulfide Linkage of the N-Terminal Domain of HMW 1Dx5 and Its Contributions to Dough Functionality.	Disulfides	15-24	cilia and flagella associated protein 97	Homo sapiens	61-64
28692254-5	2017	Moreover, Cys10 and Cys40 played a functionally important role in maintaining the structural and conformational stability and high surface hydrophobicity of the N-terminal domain of HMW-GS, which in turn facilitated the formation of HMW polymers and massive disulfide linkage of HMW-GS through hydrophobic interaction.	Disulfides	258-267	cilia and flagella associated protein 97	Homo sapiens	182-185
29743079-0	2018	HIV-1 tat expression and sulphamethoxazole hydroxylamine mediated oxidative stress alter the disulfide proteome in Jurkat T cells.	Disulfides	93-102	tyrosine aminotransferase	Homo sapiens	6-9
33250972-5	2020	High-resolution protein structures of S-proteins and ACE2 receptors highlighted the probability that two of these disulfide bonds are potentially redox-active, facilitating the primal interaction between the receptor and the spike protein.	Disulfides	114-123	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	225-230
28692254-7	2017	Therefore, these results give a deep understanding of the disulfide linkage of the N-terminal domain of HMW-GS and its functional importance, which will provide a practical guide to effectively generate a superior HMW-GS allele by artificial mutagenesis.	Disulfides	58-67	cilia and flagella associated protein 97	Homo sapiens	104-107
28692254-7	2017	Therefore, these results give a deep understanding of the disulfide linkage of the N-terminal domain of HMW-GS and its functional importance, which will provide a practical guide to effectively generate a superior HMW-GS allele by artificial mutagenesis.	Disulfides	58-67	cilia and flagella associated protein 97	Homo sapiens	214-217
33250972-6	2020	Presence of redox-active disulfides in the interacting parts of S-protein, ACE2, and a ferredoxin-like fold domain in the transmembrane part of ACE2, strongly indicate the role of redox in COVID-19 pathogenesis and severity.	Disulfides	25-35	angiotensin converting enzyme 2	Homo sapiens	75-79
33250972-6	2020	Presence of redox-active disulfides in the interacting parts of S-protein, ACE2, and a ferredoxin-like fold domain in the transmembrane part of ACE2, strongly indicate the role of redox in COVID-19 pathogenesis and severity.	Disulfides	25-35	angiotensin converting enzyme 2	Homo sapiens	144-148
28623339-2	2017	As a result of disulfide shuffling in its terminal domains, hPDI exists in two oxidation states with different conformational preferences which are important for substrate binding and functional activities.	Disulfides	15-24	prolyl 4-hydroxylase subunit beta	Homo sapiens	60-64
28545586-0	2017	Disulfide high mobility group box-1 causes bladder pain through bladder Toll-like receptor 4.	Disulfides	0-9	high mobility group box 1	Mus musculus	10-35
28545586-7	2017	RESULTS: Disulfide HMGB1 elicited abdominal mechanical hypersensitivity 24 hours after intravesical (5, 10, 20 mug/150 mul) instillation.	Disulfides	9-18	high mobility group box 1	Mus musculus	19-24
28545586-13	2017	CONCLUSIONS: The disulfide form of HMGB1 mediates bladder pain directly (not secondary to inflammation or injury) through activation of TLR4 receptors in the bladder.	Disulfides	17-26	high mobility group box 1	Mus musculus	35-40
29222746-0	2018	Cadmium favors F-actin depolymerization in rat renal mesangial cells by site-specific, disulfide-based dimerization of the CAP1 protein.	Disulfides	87-96	cyclase associated actin cytoskeleton regulatory protein 1	Rattus norvegicus	123-127
29222746-2	2018	In a survey of proteins that might undergo Cd2+-dependent disulfide crosslinking, we identified the adenylyl cyclase-associated protein, CAP1, as undergoing a dimerization in response to Cd2+ (5-40 microM) that was sensitive to disulfide reducing agents, was reproduced by the disulfide crosslinking agent diamide, and was shown by site-directed mutagenesis to involve the Cys29 residue of the protein.	Disulfides	58-67	cyclase associated actin cytoskeleton regulatory protein 1	Rattus norvegicus	137-141
29222746-2	2018	In a survey of proteins that might undergo Cd2+-dependent disulfide crosslinking, we identified the adenylyl cyclase-associated protein, CAP1, as undergoing a dimerization in response to Cd2+ (5-40 microM) that was sensitive to disulfide reducing agents, was reproduced by the disulfide crosslinking agent diamide, and was shown by site-directed mutagenesis to involve the Cys29 residue of the protein.	Disulfides	228-237	cyclase associated actin cytoskeleton regulatory protein 1	Rattus norvegicus	137-141
29222746-2	2018	In a survey of proteins that might undergo Cd2+-dependent disulfide crosslinking, we identified the adenylyl cyclase-associated protein, CAP1, as undergoing a dimerization in response to Cd2+ (5-40 microM) that was sensitive to disulfide reducing agents, was reproduced by the disulfide crosslinking agent diamide, and was shown by site-directed mutagenesis to involve the Cys29 residue of the protein.	Disulfides	228-237	cyclase associated actin cytoskeleton regulatory protein 1	Rattus norvegicus	137-141
33250972-7	2020	Resistant animals lack a redox-active disulfide (Cys133-Cys141) in ACE2 sequences, further strengthening the redox hypothesis for infectivity.	Disulfides	38-47	angiotensin converting enzyme 2	Homo sapiens	67-71
31685660-1	2019	In the endoplasmic reticulum (ER), ER oxidoreductin 1 (ERO1) catalyzes intramolecular disulfide-bond formation within its substrates in coordination with protein disulfide isomerase (PDI) and related enzymes.	Disulfides	86-95	prolyl 4-hydroxylase subunit beta	Homo sapiens	154-181
28619231-4	2018	Although not considered chaperones per se, the ER oxidoreductases of the protein disulfide isomerase (PDI) family complete the folding job by catalyzing the formation of disulfide bonds through cysteine oxidation.	Disulfides	81-90	prolyl 4-hydroxylase subunit beta	Homo sapiens	102-105
29261301-3	2018	The currently available inhibitors of Trx1 and Grx1 are thiol-reactive electrophiles or disulfides that may suffer from low selectivity because of their thiol reactivity.	Disulfides	88-98	glutaredoxin	Homo sapiens	47-51
27668669-0	2017	A Distal Disulfide Bridge in OXA-1 beta-Lactamase Stabilizes the Catalytic Center and Alters the Dynamics of the Specificity Determining Omega Loop.	Disulfides	9-18	OXA1L mitochondrial inner membrane protein	Homo sapiens	29-34
27668669-4	2017	The OXA-1 clade of class D beta-lactamases contains a pair of conserved cysteines located outside the active site that forms a disulfide bond in the periplasm.	Disulfides	127-136	OXA1L mitochondrial inner membrane protein	Homo sapiens	4-9
27668669-5	2017	Here, the effect of the distal disulfide bond on the structure and dynamics of OXA-1 was investigated via 4 mus molecular dynamics simulations.	Disulfides	31-40	OXA1L mitochondrial inner membrane protein	Homo sapiens	79-84
31685660-1	2019	In the endoplasmic reticulum (ER), ER oxidoreductin 1 (ERO1) catalyzes intramolecular disulfide-bond formation within its substrates in coordination with protein disulfide isomerase (PDI) and related enzymes.	Disulfides	86-95	prolyl 4-hydroxylase subunit beta	Homo sapiens	183-186
28393915-9	2017	We conclude that allosteric inhibition of APN functions occurs by ligand suppression of ectodomain motions necessary for catalysis and virus cell entry, as validated by locking APN with disulfides.	Disulfides	186-196	alanyl aminopeptidase, membrane	Homo sapiens	42-45
31685660-3	2019	Reduction of the regulatory disulfide bonds of the ERO1 from soybean, GmERO1a, is catalyzed by enzymes in five classes of PDI family proteins.	Disulfides	28-37	endoplasmic oxidoreductin-1-like	Glycine max	70-77
28393915-9	2017	We conclude that allosteric inhibition of APN functions occurs by ligand suppression of ectodomain motions necessary for catalysis and virus cell entry, as validated by locking APN with disulfides.	Disulfides	186-196	alanyl aminopeptidase, membrane	Homo sapiens	177-180
29197144-1	2018	The protein disulfide isomerase (PDI) family, found in the endoplasmic reticulum (ER) of the eukaryotic cell, catalyzes the formation and cleavage of disulfide bonds and thereby helps in protein folding.	Disulfides	12-21	prolyl 4-hydroxylase subunit beta	Homo sapiens	33-36
29197144-3	2018	Here we report that water-soluble cyclic diselenides mimic the multifunctional activity of the PDI family by facilitating oxidative folding, disulfide formation/reduction, and repair of the scrambled disulfide bonds in misfolded proteins.	Disulfides	141-150	prolyl 4-hydroxylase subunit beta	Homo sapiens	95-98
31685660-3	2019	Reduction of the regulatory disulfide bonds of the ERO1 from soybean, GmERO1a, is catalyzed by enzymes in five classes of PDI family proteins.	Disulfides	28-37	prolyl 4-hydroxylase subunit beta	Homo sapiens	122-125
29197144-3	2018	Here we report that water-soluble cyclic diselenides mimic the multifunctional activity of the PDI family by facilitating oxidative folding, disulfide formation/reduction, and repair of the scrambled disulfide bonds in misfolded proteins.	Disulfides	200-209	prolyl 4-hydroxylase subunit beta	Homo sapiens	95-98
31685660-4	2019	Here, using recombinant proteins, vacuum ultraviolet circular dichroism (VUVCD) spectroscopy, biochemical and protein refolding assays, and quantitative immunoblotting, we found that GmERO1a activity is regulated by reduction of intramolecular disulfide bonds involving Cys121 and Cys146, which are located in a disordered region, similarly to their locations in human ERO1.	Disulfides	244-253	endoplasmic oxidoreductin-1-like	Glycine max	183-190
28000043-6	2017	Alternatively, the subunits of TNSALP (p.G426C) were found to be aberrantly cross-linked by disulfide bonds, giving rise to a 200 kDa form lacking ALP activity.	Disulfides	92-101	alkaline phosphatase, biomineralization associated	Homo sapiens	31-37
31685660-7	2019	Unlike yeast and human ERO1s, for which PDI is the preferred substrate, GmERO1a directly transferred disulfide bonds to the specific active center of members of five classes of PDI family proteins.	Disulfides	101-110	endoplasmic oxidoreductin-1-like	Glycine max	72-79
31685660-7	2019	Unlike yeast and human ERO1s, for which PDI is the preferred substrate, GmERO1a directly transferred disulfide bonds to the specific active center of members of five classes of PDI family proteins.	Disulfides	101-110	prolyl 4-hydroxylase subunit beta	Homo sapiens	177-180
28044432-5	2017	Many of the PDI family members catalyze disulfide-bond formation, reduction, and isomerization through redox-active disulfides and perturbed PDI activity is characteristic of carcinomas and neurodegenerative diseases.	Disulfides	40-49	prolyl 4-hydroxylase subunit beta	Homo sapiens	12-15
28044432-5	2017	Many of the PDI family members catalyze disulfide-bond formation, reduction, and isomerization through redox-active disulfides and perturbed PDI activity is characteristic of carcinomas and neurodegenerative diseases.	Disulfides	40-49	prolyl 4-hydroxylase subunit beta	Homo sapiens	141-144
28044432-5	2017	Many of the PDI family members catalyze disulfide-bond formation, reduction, and isomerization through redox-active disulfides and perturbed PDI activity is characteristic of carcinomas and neurodegenerative diseases.	Disulfides	116-126	prolyl 4-hydroxylase subunit beta	Homo sapiens	12-15
28044432-8	2017	The oxidation and reduction of redox-active disulfides are mediated by cellular reactive oxygen species and activity of reductases, such as glutaredoxin and thioredoxin.	Disulfides	44-54	glutaredoxin	Homo sapiens	140-152
29507626-3	2018	DESIGN: In this study, a sarcoma-targeting peptide-decorated disulfide-crosslinked polypeptide nanogel (STP-NG) was exploited for enhanced intracellular delivery of shikonin (SHK), an extract of a medicinal herb, to inhibit osteosarcoma progression with minimal systemic toxicity.	Disulfides	61-70	sulfotransferase family 1A member 1	Homo sapiens	104-107
29330363-0	2018	Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity.	Disulfides	0-9	titin	Homo sapiens	37-42
29330363-3	2018	Using single-molecule atomic force microscopy, we show that disulfide isomerization reactions within Ig domains enable a third mechanism of titin elasticity.	Disulfides	60-69	titin	Homo sapiens	140-145
29330363-4	2018	Oxidation of Ig domains leads to non-canonical disulfide bonds that stiffen titin while enabling force-triggered isomerization reactions to more extended states of the domains.	Disulfides	47-56	titin	Homo sapiens	76-81
31655942-3	2019	RESULTS: Lp(a) is composed of LDL-like particle and characteristic apolipoprotein(a) [apo(a)] connected by a disulfide bond.	Disulfides	109-118	lipoprotein(a)	Homo sapiens	9-14
29330363-5	2018	Using sequence and structural analyses, we show that 21% of titin"s I-band Ig domains contain a conserved cysteine triad that can engage in disulfide isomerization reactions.	Disulfides	140-149	titin	Homo sapiens	60-65
29191465-8	2018	Thermal melt experiment showed that the stability of DBM RyR NTD was higher than mammalian RyRs, probably due to a stable intra-domain disulfide bond observed in the crystal structure.	Disulfides	135-144	ryanodine receptor	Plutella xylostella	57-60
27647532-5	2017	Distinct redox forms of recombinant HMGB1 (rHMGB1) were used that included fully reduced HMGB (fr-HMGB1), which acted as a chemokine, and disulfide-HMGB1 (ds-HMGB1), which possessed cytokine activity.	Disulfides	138-147	high mobility group box 1	Mus musculus	36-41
28188021-2	2017	Lipoprotein (a) [Lp(a)] is a lipoprotein defined by presenting a specific apolipoprotein, ApoA, linked to the ApoB-100 by different types of chemical bonds, including a disulfide bridge.	Disulfides	169-178	lipoprotein(a)	Homo sapiens	17-22
28188021-2	2017	Lipoprotein (a) [Lp(a)] is a lipoprotein defined by presenting a specific apolipoprotein, ApoA, linked to the ApoB-100 by different types of chemical bonds, including a disulfide bridge.	Disulfides	169-178	lipoprotein(a)	Homo sapiens	90-94
31747588-5	2019	Mechanistically, stress-activated NPGPx inhibits O-GlcNAcase (OGA) through disulfide bonding to fine-tune global O-GlcNAcylation.	Disulfides	75-84	glutathione peroxidase 7	Homo sapiens	34-39
27774630-6	2017	Furthermore, binding of HMGB1 to AIM2 is stronger with fully reduced all-thiol HMGB1 than with partially oxidized disulfide-HMGB1, and binding strength corresponds to caspase-1 activation.	Disulfides	114-123	high mobility group box 1	Mus musculus	24-29
27774630-6	2017	Furthermore, binding of HMGB1 to AIM2 is stronger with fully reduced all-thiol HMGB1 than with partially oxidized disulfide-HMGB1, and binding strength corresponds to caspase-1 activation.	Disulfides	114-123	absent in melanoma 2	Mus musculus	33-37
29263120-3	2017	All three effects are prevented by MIF inhibition while intravesical disulfide HMGB1 alone can induce bladder pain.	Disulfides	69-78	high mobility group box 1	Mus musculus	79-84
29263120-9	2017	Intravesical disulfide HMGB1 induced abdominal mechanical hypersensitivity in both strains.	Disulfides	13-22	high mobility group box 1	Mus musculus	23-28
27787842-4	2017	A mutant mammalian cell line, HEK293S GnTI-, was used as an expression host for the production of a crystallizable-quality mPlxnA2 fragment, which contains several N-glycosylation sites and disulfide bonds.	Disulfides	190-199	plexin A2	Mus musculus	123-130
31747588-5	2019	Mechanistically, stress-activated NPGPx inhibits O-GlcNAcase (OGA) through disulfide bonding to fine-tune global O-GlcNAcylation.	Disulfides	75-84	O-GlcNAcase	Homo sapiens	49-60
31747588-5	2019	Mechanistically, stress-activated NPGPx inhibits O-GlcNAcase (OGA) through disulfide bonding to fine-tune global O-GlcNAcylation.	Disulfides	75-84	O-GlcNAcase	Homo sapiens	62-65
28942648-0	2017	Dynamics of Disulfide-Bond Disruption and Formation in the Thermal Unfolding of Ribonuclease A.	Disulfides	12-21	ribonuclease A family member 1, pancreatic	Homo sapiens	80-94
31570524-4	2019	Here, using cryogenic electron microscopy (cryo-EM) and small-angle X-ray scattering (SAXS) analyses of recombinant disulfide-linked dimeric MUC5B dimerization domain we identified an asymmetric, elongated twisted structure, with a double globular base.	Disulfides	116-125	mucin 5B, oligomeric mucus/gel-forming	Homo sapiens	141-146
28942648-2	2017	RNase A contains four disulfide bonds, which were found to be necessary for the native structure of the protein to form.	Disulfides	22-31	ribonuclease A family member 1, pancreatic	Homo sapiens	0-7
28942648-6	2017	The formation/disruption of disulfide bonds was found to be temperature dependent for three out of four disulfide bonds in RNase A, except for the most stable disulfide bond between Cys65 and Cys72.	Disulfides	28-37	ribonuclease A family member 1, pancreatic	Homo sapiens	123-130
28942648-6	2017	The formation/disruption of disulfide bonds was found to be temperature dependent for three out of four disulfide bonds in RNase A, except for the most stable disulfide bond between Cys65 and Cys72.	Disulfides	104-113	ribonuclease A family member 1, pancreatic	Homo sapiens	123-130
27732889-0	2016	Two fibrinogen-like proteins, FGL1 and FGL2 are disulfide-linked subunits of oligomers that specifically bind nonviable spermatozoa.	Disulfides	48-57	fibrinogen like 1	Homo sapiens	30-34
31662505-0	2019	Increased Expression of Ecto-NOX Disulfide-thiol Exchanger 1 (ENOX1) in Diabetic Mice Retina and its Involvement in Diabetic Retinopathy Development.	Disulfides	33-42	tripartite motif-containing 33	Mus musculus	24-28
27716795-3	2016	To dissect the influence of glycans on the conformation these regions, we focused on an antigenic peptide fragment from a disulfide bridge-bounded region spanning the V1 and V2 hyper-variable domains of HIV-1 gp120.	Disulfides	122-131	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	209-214
28942648-6	2017	The formation/disruption of disulfide bonds was found to be temperature dependent for three out of four disulfide bonds in RNase A, except for the most stable disulfide bond between Cys65 and Cys72.	Disulfides	104-113	ribonuclease A family member 1, pancreatic	Homo sapiens	123-130
28942648-9	2017	By analyzing residue-position fluctuations, it was found that native disulfide bonds are located in the highly flexible regions of the protein, which is probably why their presence is necessary for the stability of RNase A.	Disulfides	69-78	ribonuclease A family member 1, pancreatic	Homo sapiens	215-222
28878015-0	2017	Thioredoxin-1 actively maintains the pseudokinase MLKL in a reduced state to suppress disulfide bond-dependent MLKL polymer formation and necroptosis.	Disulfides	86-95	mixed lineage kinase domain like pseudokinase	Homo sapiens	50-54
28878015-0	2017	Thioredoxin-1 actively maintains the pseudokinase MLKL in a reduced state to suppress disulfide bond-dependent MLKL polymer formation and necroptosis.	Disulfides	86-95	mixed lineage kinase domain like pseudokinase	Homo sapiens	111-115
27414468-0	2016	Synthesis of novel disulfide and sulfone hybrid scaffolds as potent beta-glucuronidase inhibitor.	Disulfides	19-28	glucuronidase beta	Homo sapiens	68-86
26873625-6	2016	Cofilin is activated by dephosphorylation and may be oxidized in stressed neurons to form disulfide-linked dimers, required for bundling cofilin-actin filaments into stable rods.	Disulfides	90-99	cofilin 1	Homo sapiens	0-7
26873625-6	2016	Cofilin is activated by dephosphorylation and may be oxidized in stressed neurons to form disulfide-linked dimers, required for bundling cofilin-actin filaments into stable rods.	Disulfides	90-99	cofilin 1	Homo sapiens	137-144
31662505-0	2019	Increased Expression of Ecto-NOX Disulfide-thiol Exchanger 1 (ENOX1) in Diabetic Mice Retina and its Involvement in Diabetic Retinopathy Development.	Disulfides	33-42	ecto-NOX disulfide-thiol exchanger 1	Mus musculus	62-67
31662505-2	2019	Ecto-NOX disulfide-thiol exchanger 1 (ENOX1) is a member of the ecto-NOX family involved in the plasma membrane electron transport pathway.	Disulfides	9-18	tripartite motif-containing 33	Mus musculus	0-4
28920920-9	2017	The inability to clear misfolded proAVP with highly reactive cysteine thiols in the absence of Sel1L-Hrd1 ERAD causes proAVP to accumulate and participate in inappropriate intermolecular disulfide-bonded aggregates, promoted by the enzymatic activity of protein disulfide isomerase (PDI).	Disulfides	187-196	prolyl 4-hydroxylase subunit beta	Homo sapiens	254-281
28920920-9	2017	The inability to clear misfolded proAVP with highly reactive cysteine thiols in the absence of Sel1L-Hrd1 ERAD causes proAVP to accumulate and participate in inappropriate intermolecular disulfide-bonded aggregates, promoted by the enzymatic activity of protein disulfide isomerase (PDI).	Disulfides	187-196	prolyl 4-hydroxylase subunit beta	Homo sapiens	283-286
27502485-2	2016	In this study, we show that Tim17 contains a pair of highly conserved cysteine residues that form a structural disulfide bond exposed to the intermembrane space (IMS).	Disulfides	111-120	translocase of inner mitochondrial membrane 17A	Homo sapiens	28-33
31662505-2	2019	Ecto-NOX disulfide-thiol exchanger 1 (ENOX1) is a member of the ecto-NOX family involved in the plasma membrane electron transport pathway.	Disulfides	9-18	ecto-NOX disulfide-thiol exchanger 1	Mus musculus	38-43
27502485-4	2016	The disulfide bond in Tim17 is formed during insertion of the protein into the inner membrane.	Disulfides	4-13	translocase of inner mitochondrial membrane 17A	Homo sapiens	22-27
31662505-2	2019	Ecto-NOX disulfide-thiol exchanger 1 (ENOX1) is a member of the ecto-NOX family involved in the plasma membrane electron transport pathway.	Disulfides	9-18	tripartite motif-containing 33	Mus musculus	64-68
27502485-7	2016	Thus, import and oxidation of Tim17 are mediated by the mitochondrial disulfide relay, though the mechanism by which the disulfide bond in Tim17 is formed differs considerably from that of soluble IMS proteins.	Disulfides	70-79	translocase of inner mitochondrial membrane 17A	Homo sapiens	30-35
27502488-6	2016	http://dx.doi.org/10.1083/jcb.201602074) show that the TIM23 subunit Tim17 contains a disulfide bond that is crucial for protein translocation and channel gating.	Disulfides	86-95	translocase of inner mitochondrial membrane 17A	Homo sapiens	69-74
28875601-5	2017	A newly developed spectrophotometric method was used to measure native thiol (NT) and disulfide (DS) levels in FMF patients and an age-sex matched group of healthy controls.	Disulfides	97-99	MEFV innate immuity regulator, pyrin	Homo sapiens	111-114
28875601-10	2017	FMF-AP patients had significantly higher DS levels than FMF-AFP patients (P = 0.039).	Disulfides	41-43	MEFV innate immuity regulator, pyrin	Homo sapiens	0-3
31484064-4	2019	We highlight features that make the VISTA immunoglobulin variable (IgV)-like fold unique among B7 family members, including two additional disulfide bonds and an extended loop region with an attached helix that we show forms a contiguous binding epitope for a clinically relevant anti-VISTA antibody.	Disulfides	139-148	V-set immunoregulatory receptor	Homo sapiens	36-41
28767041-5	2017	A series of methods have demonstrated that per-thiol-beta-cyclodextrin (beta-CD-(SH)7) was successfully combined with HNTs via a redox-responsive disulfide bond, and folic acid-polyethylene glycol-adamantane (FA-PEG-Ad) was immobilized on the HNTs through the strong complexation between beta-CD/Ad.	Disulfides	146-155	beta-carotene oxygenase 1	Mus musculus	72-79
27233605-7	2016	Therefore, we investigated the epigenetic changes in the Gadd45b promoter region using mouse liver genomic DNA, the methylation-specific restriction enzyme (HpaII), and disulfide conversion.	Disulfides	169-178	growth arrest and DNA-damage-inducible 45 beta	Mus musculus	57-64
27311711-7	2016	Indeed, in Xenopus, zebrafish, and lamprey Tgs, key residues, including the hormonogenic tyrosines and the disulfide bond-forming cysteines critical for Tg function, are well conserved despite overall divergence of amino acid sequences.	Disulfides	107-116	thyroglobulin	Danio rerio	43-45
30707269-9	2019	Experiments reducing and alkylating the disulfide bond of BI-32169 showed that the lasso structure is preserved and heat stable and the associated conformational changes provide new insights about the role of the disulfide bond in the inhibitory activity against the human glucagon receptor.	Disulfides	40-49	glucagon receptor	Homo sapiens	273-290
26482581-2	2016	Recent findings suggest that the redox state of HMGB1 is a critical molecular feature of HMGB1 such that the reduced form (fr-HMGB1) is chemotactic, while the disulfide form (ds-HMGB1) is pro-inflammatory.	Disulfides	159-168	high mobility group box 1	Homo sapiens	48-53
26482581-2	2016	Recent findings suggest that the redox state of HMGB1 is a critical molecular feature of HMGB1 such that the reduced form (fr-HMGB1) is chemotactic, while the disulfide form (ds-HMGB1) is pro-inflammatory.	Disulfides	159-168	high mobility group box 1	Homo sapiens	89-94
26482581-2	2016	Recent findings suggest that the redox state of HMGB1 is a critical molecular feature of HMGB1 such that the reduced form (fr-HMGB1) is chemotactic, while the disulfide form (ds-HMGB1) is pro-inflammatory.	Disulfides	159-168	high mobility group box 1	Homo sapiens	89-94
26482581-2	2016	Recent findings suggest that the redox state of HMGB1 is a critical molecular feature of HMGB1 such that the reduced form (fr-HMGB1) is chemotactic, while the disulfide form (ds-HMGB1) is pro-inflammatory.	Disulfides	159-168	high mobility group box 1	Homo sapiens	89-94
28810662-5	2017	While endogenous galectin-9 is not required for basal cell surface PDI expression, exogenous galectin-9 mediated retention of cell surface PDI shifted the disulfide/thiol equilibrium on the T cell surface.	Disulfides	155-164	prolyl 4-hydroxylase subunit beta	Homo sapiens	139-142
30707269-9	2019	Experiments reducing and alkylating the disulfide bond of BI-32169 showed that the lasso structure is preserved and heat stable and the associated conformational changes provide new insights about the role of the disulfide bond in the inhibitory activity against the human glucagon receptor.	Disulfides	213-222	glucagon receptor	Homo sapiens	273-290
28648146-1	2017	The protein disulfide isomerase (PDI) family is a group of multifunctional endoplasmic reticulum (ER) enzymes that mediate the formation of disulfide bonds, catalyze the cysteine-based redox reactions and assist the quality control of client proteins.	Disulfides	12-21	prolyl 4-hydroxylase subunit beta	Homo sapiens	33-36
26482581-16	2016	Consistent with prior reports, the present findings demonstrate that the disulfide form of HMGB1 not only potentiates the neuroinflammatory response to a subsequent immune challenge in vivo, but also potentiates the sickness response to that challenge.	Disulfides	73-82	high mobility group box 1	Homo sapiens	91-96
26482581-19	2016	Taken together, the present results suggest that the redox state of HMGB1 is a critical determinant of the priming properties of HMGB1 such that the disulfide form of HMGB1 induces a primed immunophenotype in the CNS, which may result in an exacerbated neuroinflammatory response upon exposure to a subsequent pro-inflammatory stimulus.	Disulfides	149-158	high mobility group box 1	Homo sapiens	68-73
26482581-19	2016	Taken together, the present results suggest that the redox state of HMGB1 is a critical determinant of the priming properties of HMGB1 such that the disulfide form of HMGB1 induces a primed immunophenotype in the CNS, which may result in an exacerbated neuroinflammatory response upon exposure to a subsequent pro-inflammatory stimulus.	Disulfides	149-158	high mobility group box 1	Homo sapiens	129-134
26482581-19	2016	Taken together, the present results suggest that the redox state of HMGB1 is a critical determinant of the priming properties of HMGB1 such that the disulfide form of HMGB1 induces a primed immunophenotype in the CNS, which may result in an exacerbated neuroinflammatory response upon exposure to a subsequent pro-inflammatory stimulus.	Disulfides	149-158	high mobility group box 1	Homo sapiens	129-134
27020146-3	2016	Population-based and single phagosome analyses of phagosomal chemistries in murine macrophages revealed that activation of NOX2 via the Fcgamma receptor (FcgammaR) during phagocytosis decreased rates of proteolysis and disulfide reduction.	Disulfides	219-228	cytochrome b-245, beta polypeptide	Mus musculus	123-127
27020146-4	2016	Immunoglobulin G (IgG)-stimulated reactive oxygen species (ROS) production and the inhibition of phagosomal proteolysis and disulfide reduction were dependent on NOX2, FcgammaR and protein kinase C (PKC)/spleen tyrosine kinase (Syk) signaling.	Disulfides	124-133	cytochrome b-245, beta polypeptide	Mus musculus	162-166
28753126-2	2017	Proper gp160 folding in the ER requires core glycosylation, disulfide-bond formation and proline isomerization.	Disulfides	60-69	glutamyl aminopeptidase	Homo sapiens	7-12
31414279-3	2019	Here, we developed such a system by conjugating gelatin-based nanogels with the nucleolin-targeted AS1411 aptamer and deoxynucleotide-substituted siRNA together (Apt-GS/siRNA) via a disulfide linker to achieve transient docking of siRNA.	Disulfides	182-191	nucleolin	Homo sapiens	80-89
28549585-3	2017	Orexin-A has two closely located intramolecular disulfide bonds and is prone to misfolding due to the formation of incorrect disulfide bonds.	Disulfides	48-57	hypocretin	Mus musculus	0-8
27056327-3	2016	The transmembrane (TM) domain of p75 stabilizes the receptor dimers through a disulfide bond, essential for the NGF signaling.	Disulfides	78-87	PC4 and SFRS1 interacting protein 1	Homo sapiens	33-36
27056327-5	2016	Upon reconstitution in lipid micelles, p75-TM-WT forms the disulfide-linked dimers spontaneously.	Disulfides	59-68	PC4 and SFRS1 interacting protein 1	Homo sapiens	39-42
31262730-5	2019	IL-2 fragments produced after cleavage by MMP-9 remained linked by a disulfide bond and displayed a reduced affinity for all IL-2 receptor subunits and a distinct pattern and timing of signal transduction.	Disulfides	69-78	matrix metallopeptidase 9	Mus musculus	42-47
27109452-0	2016	The removal of disulfide bonds in amylin oligomers leads to the conformational change of the "native" amylin oligomers.	Disulfides	15-24	islet amyloid polypeptide	Homo sapiens	34-40
27109452-0	2016	The removal of disulfide bonds in amylin oligomers leads to the conformational change of the "native" amylin oligomers.	Disulfides	15-24	islet amyloid polypeptide	Homo sapiens	102-108
27109452-1	2016	The alpha-helical structure of the N-terminus of the "native" amylin Lys1-Cys7 consists of a disulfide bond between Cys2 and Cys7.	Disulfides	93-102	islet amyloid polypeptide	Homo sapiens	62-68
27109452-3	2016	Removal of the disulfide bonds in the "native" amylin oligomers decreases the polymorphism and induces the formation of longer stable cross-beta strands in the N-termini.	Disulfides	15-24	islet amyloid polypeptide	Homo sapiens	47-53
28549585-3	2017	Orexin-A has two closely located intramolecular disulfide bonds and is prone to misfolding due to the formation of incorrect disulfide bonds.	Disulfides	125-134	hypocretin	Mus musculus	0-8
28549585-4	2017	Protein disulfide isomerase (PDI) possesses disulfide interchange activity.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
28549585-5	2017	PDI can modify misfolded orexin-A to its native form by rearrangement of two disulfide bonds.	Disulfides	77-86	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
28549585-5	2017	PDI can modify misfolded orexin-A to its native form by rearrangement of two disulfide bonds.	Disulfides	77-86	hypocretin	Mus musculus	25-33
31497343-4	2019	Activation of integrins can be promoted by thiol-disulfide exchanges initiated by Protein Disulfide Isomerase (PDI).	Disulfides	49-58	prolyl 4-hydroxylase subunit beta	Homo sapiens	82-109
26923188-2	2016	Our previous work on the structure of the RANK-RANKL complex revealed that Loop3 of RANK, specifically the non-canonical disulfide bond at the tip, performs a crucial role in specific recognition of RANKL.	Disulfides	121-130	TNF receptor superfamily member 11a	Homo sapiens	42-46
31497343-4	2019	Activation of integrins can be promoted by thiol-disulfide exchanges initiated by Protein Disulfide Isomerase (PDI).	Disulfides	49-58	prolyl 4-hydroxylase subunit beta	Homo sapiens	111-114
26923188-2	2016	Our previous work on the structure of the RANK-RANKL complex revealed that Loop3 of RANK, specifically the non-canonical disulfide bond at the tip, performs a crucial role in specific recognition of RANKL.	Disulfides	121-130	TNF receptor superfamily member 11a	Homo sapiens	47-51
31042499-0	2019	Integrin-mediated cell adhesion requires extracellular disulfide exchange regulated by protein disulfide isomerase.	Disulfides	55-64	prolyl 4-hydroxylase subunit beta	Homo sapiens	87-114
27068954-6	2016	This involves the direct reduction of disulfides within ER Ca(2+)handling proteins themselves, but also the regulated interaction of ER chaperones and oxidoreductases such as calnexin or ERp57 with them.	Disulfides	38-48	calnexin	Homo sapiens	175-183
26846856-4	2016	The principal client-binding site in the Pdi1pb" domain is necessary not only for the functional Ero1p-Pdi1p disulfide relay but also for the activation of Ero1p.	Disulfides	109-118	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	41-46
31042499-8	2019	These data indicate that: a) Dependence on ecto-sulfhydryls for integrin-mediated adhesion is not exclusive to the platelet; b) PDI is involved in integrin-mediated adhesion, catalyzing disulfide bond exchange; c) PDI enhances cell adhesion by both its oxidoreductase activity and as a chaperone.	Disulfides	186-195	prolyl 4-hydroxylase subunit beta	Homo sapiens	128-131
26865631-11	2016	Disulfide cross-linking with directions opposing or along the bending angle of the beta2,3-sheet toward the alpha2-helix led to loss-of-function and gain-of-function of P2X4 receptors, respectively.	Disulfides	0-9	purinergic receptor P2X 4	Homo sapiens	169-173
26878852-4	2016	The C-terminal domain (57 residues), corresponding to elafin, is a cysteine-rich domain stabilized by four disulfide bridges and is characterized by a flat core and a flexible N-terminal part.	Disulfides	107-116	peptidase inhibitor 3	Homo sapiens	54-60
31138621-7	2019	In vivo, both AtERO1 and AtERO2 have two distinct oxidized isoforms (Ox1 and Ox2), which are determined by the formation or breakage of the putative regulatory disulfide.	Disulfides	160-169	endoplasmic reticulum oxidoreductins 2	Arabidopsis thaliana	25-31
31310642-9	2019	2) That human INMT harbors significant thioether-S-methyltransferase (TEMT) activity with a higher affinity for DMSe than tryptamine, 3) The reduction of a 44C/254C disulfide bond in hINMT that increases Vmax is proposed.	Disulfides	165-174	indolethylamine N-methyltransferase	Homo sapiens	14-18
26982744-9	2016	Interestingly, the active diaryl disulfides inhibited proliferation and viability at concentrations where they stabilized Pdcd4, suggesting that Pdcd4 stabilization might contribute to the anti-proliferative properties.	Disulfides	33-43	programmed cell death 4	Homo sapiens	122-127
26982744-9	2016	Interestingly, the active diaryl disulfides inhibited proliferation and viability at concentrations where they stabilized Pdcd4, suggesting that Pdcd4 stabilization might contribute to the anti-proliferative properties.	Disulfides	33-43	programmed cell death 4	Homo sapiens	145-150
26964514-0	2016	Secreted APE1/Ref-1 inhibits TNF-alpha-stimulated endothelial inflammation via thiol-disulfide exchange in TNF receptor.	Disulfides	85-94	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	9-13
26964514-0	2016	Secreted APE1/Ref-1 inhibits TNF-alpha-stimulated endothelial inflammation via thiol-disulfide exchange in TNF receptor.	Disulfides	85-94	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	14-19
26964514-6	2016	Additionally, recombinant human (rh) APE1/Ref-1 with reducing activity induced a conformational change in rh TNF-alpha receptor 1 (TNFR1) by thiol-disulfide exchange.	Disulfides	147-156	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	37-41
26964514-6	2016	Additionally, recombinant human (rh) APE1/Ref-1 with reducing activity induced a conformational change in rh TNF-alpha receptor 1 (TNFR1) by thiol-disulfide exchange.	Disulfides	147-156	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	42-47
31310642-9	2019	2) That human INMT harbors significant thioether-S-methyltransferase (TEMT) activity with a higher affinity for DMSe than tryptamine, 3) The reduction of a 44C/254C disulfide bond in hINMT that increases Vmax is proposed.	Disulfides	165-174	indolethylamine N-methyltransferase	Homo sapiens	39-68
31310642-9	2019	2) That human INMT harbors significant thioether-S-methyltransferase (TEMT) activity with a higher affinity for DMSe than tryptamine, 3) The reduction of a 44C/254C disulfide bond in hINMT that increases Vmax is proposed.	Disulfides	165-174	indolethylamine N-methyltransferase	Homo sapiens	70-74
31310642-9	2019	2) That human INMT harbors significant thioether-S-methyltransferase (TEMT) activity with a higher affinity for DMSe than tryptamine, 3) The reduction of a 44C/254C disulfide bond in hINMT that increases Vmax is proposed.	Disulfides	165-174	indolethylamine N-methyltransferase	Homo sapiens	183-188
30470534-3	2019	The formation of disulfide bridge is mediated via protein disulfide isomerase (PDI) family and other oxidoreductases, which contribute to reactive oxygen species (ROS) generation and consumption in the ER.	Disulfides	17-26	prolyl 4-hydroxylase subunit beta	Homo sapiens	50-77
26601956-6	2016	Prx2 became glutathionylated when its disulfide was incubated with GSH and when the reduced protein was treated with H2O2 and GSH.	Disulfides	38-47	peroxiredoxin 2	Mus musculus	0-4
30470534-3	2019	The formation of disulfide bridge is mediated via protein disulfide isomerase (PDI) family and other oxidoreductases, which contribute to reactive oxygen species (ROS) generation and consumption in the ER.	Disulfides	17-26	prolyl 4-hydroxylase subunit beta	Homo sapiens	79-82
26159064-4	2016	RESULTS: The peroxidatic Cys91 residue of two Prx1p peptides can be linked by a disulfide, which can be reduced by thioredoxin and by GSH (Km=6.1 muM).	Disulfides	80-89	thioredoxin peroxidase PRX1	Saccharomyces cerevisiae S288C	46-51
30658161-13	2019	Reconstituting disulfide HMGB1 during reperfusion reversed these protective effects.	Disulfides	15-24	high mobility group box 1	Mus musculus	25-30
26159064-7	2016	The structural unit of native Prx1p is a dimer whose subunits are not covalently linked, but a hexameric assembly of three disulfide-bound dimers can also be formed.	Disulfides	123-132	thioredoxin peroxidase PRX1	Saccharomyces cerevisiae S288C	30-35
31067467-3	2019	Here, we use single-molecule force spectroscopy techniques to measure the force-velocity relation of folding titin domains that contain single internal disulfide bonds, a common feature throughout the titin I-band.	Disulfides	152-161	titin	Homo sapiens	109-114
27819029-7	2016	This work employed NMR, X-ray cryptography, and other biophysical methods to study a disulfide bond in Csk SH2 domain.	Disulfides	85-94	C-terminal Src kinase	Homo sapiens	103-106
31067467-3	2019	Here, we use single-molecule force spectroscopy techniques to measure the force-velocity relation of folding titin domains that contain single internal disulfide bonds, a common feature throughout the titin I-band.	Disulfides	152-161	titin	Homo sapiens	201-206
26864324-6	2016	The two Ang-2-targeting single-chain variable fragments are disulfide-stabilized and fused to the C-terminus of the heavy chain of bevacizumab.	Disulfides	60-69	angiopoietin 2	Homo sapiens	8-13
30710560-0	2019	Elucidation of the mechanism of disulfide exchange between staphylococcal thioredoxin2 and thioredoxin reductase2: A structural insight.	Disulfides	32-41	AT695_RS07555	Staphylococcus aureus	74-85
26515416-10	2015	Macrophages produce smooth muscle cell mitogens in response to disulfide HMGB1 also in a TLR4/myeloid differentiation primary response gene (88)/Trif-dependent manner.	Disulfides	63-72	high mobility group box 1	Mus musculus	73-78
30710560-1	2019	The redox homeostasis of cytoplasm is maintained by a series of disulfide exchange reactions mediated by proteins belonging to the thioredoxin superfamily.	Disulfides	64-73	AT695_RS07555	Staphylococcus aureus	131-142
26387067-2	2015	The drug delivery polymeric micelles lie in the covalent conjugation of each cisplatin drug to the PLG chains through a disulfide bond.	Disulfides	120-129	plasminogen	Homo sapiens	99-102
30992562-2	2019	Here, we present mechanisms of action of protein disulfide isomerase (PDI)-the most versatile disulfide-introducing enzyme in the endoplasmic reticulum-during the catalysis of oxidative protein folding.	Disulfides	49-58	prolyl 4-hydroxylase subunit beta	Homo sapiens	70-73
26349060-1	2015	Extracellular high-mobility group box 1 (HMGB1) (disulfide form), via activation of toll-like receptor 4 (TLR4)-dependent signaling, is a strong driver of pathologic inflammation in both acute and chronic conditions.	Disulfides	49-58	high mobility group box 1	Homo sapiens	14-39
26349060-1	2015	Extracellular high-mobility group box 1 (HMGB1) (disulfide form), via activation of toll-like receptor 4 (TLR4)-dependent signaling, is a strong driver of pathologic inflammation in both acute and chronic conditions.	Disulfides	49-58	high mobility group box 1	Homo sapiens	41-46
26349060-4	2015	Here we report that the first-generation HIV-PI saquinavir (SQV), as well as a newly identified mammalian protease inhibitor STO33438 (334), potently block disulfide HMGB1-induced TLR4 activation, as assayed by the production of TNF-alpha by human monocyte-derived macrophages (THP-1).	Disulfides	156-165	high mobility group box 1	Homo sapiens	166-171
26349060-10	2015	Disulfide HMGB1 drives pathologic inflammation in many models by activating signaling through TLR4.	Disulfides	0-9	high mobility group box 1	Homo sapiens	10-15
26349060-11	2015	Cell-based screening identified the mammalian protease cathepsin V as a novel therapeutic target to inhibit TLR4-mediated inflammation induced by extracellular HMGB1 (disulfide form).	Disulfides	167-176	high mobility group box 1	Homo sapiens	160-165
26349060-12	2015	We identified two protease inhibitors (PIs) that block cathepsin V and thereby inhibit disulfide HMGB1-induced TLR4 activation: saquinavir (SQV), a first-generation PI targeting viral HIV protease and STO33438 (334), targeting mammalian proteases.	Disulfides	87-96	high mobility group box 1	Homo sapiens	97-102
26514956-1	2015	INTRODUCTION: Protein disulfide isomerase (PDI) catalyzes disulfide bond exchange.	Disulfides	22-31	prolyl 4-hydroxylase subunit beta	Homo sapiens	43-46
26514956-10	2015	CONCLUSIONS: PDI-mediated disulfide bond exchange plays a pivotal role in the post-ligation phase of alphaIIbbeta3-mediated adhesion to fibrinogen, while this step in alphavbeta3-mediated adhesion is independent of disulfide exchange.	Disulfides	26-35	prolyl 4-hydroxylase subunit beta	Homo sapiens	13-16
26514956-10	2015	CONCLUSIONS: PDI-mediated disulfide bond exchange plays a pivotal role in the post-ligation phase of alphaIIbbeta3-mediated adhesion to fibrinogen, while this step in alphavbeta3-mediated adhesion is independent of disulfide exchange.	Disulfides	215-224	prolyl 4-hydroxylase subunit beta	Homo sapiens	13-16
31013569-0	2019	Disruption of Structural Disulfides of Coagulation FXIII-B Subunit; Functional Implications for a Rare Bleeding Disorder.	Disulfides	25-35	coagulation factor XIII B chain	Homo sapiens	51-58
25977307-2	2015	Engagement of CD40 with its natural trimeric ligand or with cross-linked antibodies results in disulfide-linked CD40 (dl-CD40) homodimer formation, a process mediated by the cysteine-238 residues of the cytoplasmic tail of CD40.	Disulfides	95-104	CD40 molecule	Homo sapiens	14-18
25977307-2	2015	Engagement of CD40 with its natural trimeric ligand or with cross-linked antibodies results in disulfide-linked CD40 (dl-CD40) homodimer formation, a process mediated by the cysteine-238 residues of the cytoplasmic tail of CD40.	Disulfides	95-104	CD40 molecule	Homo sapiens	112-116
25977307-2	2015	Engagement of CD40 with its natural trimeric ligand or with cross-linked antibodies results in disulfide-linked CD40 (dl-CD40) homodimer formation, a process mediated by the cysteine-238 residues of the cytoplasmic tail of CD40.	Disulfides	95-104	CD40 molecule	Homo sapiens	112-116
25977307-2	2015	Engagement of CD40 with its natural trimeric ligand or with cross-linked antibodies results in disulfide-linked CD40 (dl-CD40) homodimer formation, a process mediated by the cysteine-238 residues of the cytoplasmic tail of CD40.	Disulfides	95-104	CD40 molecule	Homo sapiens	112-116
31013569-3	2019	Three mutations in the F13B gene have been reported on its structural disulfide bonds.	Disulfides	70-79	coagulation factor XIII B chain	Homo sapiens	23-27
31013569-4	2019	In the present study, we investigate the structural and functional importance of all 20 structural disulfide bonds in FXIII-B subunit.	Disulfides	99-108	coagulation factor XIII B chain	Homo sapiens	118-125
31013569-7	2019	The structural flexibility of these disulfide bonds was studied using classical MD simulation performed on a FXIII-B subunit monomer model.	Disulfides	36-45	coagulation factor XIII B chain	Homo sapiens	109-116
30877193-1	2019	Plant gamma-glutamylcysteine ligase (GCL), catalyzing the first and tightly regulated step of glutathione (GSH) biosynthesis, is redox-activated via formation of an intramolecular disulfide bond.	Disulfides	180-189	glutamate-cysteine ligase catalytic subunit	Homo sapiens	6-35
26470705-9	2015	Additionally, genes encoding proteins known to regulate disulfide cross-linking, including sulfhydryl oxidase (QSOX1) and thioredoxin (TXN), were identified which suggests that coordinated up-regulation of genes in the white isthmus is associated with eggshell membrane fibre formation.	Disulfides	56-65	quiescin Q6 sulfhydryl oxidase 1	Gallus gallus	111-116
26470705-9	2015	Additionally, genes encoding proteins known to regulate disulfide cross-linking, including sulfhydryl oxidase (QSOX1) and thioredoxin (TXN), were identified which suggests that coordinated up-regulation of genes in the white isthmus is associated with eggshell membrane fibre formation.	Disulfides	56-65	thioredoxin	Gallus gallus	122-133
26470705-9	2015	Additionally, genes encoding proteins known to regulate disulfide cross-linking, including sulfhydryl oxidase (QSOX1) and thioredoxin (TXN), were identified which suggests that coordinated up-regulation of genes in the white isthmus is associated with eggshell membrane fibre formation.	Disulfides	56-65	thioredoxin	Gallus gallus	135-138
30877193-1	2019	Plant gamma-glutamylcysteine ligase (GCL), catalyzing the first and tightly regulated step of glutathione (GSH) biosynthesis, is redox-activated via formation of an intramolecular disulfide bond.	Disulfides	180-189	glutamate-cysteine ligase catalytic subunit	Homo sapiens	37-40
26068405-5	2015	Unraveling of the helical structure and formation of disulfide bonds due to oxidation were implicated in the altered myosin cross-linking pattern during subsequent TGase reactions.	Disulfides	53-62	transglutaminase 1	Homo sapiens	164-169
30658057-5	2019	The crystal structures of G23A-HNP4 and T27A-HNP4 were determined, both exhibiting a disulfide-stabilized canonical alpha-defensin dimer identical to wild-type HNP4.	Disulfides	85-94	defensin alpha 4	Homo sapiens	45-49
30658057-5	2019	The crystal structures of G23A-HNP4 and T27A-HNP4 were determined, both exhibiting a disulfide-stabilized canonical alpha-defensin dimer identical to wild-type HNP4.	Disulfides	85-94	defensin alpha 4	Homo sapiens	45-49
30971821-4	2019	Breakthroughs in the structural characterization of the HIV-1 Env trimer have previously been achieved by generating soluble and proteolytically cleaved trimers of gp140 Env that are stabilized by a disulfide bond, an isoleucine-to-proline substitution at residue 559 and a truncation at residue 664 (SOSIP.664 trimers)5,11-18.	Disulfides	199-208	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	62-65
26246604-2	2015	The lumen of the mammalian ER contains &gt;20 members of the protein disulfide isomerase (PDI) superfamily, which ensure formation of the correct set of intramolecular and intermolecular disulfide bonds as crucial, rate-limiting reactions of the protein folding process.	Disulfides	69-78	prolyl 4-hydroxylase subunit beta	Homo sapiens	90-93
26201258-5	2015	On the one hand, TFF2 binds to MUC6 via non-covalent lectin interactions with the glycotope GlcNAcalpha1 4Galbeta1 R. On the other hand, TFF2 is probably also covalently bound to MUC6 via disulfide bridges.	Disulfides	188-197	mucin 6, oligomeric mucus/gel-forming	Homo sapiens	31-35
26201258-5	2015	On the one hand, TFF2 binds to MUC6 via non-covalent lectin interactions with the glycotope GlcNAcalpha1 4Galbeta1 R. On the other hand, TFF2 is probably also covalently bound to MUC6 via disulfide bridges.	Disulfides	188-197	mucin 6, oligomeric mucus/gel-forming	Homo sapiens	179-183
30971821-4	2019	Breakthroughs in the structural characterization of the HIV-1 Env trimer have previously been achieved by generating soluble and proteolytically cleaved trimers of gp140 Env that are stabilized by a disulfide bond, an isoleucine-to-proline substitution at residue 559 and a truncation at residue 664 (SOSIP.664 trimers)5,11-18.	Disulfides	199-208	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	170-173
30452880-7	2019	H2O2 derived from Nox4 activated type III CD38 by forming a disulfide bond between Cys164 and Cys177, resulting in increased cADPR formation.	Disulfides	60-69	NADPH oxidase 4	Homo sapiens	18-22
26227798-3	2015	Molecular dynamics (MD) and disulfide crosslinking studies suggest that apo-GCGR can adopt both an open and closed conformation associated with extensive contacts between the ECD and 7TM domain.	Disulfides	28-37	glucagon receptor	Homo sapiens	76-80
26143924-6	2015	The catalytic activity of the MTMR8 phosphatase domain is inhibited by oxidation and is reversibly reactivated by reduction, suggesting the presence of an oxidation-protective intermediate other than a disulfide bond owing to the absence of a cysteine within a disulfide-bond distance from Cys338.	Disulfides	202-211	myotubularin related protein 8	Homo sapiens	30-35
26143924-6	2015	The catalytic activity of the MTMR8 phosphatase domain is inhibited by oxidation and is reversibly reactivated by reduction, suggesting the presence of an oxidation-protective intermediate other than a disulfide bond owing to the absence of a cysteine within a disulfide-bond distance from Cys338.	Disulfides	261-270	myotubularin related protein 8	Homo sapiens	30-35
30754725-4	2019	We have also proposed that at least two FKBPs, namely FKBP36, encoded by the Fkbp6 gene and FKBP51, encoded by the Fkbp5 gene, can form dimers bound via a disulfide bridge in the nucleus.	Disulfides	155-164	FKBP prolyl isomerase family member 6 (inactive)	Homo sapiens	54-60
25956655-3	2015	Recent data demonstrate that APE1 interacts with the mitochondrial import and assembly protein Mia40 suggesting the involvement of a redox-assisted mechanism, dependent on the disulfide transfer system, to be responsible of APE1 trafficking into the mitochondria.	Disulfides	176-185	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	29-33
25956655-3	2015	Recent data demonstrate that APE1 interacts with the mitochondrial import and assembly protein Mia40 suggesting the involvement of a redox-assisted mechanism, dependent on the disulfide transfer system, to be responsible of APE1 trafficking into the mitochondria.	Disulfides	176-185	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	224-228
25956655-6	2015	In this study, we demonstrated that: (i) APE1 and Mia40 interact through disulfide bond formation; and (ii) Mia40 expression levels directly affect APE1"s mitochondrial translocation and, consequently, play a role in the maintenance of mitochondrial DNA integrity.	Disulfides	73-82	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	41-45
25956655-6	2015	In this study, we demonstrated that: (i) APE1 and Mia40 interact through disulfide bond formation; and (ii) Mia40 expression levels directly affect APE1"s mitochondrial translocation and, consequently, play a role in the maintenance of mitochondrial DNA integrity.	Disulfides	73-82	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	148-152
25944298-0	2015	Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120.	Disulfides	39-48	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	161-166
30754725-4	2019	We have also proposed that at least two FKBPs, namely FKBP36, encoded by the Fkbp6 gene and FKBP51, encoded by the Fkbp5 gene, can form dimers bound via a disulfide bridge in the nucleus.	Disulfides	155-164	FKBP prolyl isomerase family member 6 (inactive)	Homo sapiens	77-82
30530491-3	2019	CCS1, the budding yeast (S. cerevisiae) Cu chaperone for Cu-zinc (Zn) superoxide dismutase (SOD1) activates by directly promoting both Cu delivery and disulfide formation in SOD1.	Disulfides	151-160	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	174-178
25697776-1	2015	Oxidative folding in the endoplasmic reticulum (ER) involves ER oxidoreductin 1 (Ero1)-mediated disulfide formation in protein disulfide isomerase (PDI).	Disulfides	96-105	prolyl 4-hydroxylase subunit beta	Homo sapiens	119-146
25697776-1	2015	Oxidative folding in the endoplasmic reticulum (ER) involves ER oxidoreductin 1 (Ero1)-mediated disulfide formation in protein disulfide isomerase (PDI).	Disulfides	96-105	prolyl 4-hydroxylase subunit beta	Homo sapiens	148-151
25697776-5	2015	Through its carboxyterminal active site, PDI unlocks this seal by forming a Cys(208)/Cys(241)-dependent mixed-disulfide complex with Ero1alpha.	Disulfides	110-119	prolyl 4-hydroxylase subunit beta	Homo sapiens	41-44
25697777-3	2015	Accumulating knowledge of cysteine-based redox reactions catalyzed by members of the protein disulfide isomerase (PDI) family has revealed that these enzymes play pivotal roles in productive protein folding accompanied by disulfide formation, as well as efficient ER-associated degradation accompanied by disulfide reduction.	Disulfides	93-102	prolyl 4-hydroxylase subunit beta	Homo sapiens	114-117
30530491-10	2019	We also noted that efficient transfer from the entry site to the active site is entirely dependent upon the oxidation of the conserved intrasubunit disulfide bond in SOD1.	Disulfides	148-157	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	166-170
25697777-3	2015	Accumulating knowledge of cysteine-based redox reactions catalyzed by members of the protein disulfide isomerase (PDI) family has revealed that these enzymes play pivotal roles in productive protein folding accompanied by disulfide formation, as well as efficient ER-associated degradation accompanied by disulfide reduction.	Disulfides	222-231	prolyl 4-hydroxylase subunit beta	Homo sapiens	85-112
25697777-3	2015	Accumulating knowledge of cysteine-based redox reactions catalyzed by members of the protein disulfide isomerase (PDI) family has revealed that these enzymes play pivotal roles in productive protein folding accompanied by disulfide formation, as well as efficient ER-associated degradation accompanied by disulfide reduction.	Disulfides	222-231	prolyl 4-hydroxylase subunit beta	Homo sapiens	114-117
30666186-4	2018	Previously, we have shown that moderate illumination (halogen lamp, 1,500 lx, 1-5 h) of mammalian eyes provokes disulfide dimerization of recoverin, a calcium-dependent regulator of GRK1.	Disulfides	112-121	recoverin	Homo sapiens	138-147
30666186-8	2018	Both disulfide dimer and oxidized monomer (or oxidation mimicking C39D mutant) of recoverin exhibit lowered alpha-helical content and thermal stability of their apo-forms, as well as increased Ca2+ affinity.	Disulfides	5-14	recoverin	Homo sapiens	82-91
30666186-9	2018	Meanwhile, the oxidized monomer and C39D mutant of recoverin demonstrate impaired ability to bind photoreceptor membranes and regulate GRK1, whereas disulfide dimer exhibits notably improved membrane binding and GRK1 inhibition in absence of Ca2+.	Disulfides	149-158	recoverin	Homo sapiens	51-60
25873657-1	2015	In plants, the presence of thioredoxin (Trx), peroxiredoxin (Prx), and sulfiredoxin (Srx) has been reported as a component of a redox system involved in the control of dithiol-disulfide exchanges of target proteins, which modulate redox signalling during development and stress adaptation.	Disulfides	176-185	sulfiredoxin 1	Homo sapiens	71-83
30545068-5	2018	Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems.	Disulfides	0-9	glutaredoxin	Homo sapiens	118-130
25873657-1	2015	In plants, the presence of thioredoxin (Trx), peroxiredoxin (Prx), and sulfiredoxin (Srx) has been reported as a component of a redox system involved in the control of dithiol-disulfide exchanges of target proteins, which modulate redox signalling during development and stress adaptation.	Disulfides	176-185	sulfiredoxin 1	Homo sapiens	85-88
25865227-4	2015	Compounds that disrupt extracellular disulfide bonds could inactivate EGFR, HER2, and HER3 in unison.	Disulfides	37-46	erb-b2 receptor tyrosine kinase 3	Homo sapiens	86-90
25769921-0	2015	The C-terminal disulfide bonds of Helicobacter pylori GroES are critical for IL-8 secretion via the TLR4-dependent pathway in gastric epithelial cells.	Disulfides	15-24	chemokine (C-X-C motif) ligand 15	Mus musculus	77-81
28575153-11	2017	Oxidative stress during epileptogenesis was associated with de novo brain and blood generation of disulfide high mobility group box 1 (HMGB1), a neuroinflammatory molecule implicated in seizure mechanisms.	Disulfides	98-107	high mobility group box 1	Homo sapiens	108-133
28575153-11	2017	Oxidative stress during epileptogenesis was associated with de novo brain and blood generation of disulfide high mobility group box 1 (HMGB1), a neuroinflammatory molecule implicated in seizure mechanisms.	Disulfides	98-107	high mobility group box 1	Homo sapiens	135-140
28575153-12	2017	Drug-induced reduction of oxidative stress prevented disulfide HMGB1 generation, thus highlighting a potential novel mechanism contributing to therapeutic effects.	Disulfides	53-62	high mobility group box 1	Homo sapiens	63-68
25645953-8	2015	N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters.	Disulfides	170-179	glutathione-disulfide reductase	Homo sapiens	69-90
25645953-8	2015	N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters.	Disulfides	170-179	glutathione-disulfide reductase	Homo sapiens	213-234
28658624-2	2017	NADPH-dependent reduction of thioredoxin-1 (Trx1) disulfide and glutathione disulfide by thioredoxin reductase-1 (TrxR1) and glutathione reductase (Gsr), respectively, fuels antioxidant systems and deoxyribonucleotide synthesis.	Disulfides	50-59	glutathione reductase	Mus musculus	125-146
30545068-5	2018	Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems.	Disulfides	0-9	glutathione-disulfide reductase	Homo sapiens	143-164
28658624-2	2017	NADPH-dependent reduction of thioredoxin-1 (Trx1) disulfide and glutathione disulfide by thioredoxin reductase-1 (TrxR1) and glutathione reductase (Gsr), respectively, fuels antioxidant systems and deoxyribonucleotide synthesis.	Disulfides	50-59	gutter shaped root	Mus musculus	148-151
25740509-4	2015	Multistate structural modeling revealed that the R201 residue in Kv7.2, corresponding to R230 in Kv7.3, stabilized the resting and nearby voltage-sensing domain states by forming an intricate network of electrostatic interactions with neighboring negatively charged residues, a result also confirmed by disulfide trapping experiments.	Disulfides	303-312	potassium voltage-gated channel subfamily Q member 3	Homo sapiens	97-102
30374335-3	2018	In this study, we further characterize TrxP, TrxQ and the canonical thioredoxin, TrxA, by identifying candidate protein substrates in S. aureus cells using a mechanism-based profiling assay where we trap mixed disulfides that exist between the attacking cysteine of a FLAG-tagged Trx and a persulfidated cysteine on the candidate substrate protein in cells.	Disulfides	210-220	AT695_RS07555	Staphylococcus aureus	68-79
25527541-6	2015	Cytoplasmic expression of Agp (in E. coli Origami B) gave a functional enzyme preparation (kcat for phosphoryl transfer from alphaGlc 1-P to water, 40 s(-1)) that was shown by mass spectrometry to exhibit no free cysteines and the native intramolecular disulfide bond between Cys(189) and Cys(195).	Disulfides	253-262	glucose-1-phosphatase precursor	Escherichia coli	26-29
28364042-1	2017	Thiol isomerases such as protein-disulfide isomerase (PDI) direct disulfide rearrangements required for proper folding of nascent proteins synthesized in the endoplasmic reticulum.	Disulfides	33-42	prolyl 4-hydroxylase subunit beta	Homo sapiens	54-57
30111624-3	2018	Earlier studies indicated that different UGT isoforms could exist in higher-order homo-oligomers or at least dimers within the membrane, but the formation of intermolecular disulfide bridges between UGT molecules was not often observed.	Disulfides	173-182	UDP glucuronosyltransferase family 1 member A complex locus	Homo sapiens	41-44
30111624-3	2018	Earlier studies indicated that different UGT isoforms could exist in higher-order homo-oligomers or at least dimers within the membrane, but the formation of intermolecular disulfide bridges between UGT molecules was not often observed.	Disulfides	173-182	UDP glucuronosyltransferase family 1 member A complex locus	Homo sapiens	199-202
25288108-5	2015	MeHg covalently modified protein disulfide isomerase (PDI), which is important for disulfide bond formation in nascent proteins in the ER lumen.	Disulfides	33-42	prolyl 4-hydroxylase subunit beta	Homo sapiens	54-57
29857171-5	2018	The oxidation of beta4-HbA is associated with the formation of a disulfide bridge between residues Cys112(G14) of beta1/beta4 and beta2/beta3 chains.	Disulfides	65-74	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	130-141
25433341-1	2015	The functional and structural significance of the intrasubunit disulfide bond in copper-zinc superoxide dismutase (SOD1) was studied by characterizing mutant forms of human SOD1 (hSOD) and yeast SOD1 lacking the disulfide bond.	Disulfides	63-72	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	173-177
25433341-6	2015	Using pulse radiolysis, we determined SOD activities of yeast and human SOD1s lacking disulfide bonds and found that they were enzymatically active at ~10% of the wild type rate.	Disulfides	86-95	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	38-41
25433341-7	2015	These results are contrary to earlier reports that the intrasubunit disulfide bonds in SOD1 are essential for SOD activity.	Disulfides	68-77	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	87-90
25559892-0	2015	MD-2 is required for disulfide HMGB1-dependent TLR4 signaling.	Disulfides	21-30	high mobility group box 1	Mus musculus	31-36
25559892-4	2015	Here we demonstrate that the extracellular TLR4 adaptor, myeloid differentiation factor 2 (MD-2), binds specifically to the cytokine-inducing disulfide isoform of HMGB1, to the exclusion of other isoforms.	Disulfides	142-151	high mobility group box 1	Mus musculus	163-168
28438540-6	2017	This led us to obtain a new OTR-selective analog by comprehensive amino acid substitutions of OT and replacement of the disulfide bond.	Disulfides	120-129	oxytocin receptor	Homo sapiens	28-31
28504645-6	2017	The pathologic disulfide HMGB1 isoform progressively increased in blood before epilepsy onset and prospectively identified animals that developed the disease.	Disulfides	15-24	high mobility group box 1	Homo sapiens	25-30
28504645-7	2017	Consistent with animal data, we observed early expression of disulfide HMGB1 in patients with newly diagnosed epilepsy, and its persistence was associated with subsequent seizures.	Disulfides	61-70	high mobility group box 1	Homo sapiens	71-76
30960878-3	2018	The thiophenol group would be involved with disulfide bonds between the polymer chains and siRNA modified with free thiols (thiol-siRNA) to form and pi-pi interactions between the pendent aromatic groups and coprostane ring of the bile acid.	Disulfides	44-53	glucosidase beta 2	Mus musculus	231-240
28504645-8	2017	In contrast with patients with well-controlled epilepsy, patients with chronic, drug-refractory epilepsy persistently expressed the acetylated, disulfide HMGB1 isoforms.	Disulfides	144-153	high mobility group box 1	Homo sapiens	154-159
28405784-3	2017	Three cysteine residues and one disulfide bond conserved within known alpha-amylase inhibitors were present in AhAI.	Disulfides	32-41	alpha-amylase	Tribolium castaneum	70-83
25754036-4	2015	The unique characteristics of these IgG4 MAM conformers arise from the fact that on exchange of the heavy chains between IgG4 molecules, in some of them only one noncanonical bond Cys226-Cys229 is formed in the central part of the "hinge region" instead of two canonical interchain disulfide bonds Cys226-Cys226 and Cys229-Cys229.	Disulfides	282-291	sarcoglycan gamma	Homo sapiens	41-44
25524207-4	2015	Of these non-antigen-contacting regions, the tertiary structure determined by the inter-chain disulfide bonds was found to strongly affect the FVIII-mimetic activity.	Disulfides	94-103	coagulation factor VIII	Homo sapiens	143-148
25524207-5	2015	Interestingly, IgG4-like disulfide bonds between Cys131 in the heavy chain and Cys114 in the light chain, and disulfide bonds between the two heavy chains at the hinge region were indispensable for the high FVIII-mimetic activity.	Disulfides	25-34	coagulation factor VIII	Homo sapiens	207-212
25524207-5	2015	Interestingly, IgG4-like disulfide bonds between Cys131 in the heavy chain and Cys114 in the light chain, and disulfide bonds between the two heavy chains at the hinge region were indispensable for the high FVIII-mimetic activity.	Disulfides	110-119	coagulation factor VIII	Homo sapiens	207-212
26577736-5	2015	We describe a roadmap to produce isotopically labeled (15)N and (13)C posttranslationally modified proteins, such as the outer domain of HIV-1 gp120, which has four disulfide bonds and 15 potential sites of N-linked glycosylation.	Disulfides	165-174	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	143-148
28358192-1	2017	The protein disulfide isomerase (PDI) family comprises a wide set of enzymes mainly involved in thiol-disulfide exchange reactions in the endoplasmic reticulum.	Disulfides	12-21	protein disulfide isomerase	Arabidopsis thaliana	33-36
24684506-11	2014	INNOVATION AND CONCLUSION: H2S directly targets some disulfide bonds in EGFR, which activates the EGFR/gab1/PI3K/Akt pathway and subsequent Na(+)/K(+)-ATPase endocytosis and inhibition in renal tubular epithelial cells.	Disulfides	53-62	GRB2-associated binding protein 1	Rattus norvegicus	103-107
30061385-3	2018	Detailed biochemical characterization of AUG-alpha by mass spectrometry shows that the four conserved cysteines located in the augmentor domain (AD) form two intramolecular disulfide bridges while a fifth, primate-specific cysteine located in the N-terminal variable region mediates dimerization through formation of a disulfide bridge between two AUG-alpha molecules.	Disulfides	173-182	ALK and LTK ligand 2	Homo sapiens	41-50
25190807-5	2014	Disulfide bridges formed at C349/C356 and C465/C468 of the cysteine-rich domain are necessary for the enhancement of Kv4.2 channel surface expression but not its interaction with Kv4.2 subunits.	Disulfides	0-9	potassium voltage-gated channel subfamily D member 2	Homo sapiens	117-122
28245108-0	2017	Determination of the Disulfide Structure of Murine Meteorin, a Neurotrophic Factor, by LC-MS and Electron Transfer Dissociation-High-Energy Collisional Dissociation Analysis of Proteolytic Fragments.	Disulfides	21-30	meteorin, glial cell differentiation regulator	Mus musculus	51-59
28245108-5	2017	Here, we have successfully determined the disulfide structure for murine Meteorin by LC-MS analysis of fragments generated by trypsin plus endoprotease-Asp-N. For proteolytic fragments linked by more than one disulfide bond, we used electron transfer dissociation (ETD) to partially dissociate disulfide bonds followed by high-energy collisional dissociation (HCD) to determine disulfide linkages.	Disulfides	42-51	meteorin, glial cell differentiation regulator	Mus musculus	73-81
28245108-5	2017	Here, we have successfully determined the disulfide structure for murine Meteorin by LC-MS analysis of fragments generated by trypsin plus endoprotease-Asp-N. For proteolytic fragments linked by more than one disulfide bond, we used electron transfer dissociation (ETD) to partially dissociate disulfide bonds followed by high-energy collisional dissociation (HCD) to determine disulfide linkages.	Disulfides	209-218	meteorin, glial cell differentiation regulator	Mus musculus	73-81
28245108-5	2017	Here, we have successfully determined the disulfide structure for murine Meteorin by LC-MS analysis of fragments generated by trypsin plus endoprotease-Asp-N. For proteolytic fragments linked by more than one disulfide bond, we used electron transfer dissociation (ETD) to partially dissociate disulfide bonds followed by high-energy collisional dissociation (HCD) to determine disulfide linkages.	Disulfides	209-218	meteorin, glial cell differentiation regulator	Mus musculus	73-81
28245108-5	2017	Here, we have successfully determined the disulfide structure for murine Meteorin by LC-MS analysis of fragments generated by trypsin plus endoprotease-Asp-N. For proteolytic fragments linked by more than one disulfide bond, we used electron transfer dissociation (ETD) to partially dissociate disulfide bonds followed by high-energy collisional dissociation (HCD) to determine disulfide linkages.	Disulfides	209-218	meteorin, glial cell differentiation regulator	Mus musculus	73-81
28245108-6	2017	Our analysis revealed that the ten Cys residues in murine Meteorin form five disulfide bonds with Cys7 (C1) linked to Cys28 (C2), Cys59 (C3) to Cys95 (C4), Cys148 (C5) to Cys219 (C8), Cys151 (C6) to Cys243 (C9), and Cys161 (C7) to Cys266 (C10).	Disulfides	77-86	meteorin, glial cell differentiation regulator	Mus musculus	58-66
28245108-7	2017	Since the ten Cys residues are highly conserved in Meteorin and Cometin, it is likely that the disulfide linkages are also conserved.	Disulfides	95-104	meteorin, glial cell differentiation regulator	Mus musculus	51-59
25219356-1	2014	WFDC1/ps20 is a whey acidic protein four-disulfide core member that exhibits diverse growth and immune-associated functions in vitro.	Disulfides	41-50	WAP four-disulfide core domain 1	Mus musculus	0-5
30061385-3	2018	Detailed biochemical characterization of AUG-alpha by mass spectrometry shows that the four conserved cysteines located in the augmentor domain (AD) form two intramolecular disulfide bridges while a fifth, primate-specific cysteine located in the N-terminal variable region mediates dimerization through formation of a disulfide bridge between two AUG-alpha molecules.	Disulfides	319-328	ALK and LTK ligand 2	Homo sapiens	41-50
25219356-1	2014	WFDC1/ps20 is a whey acidic protein four-disulfide core member that exhibits diverse growth and immune-associated functions in vitro.	Disulfides	41-50	WAP four-disulfide core domain 1	Mus musculus	6-10
29845893-10	2018	RESULTS: Mutations of two cysteine residues (C118 and C1165), involved in the formation of the intramolecular disulfide bridge between the N-terminal ectodomain and one of the extracellular loops, mildly altered the function and the targeting of DUOX1, while this bridge is crucial for DUOX2 function.	Disulfides	110-119	dual oxidase 1	Homo sapiens	246-251
28374821-5	2017	In contrast to the previously reported disulfide linkage between Gpi8 and Gpi16 in human and trypanosome GPIT, our data show that the luminal domains of S. cerevisiae Gpi8 and S. cerevisiae Gpi16 do not interact directly, nor do they form a disulfide bond in the intact S. cerevisiae GPIT.	Disulfides	241-250	GPI-anchor transamidase subunit GPI16	Saccharomyces cerevisiae S288C	190-195
29845893-13	2018	CONCLUSION: An intermolecular disulfide bridge rather than an intramolecular disulfide bridge is important for both the trafficking and H2O2-generating activity of the DUOX1-DUOXA1 complex.	Disulfides	30-39	dual oxidase 1	Homo sapiens	168-173
29845893-13	2018	CONCLUSION: An intermolecular disulfide bridge rather than an intramolecular disulfide bridge is important for both the trafficking and H2O2-generating activity of the DUOX1-DUOXA1 complex.	Disulfides	77-86	dual oxidase 1	Homo sapiens	168-173
25202015-4	2014	Here, we characterized the redox features of the Calvin-Benson enzyme phosphoglycerate kinase (PGK1) from the eukaryotic green alga Chlamydomonas reinhardtii, and we show that C. reinhardtii PGK1 (CrPGK1) activity is inhibited by the formation of a single regulatory disulfide bond with a low midpoint redox potential (-335 mV at pH 7.9).	Disulfides	267-276	uncharacterized protein	Chlamydomonas reinhardtii	95-99
25202015-4	2014	Here, we characterized the redox features of the Calvin-Benson enzyme phosphoglycerate kinase (PGK1) from the eukaryotic green alga Chlamydomonas reinhardtii, and we show that C. reinhardtii PGK1 (CrPGK1) activity is inhibited by the formation of a single regulatory disulfide bond with a low midpoint redox potential (-335 mV at pH 7.9).	Disulfides	267-276	uncharacterized protein	Chlamydomonas reinhardtii	191-195
25123642-8	2014	Western blot analysis, using monoclonal antibodies, demonstrated that the crucial inter-subunit disulfide bond linking the p35 and p40 subunits is intact in the purified hIL-12.	Disulfides	96-105	interleukin 9	Homo sapiens	131-134
28179147-7	2017	The structure also reveals an unexpected asymmetric disulfide bond-linked PDZ dimer that allows simultaneous parallel binding of CXCR2 to two PDZ domains.	Disulfides	52-61	C-X-C motif chemokine receptor 2	Homo sapiens	129-134
29915238-3	2018	Biophysical and mutation studies show that JMJD7 has a unique dimerization mode, with interactions between monomers involving both N- and C-terminal regions and disulfide bond formation.	Disulfides	161-170	jumonji domain containing 7	Homo sapiens	43-48
28368308-6	2017	As characterizing the native heterodimer is challenging due to interference from monomers and homodimers, we engineered a "trapped" disulfide-linked CXCL7-CXCL1 heterodimer.	Disulfides	132-141	pro-platelet basic protein	Homo sapiens	149-154
28265627-0	2017	Synthesis, structural characterization and conversion of dinuclear iron-sulfur clusters containing the disulfide ligand: [Cp*Fe(mu-eta2:eta2-bdt)(cis-mu-eta1:eta1-S2)FeCp*], [Cp*Fe(mu-S(C6H4S2))(cis-mu-eta1:eta1-S2)FeCp*], and [{Cp*Fe(bdt)}2(trans-mu-eta1:eta1-S2)].	Disulfides	103-112	DNA polymerase iota	Homo sapiens	131-135
25030891-5	2014	In addition, sperm decondensation failure in PDIA3 antibody-injected oocytes was rescued by dithiothreitol, a commonly used disulfide bond reducer.	Disulfides	124-133	protein disulfide isomerase family A member 3	Sus scrofa	45-50
28265627-0	2017	Synthesis, structural characterization and conversion of dinuclear iron-sulfur clusters containing the disulfide ligand: [Cp*Fe(mu-eta2:eta2-bdt)(cis-mu-eta1:eta1-S2)FeCp*], [Cp*Fe(mu-S(C6H4S2))(cis-mu-eta1:eta1-S2)FeCp*], and [{Cp*Fe(bdt)}2(trans-mu-eta1:eta1-S2)].	Disulfides	103-112	DNA polymerase iota	Homo sapiens	136-140
24850837-1	2014	The thiol/disulfide redox network mediated by the thioredoxin (Trx) system in chloroplasts ensures light-responsive control of diverse crucial functions.	Disulfides	10-19	thioredoxin H-type 1	Arabidopsis thaliana	50-61
29869502-15	2018	Intracellular wild-type SOD1 spontaneously binds zinc, while it needs the copper chaperone for superoxide dismutase (CCS) for copper delivery and disulfide bond formation.	Disulfides	146-155	copper chaperone for superoxide dismutase	Homo sapiens	74-115
24850837-1	2014	The thiol/disulfide redox network mediated by the thioredoxin (Trx) system in chloroplasts ensures light-responsive control of diverse crucial functions.	Disulfides	10-19	thioredoxin H-type 1	Arabidopsis thaliana	63-66
23920130-4	2014	The epitopes of the cell-, fibrin-, collagen-binding FN domains and the extra domain A (EDA) FN segment retained the ability to bind their specific monoclonal antibodies, whereas the fibrin-heparin domain (N-terminal end) and the area around the disulfide bridges (C-terminal end) of the FN polypeptide did not show any reactivities with their respective specific antibodies.	Disulfides	246-255	ectodysplasin A	Homo sapiens	88-91
27920255-5	2017	We identified two MLKL mutants that could not oligomerize into octamers, although they formed a tetramer, and also, one MLKL mutant could spontaneously form a disulfide bond-linked octamer.	Disulfides	159-168	mixed lineage kinase domain like pseudokinase	Homo sapiens	120-124
29869502-15	2018	Intracellular wild-type SOD1 spontaneously binds zinc, while it needs the copper chaperone for superoxide dismutase (CCS) for copper delivery and disulfide bond formation.	Disulfides	146-155	copper chaperone for superoxide dismutase	Homo sapiens	117-120
28271460-3	2018	Disulfide bridges identified in 3D model of CCL19 protein give extra stability to the overall protein structure.	Disulfides	0-9	C-C motif chemokine ligand 19	Homo sapiens	44-49
28166275-0	2017	Evidence for disulfide bonds in SR Protein Kinase 1 (SRPK1) that are required for activity and nuclear localization.	Disulfides	13-22	SRSF protein kinase 1	Homo sapiens	32-51
28166275-0	2017	Evidence for disulfide bonds in SR Protein Kinase 1 (SRPK1) that are required for activity and nuclear localization.	Disulfides	13-22	SRSF protein kinase 1	Homo sapiens	53-58
28166275-7	2017	We propose that such a network of intramolecular disulfide bonds mediates the bending of the spacer region thus allowing the proximal positioning of the two catalytic subunits which is a prerequisite for SRPK1 activity.	Disulfides	49-58	SRSF protein kinase 1	Homo sapiens	204-209
24752778-9	2014	Subsequent to identification of the transferrin receptor (TfR) as a component of a high molecular mass KLRG1 complex, they demonstrate that a fraction of mouse KLRG1 molecules undergoes disulfide-bonding with TfRs and colocalises with the latter at the cell surface.	Disulfides	186-195	transferrin receptor	Mus musculus	36-56
24752778-9	2014	Subsequent to identification of the transferrin receptor (TfR) as a component of a high molecular mass KLRG1 complex, they demonstrate that a fraction of mouse KLRG1 molecules undergoes disulfide-bonding with TfRs and colocalises with the latter at the cell surface.	Disulfides	186-195	transferrin receptor	Mus musculus	58-61
29697253-4	2018	hIAPP contains a strictly conserved disulfide bond between residues 2 and 7, which forms a small loop at the N-terminus of the molecule.	Disulfides	36-45	islet amyloid polypeptide	Homo sapiens	0-5
24692542-5	2014	The disulfide-bridged variant showed ~20% increased FVIII stability, and FVIIIa did not decay during the time course measured.	Disulfides	4-13	coagulation factor VIII	Homo sapiens	52-57
29697253-6	2018	Mutations in this region are rare, and the disulfide loop plays a role in receptor binding; however, the contribution of this region to the aggregation of hIAPP is not well understood.	Disulfides	43-52	islet amyloid polypeptide	Homo sapiens	155-160
29395576-9	2018	Disulfide-HMGB1 formed a complex with poly(I:C), as did reduced- and oxidized-HMGB1, albeit to a lesser extent.	Disulfides	0-9	high mobility group box 1	Homo sapiens	10-15
24636989-4	2014	PDIA5 contributed to disulfide bond rearrangement in ATF6alpha under stress conditions, thereby leading to ATF6alpha export from the ER and activation of its target genes.	Disulfides	21-30	protein disulfide isomerase family A member 5	Homo sapiens	0-5
24685145-4	2014	Here, we show that N33/Tusc3 possesses a membrane-anchored N-terminal thioredoxin domain located in the ER lumen that may form transient mixed disulfide complexes with OST substrates.	Disulfides	143-152	tumor suppressor candidate 3	Homo sapiens	19-22
24685145-4	2014	Here, we show that N33/Tusc3 possesses a membrane-anchored N-terminal thioredoxin domain located in the ER lumen that may form transient mixed disulfide complexes with OST substrates.	Disulfides	143-152	tumor suppressor candidate 3	Homo sapiens	23-28
24685145-6	2014	Structural and biochemical data show that N33/Tusc3 prefers peptides bearing a hydrophobic residue two residues away from the cysteine forming the mixed disulfide with N33/Tusc3.	Disulfides	153-162	tumor suppressor candidate 3	Homo sapiens	42-45
24685145-6	2014	Structural and biochemical data show that N33/Tusc3 prefers peptides bearing a hydrophobic residue two residues away from the cysteine forming the mixed disulfide with N33/Tusc3.	Disulfides	153-162	tumor suppressor candidate 3	Homo sapiens	46-51
24685145-6	2014	Structural and biochemical data show that N33/Tusc3 prefers peptides bearing a hydrophobic residue two residues away from the cysteine forming the mixed disulfide with N33/Tusc3.	Disulfides	153-162	tumor suppressor candidate 3	Homo sapiens	168-171
24692016-4	2014	To overcome this, chemical additives or a disulfide catalyst, protein disulfide isomerase (PDI), are generally used in refolding experiments to regulate disulfide-coupled peptide and protein folding.	Disulfides	42-51	prolyl 4-hydroxylase subunit beta	Homo sapiens	62-89
24692016-4	2014	To overcome this, chemical additives or a disulfide catalyst, protein disulfide isomerase (PDI), are generally used in refolding experiments to regulate disulfide-coupled peptide and protein folding.	Disulfides	42-51	prolyl 4-hydroxylase subunit beta	Homo sapiens	91-94
24692016-4	2014	To overcome this, chemical additives or a disulfide catalyst, protein disulfide isomerase (PDI), are generally used in refolding experiments to regulate disulfide-coupled peptide and protein folding.	Disulfides	70-79	prolyl 4-hydroxylase subunit beta	Homo sapiens	91-94
24692016-5	2014	This unit describes such methods in the context of the thermodynamic and kinetic control of peptide and protein folding, including (1) regulation of disulfide-coupled peptides and protein folding assisted by chemical additives, (2) reductive unfolding of disulfide-containing peptides and proteins, and (3) regulation of disulfide-coupled peptide and protein folding using PDI.	Disulfides	149-158	prolyl 4-hydroxylase subunit beta	Homo sapiens	373-376
24692016-5	2014	This unit describes such methods in the context of the thermodynamic and kinetic control of peptide and protein folding, including (1) regulation of disulfide-coupled peptides and protein folding assisted by chemical additives, (2) reductive unfolding of disulfide-containing peptides and proteins, and (3) regulation of disulfide-coupled peptide and protein folding using PDI.	Disulfides	255-264	prolyl 4-hydroxylase subunit beta	Homo sapiens	373-376
24692016-5	2014	This unit describes such methods in the context of the thermodynamic and kinetic control of peptide and protein folding, including (1) regulation of disulfide-coupled peptides and protein folding assisted by chemical additives, (2) reductive unfolding of disulfide-containing peptides and proteins, and (3) regulation of disulfide-coupled peptide and protein folding using PDI.	Disulfides	255-264	prolyl 4-hydroxylase subunit beta	Homo sapiens	373-376
24522867-7	2014	These differences may be attributed primarily to the very low pKa of Cys23 in hGrx1 and allow rationalisation of conclusion (ii) above: hGrx1 may catalyse the oxidation of Atox1(dithiol) by GSSG, but not the complementary reduction of the oxidised Atox1(disulfide) by GSH unless Cu(aq)(+) is present at a concentration that allows binding of Cu(I) to reduced Atox1 but not to hGrx1.	Disulfides	254-263	glutaredoxin	Homo sapiens	136-141
24522867-7	2014	These differences may be attributed primarily to the very low pKa of Cys23 in hGrx1 and allow rationalisation of conclusion (ii) above: hGrx1 may catalyse the oxidation of Atox1(dithiol) by GSSG, but not the complementary reduction of the oxidised Atox1(disulfide) by GSH unless Cu(aq)(+) is present at a concentration that allows binding of Cu(I) to reduced Atox1 but not to hGrx1.	Disulfides	254-263	glutaredoxin	Homo sapiens	136-141
23923978-10	2014	INNOVATION: The data enable the first experimentally proven structural model of occludin and its homophilic interaction sites, in which the ECL2, via intraloop disulfide formation, has a central role in occludin"s hypoxia-sensitive oligomerization and to regulate the structure of TJs.	Disulfides	160-169	occludin	Homo sapiens	80-88
23923978-10	2014	INNOVATION: The data enable the first experimentally proven structural model of occludin and its homophilic interaction sites, in which the ECL2, via intraloop disulfide formation, has a central role in occludin"s hypoxia-sensitive oligomerization and to regulate the structure of TJs.	Disulfides	160-169	occludin	Homo sapiens	203-211
24497506-4	2014	The peptide-channel complex is stabilized by a disulfide tether between Cys24 of the peptide and Cys910 of rat (r) NaV1.2.	Disulfides	47-56	sodium voltage-gated channel alpha subunit 2	Rattus norvegicus	115-121
24563858-4	2014	We will describe here three redox sensors, the transcription factors OxyR, Yap1 and Pap1, which respond by disulfide bond formation to hydrogen peroxide stress, focusing specially on the differences among the three peroxide-sensing mechanisms.	Disulfides	107-116	Yes1 associated transcriptional regulator	Homo sapiens	75-79
23919619-5	2014	H2O2 oxidizes Cys57 of GPx7 to sulfenic acid, which can be resolved by Cys86 to form an intramolecular disulfide bond.	Disulfides	103-112	glutathione peroxidase 7	Homo sapiens	23-27
23919619-6	2014	Both the disulfide form and sulfenic acid form of GPx7 can oxidize PDI for catalyzing oxidative folding.	Disulfides	9-18	prolyl 4-hydroxylase subunit beta	Homo sapiens	67-70
23919619-11	2014	Thus, the Ero1alpha/GPx7/PDI triad generates two disulfide bonds and two H2O molecules at the expense of a single O2 molecule.	Disulfides	49-58	glutathione peroxidase 7	Homo sapiens	20-24
23919619-11	2014	Thus, the Ero1alpha/GPx7/PDI triad generates two disulfide bonds and two H2O molecules at the expense of a single O2 molecule.	Disulfides	49-58	prolyl 4-hydroxylase subunit beta	Homo sapiens	25-28
24475161-1	2014	The QSOX1 protein (Quiescin Sulfhydryl oxidase 1) catalyzes the formation of disulfide bonds and is involved in the folding and stability of proteins.	Disulfides	77-86	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	4-9
24275656-8	2014	The human TIRAP TIR domain crystal structure reveals a unique N-terminal TIR domain fold containing a disulfide bond formed by Cys(89) and Cys(134).	Disulfides	102-111	TIR domain containing adaptor protein	Homo sapiens	10-15
24165122-7	2013	To test whether kinase stability directly contributed to substrate selectivity of the kinase, we engineered IPK1 mutants with disulfide bonds that artificially stabilized the N-lobe in an IP-independent manner thereby mimicking its substrate-bound state in the absence of IP.	Disulfides	126-135	inositol-pentakisphosphate 2-kinase	Homo sapiens	108-112
24165122-9	2013	The crystal structure of the IPK1 E82C/S142C mutant confirmed the presence of the disulfide bond and revealed a small shift in the N-lobe.	Disulfides	82-91	inositol-pentakisphosphate 2-kinase	Homo sapiens	29-33
24364984-7	2013	SiRNA-mediated knockdown of ATF6alpha and ERp57 during HDM administration in mice resulted in a decrease in components of HDM-induced ER stress, disulfide mediated oligomerization of Bak, and activation of caspase-3.	Disulfides	145-154	activating transcription factor 6	Mus musculus	28-37
24357805-9	2013	Furthermore, domain mapping of CST1 showed that the disulfide-bonded conformation, or conserved folding, of CST1 is important for its secretion and for the neutralization of CST3 activity.	Disulfides	52-61	cystatin SN	Homo sapiens	31-35
24357805-9	2013	Furthermore, domain mapping of CST1 showed that the disulfide-bonded conformation, or conserved folding, of CST1 is important for its secretion and for the neutralization of CST3 activity.	Disulfides	52-61	cystatin SN	Homo sapiens	108-112
24357805-9	2013	Furthermore, domain mapping of CST1 showed that the disulfide-bonded conformation, or conserved folding, of CST1 is important for its secretion and for the neutralization of CST3 activity.	Disulfides	52-61	cystatin C	Homo sapiens	174-178
24427321-11	2014	Curcumin may suppress GSTM5 expression to enhance the lethal effect of irinotecan on LOVO cells, and maybe their combination via the affection of PDI and PRDX4 to disturb the formation and reduction of disulfides results in inducing apoptosis of LOVO cell.	Disulfides	202-212	prolyl 4-hydroxylase subunit beta	Homo sapiens	146-149
24161674-3	2013	A disulfide dimer peptide of CXCL14(51-77) bound to CXCR4 with comparable affinity to full length CXCL14, and exhibited CXCL12 inhibitor activity.	Disulfides	2-11	C-X-C motif chemokine ligand 12	Homo sapiens	120-126
24427810-3	2013	Two cysteines, Cys23 and Cys45, in the A-domain of HMGB1 form a disulfide bond under oxidative conditions.	Disulfides	64-73	high mobility group box 1	Homo sapiens	51-56
24427810-8	2013	The reorientation of the Phe38 ring by the disulfide bond in the A-domain may explain the reduced HMGB1 binding affinity towards cisplatinated DNA.	Disulfides	43-52	high mobility group box 1	Homo sapiens	98-103
24062305-8	2013	Our results also showed that physiological concentrations of glutathione, NADPH, and glutathione reductase reduced the non-active site disulfide in vitro.	Disulfides	135-144	glutathione-disulfide reductase	Homo sapiens	85-106
23434683-4	2013	The initial process of introducing disulfides into substrate proteins is catalyzed by the protein disulfide isomerase (PDI) oxidoreductases which become reduced and, therefore, have to be re-oxidized to allow for further rounds of disulfide exchange.	Disulfides	35-45	prolyl 4-hydroxylase subunit beta	Homo sapiens	90-117
23434683-4	2013	The initial process of introducing disulfides into substrate proteins is catalyzed by the protein disulfide isomerase (PDI) oxidoreductases which become reduced and, therefore, have to be re-oxidized to allow for further rounds of disulfide exchange.	Disulfides	35-45	prolyl 4-hydroxylase subunit beta	Homo sapiens	119-122
23434683-4	2013	The initial process of introducing disulfides into substrate proteins is catalyzed by the protein disulfide isomerase (PDI) oxidoreductases which become reduced and, therefore, have to be re-oxidized to allow for further rounds of disulfide exchange.	Disulfides	35-44	prolyl 4-hydroxylase subunit beta	Homo sapiens	90-117
23434683-4	2013	The initial process of introducing disulfides into substrate proteins is catalyzed by the protein disulfide isomerase (PDI) oxidoreductases which become reduced and, therefore, have to be re-oxidized to allow for further rounds of disulfide exchange.	Disulfides	35-44	prolyl 4-hydroxylase subunit beta	Homo sapiens	119-122
23434683-5	2013	This review will discuss the various pathways operating in the ER that facilitate oxidation of the PDI oxidoreductases and ultimately catalyze disulfide bond formation in substrate proteins.	Disulfides	143-152	prolyl 4-hydroxylase subunit beta	Homo sapiens	99-102
24025674-4	2013	In contrast, transient ROS generation was not observed with the parental roGFP2 probe without Grx1, which exhibits slower thiol-disulfide exchange.	Disulfides	128-137	glutaredoxin	Homo sapiens	94-98
24098777-4	2013	Stimulated Tregs, which naturally express GARP, and Th cells transfected with GARP secrete a previously unknown form of latent TGF-beta1 that is disulfide-linked to GARP.	Disulfides	145-154	cyclic nucleotide gated channel subunit beta 1	Homo sapiens	78-82
24098777-4	2013	Stimulated Tregs, which naturally express GARP, and Th cells transfected with GARP secrete a previously unknown form of latent TGF-beta1 that is disulfide-linked to GARP.	Disulfides	145-154	cyclic nucleotide gated channel subunit beta 1	Homo sapiens	78-82
24098777-7	2013	We conclude that in stimulated human Tregs, GARP not only displays latent TGF-beta1 at the cell surface, but also increases its secretion by forming soluble disulfide-linked complexes.	Disulfides	157-166	cyclic nucleotide gated channel subunit beta 1	Homo sapiens	44-48
24043701-1	2013	Ero1-alpha and endoplasmic reticulum (ER) oxidoreductases of the protein disulfide isomerase (PDI) family promote the efficient introduction of disulfide bonds into nascent polypeptides in the ER.	Disulfides	73-82	prolyl 4-hydroxylase subunit beta	Homo sapiens	94-97
23827315-2	2013	ER-60, which has been implicated in apoB degradation, is a protein disulfide isomerase (PDI) that forms or rearranges disulfide bonds in substrate proteins and also possesses cysteine protease activity.	Disulfides	67-76	prolyl 4-hydroxylase subunit beta	Homo sapiens	88-91
23765404-0	2013	Extracellular disulfide bridges serve different purposes in two homologous chemokine receptors, CCR1 and CCR5.	Disulfides	14-23	C-C motif chemokine receptor 1	Homo sapiens	96-100
23207101-6	2013	Both HMGB1 containing a disulfide bond between C23 and C45, which induces chemokine and cytokine release by activating TLR4, and HMGB1 terminally oxidized to contain a cysteine sulfonate are inactive in recruiting leukocytes.	Disulfides	24-33	high mobility group box 1	Homo sapiens	5-10
23207101-6	2013	Both HMGB1 containing a disulfide bond between C23 and C45, which induces chemokine and cytokine release by activating TLR4, and HMGB1 terminally oxidized to contain a cysteine sulfonate are inactive in recruiting leukocytes.	Disulfides	24-33	nucleolin	Homo sapiens	47-50
23696644-6	2013	The actin binding domain of drebrin decreases the intrastrand disulfide cross-linking of Cys-41 (in the DNase I binding loop) to Cys-374 (C-terminal) but increases the interstrand disulfide cross-linking of Cys-265 (hydrophobic loop) to Cys-374 in the yeast mutants Q41C and S265C, respectively.	Disulfides	180-189	drebrin 1	Homo sapiens	28-35
23825428-6	2013	Here we show that human beta1 and beta2 subunits alter interactions between bound Mg2+ and gating charge R213 and disrupt the disulfide bond formation at the VSD-CTD interface of mouse Slo1, indicating that the beta subunits alter the VSD-CTD interface.	Disulfides	126-135	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	34-39
23825428-6	2013	Here we show that human beta1 and beta2 subunits alter interactions between bound Mg2+ and gating charge R213 and disrupt the disulfide bond formation at the VSD-CTD interface of mouse Slo1, indicating that the beta subunits alter the VSD-CTD interface.	Disulfides	126-135	potassium large conductance calcium-activated channel, subfamily M, alpha member 1	Mus musculus	185-189
23875128-8	2013	The amino acid sequence alignment indicated that the disulfide linkage position is conserved in all IFNalpha family members.	Disulfides	53-62	interferon alpha 2	Homo sapiens	100-108
23659383-4	2013	We prepared FVIII mutants with nascent disulfide bridges between A3 and C1 domains (Gly1750Cys/Arg2116Cys and Ala1866Cys/Ser2119Cys) or C1 and C2 domains (Ser2029Cys/Pro2292Cys).	Disulfides	39-48	coagulation factor VIII	Homo sapiens	12-17
23750247-9	2013	Additional experiments revealed that Fn14 dimerization occurs during cell lysis via formation of an intermolecular disulfide bond at cysteine residue 122.	Disulfides	115-124	TNF receptor superfamily member 12A	Homo sapiens	37-41
23395816-1	2013	Chitosan-disulfide-conjugated LMW-PEI (CS-ss-PEI) was designed to combine the biocompatibility of chitosan and the gene delivery ability of polyethylenimine (PEI) using bio-reducible disulfide for bone morphogenetic protein (BMP2) gene delivery in mediating osteogenic differentiation.	Disulfides	9-18	bone morphogenetic protein 2	Homo sapiens	225-229
23234870-4	2013	In this context, the most compelling data comes from recent studies demonstrating that around 10% of T-ALL patients display IL7R gain-of-function mutations leading, in most cases, to disulfide bond-dependent homodimerization of two mutant receptors and consequent constitutive activation of downstream signaling, with ensuing cell transformation in vitro and tumorigenic ability in vivo.	Disulfides	183-192	interleukin 7 receptor	Homo sapiens	124-128
23447529-4	2013	Using a unique NMR-based approach, we have investigated the kinetics of HMGB1 oxidation and the half-lives of all-thiol and disulfide HMGB1 species in serum, saliva, and cell culture medium.	Disulfides	124-133	high mobility group box 1	Homo sapiens	134-139
23447529-9	2013	Thus, the balance between the roles of all-thiol and disulfide HMGB1 proteins depends significantly on the extracellular environment and can also be artificially modulated by ligands.	Disulfides	53-62	high mobility group box 1	Homo sapiens	63-68
23479735-6	2013	This disulfide-linked CXCL1 dimer binds CXCR2 with nanomolar affinity and shows potent agonist activity in various cellular assays.	Disulfides	5-14	C-X-C motif chemokine receptor 2	Homo sapiens	40-45
23618462-1	2013	BACKGROUND: The disulfide-bonded region (DSR) of HIV-1 gp41 mediates association with gp120 and plays a role in transmission of receptor-induced conformational changes in gp120 to gp41 that activate membrane fusion function.	Disulfides	16-25	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	86-91
23618462-1	2013	BACKGROUND: The disulfide-bonded region (DSR) of HIV-1 gp41 mediates association with gp120 and plays a role in transmission of receptor-induced conformational changes in gp120 to gp41 that activate membrane fusion function.	Disulfides	16-25	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	171-176
23521534-5	2013	PDI catalyzes an isomerization of disulfide bridges within the thioredoxin motif C600XXC603 of the MPD and results in a drastic structural change between an active open state and an inactive closed conformation.	Disulfides	34-43	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
23083489-1	2013	AIMS: Protein disulfide isomerase (PDI) is an abundant endoplasmic reticulum (ER)-resident chaperone and oxidoreductase that catalyzes formation and rearrangement (isomerization) of disulfide bonds, thereby participating in protein folding.	Disulfides	14-23	prolyl 4-hydroxylase subunit beta	Homo sapiens	35-38
23526393-0	2013	Inter-chain disulfide bond improved protein trans-splicing increases plasma coagulation activity in C57BL/6 mice following portal vein FVIII gene delivery by dual vectors.	Disulfides	12-21	coagulation factor VIII	Mus musculus	135-140
23526393-3	2013	Dual-vector delivery of the FVIII gene in cultured cells showed that replacement of Met226 in the heavy chain and Asp1828 in the light chain with Cys residues could facilitate inter-chain disulfide linking and improve protein trans-splicing, increasing the levels of spliced FVIII protein.	Disulfides	188-197	coagulation factor VIII	Mus musculus	28-33
23526393-8	2013	These findings indicate that improving protein trans-splicing by inter-chain disulfide bonding is a promising approach for increasing the efficacy of dual-vector based FVIII gene transfer.	Disulfides	77-86	coagulation factor VIII	Mus musculus	168-173
23318500-2	2013	Linked by a specific disulfide bond (Cys(100)-Cys(650)), the N-terminal (N(t)) and the EC3 loop C-terminal (C(t)) segments of angiotensin II (AngII) receptor 1 (AT(1)R) have been identified to form an extracellular site for binding the agonist N(t) segment (Asp(1) and Arg(2) residues).	Disulfides	21-30	angiotensin II receptor type 1	Homo sapiens	126-167
23318500-4	2013	By homology, a similar site might be considered for DABK binding to B(1)R since this receptor contains the same structural elements for composing the site in AT(1)R, namely the disulfide bond and the EC3 loop Asp(712) residue.	Disulfides	177-186	angiotensin II receptor type 1	Homo sapiens	158-164
23192347-2	2013	Protein-disulfide isomerase (PDI) and related members of the PDI family assist in the folding of substrates by catalyzing the oxidation of two cysteines and isomerization of disulfide bonds as well as by acting as chaperones.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
23192347-2	2013	Protein-disulfide isomerase (PDI) and related members of the PDI family assist in the folding of substrates by catalyzing the oxidation of two cysteines and isomerization of disulfide bonds as well as by acting as chaperones.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	61-64
23122408-1	2013	The kinetics of folding and dimerization of bone morphogenetic protein-2 (BMP-2), a disulfide-connected, homodimeric cystine-knot protein and a member of the transforming growth factor-beta superfamily, was analyzed under a variety of different conditions.	Disulfides	84-93	bone morphogenetic protein 2	Homo sapiens	44-72
23122408-1	2013	The kinetics of folding and dimerization of bone morphogenetic protein-2 (BMP-2), a disulfide-connected, homodimeric cystine-knot protein and a member of the transforming growth factor-beta superfamily, was analyzed under a variety of different conditions.	Disulfides	84-93	bone morphogenetic protein 2	Homo sapiens	74-79
23208745-0	2013	Complete mapping of a cystine knot and nested disulfides of recombinant human arylsulfatase A by multi-enzyme digestion and LC-MS analysis using CID and ETD.	Disulfides	46-56	arylsulfatase A	Homo sapiens	78-93
23208745-2	2013	In the case of recombinant human arylsulfatase A (rhASA), there is one cystine knot at the C-terminal, a pair of nested disulfides at the middle, and two out of three unpaired cysteines in the N-terminal region.	Disulfides	120-130	arylsulfatase A	Homo sapiens	33-48
23472109-3	2013	Here, we report two crystal structures of the p75(NTR) death domain in the form of a non-covalent asymmetric dimer and a Cys379-Cys379 disulfide bond linked symmetric dimer, respectively.	Disulfides	135-144	PC4 and SFRS1 interacting protein 1	Homo sapiens	46-49
23472109-3	2013	Here, we report two crystal structures of the p75(NTR) death domain in the form of a non-covalent asymmetric dimer and a Cys379-Cys379 disulfide bond linked symmetric dimer, respectively.	Disulfides	135-144	neurotensin receptor 1	Homo sapiens	50-53
23451088-0	2013	Identification of a disulfide bridge important for transport function of SNAT4 neutral amino acid transporter.	Disulfides	20-29	solute carrier family 38 member 4	Homo sapiens	73-78
23451088-3	2013	In this study, we showed a dose-dependent inhibition in transporter activity of SNAT4 with the treatment of reducing agents, dithiothreitol (DTT) and Tris(2-carboxyethyl)phosphine (TCEP), indicating the possible involvement of disulfide bridge(s).	Disulfides	227-236	solute carrier family 38 member 4	Homo sapiens	80-85
23933601-1	2013	A supramolecular lithium cation assemblies of crown ether, [Li 12-crown-4](+), has been used to replace conventional tetraalkylammonium counterion in thiolate/disulfide (ET(-)/BET) mediated dye-sensitized solar cells (DSCs), which exhibit high stability and efficiency of 6.61% under 100 mW cm(-2) simulated sunlight illumination.	Disulfides	159-168	delta/notch like EGF repeat containing	Homo sapiens	176-179
23073660-4	2012	Reduced all-thiol-HMGB1 has sole chemokine activity, whereas disulfide-HMGB1 has only cytokine activity, and oxidized, denatured HMGB1 has neither.	Disulfides	61-70	high mobility group box 1	Homo sapiens	71-76
23073660-4	2012	Reduced all-thiol-HMGB1 has sole chemokine activity, whereas disulfide-HMGB1 has only cytokine activity, and oxidized, denatured HMGB1 has neither.	Disulfides	61-70	high mobility group box 1	Homo sapiens	71-76
23143686-5	2012	GPIbalpha complexed with GPIbbeta by disulfide bonding was expressed on GPIXW127X platelets and stable CHO-K1 cells lacking GPIX but expressing GPIbalpha and GPIbbeta.	Disulfides	37-46	glycoprotein IX platelet	Homo sapiens	72-76
23010982-3	2012	Compared to the reported and most promising thiolate/disulfide mediator T(-)/T(2), this new analogous mediator produced a major enhancement in open circuit potential (V(OC)) by about 40 mV and correspondingly a higher power conversion efficiency (eta) for DSCs.	Disulfides	53-62	endothelin receptor type A	Homo sapiens	247-250
22902018-1	2012	PURPOSE: CLU is a disulfide linked, heterodimeric protein associated with the clearance of cellular debris and apoptosis.	Disulfides	18-27	clusterin	Homo sapiens	9-12
22704541-2	2012	We present evidence that disulfide bonds in FXI are reduced to free thiols by oxidoreductases thioredoxin-1 (TRX-1) and protein disulfide isomerase (PDI).	Disulfides	25-34	prolyl 4-hydroxylase subunit beta	Homo sapiens	120-147
22704541-2	2012	We present evidence that disulfide bonds in FXI are reduced to free thiols by oxidoreductases thioredoxin-1 (TRX-1) and protein disulfide isomerase (PDI).	Disulfides	25-34	prolyl 4-hydroxylase subunit beta	Homo sapiens	149-152
22740698-5	2012	Using a model peptide of the N terminus of human TRPA1, we demonstrate the formation of disulfide bonds based on MG-induced modification of cysteines as a novel mechanism.	Disulfides	88-97	transient receptor potential cation channel subfamily A member 1	Homo sapiens	49-54
22807135-2	2012	Nucleophilic thiol-disulfide exchange reactions within the I27 domain of titin were previously investigated with force clamp AFM.	Disulfides	19-28	titin	Homo sapiens	73-78
22354542-8	2012	A disulfide bond between Cys6 and Cys113 was identified in 3-morpholinosydnonimine hydrochloride (SIN-1)-treated SR monomer and dimer.	Disulfides	2-11	serine racemase	Homo sapiens	113-115
22744182-2	2012	We recently demonstrated that co-delivery of two vectors expressing M662C mutated heavy and D1828C mutated light chain genes of B-domain-deleted coagulation factor VIII (BDD-FVIII) leads to inter-chain disulfide cross-linking and improved heavy chain secretion in vitro.	Disulfides	202-211	coagulation factor VIII	Mus musculus	157-168
22744182-2	2012	We recently demonstrated that co-delivery of two vectors expressing M662C mutated heavy and D1828C mutated light chain genes of B-domain-deleted coagulation factor VIII (BDD-FVIII) leads to inter-chain disulfide cross-linking and improved heavy chain secretion in vitro.	Disulfides	202-211	coagulation factor VIII	Mus musculus	174-179
22744182-6	2012	These data demonstrate that inter-chain disulfide bonds likely increase heavy chain secretion and coagulation activity in the plasma of transgenic mice with an improved efficacy of a dual-vector delivery of BDD-FVIII gene.	Disulfides	40-49	coagulation factor VIII	Mus musculus	211-216
22387470-2	2012	The approach was applied to the identification of disulfide bonds that stabilize the active state of the yeast alpha-mating pheromone receptor Ste2p, a member of the superfamily of G protein-coupled receptors.	Disulfides	50-59	alpha-factor pheromone receptor STE2	Saccharomyces cerevisiae S288C	143-148
22465014-1	2012	Clusterin is a disulfide-linked heterodimeric glycoprotein that has been implicated in a variety of biological processes.	Disulfides	15-24	clusterin	Homo sapiens	0-9
22465014-10	2012	Taken together, these results suggest that a disulfide-linked form of clusterin functions as an antioxidant protein via its cysteine sulfhydryl groups to reduce ROS levels and delay the organismal aging in fruit flies.	Disulfides	45-54	clusterin	Homo sapiens	70-79
22266140-2	2012	Two missense mutations (C201Y and C489S, standardized nomenclature) of TNSALP, involved in intra-chain disulfide bonds, were reported in patients diagnosed with perinatal HPP (Taillandier A. et al.	Disulfides	103-112	alkaline phosphatase, biomineralization associated	Homo sapiens	71-77
22266140-12	2012	Collectively, these results indicate not only that the intra-subunit disulfide bonds are crucial for TNSALP to properly fold and assemble into the dimeric enzyme, but also that the development of HPP associated with TNSALP (C201Y) or TNSALP (C489S) is attributed to decreased cell surface appearance of the functional enzyme.	Disulfides	69-78	alkaline phosphatase, biomineralization associated	Homo sapiens	101-107
22266140-12	2012	Collectively, these results indicate not only that the intra-subunit disulfide bonds are crucial for TNSALP to properly fold and assemble into the dimeric enzyme, but also that the development of HPP associated with TNSALP (C201Y) or TNSALP (C489S) is attributed to decreased cell surface appearance of the functional enzyme.	Disulfides	69-78	alkaline phosphatase, biomineralization associated	Homo sapiens	216-222
22266140-12	2012	Collectively, these results indicate not only that the intra-subunit disulfide bonds are crucial for TNSALP to properly fold and assemble into the dimeric enzyme, but also that the development of HPP associated with TNSALP (C201Y) or TNSALP (C489S) is attributed to decreased cell surface appearance of the functional enzyme.	Disulfides	69-78	alkaline phosphatase, biomineralization associated	Homo sapiens	216-222
22105604-3	2012	HMGB1 contains three conserved redox-sensitive cysteine residues: C23 and C45 can form an intramolecular disulfide bond, whereas C106 is unpaired and is essential for the interaction with Toll-Like Receptor (TLR) 4.	Disulfides	105-114	high mobility group box 1	Mus musculus	0-5
22105604-5	2012	Using tandem mass spectrometric analysis, we now have established that the C106 thiol and the C23-C45 disulfide bond are required for HMGB1 to induce nuclear NF-kappaB translocation and tumor necrosis factor (TNF) production in macrophages.	Disulfides	102-111	high mobility group box 1	Mus musculus	134-139
22105604-7	2012	In a proof of concept murine model of hepatic necrosis induced by acetaminophen, during inflammation, the predominant form of serum HMGB1 is the active one, containing a C106 thiol group and a disulfide bond between C23 and C45, whereas the inactive form of HMGB1, containing terminally oxidized cysteines, accumulates during inflammation resolution and hepatic regeneration.	Disulfides	193-202	high mobility group box 1	Mus musculus	132-137
22296587-11	2012	SE-HPLC analyses showed that the purity of the CA12.10C12 conjugated via reduced disulfides was lower than that obtained with amine-reactive conjugation reagents, and nonreducing SDS-PAGE analyses indicated protein fragments were present in the disulfide reduced conjugate.	Disulfides	81-91	carbonic anhydrase 12	Canis lupus familiaris	47-51
22296587-11	2012	SE-HPLC analyses showed that the purity of the CA12.10C12 conjugated via reduced disulfides was lower than that obtained with amine-reactive conjugation reagents, and nonreducing SDS-PAGE analyses indicated protein fragments were present in the disulfide reduced conjugate.	Disulfides	81-90	carbonic anhydrase 12	Canis lupus familiaris	47-51
22296036-0	2012	Effects of adding low levels of a disulfide reducing agent on the disulfide interactions of beta-lactoglobulin and kappa-casein in skim milk.	Disulfides	34-43	casein kappa	Homo sapiens	115-127
22296036-2	2012	The reduction of the beta-lactoglobulin and kappa-casein disulfide bonds was monitored over time using electrophoresis.	Disulfides	57-66	casein kappa	Homo sapiens	44-56
22296036-4	2012	kappa-Casein disulfide bonds were reduced in preference to those of beta-lactoglobulin in both unheated and heated skim milk (with or without added whey protein).	Disulfides	13-22	casein kappa	Homo sapiens	0-12
22085909-0	2012	The role of a disulfide bridge in the stability and folding kinetics of Arabidopsis thaliana cytochrome c(6A).	Disulfides	14-23	Cytochrome c	Arabidopsis thaliana	93-105
22085909-1	2012	Cytochrome c(6A) is a eukaryotic member of the Class I cytochrome c family possessing a high structural homology with photosynthetic cytochrome c(6) from cyanobacteria, but structurally and functionally distinct through the presence of a disulfide bond and a heme mid-point redox potential of +71mV (vs normal hydrogen electrode).	Disulfides	238-247	Cytochrome c	Arabidopsis thaliana	0-12
22085909-1	2012	Cytochrome c(6A) is a eukaryotic member of the Class I cytochrome c family possessing a high structural homology with photosynthetic cytochrome c(6) from cyanobacteria, but structurally and functionally distinct through the presence of a disulfide bond and a heme mid-point redox potential of +71mV (vs normal hydrogen electrode).	Disulfides	238-247	Cytochrome c	Arabidopsis thaliana	55-67
22085909-3	2012	We have investigated the contribution of the disulfide bond to thermodynamic stability and (un)folding kinetics in cytochrome c(6A) from Arabidopsis thaliana by making comparison with a photosynthetic cytochrome c(6) from Phormidium laminosum and through a mutant in which the Cys residues have been replaced with Ser residues (C67/73S).	Disulfides	45-54	Cytochrome c	Arabidopsis thaliana	115-127
22085909-7	2012	We conclude that the disulfide bridge in cytochrome c(6A) acts as a conformational restraint in both the folding intermediate and native state of the protein and that it likely serves a structural rather than a previously proposed catalytic role.	Disulfides	21-30	Cytochrome c	Arabidopsis thaliana	41-53
22111690-9	2012	For instance, while Cys4 but not Cys2 is essential for activity, the latter seems to be involved in the formation of intermolecular (regulatory) disulfide bonds.	Disulfides	145-154	Cystatin/monellin superfamily protein	Arabidopsis thaliana	20-24
22105075-4	2012	The data establish that upon PDI-KD, oxidation of proinsulin to form native disulfide bonds is unimpaired and in fact enhanced.	Disulfides	76-85	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
22154292-1	2012	For the quantitative assessment of the glutathione reductase (GR) activity with a (19)F NMR spectroscopy, we developed the heavy metal-free probes based on silica nanoparticles modified with water-soluble perfluorinated dendrimers via the disulfide linkers.	Disulfides	239-248	glutathione-disulfide reductase	Homo sapiens	39-60
22154292-1	2012	For the quantitative assessment of the glutathione reductase (GR) activity with a (19)F NMR spectroscopy, we developed the heavy metal-free probes based on silica nanoparticles modified with water-soluble perfluorinated dendrimers via the disulfide linkers.	Disulfides	239-248	glutathione-disulfide reductase	Homo sapiens	62-64
22154292-3	2012	By the reductive cleavage of the disulfide linkers with the reduced glutathione-mediated enzymatic reaction of GR, perfluorinated dendrimers can be released from the surfaces of the nanoparticles.	Disulfides	33-42	glutathione-disulfide reductase	Homo sapiens	111-113
27923987-3	2017	Interaction with AtMIA40 is necessary for the phosphatase activity of AtSLP2 and is dependent on the formation of disulfide bridges on AtSLP2.	Disulfides	114-123	Calcineurin-like metallo-phosphoesterase superfamily protein	Arabidopsis thaliana	70-76
27923987-3	2017	Interaction with AtMIA40 is necessary for the phosphatase activity of AtSLP2 and is dependent on the formation of disulfide bridges on AtSLP2.	Disulfides	114-123	Calcineurin-like metallo-phosphoesterase superfamily protein	Arabidopsis thaliana	135-141
28025146-7	2017	The ATPase activity was restored however, when the L175C/N820C/Q475A/Q1118A mutant was cross-linked with a flexible disulfide cross-linker.	Disulfides	116-125	dynein axonemal heavy chain 8	Homo sapiens	4-10
27956531-5	2017	Using Clr-a-specific mAb, we characterize Clr-a as a disulfide-linked homodimeric cell surface glycoprotein.	Disulfides	53-62	C-type lectin domain family 2, member e	Mus musculus	6-11
27956531-5	2017	Using Clr-a-specific mAb, we characterize Clr-a as a disulfide-linked homodimeric cell surface glycoprotein.	Disulfides	53-62	C-type lectin domain family 2, member e	Mus musculus	42-47
28867746-3	2017	Because PDI is a key enzyme for the maturation of nascent protein harboring a disulfide bond, the disruption in PDI function by MeHg results in ER stress via the accumulation of misfolded proteins.	Disulfides	78-87	prolyl 4-hydroxylase subunit beta	Homo sapiens	8-11
28867746-3	2017	Because PDI is a key enzyme for the maturation of nascent protein harboring a disulfide bond, the disruption in PDI function by MeHg results in ER stress via the accumulation of misfolded proteins.	Disulfides	78-87	prolyl 4-hydroxylase subunit beta	Homo sapiens	112-115
28429674-4	2017	Lipoprotein (a), or Lp(a), is a type of low-density lipoprotein containing an integral apolipoprotein B100 (apoB100) component with an attached apolipoprotein A-1 (ApoA-1) isoform via a disulfide linkage.	Disulfides	186-195	lipoprotein(a)	Homo sapiens	20-25
27825135-2	2016	Triplebody SPM-1 was designed for lysis of CD19-bearing malignant B-lymphoid cells through the engagement of CD16-expressing cytolytic effectors, including NK and gammadelta T cells.SPM-1 is an optimized version of triplebody ds(19-16-19) and includes humanization, disulfide stabilization and the removal of potentially immunogenic sequences.	Disulfides	266-275	CD19 molecule	Homo sapiens	43-47
27959866-4	2016	Quiescin-sulfhydryl oxidase (QSOX) plays a role in protein folding by introducing disulfides into unfolded reduced proteins.	Disulfides	82-92	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	29-33
27720842-4	2016	Upon oxidation, MyD88 forms distinct disulfide-linked conjugates which are reduced by the MyD88-interacting oxidoreductase nucleoredoxin (Nrx).	Disulfides	37-46	MYD88 innate immune signal transduction adaptor	Homo sapiens	16-21
27720842-4	2016	Upon oxidation, MyD88 forms distinct disulfide-linked conjugates which are reduced by the MyD88-interacting oxidoreductase nucleoredoxin (Nrx).	Disulfides	37-46	MYD88 innate immune signal transduction adaptor	Homo sapiens	90-95
27720842-4	2016	Upon oxidation, MyD88 forms distinct disulfide-linked conjugates which are reduced by the MyD88-interacting oxidoreductase nucleoredoxin (Nrx).	Disulfides	37-46	nucleoredoxin	Homo sapiens	138-141
27580728-12	2016	Step-wise extraction of storage proteins from rice seeds suggested that the mTGF-beta strongly interacted with cysteine-rich prolamins via disulfide bonds.	Disulfides	139-148	transforming growth factor, beta 1	Mus musculus	76-85
27574188-0	2016	Disulfide HMGB1 derived from platelets coordinates venous thrombosis in mice.	Disulfides	0-9	high mobility group box 1	Mus musculus	10-15
27574188-7	2016	Moreover, disulfide HMGB1 facilitates formation of prothrombotic neutrophil extracellular traps (NETs) mediated by RAGE, exposing additional HMGB1 on their extracellular DNA strands.	Disulfides	10-19	high mobility group box 1	Mus musculus	20-25
27574188-7	2016	Moreover, disulfide HMGB1 facilitates formation of prothrombotic neutrophil extracellular traps (NETs) mediated by RAGE, exposing additional HMGB1 on their extracellular DNA strands.	Disulfides	10-19	high mobility group box 1	Mus musculus	141-146
27574188-9	2016	Therefore, platelet-derived disulfide HMGB1 is a central mediator of the sterile inflammatory process in venous thrombosis and could be an attractive target for an anti-inflammatory approach for DVT prophylaxis.	Disulfides	28-37	high mobility group box 1	Mus musculus	38-43
27687970-4	2016	Here, we designed and developed an antibody drug conjugate (CD123-CPT) by integrating anti-CD123 antibody with a chemotherapeutic agent, Camptothecin (CPT), via a disulfide linker.	Disulfides	163-172	interleukin 3 receptor subunit alpha	Homo sapiens	60-65
27687970-4	2016	Here, we designed and developed an antibody drug conjugate (CD123-CPT) by integrating anti-CD123 antibody with a chemotherapeutic agent, Camptothecin (CPT), via a disulfide linker.	Disulfides	163-172	interleukin 3 receptor subunit alpha	Homo sapiens	91-96
27739308-2	2016	The phosphatase domain (PD) of DUSP5 has unique structural features absent from other nuclear DUSPs, such as the presence of a secondary anion-binding site in the proximity of the reaction center and a glutamic acid E264 positioned next to the catalytic cysteine C263, as well as a remote intramolecular disulfide linkage.	Disulfides	304-313	dual specificity phosphatase 5	Homo sapiens	31-36
27739308-7	2016	The role of the secondary binding site in assembling the DUSP5-pERK pre-reactive complex was further demonstrated by molecular dynamics simulations that showed that the remote C197-C219 disulfide linkage controls the structure of the secondary binding pocket based on its redox state (i.e., disulfide/dithiol) and, in turn, the enzymatic activity of DUSP5.	Disulfides	186-195	dual specificity phosphatase 5	Homo sapiens	57-62
27739308-7	2016	The role of the secondary binding site in assembling the DUSP5-pERK pre-reactive complex was further demonstrated by molecular dynamics simulations that showed that the remote C197-C219 disulfide linkage controls the structure of the secondary binding pocket based on its redox state (i.e., disulfide/dithiol) and, in turn, the enzymatic activity of DUSP5.	Disulfides	186-195	dual specificity phosphatase 5	Homo sapiens	350-355
27739308-7	2016	The role of the secondary binding site in assembling the DUSP5-pERK pre-reactive complex was further demonstrated by molecular dynamics simulations that showed that the remote C197-C219 disulfide linkage controls the structure of the secondary binding pocket based on its redox state (i.e., disulfide/dithiol) and, in turn, the enzymatic activity of DUSP5.	Disulfides	291-300	dual specificity phosphatase 5	Homo sapiens	57-62
27739308-7	2016	The role of the secondary binding site in assembling the DUSP5-pERK pre-reactive complex was further demonstrated by molecular dynamics simulations that showed that the remote C197-C219 disulfide linkage controls the structure of the secondary binding pocket based on its redox state (i.e., disulfide/dithiol) and, in turn, the enzymatic activity of DUSP5.	Disulfides	291-300	dual specificity phosphatase 5	Homo sapiens	350-355
27575053-0	2016	An allosteric disulfide bond is involved in enhanced activation of factor XI by protein disulfide isomerase.	Disulfides	14-23	prolyl 4-hydroxylase subunit beta	Homo sapiens	80-107
27497909-8	2016	Cytosolic Srx was found to be imported into mitochondria via a mechanism that requires formation of a disulfide-linked complex with heat shock protein 90, which is likely promoted by H2O2 released from mitochondria.	Disulfides	102-111	sulfiredoxin 1	Homo sapiens	10-13
27378565-9	2016	Notably, high levels of serum HMGB1, in particular of the hyper-acetylated and disulfide isoforms, are sensitive disease biomarkers and are associated with different disease stages.	Disulfides	79-88	high mobility group box 1	Homo sapiens	30-35
27562645-0	2016	The drosomycin multigene family: three-disulfide variants from Drosophila takahashii possess antibacterial activity.	Disulfides	39-48	drosomycin	Drosophila takahashii	4-14
27502485-7	2016	Thus, import and oxidation of Tim17 are mediated by the mitochondrial disulfide relay, though the mechanism by which the disulfide bond in Tim17 is formed differs considerably from that of soluble IMS proteins.	Disulfides	121-130	translocase of inner mitochondrial membrane 17A	Homo sapiens	139-144
27479507-7	2016	Example of the expression and purification of a model disulfide-bonded protein DsbC is described in detail.	Disulfides	54-63	putative protein DsbC	Escherichia coli	79-83
27393305-5	2016	Here, we directly imaged GroEL-GroES interaction in the presence of disulfide-reduced alpha-lactalbumin as a substrate protein using high-speed atomic force microscopy.	Disulfides	68-77	heat shock protein family E (Hsp10) member 1	Homo sapiens	31-36
27346342-3	2016	Conversely, the nuclease activity of CPS-6 is enhanced, and its dimeric structure is stabilized by its interaction with the worm AIF homolog, WAH-1, which shifts to disulfide cross-linked dimers under high ROS levels.	Disulfides	165-174	Worm AIF (apoptosis inducing factor) Homolog	Caenorhabditis elegans	142-147
27265872-3	2016	Tim22, a membrane protein and core component of the mitochondrial translocase TIM22, forms an intramolecular disulfide bond in yeast.	Disulfides	109-118	translocation channel protein TIM22	Saccharomyces cerevisiae S288C	0-5
27265872-3	2016	Tim22, a membrane protein and core component of the mitochondrial translocase TIM22, forms an intramolecular disulfide bond in yeast.	Disulfides	109-118	translocation channel protein TIM22	Saccharomyces cerevisiae S288C	78-83
27265872-5	2016	Here, we present evidence of the high evolutionary conservation of disulfide bond formation in Tim17 and Tim22 among fungi and metazoa.	Disulfides	67-76	translocation channel protein TIM22	Saccharomyces cerevisiae S288C	105-110
26983927-3	2016	Using a model system to mimic mitochondrial oxidative and nitrosative stress, we demonstrate a PDI-independent mechanism whereby reactive oxygen species (ROS) compromise regeneration rates of disulfide bond-containing ER-processed proteins.	Disulfides	192-201	prolyl 4-hydroxylase subunit beta	Homo sapiens	95-98
27186289-2	2016	GPx7 displays a unique function which serves as a stress sensor/transmitter to transfer the signal to its interacting proteins by shuttling disulfide bonds in response to various stresses.	Disulfides	140-149	glutathione peroxidase 7	Homo sapiens	0-4
26819240-1	2016	The secreted disulfide catalyst Quiescin sulfhydryl oxidase-1 (QSOX1) affects extracellular matrix organization and is overexpressed in various adenocarcinomas and associated stroma.	Disulfides	13-22	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	41-61
26819240-1	2016	The secreted disulfide catalyst Quiescin sulfhydryl oxidase-1 (QSOX1) affects extracellular matrix organization and is overexpressed in various adenocarcinomas and associated stroma.	Disulfides	13-22	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	63-68
26670633-9	2016	On the basis of protein-protein docking and molecular dynamics simulations, combined with fluorescence microscopy studies of VWF CK-domain mutants, we suggest the following mechanism of VWF dimerization: PDI initiates VWF dimerization by forming the first 2 disulfide bonds Cys2771-2773" and Cys2771"-2773.	Disulfides	258-267	prolyl 4-hydroxylase subunit beta	Homo sapiens	204-207
26928300-0	2016	Ligand-dependent responses of the silkworm prothoracicotropic hormone receptor, Torso, are maintained by unusual intermolecular disulfide bridges in the transmembrane region.	Disulfides	128-137	prothoracicotropic hormone	Bombyx mori	43-69
26861293-2	2016	Both characteristic types of eukaryotic ferritin subunits are present in secreted ferritins from insects, but here dimers between Ferritin 1 Heavy Chain Homolog (Fer1HCH) and Ferritin 2 Light Chain Homolog (Fer2LCH) are further stabilized by disulfide-bridge in the 24-subunit complex.	Disulfides	242-251	Ferritin 1 heavy chain homologue	Drosophila melanogaster	40-48
26861293-2	2016	Both characteristic types of eukaryotic ferritin subunits are present in secreted ferritins from insects, but here dimers between Ferritin 1 Heavy Chain Homolog (Fer1HCH) and Ferritin 2 Light Chain Homolog (Fer2LCH) are further stabilized by disulfide-bridge in the 24-subunit complex.	Disulfides	242-251	Ferritin 1 heavy chain homologue	Drosophila melanogaster	130-160
26861293-2	2016	Both characteristic types of eukaryotic ferritin subunits are present in secreted ferritins from insects, but here dimers between Ferritin 1 Heavy Chain Homolog (Fer1HCH) and Ferritin 2 Light Chain Homolog (Fer2LCH) are further stabilized by disulfide-bridge in the 24-subunit complex.	Disulfides	242-251	Ferritin 1 heavy chain homologue	Drosophila melanogaster	162-169
26702586-3	2016	We hypothesized that this cysteine-containing ELP (cELP) can be readily crosslinked through disulfide bonds upon exposure to oxidative agents, specifically the singlet oxygen produced during photodynamic stimulation.	Disulfides	92-101	diazepam binding inhibitor-like 5	Mus musculus	46-49
26702586-8	2016	The ROS induce in situ disulfide crosslinking of the cysteine thiols, stabilizing the ELP biopolymer into a stable therapeutic depot.	Disulfides	23-32	diazepam binding inhibitor-like 5	Mus musculus	86-89
26595189-1	2016	Thyroglobulin (Tg) is a vertebrate secretory protein synthesized in the thyrocyte endoplasmic reticulum (ER), where it acquires N-linked glycosylation and conformational maturation (including formation of many disulfide bonds), leading to homodimerization.	Disulfides	210-219	thyroglobulin	Homo sapiens	0-13
26795153-4	2016	Thiol-disulfide redox regulation is dependent on the conserved redox proteins, glutathione/glutaredoxin (GRX) and thioredoxin (TRX) systems.	Disulfides	6-15	glutaredoxin	Homo sapiens	79-103
26795153-4	2016	Thiol-disulfide redox regulation is dependent on the conserved redox proteins, glutathione/glutaredoxin (GRX) and thioredoxin (TRX) systems.	Disulfides	6-15	glutaredoxin	Homo sapiens	105-108
26566734-6	2016	NMR data showed that the three-disulfide theta-defensin and cyclotide scaffolds accommodated the LyP1 and RGDS epitopes but that scaffolds with fewer disulfide bonds were structurally compromised by inclusion of the LyP1 epitope.	Disulfides	31-40	ral guanine nucleotide dissociation stimulator	Homo sapiens	106-110
26585763-7	2016	PDI inhibition was confirmed using a reduced peptide that contained a disulfide containing peptide as a substrate.	Disulfides	70-79	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
26264612-1	2016	The 15-kDa selenoprotein (Sep15) is a selenocysteine-containing oxidoreductase in the endoplasmic reticulum that participates in disulfide-bond formation and protein folding control.	Disulfides	129-138	selenoprotein F	Homo sapiens	4-24
26264612-1	2016	The 15-kDa selenoprotein (Sep15) is a selenocysteine-containing oxidoreductase in the endoplasmic reticulum that participates in disulfide-bond formation and protein folding control.	Disulfides	129-138	selenoprotein F	Homo sapiens	26-31
26458166-0	2015	Disulfide Sensitivity in the Env Protein Underlies Lytic Inactivation of HIV-1 by Peptide Triazole Thiols.	Disulfides	0-9	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	29-32
26515416-9	2015	The specific HMGB1 isoform known to activate TLR4 signaling (disulfide HMGB1) stimulates smooth muscle cell to migrate and produce monocyte chemotactic protein 1/CCL2) via TLR4.	Disulfides	61-70	high mobility group box 1	Mus musculus	13-18
26515416-9	2015	The specific HMGB1 isoform known to activate TLR4 signaling (disulfide HMGB1) stimulates smooth muscle cell to migrate and produce monocyte chemotactic protein 1/CCL2) via TLR4.	Disulfides	61-70	high mobility group box 1	Mus musculus	71-76
26451472-11	2015	Inhibition of the Trx system by HN2 can disrupt cellular thiol-disulfide balance, contributing to vesicant-induced lung toxicity.	Disulfides	63-72	MT-RNR2 like 2 (pseudogene)	Homo sapiens	32-35
26367307-0	2015	Toll-like receptor 4 signaling: A common pathway for interactions between prooxidants and extracellular disulfide high mobility group box 1 (HMGB1) protein-coupled activation.	Disulfides	104-113	high mobility group box 1	Mus musculus	114-139
26367307-0	2015	Toll-like receptor 4 signaling: A common pathway for interactions between prooxidants and extracellular disulfide high mobility group box 1 (HMGB1) protein-coupled activation.	Disulfides	104-113	high mobility group box 1	Mus musculus	141-146
26446990-1	2015	Non-selenocysteine-containing phospholipid hydroperoxide glutathione peroxidase (NPGPx or GPx7) is an oxidative stress sensor that modulates the antioxidative activity of its target proteins through intermolecular disulfide bond formation.	Disulfides	214-223	glutathione peroxidase 7	Homo sapiens	81-86
26446990-1	2015	Non-selenocysteine-containing phospholipid hydroperoxide glutathione peroxidase (NPGPx or GPx7) is an oxidative stress sensor that modulates the antioxidative activity of its target proteins through intermolecular disulfide bond formation.	Disulfides	214-223	glutathione peroxidase 7	Homo sapiens	90-94
26446990-3	2015	Here, we show that NPGPx forms a disulfide bond with the translational regulator cytoplasmic polyadenylation element-binding protein 2 (CPEB2) that results in negative regulation of hypoxia-inducible factor 1-alpha (HIF-1alpha) RNA translation.	Disulfides	33-42	glutathione peroxidase 7	Homo sapiens	19-24
26446990-3	2015	Here, we show that NPGPx forms a disulfide bond with the translational regulator cytoplasmic polyadenylation element-binding protein 2 (CPEB2) that results in negative regulation of hypoxia-inducible factor 1-alpha (HIF-1alpha) RNA translation.	Disulfides	33-42	cytoplasmic polyadenylation element binding protein 2	Homo sapiens	81-134
26446990-3	2015	Here, we show that NPGPx forms a disulfide bond with the translational regulator cytoplasmic polyadenylation element-binding protein 2 (CPEB2) that results in negative regulation of hypoxia-inducible factor 1-alpha (HIF-1alpha) RNA translation.	Disulfides	33-42	cytoplasmic polyadenylation element binding protein 2	Homo sapiens	136-141
26254010-5	2015	Oxidation occurred on methionine and tryptophan residues, and on the unique cysteine residue, in position 42 in S100A8, and 3 in S100A9, that generated glutathionylated, cysteinylated, sulfinic, sulfonic, and disulfide dimeric forms.	Disulfides	209-218	S100 calcium binding protein A8	Homo sapiens	112-118
26387864-4	2015	We examined the biogenesis of MICU1 and find that Mia40 introduces an intermolecular disulfide bond that links MICU1 and its inhibitory paralog MICU2 in a heterodimer.	Disulfides	85-94	mitochondrial calcium uptake 1	Homo sapiens	30-35
26387864-4	2015	We examined the biogenesis of MICU1 and find that Mia40 introduces an intermolecular disulfide bond that links MICU1 and its inhibitory paralog MICU2 in a heterodimer.	Disulfides	85-94	mitochondrial calcium uptake 1	Homo sapiens	111-116
26387864-4	2015	We examined the biogenesis of MICU1 and find that Mia40 introduces an intermolecular disulfide bond that links MICU1 and its inhibitory paralog MICU2 in a heterodimer.	Disulfides	85-94	mitochondrial calcium uptake 2	Homo sapiens	144-149
26387864-6	2015	In the presence of the disulfide bond, MICU1-MICU2 heterodimer binding to MCU is controlled by Ca(2+) levels: the dimer associates with MCU at low levels of Ca(2+) and dissociates upon high Ca(2+) concentrations.	Disulfides	23-32	mitochondrial calcium uptake 1	Homo sapiens	39-44
26387864-6	2015	In the presence of the disulfide bond, MICU1-MICU2 heterodimer binding to MCU is controlled by Ca(2+) levels: the dimer associates with MCU at low levels of Ca(2+) and dissociates upon high Ca(2+) concentrations.	Disulfides	23-32	mitochondrial calcium uptake 2	Homo sapiens	45-50
26269577-5	2015	Surprisingly, we find that protein disulfide isomerase (PDI), the major protein oxidase of the ER lumen, engages Akita proinsulin in a novel way, reducing proinsulin disulfide bonds and priming the Akita protein for ERAD.	Disulfides	35-44	prolyl 4-hydroxylase subunit beta	Homo sapiens	56-59
26406477-4	2015	Although SBP(A18C) binds to SAVSBPM32 more weakly than SBP-tag, the binding affinity is sufficient to bring the two binding partners together efficiently before they are locked together via disulfide bond formation-a phenomenon we have named affinity-driven thiol coupling.	Disulfides	190-199	selenium binding protein 1	Homo sapiens	9-13
26406477-4	2015	Although SBP(A18C) binds to SAVSBPM32 more weakly than SBP-tag, the binding affinity is sufficient to bring the two binding partners together efficiently before they are locked together via disulfide bond formation-a phenomenon we have named affinity-driven thiol coupling.	Disulfides	190-199	selenium binding protein 1	Homo sapiens	9-12
26406477-6	2015	The stoichiometry of the disulfide-bonded SAVSBPM32-SBP(A18C) complex was determined using a novel two-dimensional electrophoresis method which has general applications for analyzing the composition of disulfide-bonded protein complexes.	Disulfides	25-34	selenium binding protein 1	Homo sapiens	45-48
26406477-6	2015	The stoichiometry of the disulfide-bonded SAVSBPM32-SBP(A18C) complex was determined using a novel two-dimensional electrophoresis method which has general applications for analyzing the composition of disulfide-bonded protein complexes.	Disulfides	202-211	selenium binding protein 1	Homo sapiens	45-48
26092730-9	2015	Disulfide cross-linking experiments indicate that SMN tetramers are formed by self-association of stable, non-dissociating dimers.	Disulfides	0-9	survival of motor neuron 1, telomeric	Homo sapiens	50-53
26244732-5	2015	However, a covalent disulfide bond between two highly conserved cysteine residues of SUN2 and KASH2 is crucial for the stability of this interaction and the transmission of forces through the complex.	Disulfides	20-29	Sad1 and UNC84 domain containing 2	Homo sapiens	85-89
26179372-10	2015	One of those is a frameshift mutation leading to a loss of secreted protein, and the other two mutations are amino acid substitutions in the disulfide bridge region, possibly interfering with heterodimerization of the alpha- and beta-chain of CLU.	Disulfides	141-150	clusterin	Homo sapiens	243-246
25989104-0	2015	Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme.	Disulfides	6-15	prolyl 4-hydroxylase subunit beta	Homo sapiens	37-40
25989104-1	2015	The formation of disulfides in proteins entering the secretory pathway is catalysed by the protein disulfide isomerase (PDI) family of enzymes.	Disulfides	17-27	prolyl 4-hydroxylase subunit beta	Homo sapiens	91-118
25989104-1	2015	The formation of disulfides in proteins entering the secretory pathway is catalysed by the protein disulfide isomerase (PDI) family of enzymes.	Disulfides	17-27	prolyl 4-hydroxylase subunit beta	Homo sapiens	120-123
25989104-7	2015	These results have allowed us to define a hierarchy for members of the PDI family, in terms of ability to act as electron acceptors or donors during thiol-disulfide exchange reactions and indicate that there is no kinetic barrier to the exchange of disulfides between several PDI proteins.	Disulfides	155-164	prolyl 4-hydroxylase subunit beta	Homo sapiens	71-74
25989104-7	2015	These results have allowed us to define a hierarchy for members of the PDI family, in terms of ability to act as electron acceptors or donors during thiol-disulfide exchange reactions and indicate that there is no kinetic barrier to the exchange of disulfides between several PDI proteins.	Disulfides	249-259	prolyl 4-hydroxylase subunit beta	Homo sapiens	71-74
25959394-3	2015	Here, we show that angiotensin II is regulated by ERp44, a factor involved in disulfide bond formation in the ER.	Disulfides	78-87	endoplasmic reticulum protein 44	Mus musculus	50-55
25959394-5	2015	We show that ERp44 forms a mixed disulfide bond with ERAP1, an aminopeptidase that cleaves angiotensin II.	Disulfides	33-42	endoplasmic reticulum protein 44	Mus musculus	13-18
25940440-2	2015	It belongs to the protein disulfide isomerize (PDI) family, whose members have been implicated in development of breast, ovarian and gastrointestinal cancers.	Disulfides	26-35	prolyl 4-hydroxylase subunit beta	Homo sapiens	47-50
25853617-4	2015	In an effort to understand how the HRMs are involved in binding of heme to disulfide-reduced HO2sol, in the work described here, we further investigated the properties of Fe(3+)-heme bound to HO2.	Disulfides	75-84	heme oxygenase 2	Homo sapiens	93-96
25853617-6	2015	We found that HO2tail in the disulfide-reduced state binds Fe(3+)-heme and accounts for the spectral features observed upon binding of heme to the disulfide-reduced form of HO2sol that cannot be attributed to heme binding at the catalytic site.	Disulfides	29-38	heme oxygenase 2	Homo sapiens	14-17
25853617-6	2015	We found that HO2tail in the disulfide-reduced state binds Fe(3+)-heme and accounts for the spectral features observed upon binding of heme to the disulfide-reduced form of HO2sol that cannot be attributed to heme binding at the catalytic site.	Disulfides	147-156	heme oxygenase 2	Homo sapiens	14-17
25853617-10	2015	In summary, disulfide-reduced HO2 has multiple binding sites with varying affinities for Fe(3+)-heme.	Disulfides	12-21	heme oxygenase 2	Homo sapiens	30-33
25623399-5	2015	The His176Cys mutation is critical for C-type lectin-like domain stability, leading to the reconstruction of third canonical disulfide bridge in LLT1, as shown by mass spectrometry.	Disulfides	125-134	C-type lectin domain family 2 member D	Homo sapiens	145-149
22761783-1	2012	Thimet oligopeptidase (EP24.15) is a cysteine-rich metallopeptidase containing fifteen Cys residues and no intra-protein disulfide bonds.	Disulfides	121-130	thimet oligopeptidase 1	Homo sapiens	0-21
22448222-10	2012	Thus, NE and PR3 possess proHNP1 convertase activity that requires the presence of the native HNP1 disulfide motif for high fidelity activation of the precursor in vitro.	Disulfides	99-108	elastase, neutrophil expressed	Homo sapiens	6-8
22448222-10	2012	Thus, NE and PR3 possess proHNP1 convertase activity that requires the presence of the native HNP1 disulfide motif for high fidelity activation of the precursor in vitro.	Disulfides	99-108	proteinase 3	Homo sapiens	13-16
22927815-7	2012	YLDV-IL18BP forms a disulfide bonded homo-dimer engaging IL18 in a 2:2 stoichiometry, in contrast to the 1:1 complex of ectromelia virus (ECTV) IL18BP and IL18.	Disulfides	20-29	interleukin 18 binding protein	Homo sapiens	5-11
21867670-0	2011	Display of disulfide-rich proteins by complementary DNA display and disulfide shuffling assisted by protein disulfide isomerase.	Disulfides	11-20	prolyl 4-hydroxylase subunit beta	Homo sapiens	100-127
21867670-1	2011	We report an efficient system to produce and display properly folded disulfide-rich proteins facilitated by coupled complementary DNA (cDNA) display and protein disulfide isomerase-assisted folding.	Disulfides	69-78	prolyl 4-hydroxylase subunit beta	Homo sapiens	153-180
22209765-7	2011	In a yeast two-hybrid assay, the thioredoxin-like domain of LTO1 interacts with PsbO, a lumenal PSII subunit known to be disulfide bonded, and a recombinant form of the molecule can introduce a disulfide bond in PsbO in vitro.	Disulfides	121-130	PS II oxygen-evolving complex 1	Arabidopsis thaliana	80-84
22209765-7	2011	In a yeast two-hybrid assay, the thioredoxin-like domain of LTO1 interacts with PsbO, a lumenal PSII subunit known to be disulfide bonded, and a recombinant form of the molecule can introduce a disulfide bond in PsbO in vitro.	Disulfides	194-203	PS II oxygen-evolving complex 1	Arabidopsis thaliana	80-84
21955842-4	2011	In the present study, the effect of dithionite on the disulfides of NP4 and NP7 is addressed.	Disulfides	54-64	proteinase 3	Homo sapiens	68-71
21955842-8	2011	Furthermore, prolonged electrochemical reduction of NP4 and NP7 in the presence of electrochemical mediators also leads to disulfide breakage.	Disulfides	123-132	proteinase 3	Homo sapiens	52-55
21955842-9	2011	However, due to sterical shielding of the disulfide bridges in NP4 and NP7, the cystine reduction can be largely prevented by the use of stoichiometric amounts of reductant or limited electrochemical reduction.	Disulfides	42-51	proteinase 3	Homo sapiens	63-66
21862689-6	2011	It is noteworthy that this adduct can be cleaved from the protein matrix by incubation with dithiothreitol, confirming that the active metabolite is linked to a cysteinyl residue of CYP2B6 via a disulfide bond.	Disulfides	195-204	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	182-188
21805521-0	2011	Human Dickkopf-1 (huDKK1) protein: characterization of glycosylation and determination of disulfide linkages in the two cysteine-rich domains.	Disulfides	90-99	dickkopf WNT signaling pathway inhibitor 1	Homo sapiens	6-16
21689057-2	2011	Protein disulfide isomerase (PDI) is a member of the thioredoxin superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER).	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
21689057-2	2011	Protein disulfide isomerase (PDI) is a member of the thioredoxin superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER).	Disulfides	122-131	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
21689057-2	2011	Protein disulfide isomerase (PDI) is a member of the thioredoxin superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER).	Disulfides	122-131	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
29643478-0	2018	Mucin gel assembly is controlled by a collective action of non-mucin proteins, disulfide bridges, Ca2+-mediated links, and hydrogen bonding.	Disulfides	79-88	LOC100508689	Homo sapiens	0-5
21865601-0	2011	Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system.	Disulfides	41-50	copper chaperone CCS1	Saccharomyces cerevisiae S288C	14-18
21865601-0	2011	Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system.	Disulfides	119-128	copper chaperone CCS1	Saccharomyces cerevisiae S288C	14-18
21865601-4	2011	We report on the molecular mechanism of the mitochondrial import of Saccharomyces cerevisiae Ccs1 as the first member of a novel class of unconventional substrates of the disulfide relay system.	Disulfides	171-180	copper chaperone CCS1	Saccharomyces cerevisiae S288C	93-97
21865601-5	2011	We show that the mitochondrial form of Ccs1 contains a stable disulfide bond between cysteine residues C27 and C64.	Disulfides	62-71	copper chaperone CCS1	Saccharomyces cerevisiae S288C	39-43
21865601-7	2011	Furthermore, C64 of Ccs1 is required for formation of a Ccs1 disulfide intermediate with Mia40.	Disulfides	61-70	copper chaperone CCS1	Saccharomyces cerevisiae S288C	20-24
21865601-7	2011	Furthermore, C64 of Ccs1 is required for formation of a Ccs1 disulfide intermediate with Mia40.	Disulfides	61-70	copper chaperone CCS1	Saccharomyces cerevisiae S288C	56-60
21865601-8	2011	We conclude that the Mia40/Erv1 disulfide relay system introduces a structural disulfide bond in Ccs1 between the cysteine residues C27 and C64, thereby promoting mitochondrial import of this unconventional substrate.	Disulfides	32-41	copper chaperone CCS1	Saccharomyces cerevisiae S288C	97-101
21865601-8	2011	We conclude that the Mia40/Erv1 disulfide relay system introduces a structural disulfide bond in Ccs1 between the cysteine residues C27 and C64, thereby promoting mitochondrial import of this unconventional substrate.	Disulfides	79-88	copper chaperone CCS1	Saccharomyces cerevisiae S288C	97-101
21771788-2	2011	Here, ZPR9 was found to physically interact with apoptosis signal-regulating kinase 1 (ASK1) through a disulfide linkage involving Cys(1351) and Cys(1360) of ASK1 and Cys(305) and Cys(308) of ZPR9.	Disulfides	103-112	zinc finger protein 622	Mus musculus	6-10
29412660-6	2018	Crystal structure analysis of the MIF-derived EPCALCS peptide, bound in its oxMIF-like conformation by the Fab fragment of BaxB01, revealed that this peptide adopts a curved conformation, making the central thiol protein oxidoreductase motif competent to undergo disulfide shuffling.	Disulfides	263-272	macrophage migration inhibitory factor	Homo sapiens	34-37
21892159-4	2011	In most cases, these IL7R mutations introduce an unpaired cysteine in the extracellular juxtamembrane-transmembrane region and promote de novo formation of intermolecular disulfide bonds between mutant IL-7Ralpha subunits, thereby driving constitutive signaling via JAK1 and independently of IL-7, gammac or JAK3.	Disulfides	171-180	interleukin 7 receptor	Homo sapiens	21-25
21892159-4	2011	In most cases, these IL7R mutations introduce an unpaired cysteine in the extracellular juxtamembrane-transmembrane region and promote de novo formation of intermolecular disulfide bonds between mutant IL-7Ralpha subunits, thereby driving constitutive signaling via JAK1 and independently of IL-7, gammac or JAK3.	Disulfides	171-180	interleukin 7 receptor	Homo sapiens	202-212
21778880-4	2011	PDI is a prime candidate to modify the allosteric disulfide by reduction, S-nitrosylation and glutathionation, implicated as regulators of TF procoagulant activity.	Disulfides	50-59	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
29247580-0	2018	Successful refolding and NMR structure of rMagi3: A disulfide-rich insecticidal spider toxin.	Disulfides	52-61	membrane associated guanylate kinase, WW and PDZ domain containing 3	Rattus norvegicus	42-48
21598303-8	2011	To determine if an interaction between the rel homology binding domain in ERp57 and the nuclear factor-kappaB subunit, p65, occurred after TNF-alpha treatment and could account for nuclear movement, co-immunoprecipitation was performed under control and conditions that stabilized labile disulfide bonds.	Disulfides	288-297	RELA proto-oncogene, NF-kB subunit	Homo sapiens	119-122
21728340-3	2011	In this study using disulfide cross-linking experiments we show that the Ste2p cytoplasmic ends of helix 5 (TM5) and helix 6 (TM6) that flank the amino and carboxyl sides of IL3 undergo conformational changes upon ligand binding, whereas the center of the IL3 loop does not.	Disulfides	20-29	alpha-factor pheromone receptor STE2	Saccharomyces cerevisiae S288C	73-78
29080907-5	2018	In this study, we demonstrate that the m-type thioredoxins TRX-m1, TRX-m2, and TRX-m4 (TRX-ms) interact with the xanthophyll cycle enzyme zeaxanthin epoxidase (ZE) and are required for maintaining the redox-dependent stabilization of ZE by regulating its intermolecular disulfide bridges.	Disulfides	270-279	thioredoxin M-type 4	Arabidopsis thaliana	79-85
21621812-8	2011	The identified products of the reaction between oxidized mercury species with selected alkanethiols (C3-C5) were Hg0 and disulfides (RS-SR).	Disulfides	121-131	ADAM metallopeptidase with thrombospondin type 1 motif 1	Homo sapiens	101-106
27346583-1	2018	Lipoprotein(a) [Lp(a)] is composed of a low density lipoprotein (LDL)-like particle to which apolipoprotein (a) [apo(a)] is linked by a single disulfide bridge.	Disulfides	143-152	lipoprotein(a)	Homo sapiens	0-14
21876369-0	2011	Enhancement of gene delivery using novel homodimeric tat peptide formed by disulfide bond.	Disulfides	75-84	tyrosine aminotransferase	Homo sapiens	53-56
21876369-3	2011	Therefore, we designed a novel modified Tat peptide having a homodimeric (Tat-CTHD, Tat-NTHD) and closed structure (cyclic Tat) simply by using the disulfide bond between cysteines to develop a more efficient and safe nonviral gene delivery system.	Disulfides	148-157	tyrosine aminotransferase	Homo sapiens	40-43
27346583-1	2018	Lipoprotein(a) [Lp(a)] is composed of a low density lipoprotein (LDL)-like particle to which apolipoprotein (a) [apo(a)] is linked by a single disulfide bridge.	Disulfides	143-152	lipoprotein(a)	Homo sapiens	16-21
29191937-6	2018	Limited proteolysis, kinetic simulations, and MS analyses confirmed that peroxynitrite preferentially oxidizes the redox-active Cys residues of PDI to the corresponding sulfenic acids, which reacted with the resolving thiols at the active sites to produce disulfides (i.e. Cys53-Cys56 and Cys397-Cys400).	Disulfides	256-266	prolyl 4-hydroxylase subunit beta	Homo sapiens	144-147
21500299-4	2011	Protein disulfide isomerase (PDI) was most effective at the reduced/oxidized glutathione ratio of 2:1 for refolding the denatured sample NRG1-beta1 with the native disulfide bonds.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
21500299-4	2011	Protein disulfide isomerase (PDI) was most effective at the reduced/oxidized glutathione ratio of 2:1 for refolding the denatured sample NRG1-beta1 with the native disulfide bonds.	Disulfides	8-17	neuregulin 1	Homo sapiens	137-141
21338337-1	2011	The colonic human MUC2 mucin forms a polymeric gel by covalent disulfide bonds in its N- and C-termini.	Disulfides	63-72	LOC100508689	Homo sapiens	23-28
29101227-2	2018	The pre-TCR is a disulfide-linked heterodimer composed of an invariant pre-TCR alpha (pTalpha) subunit and a variable beta subunit, the latter of which is incorporated into the mature TCR in subsequent developmental progression.	Disulfides	17-26	T cell receptor alpha constant	Homo sapiens	75-84
21521879-3	2011	Sema3A stimulation generated hydrogen peroxide (H2O2) through MICAL (molecule interacting with CasL) and oxidized CRMP2, enabling it to form a disulfide-linked homodimer through cysteine-504.	Disulfides	143-152	semaphorin 3A	Homo sapiens	0-6
29101227-2	2018	The pre-TCR is a disulfide-linked heterodimer composed of an invariant pre-TCR alpha (pTalpha) subunit and a variable beta subunit, the latter of which is incorporated into the mature TCR in subsequent developmental progression.	Disulfides	17-26	pre T cell antigen receptor alpha	Homo sapiens	86-93
29030255-9	2018	Three potential N-linked glycosylation sites and two cysteine residues (Cys-28 and Cys-209) that are likely to form one disulfide bond were present in pufferfish CA VI.	Disulfides	120-129	carbonic anhydrase 6	Homo sapiens	162-167
21366304-2	2011	Specifically, we apply the COGEF (constrained geometry simulates external force) approach to characterize the mechanochemistry of the disulfide bond in three different chemical environments: dimethyl disulfide, cystine, and a 102-atom model of the I27 domain in the titin protein.	Disulfides	134-143	titin	Homo sapiens	266-271
21121641-2	2011	PDI mediates proper protein folding by oxidation or isomerization and disrupts disulfide bonds by reduction.	Disulfides	79-88	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
21121641-3	2011	The entry of HIV-1 into cells is facilitated by the PDI-catalyzed reductive cleavage of disulfide bonds in gp120.	Disulfides	88-97	prolyl 4-hydroxylase subunit beta	Homo sapiens	52-55
21121641-3	2011	The entry of HIV-1 into cells is facilitated by the PDI-catalyzed reductive cleavage of disulfide bonds in gp120.	Disulfides	88-97	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	107-112
21215271-6	2011	Hence, GPx7 and GPx8 may represent a novel route for the productive use of peroxide produced by Ero1alpha during disulfide bond formation.	Disulfides	113-122	glutathione peroxidase 7	Homo sapiens	7-11
21091435-1	2011	In eukaryotes, disulfide bonds are formed in the endoplasmic reticulum, facilitated by the Ero1 (endoplasmic reticulum oxidoreductin 1) oxidase/PDI (protein disulfide-isomerase) system.	Disulfides	15-24	prolyl 4-hydroxylase subunit beta	Homo sapiens	97-147
21091435-1	2011	In eukaryotes, disulfide bonds are formed in the endoplasmic reticulum, facilitated by the Ero1 (endoplasmic reticulum oxidoreductin 1) oxidase/PDI (protein disulfide-isomerase) system.	Disulfides	15-24	prolyl 4-hydroxylase subunit beta	Homo sapiens	149-176
29203246-4	2018	Modifications of integrin disulfide bonds dependent on oxidation-reduction can be mediated by Protein Disulfide Isomerse (PDI).	Disulfides	26-35	prolyl 4-hydroxylase subunit beta	Homo sapiens	94-120
21036950-8	2011	This study is the first in vitro observation indicating that glutaredoxin and thioredoxin in human liver are active in reducing the mixed disulfide formed between xenobiotics and glutathione.	Disulfides	138-147	glutaredoxin	Homo sapiens	61-73
29203246-4	2018	Modifications of integrin disulfide bonds dependent on oxidation-reduction can be mediated by Protein Disulfide Isomerse (PDI).	Disulfides	26-35	prolyl 4-hydroxylase subunit beta	Homo sapiens	122-125
29203246-5	2018	This paper provides evidences that binding to integrin ligands initiate changes in free thiol pattern on cell surface and that thiol-disulfide exchange mediated by PDI leads to activation of integrin subunit alpha11.	Disulfides	133-142	prolyl 4-hydroxylase subunit beta	Homo sapiens	164-167
29203246-6	2018	By employing co-immunoprecipitation and confocal microscopy analysis we showed that alpha11beta1 and PDI create complexes bounded by disulfide bonds.	Disulfides	133-142	prolyl 4-hydroxylase subunit beta	Homo sapiens	101-104
29298981-3	2018	PRIN2 dimers can be reduced into the active monomeric form by thioredoxins through reduction of a disulfide bond.	Disulfides	98-107	Serine/Threonine-kinase	Arabidopsis thaliana	0-5
21117239-1	2011	Using all-atom simulations, we examine the role of the I109C/Q428C disulfide "stitch" in altering the conformational distribution of engineered HIV-1 gp120 core relevant for binding of the broadly neutralizing recombinant antibody b12.	Disulfides	67-76	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	150-155
29146186-5	2018	TMalpha and TM"s D123, but not D1, promoted the thrombin-dependent degradation of all-thiol (at-HMGB1) and disulfide HMGB1 (ds-HMGB1), an effect mimicked by TM"s D2, though to a lesser extent.	Disulfides	107-116	high mobility group box 1	Mus musculus	117-122
21209210-9	2011	PRX2 overexpression maintained Trx in a reduced state by inhibiting the cysteine thiol-disulfide exchange, thereby preventing its dissociation from ASK1.	Disulfides	87-96	paired related homeobox 2	Mus musculus	0-4
29146186-5	2018	TMalpha and TM"s D123, but not D1, promoted the thrombin-dependent degradation of all-thiol (at-HMGB1) and disulfide HMGB1 (ds-HMGB1), an effect mimicked by TM"s D2, though to a lesser extent.	Disulfides	107-116	high mobility group box 1	Mus musculus	117-122
28832225-2	2018	MSNs were synthesized and functionalized with 3-mercaptopropyltrimethoxysilane (3-MPTMS), followed by MUC1 aptamer conjugation through disulfide bonds.	Disulfides	135-144	mucin 1, cell surface associated	Homo sapiens	102-106
21845100-10	2011	Since PDI may be implicated in the protection of cells against ER stress, including cancer cells, inhibitors of PDI might be able to enhance the efficacy of cancer chemotherapy; furthermore, it has been demonstrated that blocking the reductive cleavage of disulfide bonds of proteins associated with the cell surface markedly reduces the infectivity of the human immunodeficiency virus.	Disulfides	256-265	prolyl 4-hydroxylase subunit beta	Homo sapiens	6-9
21845100-10	2011	Since PDI may be implicated in the protection of cells against ER stress, including cancer cells, inhibitors of PDI might be able to enhance the efficacy of cancer chemotherapy; furthermore, it has been demonstrated that blocking the reductive cleavage of disulfide bonds of proteins associated with the cell surface markedly reduces the infectivity of the human immunodeficiency virus.	Disulfides	256-265	prolyl 4-hydroxylase subunit beta	Homo sapiens	112-115
21037007-6	2011	Site-directed mutagenesis was performed to assess the role of these residues in the ColM immunity-conferring activity of Cmi, which showed that the disulfide bond and residues from the C-terminal extremity of the protein were functionally essential.	Disulfides	148-157	Colicin M activity protein	Escherichia coli	121-124
21037007-7	2011	The involvement of DsbA oxidase in the formation of the Cmi disulfide bond is also demonstrated.	Disulfides	60-69	Colicin M activity protein	Escherichia coli	56-59
29138259-8	2017	We conclude that while at least one specific intermolecular disulfide bond links two SMOX molecules to form the homodimer, the thermal denaturation profiles can be justified by the presence of at least one intramolecular disulfide bond, which also plays a critical role in the stabilization of the overall three-dimensional SMOX structure, and in particular of its flavin adenine dinucleotide-containing active site.	Disulfides	60-69	spermine oxidase	Homo sapiens	85-89
22715587-2	2011	PDI mediates proper protein folding by oxidation or isomerization and disrupts disulfide bonds by reduction; it also has chaperone and antichaperone activities.	Disulfides	79-88	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
22715587-4	2011	In the ER, PDI is primarily involved in protein folding, whereas on the cell surface, it reduces disulfide bonds.	Disulfides	97-106	prolyl 4-hydroxylase subunit beta	Homo sapiens	11-14
29234142-3	2017	The Copper Chaperone for SOD1 (CCS) transiently interacts with SOD1 and promotes its correct maturation by transferring copper and catalyzing disulfide bond formation.	Disulfides	142-151	copper chaperone for superoxide dismutase	Homo sapiens	31-34
27766889-6	2017	During the theoretical analysis of homology models, unexpected role of number of disulfide bonds and secondary structure elements has been witnessed in case of Wnt3 and Wnt3a proteins.	Disulfides	81-90	Wnt family member 3A	Homo sapiens	169-174
22073283-1	2011	BACKGROUND: Earlier studies showed that 17beta-estradiol (E(2)), an endogenous female sex hormone, can bind to human protein disulfide isomerase (PDI), a protein folding catalyst for disulfide bond formation and rearrangement.	Disulfides	125-134	prolyl 4-hydroxylase subunit beta	Homo sapiens	146-149
20869417-0	2010	Functional coupling of Cys-226 and Cys-296 in the glucagon-like peptide-1 (GLP-1) receptor indicates a disulfide bond that is close to the activation pocket.	Disulfides	103-112	glucagon like peptide 1 receptor	Homo sapiens	75-90
20829229-5	2010	We have exploited the ability of glutaredoxins (Grxs) to reduce mixed disulfides to protein thiols either in the cytoplasm and in the IMS (Grx1) or in the mitochondrial matrix (Grx2) as a tool for restoring a correct redox environment and preventing the aggregation of mutant SOD1.	Disulfides	70-80	glutaredoxin	Homo sapiens	139-143
20801878-2	2010	One notable exception is the complex of ERp57 and calnexin that functions as part the calnexin cycle to direct disulfide bond formation in N-glycoproteins.	Disulfides	111-120	calnexin	Homo sapiens	50-58
20801878-2	2010	One notable exception is the complex of ERp57 and calnexin that functions as part the calnexin cycle to direct disulfide bond formation in N-glycoproteins.	Disulfides	111-120	calnexin	Homo sapiens	86-94
28963348-0	2017	Reduction potentials of protein disulfides and catalysis of glutathionylation and deglutathionylation by glutaredoxin enzymes.	Disulfides	32-42	glutaredoxin	Homo sapiens	105-117
20652244-9	2010	The polyanionic sites on the surface of VLPs and capsomeres were decorated with a polycationic MUC1 peptide containing a polyarginine-cysteine residue fused to 20 amino acids of the MUC1 tandem repeat through electrostatic interactions and redox-induced disulfide bond formation.	Disulfides	254-263	mucin 1, transmembrane	Mus musculus	95-99
20652244-9	2010	The polyanionic sites on the surface of VLPs and capsomeres were decorated with a polycationic MUC1 peptide containing a polyarginine-cysteine residue fused to 20 amino acids of the MUC1 tandem repeat through electrostatic interactions and redox-induced disulfide bond formation.	Disulfides	254-263	mucin 1, transmembrane	Mus musculus	182-186
20675861-5	2010	Although both HP1alpha and HP1gamma contain reactive cysteine residues, only HP1gamma readily and reversibly formed disulfide homodimers under oxidative conditions.	Disulfides	116-125	chromobox 3	Homo sapiens	77-85
28963348-3	2017	Grxs feature dithiol active sites and can shuttle rapidly between three oxidation states, namely dithiol Grx(SH)2, mixed disulfide Grx(SH)(SSG) and oxidized disulfide Grx(SS).	Disulfides	121-130	glutaredoxin	Homo sapiens	0-3
20486761-2	2010	Ero1 oxidizes protein disulfide isomerase (PDI), which, in turn, introduces disulfides into ER client proteins.	Disulfides	76-86	prolyl 4-hydroxylase subunit beta	Homo sapiens	14-41
28963348-3	2017	Grxs feature dithiol active sites and can shuttle rapidly between three oxidation states, namely dithiol Grx(SH)2, mixed disulfide Grx(SH)(SSG) and oxidized disulfide Grx(SS).	Disulfides	157-166	glutaredoxin	Homo sapiens	0-3
20486761-2	2010	Ero1 oxidizes protein disulfide isomerase (PDI), which, in turn, introduces disulfides into ER client proteins.	Disulfides	76-86	prolyl 4-hydroxylase subunit beta	Homo sapiens	43-46
28878015-3	2017	Specifically, RIPK3-dependent MLKL phosphorylation promotes the assembly of disulfide bond-dependent MLKL polymers that drive the execution of necroptosis.	Disulfides	76-85	mixed lineage kinase domain like pseudokinase	Homo sapiens	30-34
20486761-3	2010	To maintain an oxidized state, Ero1 couples disulfide transfer to PDI with reduction of molecular oxygen, forming hydrogen peroxide.	Disulfides	44-53	prolyl 4-hydroxylase subunit beta	Homo sapiens	66-69
28878015-3	2017	Specifically, RIPK3-dependent MLKL phosphorylation promotes the assembly of disulfide bond-dependent MLKL polymers that drive the execution of necroptosis.	Disulfides	76-85	mixed lineage kinase domain like pseudokinase	Homo sapiens	101-105
28878015-4	2017	However, how MLKL disulfide bond formation is regulated is not clear.	Disulfides	18-27	mixed lineage kinase domain like pseudokinase	Homo sapiens	13-17
28878015-6	2017	Recombinant Trx1 preferentially binds to monomeric MLKL and blocks MLKL disulfide bond formation and polymerization in vitro Inhibition of MLKL polymer formation requires the reducing activity of Trx1.	Disulfides	72-81	mixed lineage kinase domain like pseudokinase	Homo sapiens	67-71
28878015-6	2017	Recombinant Trx1 preferentially binds to monomeric MLKL and blocks MLKL disulfide bond formation and polymerization in vitro Inhibition of MLKL polymer formation requires the reducing activity of Trx1.	Disulfides	72-81	mixed lineage kinase domain like pseudokinase	Homo sapiens	67-71
20584868-2	2010	Lp(a) is a subfraction of LDL, where apolipoprotein(a) [apo(a)] is disulfide bound to apolipoprotein B-100 (apoB).	Disulfides	67-76	lipoprotein(a)	Homo sapiens	0-5
29035299-6	2017	Here we present crystal structures of Bet v 2 in the reduced and the oxidized state, i.e., without and with a disulfide bridge.	Disulfides	110-119	delta/notch like EGF repeat containing	Homo sapiens	38-41
20584868-2	2010	Lp(a) is a subfraction of LDL, where apolipoprotein(a) [apo(a)] is disulfide bound to apolipoprotein B-100 (apoB).	Disulfides	67-76	lipoprotein(a)	Homo sapiens	56-62
29035299-10	2017	By contrast, both Bet v 2 forms exhibit similar immunological properties as evidenced by their binding to IgE antibodies from birch pollen allergic patients and by their ability to trigger histamine release in a humanized rat basophilic leukemia cells (RBL) assay, independent of the presence or absence of the disulfide bridge.	Disulfides	311-320	delta/notch like EGF repeat containing	Homo sapiens	18-21
28814504-6	2017	In reconstitution studies with reduced Tim13, Mia40, and Erv1, the addition of Osm1 and fumarate completes the disulfide exchange pathway that results in Tim13 oxidation.	Disulfides	111-120	intraflagellar transport 172	Homo sapiens	79-83
20566323-1	2010	The formation of aberrant disulfide bonds is a structural consideration for the manufacturing of the extracellular domain of human CD83 (hCD83ext), a potential therapeutic protein.	Disulfides	26-35	exostosin glycosyltransferase 1	Homo sapiens	101-104
20095866-3	2010	During protein folding, Ero1p oxidizes protein disulfide isomerase (PDI), which then directly catalyzes the formation of disulfide bonds in folding proteins.	Disulfides	47-56	prolyl 4-hydroxylase subunit beta	Homo sapiens	68-71
28216341-10	2017	6) Only in some ALDH2, ALDH9, ALDH16 and ALDH23 enzymes, Cys303, alone or in conjunction with Cys301, allows disulfide formation.	Disulfides	109-118	aldehyde dehydrogenase 9 family member A1	Homo sapiens	23-28
23350160-2	2010	Several systems are able to control the activity, stability, and correct folding of enzymes through dithiol/disulfide isomerization reactions including the enzyme protein disulfide-isomerase, the glutathione-dependent glutaredoxin system, and the thioredoxin systems.	Disulfides	108-117	prolyl 4-hydroxylase subunit beta	Homo sapiens	163-190
28780408-3	2017	In a eukaryotic cell, a copper chaperone for SOD1 (CCS) has been known to supply a copper ion and also introduce the disulfide bond into SOD1; however, a mechanism controlling the CCS-dependent activation of SOD1 remains obscure.	Disulfides	117-126	copper chaperone for superoxide dismutase	Homo sapiens	51-54
20738721-3	2010	It has been proposed that disulfide bonds might be formed through two cysteine pairs in the extracellular LRR domains of CLV1 and CLV2 to stabilize the receptor complex.	Disulfides	26-35	Leucine-rich receptor-like protein kinase family protein	Arabidopsis thaliana	121-125
28780408-3	2017	In a eukaryotic cell, a copper chaperone for SOD1 (CCS) has been known to supply a copper ion and also introduce the disulfide bond into SOD1; however, a mechanism controlling the CCS-dependent activation of SOD1 remains obscure.	Disulfides	117-126	copper chaperone for superoxide dismutase	Homo sapiens	180-183
20538591-0	2010	Stabilization of HIV-1 gp120-CD4 receptor complex through targeted interchain disulfide exchange.	Disulfides	78-87	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	23-28
28780408-7	2017	Nonetheless, the N-terminally truncated CCS with the bound copper ion was found to correctly introduce the disulfide bond into SOD1.	Disulfides	107-116	copper chaperone for superoxide dismutase	Homo sapiens	40-43
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	186-195	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	38-43
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	186-195	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	169-174
28827318-0	2017	MLKL forms disulfide bond-dependent amyloid-like polymers to induce necroptosis.	Disulfides	11-20	mixed lineage kinase domain like pseudokinase	Homo sapiens	0-4
20442408-1	2010	Endoplasmic reticulum oxidation 1 (ERO1) is a conserved eukaryotic flavin adenine nucleotide-containing enzyme that promotes disulfide bond formation by accepting electrons from reduced protein disulfide isomerase (PDI) and passing them on to molecular oxygen.	Disulfides	125-134	prolyl 4-hydroxylase subunit beta	Homo sapiens	186-213
28827318-3	2017	Here we report that MLKL forms SDS-resistant, disulfide bond-dependent polymers during necroptosis in both human and mouse cells.	Disulfides	46-55	mixed lineage kinase domain like pseudokinase	Homo sapiens	20-24
20442408-1	2010	Endoplasmic reticulum oxidation 1 (ERO1) is a conserved eukaryotic flavin adenine nucleotide-containing enzyme that promotes disulfide bond formation by accepting electrons from reduced protein disulfide isomerase (PDI) and passing them on to molecular oxygen.	Disulfides	125-134	prolyl 4-hydroxylase subunit beta	Homo sapiens	215-218
25712564-3	2015	However, over-expression of HIV-1 gp120 in mammalian cells leads to the formation of aberrant disulfide-linked dimers that can bias the results of experiments aimed at measuring gp120 affinity with different ligands.	Disulfides	94-103	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	34-39
28655768-6	2017	PORCN-mediated Wnt acylation was abolished when the Wnt peptide was treated with DTT, and did not occur with a linear (non-disulfide-bonded) peptide, or when the double disulfide-bonded Wnt peptide contained Ala substituted for the Ser acylation site.	Disulfides	123-132	porcupine O-acyltransferase	Homo sapiens	0-5
25703060-6	2015	RNase A was used as a model protein in this study because the disulfide bonds of this protein have been well characterized.	Disulfides	62-71	ribonuclease A family member 1, pancreatic	Homo sapiens	0-7
25703060-7	2015	Application of this approach to peptides digested with Asp-N/C (chemical digestion) and trypsin under acid hydrolysis conditions identified the four native disulfide bonds of RNase A.	Disulfides	156-165	ribonuclease A family member 1, pancreatic	Homo sapiens	175-182
20423326-1	2010	Members of the PDI (protein disulfide-isomerase) family are critical for the correct folding of secretory proteins by catalysing disulfide bond formation as well as by serving as molecular chaperones to prevent protein aggregation.	Disulfides	28-37	prolyl 4-hydroxylase subunit beta	Homo sapiens	15-18
20351055-7	2010	The gene expression and activity of glutaredoxin-1 (Grx-1), which catalyzes the formation of protein-glutathione mixed disulfides (protein-SSG), were also found to be increased after cinnamaldehyde treatment.	Disulfides	119-129	glutaredoxin	Homo sapiens	36-50
20351055-7	2010	The gene expression and activity of glutaredoxin-1 (Grx-1), which catalyzes the formation of protein-glutathione mixed disulfides (protein-SSG), were also found to be increased after cinnamaldehyde treatment.	Disulfides	119-129	glutaredoxin	Homo sapiens	52-57
28655768-6	2017	PORCN-mediated Wnt acylation was abolished when the Wnt peptide was treated with DTT, and did not occur with a linear (non-disulfide-bonded) peptide, or when the double disulfide-bonded Wnt peptide contained Ala substituted for the Ser acylation site.	Disulfides	169-178	porcupine O-acyltransferase	Homo sapiens	0-5
20423149-4	2010	Purification of this heteromer and characterization by LC-ESI-MS/MS analysis identified the IgG Fc binding protein (FCGBP) as the disulfide-linked partner protein of TFF3.	Disulfides	130-139	Fc gamma binding protein	Homo sapiens	92-114
20423149-4	2010	Purification of this heteromer and characterization by LC-ESI-MS/MS analysis identified the IgG Fc binding protein (FCGBP) as the disulfide-linked partner protein of TFF3.	Disulfides	130-139	Fc gamma binding protein	Homo sapiens	116-121
28642368-5	2017	For this purpose, we chose the pilus protein FimG from Gram-negative bacteria and a disulfide-bonded variant of the I91 human cardiac titin polyprotein.	Disulfides	84-93	titin	Homo sapiens	134-139
20351095-3	2010	To determine whether these interactions are directly mediated by contacts between the histone H4 amino-terminal tail and the acidic patch of the H2A/H2B interface, as previously demonstrated for short range nucleosomal interactions, we have characterized the extent and effect of disulfide cross-linking between residues in histones contained in different strands of nucleosomal arrays.	Disulfides	280-289	H2A clustered histone 18	Homo sapiens	145-148
25805991-3	2015	Glutaredoxin is homologous to the disulfide-reducing thioredoxin and shares similar binding modes of the protein substrate.	Disulfides	34-43	glutaredoxin	Homo sapiens	0-12
28686257-1	2017	A bifunctional linker molecule containing nitrogen mustard and a cyclic disulfide group has been developed for the covalent immobilization of intact DNA, which allows quantitative analysis of epigenomic modification in immobilized DNA using SPR-based immune sensing.	Disulfides	72-81	sepiapterin reductase	Homo sapiens	241-244
25519729-8	2015	The protein sequences of the COX4-2 peptide showed that the disulfide bridge seen in human and rodent orthologs would be precluded in other mammalian lineages and lower vertebrates, all of which lack the requisite pair of cysteines.	Disulfides	60-69	cytochrome c oxidase subunit 4I2	Homo sapiens	29-35
25699251-7	2015	This led to the hypothesis that Nox2 establishes disulfide bonds with p67 (phox) via a thiol-dilsulfide exchange reaction and, thus, functions as a PDI.	Disulfides	49-58	prolyl 4-hydroxylase subunit beta	Homo sapiens	148-151
25699251-9	2015	We propose a model of oxidase assembly in which binding of p67 (phox) to Nox2 via disulfide bonds, by virtue of the intrinsic PDI activity of Nox2, stabilizes the primary interaction between the two components.	Disulfides	82-91	prolyl 4-hydroxylase subunit beta	Homo sapiens	126-129
20144905-0	2010	Thiol-disulfide exchanges modulate aldo-keto reductase family 1 member B10 activity and sensitivity to inhibitors.	Disulfides	6-15	aldo-keto reductase family 1 member B10	Homo sapiens	35-74
28958138-2	2017	Clusterin (Clu), also known as apolipoprotein J (ApoJ), is a highly conserved disulfide-linked heterodimeric glycoprotein implicated in a great variety of physiological and pathophysiological processes including lipid transportation, tissue remodeling, senescence, cell interaction, stress response, inflammation, apoptosis, diabetes mellitus and metabolic syndrome.	Disulfides	78-87	clusterin	Homo sapiens	0-9
20112420-1	2010	The insulin receptor (IR) is a homo-dimeric, disulfide-linked, membrane-spanning tyrosine kinase.	Disulfides	45-54	insulin receptor	Homo sapiens	4-20
20112420-1	2010	The insulin receptor (IR) is a homo-dimeric, disulfide-linked, membrane-spanning tyrosine kinase.	Disulfides	45-54	insulin receptor	Homo sapiens	22-24
20202930-1	2010	The cell catalysts calnexin (CNX) and protein-disulfide isomerase (PDI) cooperate in establishing the disulfide bonding of the HIV envelope (Env) glycoprotein.	Disulfides	46-55	prolyl 4-hydroxylase subunit beta	Homo sapiens	67-70
20379517-5	2010	The two hIAPP peptides studied (with and without disulfide bridge) show negative alpha(p), which is close to zero at 250 K and decreases to approximately -1.5 x 10(-3) K(-1) upon heating to 450 K. The analysis of various structural properties of peptides shows a correlation between the intrinsic peptide volumes and the number of intrapeptide hydrogen bonds.	Disulfides	49-58	islet amyloid polypeptide	Homo sapiens	8-13
25384421-4	2015	Introducing cysteines at YAP sites 87 and 96 can induce disulfide formation, as confirmed by crystallography.	Disulfides	56-65	Yes1 associated transcriptional regulator	Homo sapiens	25-28
25373878-5	2015	Direct modifications of titin include reversible disulfide bonding within the cardiac-specific N2-Bus domain, which increases titin stiffness, and reversible S-glutathionylation of cryptic cysteines in immunoglobulin-like domains, which only takes place after the domains have unfolded and which reduces titin stiffness in cardiac and skeletal muscle.	Disulfides	49-58	titin	Homo sapiens	24-29
25288022-4	2015	Mutations C137S and C14S in the HA2 and HA1 subunits, respectively, were introduced to prevent any possible disulfide linkage between the two subunit proteins.	Disulfides	108-117	keratin 34	Mus musculus	32-35
28958138-2	2017	Clusterin (Clu), also known as apolipoprotein J (ApoJ), is a highly conserved disulfide-linked heterodimeric glycoprotein implicated in a great variety of physiological and pathophysiological processes including lipid transportation, tissue remodeling, senescence, cell interaction, stress response, inflammation, apoptosis, diabetes mellitus and metabolic syndrome.	Disulfides	78-87	clusterin	Homo sapiens	0-3
20351257-2	2010	Two crystal forms of XRCC1-NTD complexed with Pol beta have been solved, revealing that the XRCC1-NTD is able to adopt a redox-dependent alternate fold, characterized by a disulfide bond, and substantial variations of secondary structure, folding topology, and electrostatic surface.	Disulfides	172-181	DNA polymerase beta	Homo sapiens	46-54
28958138-2	2017	Clusterin (Clu), also known as apolipoprotein J (ApoJ), is a highly conserved disulfide-linked heterodimeric glycoprotein implicated in a great variety of physiological and pathophysiological processes including lipid transportation, tissue remodeling, senescence, cell interaction, stress response, inflammation, apoptosis, diabetes mellitus and metabolic syndrome.	Disulfides	78-87	clusterin	Homo sapiens	31-47
20145245-0	2010	Peroxiredoxin Ahp1 acts as a receptor for alkylhydroperoxides to induce disulfide bond formation in the Cad1 transcription factor.	Disulfides	72-81	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	14-18
28958138-2	2017	Clusterin (Clu), also known as apolipoprotein J (ApoJ), is a highly conserved disulfide-linked heterodimeric glycoprotein implicated in a great variety of physiological and pathophysiological processes including lipid transportation, tissue remodeling, senescence, cell interaction, stress response, inflammation, apoptosis, diabetes mellitus and metabolic syndrome.	Disulfides	78-87	clusterin	Homo sapiens	49-53
20145245-5	2010	We demonstrate that Ahp1 is required for the formation of intermolecular Cad1 disulfide bond(s) in both an in vitro redox system and in cells treated with alkylhydroperoxide.	Disulfides	78-87	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	20-24
25449110-3	2014	In this paper, in order to enhance soluble expression of recombinant reteplase in E. coli, DsbA/DsbC foldases were used to introduce disulfide bonds into the reduced polypeptide chain and catalyze their isomerization to the native disulfide linkage during the folding process.	Disulfides	133-142	putative protein DsbC	Escherichia coli	96-100
28444390-8	2017	The disulfide isoform of HMGB1 stimulated dendritic cell cytokine release and enhanced the priming of naive T-cells.	Disulfides	4-13	high mobility group box 1	Homo sapiens	25-30
25449110-3	2014	In this paper, in order to enhance soluble expression of recombinant reteplase in E. coli, DsbA/DsbC foldases were used to introduce disulfide bonds into the reduced polypeptide chain and catalyze their isomerization to the native disulfide linkage during the folding process.	Disulfides	231-240	putative protein DsbC	Escherichia coli	96-100
25208735-1	2014	Protein disulfide isomerase (PDI) and glutathione peroxidase 7 (GPx7) cooperatively promote the oxidative folding of disulfide (SS)-containing proteins in endoplasmic reticulum by recognizing the nascent proteins to convert them into the native folds by means of SS formation and SS isomerization and by catalyzing reoxidation of reduced PDI with H2O2, respectively.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
20175878-5	2010	We have created monomer-stabilized human cystatin C, with an engineered disulfide bond (L47C)-(G69C) between the structural elements that become separated upon domain swapping.	Disulfides	72-81	cystatin C	Homo sapiens	41-51
28559343-5	2017	Our results also suggest that the catalysis by protein disulfide isomerase (PDI) and thiol-disulfide exchange is mostly enthalpy-driven (entropy changes below 2 kcal mol-1 at all stages of the reaction).	Disulfides	55-64	prolyl 4-hydroxylase subunit beta	Homo sapiens	76-79
20026073-0	2010	Modulation of an active-site cysteine pKa allows PDI to act as a catalyst of both disulfide bond formation and isomerization.	Disulfides	82-91	prolyl 4-hydroxylase subunit beta	Homo sapiens	49-52
20026073-1	2010	Protein disulfide isomerase (PDI) plays a central role in disulfide bond formation in the endoplasmic reticulum.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
20026073-7	2010	Mutation of arginine 120 and the corresponding residue, arginine 461, in the a" domain severely reduces the ability of PDI to catalyze disulfide bond formation and reduction but enhances the ability to catalyze disulfide bond isomerization due to the formation of more stable PDI-substrate mixed disulfides.	Disulfides	135-144	prolyl 4-hydroxylase subunit beta	Homo sapiens	119-122
20026073-7	2010	Mutation of arginine 120 and the corresponding residue, arginine 461, in the a" domain severely reduces the ability of PDI to catalyze disulfide bond formation and reduction but enhances the ability to catalyze disulfide bond isomerization due to the formation of more stable PDI-substrate mixed disulfides.	Disulfides	296-306	prolyl 4-hydroxylase subunit beta	Homo sapiens	119-122
25208735-1	2014	Protein disulfide isomerase (PDI) and glutathione peroxidase 7 (GPx7) cooperatively promote the oxidative folding of disulfide (SS)-containing proteins in endoplasmic reticulum by recognizing the nascent proteins to convert them into the native folds by means of SS formation and SS isomerization and by catalyzing reoxidation of reduced PDI with H2O2, respectively.	Disulfides	8-17	glutathione peroxidase 7	Homo sapiens	64-68
25208735-1	2014	Protein disulfide isomerase (PDI) and glutathione peroxidase 7 (GPx7) cooperatively promote the oxidative folding of disulfide (SS)-containing proteins in endoplasmic reticulum by recognizing the nascent proteins to convert them into the native folds by means of SS formation and SS isomerization and by catalyzing reoxidation of reduced PDI with H2O2, respectively.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	338-341
28559343-9	2017	In the intramolecular oxidation of PDI, a transition state is only observed if hydrogen bond donors are nearby the mixed disulfide intermediate, which emphasizes that the thermochemistry of thiol-disulfide exchange in PDI is influenced by the presence of hydrogen bond donors.	Disulfides	121-130	prolyl 4-hydroxylase subunit beta	Homo sapiens	35-38
20028970-6	2010	These homologies were localized in the disulfide constraint region of CLU.	Disulfides	39-48	clusterin	Homo sapiens	70-73
19950203-4	2010	Western blot analysis in the presence or absence of reducing agents, revealed that H(2)O(2) induces the rapid formation of an intermolecular disulfide bond between Twist1 homodimers and Twist/E2a proteins heterodimers.	Disulfides	141-150	transcription factor 3	Homo sapiens	192-195
25258311-2	2014	Ero1alpha oxidizes PDI to introduce disulfides into substrates, and PDI can feedback-regulate Ero1alpha activity.	Disulfides	36-46	prolyl 4-hydroxylase subunit beta	Homo sapiens	19-22
25258311-3	2014	Here, we show the regulatory disulfide of Ero1alpha responds to the redox fluctuation in ER very sensitively, relying on the availability of redox active PDI.	Disulfides	29-38	prolyl 4-hydroxylase subunit beta	Homo sapiens	154-157
28559343-9	2017	In the intramolecular oxidation of PDI, a transition state is only observed if hydrogen bond donors are nearby the mixed disulfide intermediate, which emphasizes that the thermochemistry of thiol-disulfide exchange in PDI is influenced by the presence of hydrogen bond donors.	Disulfides	121-130	prolyl 4-hydroxylase subunit beta	Homo sapiens	218-221
24094148-0	2014	Disulfide-containing high mobility group box-1 promotes N-methyl-D-aspartate receptor function and excitotoxicity by activating Toll-like receptor 4-dependent signaling in hippocampal neurons.	Disulfides	0-9	high mobility group box 1	Mus musculus	21-46
20024330-1	2010	In this communication, we report the spontaneous and reversible in vitro self-assembly of a polypeptide fragment derived from the C-terminal domain of Insulin-like Growth Factor Binding Protein (IGFBP-2) into soluble nanotubular structures several micrometres long via a mechanism involving inter-molecular disulfide bonds and exhibiting enhanced fluorescence.	Disulfides	307-316	insulin like growth factor binding protein 2	Homo sapiens	195-202
28559343-9	2017	In the intramolecular oxidation of PDI, a transition state is only observed if hydrogen bond donors are nearby the mixed disulfide intermediate, which emphasizes that the thermochemistry of thiol-disulfide exchange in PDI is influenced by the presence of hydrogen bond donors.	Disulfides	196-205	prolyl 4-hydroxylase subunit beta	Homo sapiens	35-38
28559343-9	2017	In the intramolecular oxidation of PDI, a transition state is only observed if hydrogen bond donors are nearby the mixed disulfide intermediate, which emphasizes that the thermochemistry of thiol-disulfide exchange in PDI is influenced by the presence of hydrogen bond donors.	Disulfides	196-205	prolyl 4-hydroxylase subunit beta	Homo sapiens	218-221
28411237-3	2017	Thioredoxin (Trx) and glutaredoxin (Grx) are ubiquitous redox proteins, catalyzing thiol-disulfide exchange reactions.	Disulfides	89-98	glutaredoxin	Homo sapiens	22-34
19892701-2	2010	The ectodomain of FIBCD1 comprises a coiled coil, a polycationic region, and a C-terminal FReD (fibrinogen-related domain) that assembles into disulfide-linked homotetramers.	Disulfides	143-152	fibrinogen C domain containing 1	Homo sapiens	18-24
20069636-0	2010	Synthesis of the proteinase inhibitor LEKTI domain 6 by the fragment condensation method and regioselective disulfide bond formation.	Disulfides	108-117	serine peptidase inhibitor Kazal type 5	Homo sapiens	38-43
25090939-3	2014	All six CgIL-17 members (including a previously reported homolog) contained four conserved cysteines that were used in the formation of disulfide bonds.	Disulfides	136-145	interleukin 17-like protein	Crassostrea gigas	8-15
28411237-3	2017	Thioredoxin (Trx) and glutaredoxin (Grx) are ubiquitous redox proteins, catalyzing thiol-disulfide exchange reactions.	Disulfides	89-98	glutaredoxin	Homo sapiens	36-39
25026075-5	2014	In this study, we compared the disulfide bond network and glycosylation profiles of clade C recombinant HIV-1 Env trimers, C97ZA012 gp140, expressed by stable and transient transfections using an integrated mass mapping workflow that combines collision induced dissociation (CID) and electron transfer dissociation (ETD).	Disulfides	31-40	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	110-113
21125805-2	2010	A very large glycoprotein, the apoprotein (a) (apoA) is firmly linked to apo-B-100 by two covalent disulfide bonds.	Disulfides	99-108	lipoprotein(a)	Homo sapiens	47-51
28552907-3	2017	By leveraging our versatile disulfide cross-linked micelles (DCMs) platform, we developed nanoformulations of DTX and BTZ (named DTX-DCMs and BTZ-DCMs).	Disulfides	28-37	CASC3 exon junction complex subunit	Homo sapiens	118-121
19943337-1	2010	A 12-mer peptide nucleic acid (PNA) directed against the nociceptin/orphanin FQ receptor mRNA was disulfide bridged with various peptides without and with cell-penetrating features.	Disulfides	98-107	opioid related nociceptin receptor 1	Rattus norvegicus	68-88
24954167-8	2014	Importantly, only HMGB1 in its partially oxidized isoform (disulfide HMGB1), which activates toll-like receptor 4 (TLR4), but not in its fully reduced or fully oxidized isoforms, evoked mechanical hypersensitivity upon i.t.	Disulfides	59-68	high mobility group box 1	Mus musculus	18-23
24954167-8	2014	Importantly, only HMGB1 in its partially oxidized isoform (disulfide HMGB1), which activates toll-like receptor 4 (TLR4), but not in its fully reduced or fully oxidized isoforms, evoked mechanical hypersensitivity upon i.t.	Disulfides	59-68	high mobility group box 1	Mus musculus	69-74
24954167-15	2014	These results demonstrate that spinal HMGB1 contributes to nociceptive signal transmission via activation of TLR4 and point to disulfide HMGB1 inhibition as a potential therapeutic strategy in treatment of chronic inflammatory pain.	Disulfides	127-136	high mobility group box 1	Mus musculus	38-43
24954167-15	2014	These results demonstrate that spinal HMGB1 contributes to nociceptive signal transmission via activation of TLR4 and point to disulfide HMGB1 inhibition as a potential therapeutic strategy in treatment of chronic inflammatory pain.	Disulfides	127-136	high mobility group box 1	Mus musculus	137-142
28552907-3	2017	By leveraging our versatile disulfide cross-linked micelles (DCMs) platform, we developed nanoformulations of DTX and BTZ (named DTX-DCMs and BTZ-DCMs).	Disulfides	28-37	CASC3 exon junction complex subunit	Homo sapiens	142-150
28552907-12	2017	This study demonstrates that DTX and BTZ could be successfully nanoformulated into disulfide cross-linked micelles.	Disulfides	83-92	CASC3 exon junction complex subunit	Homo sapiens	37-40
24792702-1	2014	UNLABELLED: Protein disulfide-isomerase (PDI) is a four-domain flexible protein that catalyzes the formation of disulfide bonds in the endoplasmic reticulum.	Disulfides	20-29	prolyl 4-hydroxylase subunit beta	Homo sapiens	41-44
19811453-1	2009	The thiol-disulfide oxidoreductases of the PDI (protein disulfide isomerase) family assist in disulfide-bond formation in the ER (endoplasmic reticulum).	Disulfides	10-19	prolyl 4-hydroxylase subunit beta	Homo sapiens	43-46
28389559-9	2017	Furthermore, we also show that whereas STEP and PTPRR stabilize their reversibly oxidized state by forming an intramolecular disulfide bond, HePTP uses an unexpected mechanism, namely, formation of a reversible intermolecular disulfide bond.	Disulfides	125-134	protein tyrosine phosphatase non-receptor type 5	Homo sapiens	39-43
19811453-1	2009	The thiol-disulfide oxidoreductases of the PDI (protein disulfide isomerase) family assist in disulfide-bond formation in the ER (endoplasmic reticulum).	Disulfides	10-19	prolyl 4-hydroxylase subunit beta	Homo sapiens	48-75
19874033-4	2009	Bovine liver catalase, in which the heme groups are remote from the surface of the protein, and horseradish peroxidase, which has four disulfide bonds and just three histidyl residues, exhibit a much smaller spectroscopic response.	Disulfides	135-144	catalase	Bos taurus	13-21
28389559-9	2017	Furthermore, we also show that whereas STEP and PTPRR stabilize their reversibly oxidized state by forming an intramolecular disulfide bond, HePTP uses an unexpected mechanism, namely, formation of a reversible intermolecular disulfide bond.	Disulfides	226-235	protein tyrosine phosphatase non-receptor type 5	Homo sapiens	39-43
19855005-6	2009	The results of high throughput expression microarray and chromatin occupancy analyses reveal that Pdx1 regulates a broad array of genes involved in diverse functions of the ER, including proper disulfide bond formation, protein folding, and the unfolded protein response.	Disulfides	194-203	pancreatic and duodenal homeobox 1	Mus musculus	98-102
24928512-12	2014	In serum from ethanol-fed mice and from patients with ALD, there was disulfide-bonded hyperacetylated HMGB1, disulfide-bonded non-acetylated HMGB1, and HMGB1 phosphorylated in serine 35.	Disulfides	69-78	high mobility group box 1	Homo sapiens	102-107
25109988-7	2014	The consequences of the regulation of the FOXO4 (forkhead box O4) transcription factor by formation of intermolecular disulfides with both TNPO1 (transportin 1) and p300/CBP [CREB (cAMP-response-element-binding protein)-binding protein] are discussed in more detail.	Disulfides	118-128	E1A binding protein p300	Homo sapiens	165-169
28298446-5	2017	Protein disulfide isomerase (PDI) interacts with these early intermediates, but disulfide formation does not occur unless the entire sequence of the protein domain is translocated.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
24863694-2	2014	The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress.	Disulfides	126-136	glutaredoxin	Homo sapiens	40-43
24863694-2	2014	The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress.	Disulfides	147-157	glutaredoxin	Homo sapiens	26-38
24863694-2	2014	The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress.	Disulfides	147-157	glutaredoxin	Homo sapiens	40-43
19388824-6	2009	Enzymatic mechanisms of ROS generation during UPR include: (a) Multiple thiol-disulfide exchanges involving ER oxidoreductases including flavooxidase Ero1 and protein disulfide isomerase (PDI); (b) Mitochondrial electron transport; (c) Nox4 NADPH oxidase complex, particularly Nox4.	Disulfides	78-87	prolyl 4-hydroxylase subunit beta	Homo sapiens	159-186
19388824-6	2009	Enzymatic mechanisms of ROS generation during UPR include: (a) Multiple thiol-disulfide exchanges involving ER oxidoreductases including flavooxidase Ero1 and protein disulfide isomerase (PDI); (b) Mitochondrial electron transport; (c) Nox4 NADPH oxidase complex, particularly Nox4.	Disulfides	78-87	prolyl 4-hydroxylase subunit beta	Homo sapiens	188-191
19388826-4	2009	Here, we show that protein disulfide isomerase (PDI) catalyzes the disulfide bond formation of MHC class I molecules and thereby facilitates the assembly of MHC class I heavy chain with beta(2)-microglobulin (beta(2)m).	Disulfides	27-36	prolyl 4-hydroxylase subunit beta	Homo sapiens	48-51
19388826-5	2009	Depletion of PDI but not ERp57 by RNAi interfered with the disulfide bond formation in the MHC class I molecules.	Disulfides	59-68	prolyl 4-hydroxylase subunit beta	Homo sapiens	13-16
19388826-7	2009	These observations suggest that PDI-catalyzed disulfide bond formation of MHC class I molecules is an event downstream of the interaction of class I molecules with calnexin and upstream of their interaction with beta(2)m.	Disulfides	46-55	prolyl 4-hydroxylase subunit beta	Homo sapiens	32-35
19388826-7	2009	These observations suggest that PDI-catalyzed disulfide bond formation of MHC class I molecules is an event downstream of the interaction of class I molecules with calnexin and upstream of their interaction with beta(2)m.	Disulfides	46-55	calnexin	Homo sapiens	164-172
28374771-6	2017	We propose that the requirement of two distinct glutathione interaction sites for the efficient reduction of glutathionylated disulfide substrates explains the deviating structure-function relationships, activities and substrate preferences of different glutaredoxin subfamilies as well as thioredoxins.	Disulfides	126-135	glutaredoxin	Homo sapiens	254-266
24927250-5	2014	We report here the design and synthesis of new pro-drugs, derived from co-drugs combining a NEP and an APN inhibitor through a disulfide bond with side chains improving oral bioavailability.	Disulfides	127-136	alanyl aminopeptidase, membrane	Homo sapiens	103-106
28284864-6	2017	We have designed a novel dual action CA-4 prodrug, YK-5-252, which releases the drug through a disulfide bond cleavage mechanism and contains a near-infrared (NIR) fluorophore, which allows fluorescence monitoring of cleavage.	Disulfides	95-104	carbonic anhydrase 4	Homo sapiens	37-41
24849605-4	2014	These mutant RPE65s were misfolded and formed aggregates or high molecular complexes via disulfide bonds.	Disulfides	89-98	retinoid isomerohydrolase RPE65	Homo sapiens	13-18
19326051-8	2009	SDS-PAGE analysis showed that the purified FBP is a homomultimer composed of 31 kDa monomeric subunits connected by intermolecular disulfide bonds.	Disulfides	131-140	folate receptor beta	Canis lupus familiaris	43-46
19754879-4	2009	Here, the effects of the presence of a naturally occurring disulfide bridge on liver BABP ligand-binding properties and backbone dynamics have been investigated by NMR.	Disulfides	59-68	aldo-keto reductase family 1 member C2	Homo sapiens	85-89
28284864-7	2017	This disulfide linkage causes CA-4 to become effective only when released by glutathione (GSH) reducing the toxicity of the drug while simultaneously releasing the NIR fluorophore.	Disulfides	5-14	carbonic anhydrase 4	Homo sapiens	30-34
28064023-1	2017	Gamma-interferon-inducible lysosomal thiol reductase (GILT) is a key enzyme in the antigen processing and presentation pathway whereby it reduces disulfide bonds at an acidic pH.	Disulfides	146-155	gamma-interferon-inducible lysosomal thiol reductase	Cavia porcellus	0-52
19805286-6	2009	Thus, two catalytic domains of CA IX associate to form a dimer, which is stabilized by the formation of an intermolecular disulfide bond.	Disulfides	122-131	carbonic anhydrase 9	Homo sapiens	31-36
19586921-3	2009	To date, two such activation pathways have been identified: one requiring the CCS copper chaperone and one that works independently of CCS to insert copper and activate SOD1 through oxidation of an intramolecular disulfide.	Disulfides	213-222	copper chaperone for superoxide dismutase	Homo sapiens	78-81
19586921-3	2009	To date, two such activation pathways have been identified: one requiring the CCS copper chaperone and one that works independently of CCS to insert copper and activate SOD1 through oxidation of an intramolecular disulfide.	Disulfides	213-222	copper chaperone for superoxide dismutase	Homo sapiens	135-138
19482076-6	2009	Our data also reveal that 4-HPR-mediated ROS evoke Akt conformational change by forming an intramolecular disulfide bond; N-acetylcysteine and glutathione, as thiol antioxidants, significantly abate the ROS generation in 4-HPR-exposed cells.	Disulfides	106-115	haptoglobin-related protein	Homo sapiens	28-31
24841207-4	2014	We systematically analyzed cysteines and associated disulfide bonds in the prototypic Wnt3a.	Disulfides	52-61	Wnt family member 3A	Homo sapiens	86-91
24841207-5	2014	Our data show that mutation of any individual cysteine of Wnt3a results in covalent Wnt oligomers through ectopic intermolecular disulfide bond formation and diminishes/abolishes Wnt signaling.	Disulfides	129-138	Wnt family member 3A	Homo sapiens	58-63
28064023-1	2017	Gamma-interferon-inducible lysosomal thiol reductase (GILT) is a key enzyme in the antigen processing and presentation pathway whereby it reduces disulfide bonds at an acidic pH.	Disulfides	146-155	gamma-interferon-inducible lysosomal thiol reductase	Cavia porcellus	54-58
24778178-6	2014	The structural analysis reveals that a loop region of ALKBH5 is immobilized by a disulfide bond that apparently excludes the binding of dsDNA to ALKBH5.	Disulfides	81-90	alkB homolog 5, RNA demethylase	Homo sapiens	54-60
24778178-6	2014	The structural analysis reveals that a loop region of ALKBH5 is immobilized by a disulfide bond that apparently excludes the binding of dsDNA to ALKBH5.	Disulfides	81-90	alkB homolog 5, RNA demethylase	Homo sapiens	145-151
19712479-9	2009	Mass spectroscopy analysis of the recombinant protein allowed to assign the five intramolecular disulfide bridges as well as the dimerization Cys202, thereby confirming the conservation of the disulfide pattern previously described for fish STC1.	Disulfides	193-202	stanniocalcin 1	Homo sapiens	241-245
19712479-13	2009	The dimerization was confirmed by mass spectrometry as was the highly conserved disulfide pattern, which is identical to that found in fish STC1.	Disulfides	80-89	stanniocalcin 1	Homo sapiens	140-144
28146312-4	2017	The aggregation between beta-Lg and kappa-CN is proposed to proceed via disulfide bond formation leading to amorphous aggregates, although the exact mechanism is not known.	Disulfides	72-81	casein kappa	Homo sapiens	36-44
19667192-2	2009	Bv8/prokineticin 2 (PK2), a chemokine characterized by a unique structural motif comprising five disulfide bonds, is highly expressed in inflamed tissues associated to infiltrating cells.	Disulfides	97-106	prokineticin 2	Mus musculus	0-3
19667192-2	2009	Bv8/prokineticin 2 (PK2), a chemokine characterized by a unique structural motif comprising five disulfide bonds, is highly expressed in inflamed tissues associated to infiltrating cells.	Disulfides	97-106	prokineticin 2	Mus musculus	4-18
19667192-2	2009	Bv8/prokineticin 2 (PK2), a chemokine characterized by a unique structural motif comprising five disulfide bonds, is highly expressed in inflamed tissues associated to infiltrating cells.	Disulfides	97-106	prokineticin 2	Mus musculus	20-23
24932912-2	2014	They contain thioredoxin-like domains and catalyze the physiological oxidation, reduction and isomerization of protein disulfide bonds, which are involved in cell function and development in prokaryotes and eukaryotes.	Disulfides	119-128	ETH_00011875	Eimeria tenella	13-24
24914717-4	2014	Cyclization of peptide ligands by formation of disulfide bridges is preferable for designing inhibitors of neuraminidase-1 because of their high activity and specificity.	Disulfides	47-56	neuraminidase 1	Homo sapiens	107-122
28146312-6	2017	A new mechanism of aggregation is proposed whereby beta-Lg and kappa-CN not only form disulfide-linked aggregates, but also amyloid fibrillar coaggregates.	Disulfides	86-95	casein kappa	Homo sapiens	63-71
28040730-6	2017	We found that during its mitochondrial import and maturation NDUFB10 transiently interacts with CHCHD4 and acquires disulfide bonds.	Disulfides	116-125	NADH:ubiquinone oxidoreductase subunit B10	Homo sapiens	61-68
24598312-9	2014	The results indicated that the mismatched disulfide bond of FV57 linking the light chain FR1 and CDR3 would confer deleterious negative effects on its activity against RV, likely due to spatial hindrance in the light chain CDR3.	Disulfides	42-51	CDR3	Homo sapiens	97-101
24598312-9	2014	The results indicated that the mismatched disulfide bond of FV57 linking the light chain FR1 and CDR3 would confer deleterious negative effects on its activity against RV, likely due to spatial hindrance in the light chain CDR3.	Disulfides	42-51	CDR3	Homo sapiens	223-227
19719226-9	2009	The results of electrophoretic studies appear to confirm that the process of N-homocysteinylation-mediated PGN assembly culminates in covalent interparticle association by disulfide cross-linking among modified proteins.	Disulfides	172-181	SPG7 matrix AAA peptidase subunit, paraplegin	Homo sapiens	107-110
19722686-8	2009	In addition, the treatment with TTN, a thiol-oxidizing reagent that forms intermolecular disulfide bonds, appeared to oxidize thiol groups in both the N-CPD and the membrane domain of AE1, which resulted in complete inhibition of the selenium export even during the initial period in which the export had a maximum velocity when using the thiol reagent-free treatment.	Disulfides	89-98	solute carrier family 4 member 1 (Diego blood group)	Homo sapiens	184-187
19722686-9	2009	Such complete inhibition of the selenium export from the TTN-treated RBC appeared to be due to the oligomerized AE1 proteins resulting from the intermolecularly formed disulfide bonds.	Disulfides	168-177	solute carrier family 4 member 1 (Diego blood group)	Homo sapiens	112-115
27170226-6	2017	We designed a modified type of nona-arginine (mR9) and synthesized a branched-mR9 (B-mR9) using disulfide bonds.	Disulfides	96-105	eosinophil-associated, ribonuclease A family, member 9	Mus musculus	78-81
19549190-2	2009	Zebrafish RNases have three intramolecular disulfide bonds, a characteristic structural feature of angiogenin, different from the typical four disulfide bonds of the other members of the RNase A superfamily.	Disulfides	43-52	angiogenin	Homo sapiens	99-109
19477928-1	2009	Mia40 and Erv1 execute a disulfide relay to import the small Tim proteins into the mitochondrial intermembrane space.	Disulfides	25-34	Rho guanine nucleotide exchange factor 5	Homo sapiens	61-64
24934525-6	2014	The rearrangement of disulfide bonds is modulated by protein disulfide isomerase (PDI).	Disulfides	21-30	prolyl 4-hydroxylase subunit beta	Homo sapiens	53-80
24934525-6	2014	The rearrangement of disulfide bonds is modulated by protein disulfide isomerase (PDI).	Disulfides	21-30	prolyl 4-hydroxylase subunit beta	Homo sapiens	82-85
24934525-10	2014	Disulfide-thiol exchange mediated by PDI appears to be involved in the conformational changes in integrin activation.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	37-40
27170226-6	2017	We designed a modified type of nona-arginine (mR9) and synthesized a branched-mR9 (B-mR9) using disulfide bonds.	Disulfides	96-105	eosinophil-associated, ribonuclease A family, member 9	Mus musculus	78-81
19369327-0	2009	Disulfide bond formation at the C termini of vaccinia virus A26 and A27 proteins does not require viral redox enzymes and suppresses glycosaminoglycan-mediated cell fusion.	Disulfides	0-9	immunoglobulin kappa variable 3-20	Homo sapiens	68-71
19369327-5	2009	A26 protein contains six cysteine residues, and in vitro mutagenesis showed that Cys441 and Cys442 mediated intermolecular disulfide bonds with Cys71 and Cys72 of viral A27 protein, whereas Cys43 and Cys342 mediated intramolecular disulfide bonds.	Disulfides	123-132	immunoglobulin kappa variable 3-20	Homo sapiens	169-172
28104838-5	2017	Preventing octamer distortion by site-specific disulfide linkages inhibits nucleosome sliding by SNF2h while promoting octamer eviction by the SWI-SNF complex, RSC.	Disulfides	47-56	SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 5	Homo sapiens	97-102
19369327-6	2009	A26 and A27 proteins formed disulfide-linked complexes in transfected 293T cells, showing that the intermolecular disulfide bond formation did not depend on viral redox pathways.	Disulfides	28-37	immunoglobulin kappa variable 3-20	Homo sapiens	8-11
19369327-6	2009	A26 and A27 proteins formed disulfide-linked complexes in transfected 293T cells, showing that the intermolecular disulfide bond formation did not depend on viral redox pathways.	Disulfides	114-123	immunoglobulin kappa variable 3-20	Homo sapiens	8-11
19477919-3	2009	We now show that protein disulfide isomerase (PDI) controls MHC class I disassembly by regulating dissociation of the tapasin-ERp57 disulfide conjugate.	Disulfides	25-34	prolyl 4-hydroxylase subunit beta	Homo sapiens	46-49
19385064-5	2009	Cysteine assignments in a Rspo2 derivative containing only the two furin-like domains (Rspo2-2F) provided the first information about the disulfide bonding pattern of this motif, which was characterized by multiple short loops and unpaired cysteine residues, and established that the loss-of-function cysteine mutants disrupted disulfide bond formation.	Disulfides	138-147	furin, paired basic amino acid cleaving enzyme	Homo sapiens	67-72
19462475-1	2009	Interferon-alpha2b (IFN-alpha2b) and human serum albumin (HSA) fusion protein (IFN-alpha2b-HSA) is a promising long acting formulation of IFN-alpha2b for the treatment of hepatitis C. However, accelerated mechanical and thermal stress tests revealed that IFN-alpha2b-HSA was prone to disulfide-linked aggregation.	Disulfides	284-293	interferon alpha 2	Homo sapiens	0-18
19349277-5	2009	Mutant Txnl1 with one active site cysteine replaced by serine formed disulfide bonds to eEF1A1, a substrate-recruiting factor of the 26 S proteasome.	Disulfides	69-78	eukaryotic translation elongation factor 1 alpha 1	Homo sapiens	88-94
24352565-7	2014	In addition, CalDAG-GEFI formed disulfide-linked oligomers in platelets treated with the thiol-oxidant diamide, indicating that CalDAG-GEFI contains redox-sensitive thiols.	Disulfides	32-41	RAS guanyl releasing protein 2	Homo sapiens	13-24
24352565-7	2014	In addition, CalDAG-GEFI formed disulfide-linked oligomers in platelets treated with the thiol-oxidant diamide, indicating that CalDAG-GEFI contains redox-sensitive thiols.	Disulfides	32-41	RAS guanyl releasing protein 2	Homo sapiens	128-139
24456905-10	2014	Two types of targets of disulfide stress were identified: redox buffers, such as ribonuclease inhibitor or albumin, and redox-signaling thiols, which include thioredoxin 1, APE1/Ref1, Keap1, tyrosine and serine/threonine phosphatases, and protein disulfide isomerase.	Disulfides	24-33	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	173-177
28063498-1	2017	A family of 14-20kDa, disulfide-rich, calcium-dependent secreted phospholipases A2 (sPLA2s) that release fatty acids from the sn-2 position of glycerophospholipids can be found in mammals.	Disulfides	22-31	phospholipase A2 group IID	Homo sapiens	84-90
24758840-5	2014	The non-covalently associated dimeric structures are reminiscent of those of the IR family, which has a disulfide-linked dimeric structure.	Disulfides	104-113	insulin receptor	Homo sapiens	81-83
19463173-10	2009	These data suggest that it inhibits RGS4 by forming disulfide bridges with the protein.	Disulfides	52-61	regulator of G protein signaling 4	Homo sapiens	36-40
19338268-0	2009	Aromatic-participant interactions are essential for disulfide-bond-based trimerization in human heat shock transcription factor 1.	Disulfides	52-61	heat shock transcription factor 1	Homo sapiens	96-129
19338268-6	2009	Thus, the existence of two differential interactions facilitates the formation of intermolecular disulfide bonds, leading to the heat-induced HSF1 trimerization.	Disulfides	97-106	heat shock transcription factor 1	Homo sapiens	142-146
24599957-5	2014	We present evidence suggesting that disulfide maturation occurs within Tg monomers engaged in each of the adduct bands.	Disulfides	36-45	thyroglobulin	Homo sapiens	71-73
28063893-1	2017	The Pseudomonas aeruginosa plasmid pUM505 contains in a pathogenicity island the dsbA2 gene, which encodes a product with similarity to DsbA protein disulfide isomerases, enzymes that catalyze formation and isomerization of disulfide bonds in protein cysteine residues.	Disulfides	149-158	thiol:disulfide interchange protein DsbA	Pseudomonas aeruginosa PAO1	136-140
24599957-6	2014	Moreover, the same Tg substrate molecules can form simultaneous mixed disulfides with both CaBP1/P5 and protein disulfide isomerase, although these are generally viewed as components of distinct oxidoreductase-chaperone protein complexes.	Disulfides	70-80	thyroglobulin	Homo sapiens	19-21
19344116-1	2009	Ribonuclease A (RNase A) undergoes more rapid conformational folding with its disulfide bonds intact than during oxidative folding from its reduced form.	Disulfides	78-87	ribonuclease A family member 1, pancreatic	Homo sapiens	0-14
19344116-1	2009	Ribonuclease A (RNase A) undergoes more rapid conformational folding with its disulfide bonds intact than during oxidative folding from its reduced form.	Disulfides	78-87	ribonuclease A family member 1, pancreatic	Homo sapiens	16-23
19344116-4	2009	However, in the mutants Y92G and Y92A, a key structured disulfide-bonded species, des-[65-72], involved in the oxidative folding pathway of RNase A, was destabilized.	Disulfides	56-65	ribonuclease A family member 1, pancreatic	Homo sapiens	140-147
28063893-3	2017	Transfer of the pUM505 dsbA2 gene to a cadmium-sensitive P. aeruginosa PAO1-derivative affected in the chromosomal dsbA gene, restored cadmium resistance, suggesting a role of DsbA2 in protecting protein disulfide bonds.	Disulfides	204-213	thiol:disulfide interchange protein DsbA	Pseudomonas aeruginosa PAO1	23-27
24649965-4	2014	When a Pt nanoparticle is attached to the molecular wire by reductive cleavage of the disulfide and reaction with the resulting thiol, the PS I-NQ(CH2)15S-Pt nanoconstruct evolves dihydrogen at a rate of 67.3 mumol of H2 (mg of Chl)(-1) h(-1) [3.4 e(-) (PS I)(-1) s(-1)] after illumination for 1 h at pH 6.4.	Disulfides	86-95	chordin like 1	Homo sapiens	228-231
27881076-0	2016	Clustering of disulfide-rich peptides provides scaffolds for hit discovery by phage display: application to interleukin-23.	Disulfides	14-23	interleukin 37	Homo sapiens	108-122
24452853-5	2014	This article will review some of the still controversial mechanisms implicated in cellular TF activation or decryption with particular focus on the coordinated effects of outer leaflet phosphatidylserine exposure and thiol-disulfide exchange pathways involving protein disulfide isomerase (PDI).	Disulfides	223-232	prolyl 4-hydroxylase subunit beta	Homo sapiens	261-288
19374345-1	2009	Protein disulfide isomerase (PDI) is a catalyst of isomerization of substrate protein intra- and extra-molecular disulfide bridges and also has 3,3",5-triiodo-l-thyronine (T(3))-binding activity and molecular chaperone-like activity.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
27703014-1	2016	In the mammalian endoplasmic reticulum, oxidoreductin-1alpha (Ero1alpha) generates protein disulfide bonds and transfers them specifically to canonical protein-disulfide isomerase (PDI) to sustain oxidative protein folding.	Disulfides	91-100	prolyl 4-hydroxylase subunit beta	Homo sapiens	181-184
19297523-3	2009	We have developed two novel assays to assess Cx43 folding and assembly: acquisition of resistance of disulfide bonds to reduction by extracellularly added DTT and Triton X-114 detergent phase partitioning.	Disulfides	101-110	gap junction protein alpha 1	Homo sapiens	45-49
23373897-6	2014	RECENT ADVANCES: The activity of HMGB1 strongly depends on its redox state: Inflammatory-active HMGB1 requires an intramolecular disulfide bond (Cys23 and Cys45) and a reduced Cys106.	Disulfides	129-138	high mobility group box 1	Homo sapiens	33-38
27703014-5	2016	The present study revealed that the Cys208-Cys241 disulfide was reduced by PDI and other PDI family members during PDI oxidation.	Disulfides	50-59	prolyl 4-hydroxylase subunit beta	Homo sapiens	75-78
23373897-6	2014	RECENT ADVANCES: The activity of HMGB1 strongly depends on its redox state: Inflammatory-active HMGB1 requires an intramolecular disulfide bond (Cys23 and Cys45) and a reduced Cys106.	Disulfides	129-138	high mobility group box 1	Homo sapiens	96-101
19176520-8	2009	This demonstrates a GSH-mixed disulfide mechanism for glutaredoxin catalysis in contrast to the dithiol mechanism for thioredoxin.	Disulfides	30-39	glutaredoxin	Homo sapiens	54-66
27703014-5	2016	The present study revealed that the Cys208-Cys241 disulfide was reduced by PDI and other PDI family members during PDI oxidation.	Disulfides	50-59	prolyl 4-hydroxylase subunit beta	Homo sapiens	89-92
19039312-2	2009	The AT1R contains two extracellular disulfides bonds but its ligand contains none, whereas the V1R contains no extracellular disufides bonds but its ligand contains 1.	Disulfides	36-46	angiotensin II receptor, type 1a	Rattus norvegicus	4-8
19039312-4	2009	RESULTS: Preincubation of cells with DTT, a maneuver designed to target receptor disulfides, resulted in concentration-dependent decreases in specific (125)I-AngII binding to AT1Rs and acute angiotensin-stimulated intracellular calcium mobilization but no decreases in specific (125)I-AVP binding to V1Rs or AVP-stimulated intracellular calcium mobilization.	Disulfides	81-91	angiotensin II receptor, type 1a	Rattus norvegicus	175-178
18977489-6	2009	The resulting material shows good thermal stability with the decomposition of the interacted chains within the disulfide galleries occurring at around 400 degrees C. The electrical conductivity of PPy/WS(2) nanocomposite was found to be high in the order of 10(-2) S cm(-1) at ambient temperature.	Disulfides	111-120	pancreatic polypeptide	Homo sapiens	197-200
24072177-2	2014	Titin stiffness is modulated by isoform variation, phosphorylation by protein kinases, and, possibly, oxidative stress through disulfide bond formation.	Disulfides	127-136	titin	Homo sapiens	0-5
24415753-2	2014	The aim of this study was to explain whether protein disulfide isomerase (PDI) is responsible for the thiol-disulfide rearrangement in the beta-actin molecule of adhering cells.	Disulfides	53-62	prolyl 4-hydroxylase subunit beta	Homo sapiens	74-77
24415753-3	2014	First, we showed that PDI forms a disulfide-bonded complex with beta-actin with a molecular mass of 110 kDa.	Disulfides	34-43	prolyl 4-hydroxylase subunit beta	Homo sapiens	22-25
24415753-10	2014	Our data suggest that PDI is released from subcellular compartments to the cytosol and translocated toward the periphery of the cell, where it forms a disulfide bond with beta-actin when MEG-01 cells adhere via the alphaIIbbeta3 integrin to fibronectin.	Disulfides	151-160	prolyl 4-hydroxylase subunit beta	Homo sapiens	22-25
24415753-11	2014	Thus, PDI appears to regulate cytoskeletal reorganization by the thiol-disulfide exchange in beta-actin via a redox-dependent mechanism.	Disulfides	71-80	prolyl 4-hydroxylase subunit beta	Homo sapiens	6-9
19054761-5	2009	In addition, some glycoproteins only require ERp57 for correct disulfide formation if they enter the calnexin cycle.	Disulfides	63-72	calnexin	Homo sapiens	101-109
19054761-7	2009	These conclusions suggest that the calnexin cycle has evolved with a specialized oxidoreductase to facilitate native disulfide formation in complex glycoproteins.	Disulfides	117-126	calnexin	Homo sapiens	35-43
27703014-5	2016	The present study revealed that the Cys208-Cys241 disulfide was reduced by PDI and other PDI family members during PDI oxidation.	Disulfides	50-59	prolyl 4-hydroxylase subunit beta	Homo sapiens	89-92
28236420-8	2016	Cytosolic Srx was found to be imported into mitochondria via a mechanism that requires formation of a disulfide-linked complex with heat shock protein 90, which is likely promoted by H2O2 released from mitochondria.	Disulfides	102-111	sulfiredoxin 1	Homo sapiens	10-13
19010334-0	2009	The disulfide relay system of mitochondria is required for the biogenesis of mitochondrial Ccs1 and Sod1.	Disulfides	4-13	copper chaperone CCS1	Saccharomyces cerevisiae S288C	91-95
19010334-0	2009	The disulfide relay system of mitochondria is required for the biogenesis of mitochondrial Ccs1 and Sod1.	Disulfides	4-13	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	100-104
19010334-3	2009	The biogenesis of functional Sod1 is dependent on its copper chaperone, Ccs1, which introduces a disulfide bond and a copper ion into Sod1.	Disulfides	97-106	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	29-33
19010334-3	2009	The biogenesis of functional Sod1 is dependent on its copper chaperone, Ccs1, which introduces a disulfide bond and a copper ion into Sod1.	Disulfides	97-106	copper chaperone CCS1	Saccharomyces cerevisiae S288C	72-76
24385427-0	2014	Intramolecular disulfide bond of Tim22 protein maintains integrity of the TIM22 complex in the mitochondrial inner membrane.	Disulfides	15-24	translocase of inner mitochondrial membrane 22	Homo sapiens	33-38
24385427-0	2014	Intramolecular disulfide bond of Tim22 protein maintains integrity of the TIM22 complex in the mitochondrial inner membrane.	Disulfides	15-24	translocase of inner mitochondrial membrane 22	Homo sapiens	74-79
24385427-3	2014	Here we report that the conserved Cys residues of Tim22 form an intramolecular disulfide bond.	Disulfides	79-88	translocase of inner mitochondrial membrane 22	Homo sapiens	50-55
19010334-3	2009	The biogenesis of functional Sod1 is dependent on its copper chaperone, Ccs1, which introduces a disulfide bond and a copper ion into Sod1.	Disulfides	97-106	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	134-138
27729062-3	2016	METHODS: IL-7Ralpha-targeted peptides were searched within a disulfide-constrained combinatorial phage displayed library of random linear heptapeptides.	Disulfides	61-70	interleukin 7 receptor	Homo sapiens	9-19
19010334-11	2009	Mia40 forms mixed disulfides with Ccs1, suggesting a role of Mia40 for the generation of disulfide bonds in Ccs1.	Disulfides	18-28	copper chaperone CCS1	Saccharomyces cerevisiae S288C	108-112
19010334-11	2009	Mia40 forms mixed disulfides with Ccs1, suggesting a role of Mia40 for the generation of disulfide bonds in Ccs1.	Disulfides	18-27	copper chaperone CCS1	Saccharomyces cerevisiae S288C	108-112
19010334-12	2009	We suggest that the disulfide relay system transfers disulfide bonds via Mia40 to Ccs1, which then shuttles disulfide bonds to Sod1.	Disulfides	20-29	copper chaperone CCS1	Saccharomyces cerevisiae S288C	82-86
19010334-12	2009	We suggest that the disulfide relay system transfers disulfide bonds via Mia40 to Ccs1, which then shuttles disulfide bonds to Sod1.	Disulfides	20-29	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	127-131
19010334-12	2009	We suggest that the disulfide relay system transfers disulfide bonds via Mia40 to Ccs1, which then shuttles disulfide bonds to Sod1.	Disulfides	53-62	copper chaperone CCS1	Saccharomyces cerevisiae S288C	82-86
19010334-12	2009	We suggest that the disulfide relay system transfers disulfide bonds via Mia40 to Ccs1, which then shuttles disulfide bonds to Sod1.	Disulfides	53-62	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	127-131
19010334-12	2009	We suggest that the disulfide relay system transfers disulfide bonds via Mia40 to Ccs1, which then shuttles disulfide bonds to Sod1.	Disulfides	53-62	copper chaperone CCS1	Saccharomyces cerevisiae S288C	82-86
24385427-4	2014	By comparison of Tim22 Cys   Ser mutants with wild-type Tim22, we show that the disulfide bond of Tim22 stabilizes Tim22 especially at elevated temperature through interactions with Tim18, which are also important for the stability of the TIM22 complex.	Disulfides	80-89	translocase of inner mitochondrial membrane 22	Homo sapiens	17-22
24385427-4	2014	By comparison of Tim22 Cys   Ser mutants with wild-type Tim22, we show that the disulfide bond of Tim22 stabilizes Tim22 especially at elevated temperature through interactions with Tim18, which are also important for the stability of the TIM22 complex.	Disulfides	80-89	translocase of inner mitochondrial membrane 22	Homo sapiens	56-61
24385427-4	2014	By comparison of Tim22 Cys   Ser mutants with wild-type Tim22, we show that the disulfide bond of Tim22 stabilizes Tim22 especially at elevated temperature through interactions with Tim18, which are also important for the stability of the TIM22 complex.	Disulfides	80-89	translocase of inner mitochondrial membrane 22	Homo sapiens	56-61
24385427-4	2014	By comparison of Tim22 Cys   Ser mutants with wild-type Tim22, we show that the disulfide bond of Tim22 stabilizes Tim22 especially at elevated temperature through interactions with Tim18, which are also important for the stability of the TIM22 complex.	Disulfides	80-89	translocase of inner mitochondrial membrane 22	Homo sapiens	239-244
24385427-5	2014	We also show that lack of the disulfide bond in Tim22 impairs the assembly of TIM22 pathway substrate proteins into the inner membrane especially when the TIM22 complex handles excess amounts of substrate proteins.	Disulfides	30-39	translocase of inner mitochondrial membrane 22	Homo sapiens	48-53
24385427-5	2014	We also show that lack of the disulfide bond in Tim22 impairs the assembly of TIM22 pathway substrate proteins into the inner membrane especially when the TIM22 complex handles excess amounts of substrate proteins.	Disulfides	30-39	translocase of inner mitochondrial membrane 22	Homo sapiens	78-83
24385427-5	2014	We also show that lack of the disulfide bond in Tim22 impairs the assembly of TIM22 pathway substrate proteins into the inner membrane especially when the TIM22 complex handles excess amounts of substrate proteins.	Disulfides	30-39	translocase of inner mitochondrial membrane 22	Homo sapiens	155-160
24437386-7	2014	Employing alpha-globin as a model substrate, we demonstrate the facile conjugation to K48-linked ubiquitin chains, bearing up to four ubiquitins, through disulfide and thioether linkages.	Disulfides	154-163	hemoglobin subunit alpha 2	Homo sapiens	10-22
19010334-12	2009	We suggest that the disulfide relay system transfers disulfide bonds via Mia40 to Ccs1, which then shuttles disulfide bonds to Sod1.	Disulfides	53-62	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	127-131
19010334-13	2009	In conclusion, the disulfide relay system is crucial for the import of Ccs1, thereby affecting the transport of Sod1, and it can control the distribution of Ccs1 and Sod1 between the IMS of mitochondria and the cytosol.	Disulfides	19-28	copper chaperone CCS1	Saccharomyces cerevisiae S288C	71-75
19010334-13	2009	In conclusion, the disulfide relay system is crucial for the import of Ccs1, thereby affecting the transport of Sod1, and it can control the distribution of Ccs1 and Sod1 between the IMS of mitochondria and the cytosol.	Disulfides	19-28	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	112-116
19010334-13	2009	In conclusion, the disulfide relay system is crucial for the import of Ccs1, thereby affecting the transport of Sod1, and it can control the distribution of Ccs1 and Sod1 between the IMS of mitochondria and the cytosol.	Disulfides	19-28	copper chaperone CCS1	Saccharomyces cerevisiae S288C	157-161
19010334-13	2009	In conclusion, the disulfide relay system is crucial for the import of Ccs1, thereby affecting the transport of Sod1, and it can control the distribution of Ccs1 and Sod1 between the IMS of mitochondria and the cytosol.	Disulfides	19-28	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	166-170
18814280-1	2008	In addition to the known function in the glycolytic pathway, phosphoglycerate kinase 1 (PGK-1) promotes reduction of plasmin disulfide bonds leading to angiostatin formation and inhibition of tumor angiogenesis.	Disulfides	125-134	phosphoglycerate kinase 1	Mus musculus	61-86
18814280-1	2008	In addition to the known function in the glycolytic pathway, phosphoglycerate kinase 1 (PGK-1) promotes reduction of plasmin disulfide bonds leading to angiostatin formation and inhibition of tumor angiogenesis.	Disulfides	125-134	phosphoglycerate kinase 1	Mus musculus	88-93
27608665-3	2016	HGF is secreted as a single-chain (sc) precursor and is processed by extracellular proteases to generate disulfide-bonded two-chain (tc) HGF.	Disulfides	105-114	hepatocyte growth factor	Homo sapiens	0-3
18936094-2	2008	We previously showed that natural MT6-MMP is expressed on the cell surface as a major reduction-sensitive form of M(r) 120, likely representing enzyme homodimers held by disulfide bridges.	Disulfides	170-179	matrix metallopeptidase 25	Homo sapiens	34-41
18936094-4	2008	A systematic site-directed mutagenesis study of the Cys residues in the stem region shows that Cys(532) is involved in MT6-MMP dimerization by forming an intermolecular disulfide bond.	Disulfides	169-178	matrix metallopeptidase 25	Homo sapiens	119-126
24506865-6	2014	Thioredoxin1 (Trx1), an important reducing enzyme that cleaves disulfides in proteins, prevents AMPK oxidation, serving as an essential cofactor for AMPK activation.	Disulfides	63-73	protein kinase AMP-activated catalytic subunit alpha 1	Homo sapiens	96-100
24506865-6	2014	Thioredoxin1 (Trx1), an important reducing enzyme that cleaves disulfides in proteins, prevents AMPK oxidation, serving as an essential cofactor for AMPK activation.	Disulfides	63-73	protein kinase AMP-activated catalytic subunit alpha 1	Homo sapiens	149-153
24198232-7	2014	Furthermore, we were able to demonstrate that thioredoxin can cleave diverse intra- as well as intermolecular disulfide bridges, which strongly enhances the activity of the enzyme.	Disulfides	110-119	thioredoxin H-type 1	Arabidopsis thaliana	46-57
18783346-11	2008	CTRP3, CTRP5, CTRP6 and CTRP10 trimers are further assembled into higher-order oligomeric complexes via disulfide bonding mediated by their N-terminal cysteine residues.	Disulfides	104-113	C1q and tumor necrosis factor related protein 3	Mus musculus	0-5
18783346-11	2008	CTRP3, CTRP5, CTRP6 and CTRP10 trimers are further assembled into higher-order oligomeric complexes via disulfide bonding mediated by their N-terminal cysteine residues.	Disulfides	104-113	C1q and tumor necrosis factor related protein 5	Mus musculus	7-12
27608665-3	2016	HGF is secreted as a single-chain (sc) precursor and is processed by extracellular proteases to generate disulfide-bonded two-chain (tc) HGF.	Disulfides	105-114	hepatocyte growth factor	Homo sapiens	137-140
27607147-8	2016	The eight N-terminal amino acid residues of IAPP, forming a ring-like structure due to a disulfide bridge between residues C2 and C7, appear to be well defined but with an increased degree of flexibility.	Disulfides	89-98	islet amyloid polypeptide	Homo sapiens	44-48
18775986-9	2008	Although native RMAD-4((62-94)) resists NE, CG, and P3 proteolysis completely, RMAD-4((62-94)) variants with disulfide pairing disruptions or lacking disulfide bonds were degraded extensively, evidence that the disulfide array protects the alpha-defensin moiety from degradation by the myeloid converting enzymes.	Disulfides	109-118	neutrophil defensin 6	Macaca mulatta	79-85
24203231-7	2014	Besides, a monomeric glutathionylated form and a dimeric disulfide-bridged form of BolA2 can be preferentially reduced by the nucleo-cytoplasmic GrxS17.	Disulfides	57-66	thioredoxin family protein	Arabidopsis thaliana	145-151
27606074-4	2016	Thus, here we designed a branched CPP using disulfide bridges based on the linear TAT peptide, to enhance the gene delivery efficiency in a better way.	Disulfides	44-53	tyrosine aminotransferase	Homo sapiens	82-85
24061560-5	2013	In addition, we show CCS-independent oxidation of the disulfide bond in S. cerevisiae Sod1.	Disulfides	54-63	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	86-90
28503550-2	2016	SP-B is a member of the Saposin or Saposin-like proteins (SAPLIP) family of proteins that share an overall three-dimensional folding pattern based on secondary structures and disulfide connectivity and exhibit a wide diversity of biological functions.	Disulfides	175-184	surfactant protein B	Homo sapiens	0-4
23948593-3	2013	Cys residues which could form disulfides suggest the involvement of CAC in redox switches.	Disulfides	30-40	solute carrier family 25 member 20	Homo sapiens	68-71
24146829-0	2013	Stabilizing exposure of conserved epitopes by structure guided insertion of disulfide bond in HIV-1 envelope glycoprotein.	Disulfides	76-85	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	100-121
18753405-0	2008	Evolution rescues folding of human immunodeficiency virus-1 envelope glycoprotein GP120 lacking a conserved disulfide bond.	Disulfides	108-117	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	82-87
18703501-7	2008	Mass spectrometry experiments showed that CA IX contains an intramolecular disulfide bridge (Cys(119)-Cys(299)) and a unique N-linked glycosylation site (Asn(309)) that bears high mannose-type glycan structures.	Disulfides	75-84	carbonic anhydrase 9	Homo sapiens	42-47
18647229-0	2008	The membrane-proximal intermolecular disulfide bonds in glycoprotein Ib influence receptor binding to von Willebrand factor.	Disulfides	37-46	von Willebrand factor	Cricetulus griseus	102-123
18647229-7	2008	CONCLUSIONS: The disulfide bonds between GPIbalpha and GPIbbeta are necessary for optimal GPIbalpha binding to VWF.	Disulfides	17-26	von Willebrand factor	Cricetulus griseus	111-114
18647229-8	2008	The structural plasticity around the disulfide bonds may also help to shed light on the inside-out mechanism underlying GPIbbeta modulation of VWF binding.	Disulfides	37-46	von Willebrand factor	Cricetulus griseus	143-146
23843626-4	2013	In the case of Fz4-FEVR, CRYAB prevents the formation of inter-chain disulfide bridges between the lumenal ectodomains of the aggregated mutant chains, which enables correct folding and promotes appropriate compartmentalization on the plasma membrane.	Disulfides	69-78	frizzled class receptor 4	Homo sapiens	15-23
27402834-2	2016	We demonstrate that interleukin-12, a heterodimeric pro-inflammatory cytokine consisting of the disulfide-linked p40 and p35 subunits, can be reconstituted by sequential reassembly of fusion proteins based on antibody fragments and interleukin-12 subunit mutants.	Disulfides	96-105	interleukin 9	Homo sapiens	113-116
23698001-5	2013	The crystal structure of MST reveals a mixture of the product complex containing pyruvate and an active site cysteine persulfide (Cys(248)-SSH) and a nonproductive intermediate in which 3-MP is covalently linked via a disulfide bond to an active site cysteine.	Disulfides	218-227	mercaptopyruvate sulfurtransferase	Homo sapiens	25-28
23696644-6	2013	The actin binding domain of drebrin decreases the intrastrand disulfide cross-linking of Cys-41 (in the DNase I binding loop) to Cys-374 (C-terminal) but increases the interstrand disulfide cross-linking of Cys-265 (hydrophobic loop) to Cys-374 in the yeast mutants Q41C and S265C, respectively.	Disulfides	62-71	drebrin 1	Homo sapiens	28-35
18771940-9	2008	Cofilin oxidation induced formation of an intramolecular disulfide bridge and loss of its Ser3 phosphorylation.	Disulfides	57-66	cofilin 1	Homo sapiens	0-7
27334695-6	2016	Our pull-down and co-immunoprecipitation assays suggest that, in addition to disulfide bonds, salt bridges also contribute to MICU1-MICU2 heterodimer formation.	Disulfides	77-86	mitochondrial calcium uptake 1	Homo sapiens	126-131
18171593-7	2008	The specific interaction of roGFP with GRX results in continuous formation and release of the roGFP disulfide bridge depending on the actual redox potential of the cellular glutathione buffer.	Disulfides	100-109	glutaredoxin	Homo sapiens	39-42
23776208-0	2013	MIF intersubunit disulfide mutant antagonist supports activation of CD74 by endogenous MIF trimer at physiologic concentrations.	Disulfides	17-26	macrophage migration inhibitory factor	Homo sapiens	0-3
23776208-0	2013	MIF intersubunit disulfide mutant antagonist supports activation of CD74 by endogenous MIF trimer at physiologic concentrations.	Disulfides	17-26	CD74 molecule	Homo sapiens	68-72
27334695-6	2016	Our pull-down and co-immunoprecipitation assays suggest that, in addition to disulfide bonds, salt bridges also contribute to MICU1-MICU2 heterodimer formation.	Disulfides	77-86	mitochondrial calcium uptake 2	Homo sapiens	132-137
23776208-0	2013	MIF intersubunit disulfide mutant antagonist supports activation of CD74 by endogenous MIF trimer at physiologic concentrations.	Disulfides	17-26	macrophage migration inhibitory factor	Homo sapiens	87-90
23776208-5	2013	A cysteine mutant (N110C) that covalently locks MIF into a trimer by forming a disulfide with Cys-80 of an adjacent subunit is used to study this issue.	Disulfides	79-88	macrophage migration inhibitory factor	Homo sapiens	48-51
27015373-7	2016	Silver ions from AgNO3 and Ag2O remarkably decreased enzymatic activity of neuraminidase through the breakage of disulfide (SS) bonds, corresponding to the selective inactivation of influenza A virus.	Disulfides	113-122	neuraminidase 1	Homo sapiens	75-88
23799067-3	2013	While several molecules have been identified that modulate the release of HMGB1, less attention has been paid to identify pharmacological inhibitors of the downstream inflammatory processes elicited by HMGB1 (C23-C45 disulfide C106 thiol form).	Disulfides	217-226	high mobility group box 1	Mus musculus	202-207
18606809-0	2008	Nitrosylation of ISG15 prevents the disulfide bond-mediated dimerization of ISG15 and contributes to effective ISGylation.	Disulfides	36-45	ISG15 ubiquitin like modifier	Homo sapiens	17-22
18606809-0	2008	Nitrosylation of ISG15 prevents the disulfide bond-mediated dimerization of ISG15 and contributes to effective ISGylation.	Disulfides	36-45	ISG15 ubiquitin like modifier	Homo sapiens	76-81
27189887-2	2016	ASPF and ASPG are composed of 33 and 32 amino acids, respectively, and contain six cysteines which are involved in three disulfide bonds.	Disulfides	121-130	asparaginase	Homo sapiens	9-13
18479207-3	2008	Low thioredoxin reductase activity in the erythrocyte is able to keep up with this basal oxidation and maintain the Prx2 in its reduced form, but exposure to exogenous hydrogen peroxide causes accumulation of the disulfide-linked dimer.	Disulfides	213-222	peroxiredoxin 2	Mus musculus	4-25
23583257-6	2013	Interestingly, Nox4 activity is also stimulated by reducing agents that possibly act by reducing the disulfide bridge (Cys226, Cys270) located in the extracellular E-loop of Nox4.	Disulfides	101-110	NADPH oxidase 4	Homo sapiens	15-19
23583257-6	2013	Interestingly, Nox4 activity is also stimulated by reducing agents that possibly act by reducing the disulfide bridge (Cys226, Cys270) located in the extracellular E-loop of Nox4.	Disulfides	101-110	NADPH oxidase 4	Homo sapiens	174-178
26710800-4	2016	In particular, known inhibitors of the NADPH-dependent selenoprotein, thioredoxin reductase, were shown to inhibit phagosomal disulfide reduction and phagosomal proteolysis.	Disulfides	126-135	2,4-dienoyl CoA reductase 1, mitochondrial	Mus musculus	39-44
23508573-1	2013	High mobility group box 1 (HMGB1) is a DNA-binding protein that possesses cytokinelike, proinflammatory properties when released extracellularly in the C23-C45 disulfide form.	Disulfides	160-169	high mobility group box 1	Homo sapiens	0-25
23508573-1	2013	High mobility group box 1 (HMGB1) is a DNA-binding protein that possesses cytokinelike, proinflammatory properties when released extracellularly in the C23-C45 disulfide form.	Disulfides	160-169	high mobility group box 1	Homo sapiens	27-32
18636684-0	2008	Improving digestibility of soy flour by reducing disulfide bonds with thioredoxin.	Disulfides	49-58	thioredoxin	Glycine max	70-81
18636684-3	2008	Treatment of soy white flour with a NADP-thioredoxin system (NTS) effectively reduced disulfide bonds in soy flour and increased protein digestibility by trypsin and pancreatin as measured by the pH stat method.	Disulfides	86-95	thioredoxin	Glycine max	41-52
26710800-4	2016	In particular, known inhibitors of the NADPH-dependent selenoprotein, thioredoxin reductase, were shown to inhibit phagosomal disulfide reduction and phagosomal proteolysis.	Disulfides	126-135	peroxiredoxin 2	Mus musculus	70-91
18660822-2	2008	Ligands contain a disulfide-rich Delta/Serrate/LAG-2 (DSL) domain required for Notch trans-activation or cis-inhibition.	Disulfides	18-27	granulysin	Homo sapiens	47-52
26710800-6	2016	In addition, pharmacologic inhibition of the pentose phosphate pathway decreased rates of disulfide reduction and proteolysis in the phagosome, implicating NADPH as a source of phagosomal reductive energy.	Disulfides	90-99	2,4-dienoyl CoA reductase 1, mitochondrial	Mus musculus	156-161
18511416-3	2008	ColQ has two cysteines upstream of the PRAD, which are disulfide-linked to two AChE(T) subunits ("heavy" dimer), and the other two subunits are disulfide-linked together ("light" dimer).	Disulfides	55-64	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	0-4
18511416-3	2008	ColQ has two cysteines upstream of the PRAD, which are disulfide-linked to two AChE(T) subunits ("heavy" dimer), and the other two subunits are disulfide-linked together ("light" dimer).	Disulfides	144-153	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	0-4
18457423-0	2008	Two distinct disulfide bonds formed in human heat shock transcription factor 1 act in opposition to regulate its DNA binding activity.	Disulfides	13-22	heat shock transcription factor 1	Homo sapiens	45-78
23486473-1	2013	The chloroplast CF0-CF1-ATP synthase (ATP synthase) is activated in the light and inactivated in the dark by thioredoxin-mediated redox modulation of a disulfide bridge on its gamma subunit.	Disulfides	152-161	thioredoxin H-type 1	Arabidopsis thaliana	109-120
23337974-1	2013	Protein disulfide isomerase (PDI) plays an important role in the endoplasmic reticulum (ER) by facilitating the exchange of disulfide bonds and, together with other ER stress proteins, is induced in amyotrophic lateral sclerosis (ALS).	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
18457423-3	2008	Our in vitro experiments show that the heat-induced bonding between the cysteine C36 and C103 residues of HSF1 forms an intermolecular disulfide covalent bond (SS-I bond) and that it directly causes HSF1 to trimerize and bond to DNA.	Disulfides	135-144	heat shock transcription factor 1	Homo sapiens	106-110
27126903-2	2016	In the present study, hydrophobic doxorubicin (DOX) and negatively charged miR-34a were simultaneously delivered via a reducible self-assembling disulfide cross-linked stearyl-peptide-based micellar system (SHRss) using poly(l-arginine)-poly(l-histidine)-stearoyl as the copolymer building unit.	Disulfides	145-154	microRNA 34a	Homo sapiens	75-82
18457423-3	2008	Our in vitro experiments show that the heat-induced bonding between the cysteine C36 and C103 residues of HSF1 forms an intermolecular disulfide covalent bond (SS-I bond) and that it directly causes HSF1 to trimerize and bond to DNA.	Disulfides	135-144	heat shock transcription factor 1	Homo sapiens	199-203
18358819-3	2008	We have successfully determined the disulfide linkages for Fn14 and independently confirmed those of the IgV domain of TIM-1, whose crystal structure was published recently.	Disulfides	36-45	TNF receptor superfamily member 12A	Homo sapiens	59-63
23540684-7	2013	These results provide new insights into the formation of disulfide-based SAMs on gold but also raise some fundamental questions about the intimate mechanism involved in the facilitated adsorption/desorption of SAMs under electrode polarization.	Disulfides	57-66	methionine adenosyltransferase 1A	Homo sapiens	73-77
23540684-7	2013	These results provide new insights into the formation of disulfide-based SAMs on gold but also raise some fundamental questions about the intimate mechanism involved in the facilitated adsorption/desorption of SAMs under electrode polarization.	Disulfides	57-66	methionine adenosyltransferase 1A	Homo sapiens	210-214
27271225-3	2016	Functionalization of GO with a peptide substrate for MMP-2 bearing a thiol group leads to its self-assembly via disulfide bonding, accompanied by self-quenching of GO"s strong fluorescence.	Disulfides	112-121	matrix metallopeptidase 2	Homo sapiens	53-58
23550886-1	2013	Pantetheine and its corresponding disulfide pantethine play a key role in metabolism as building blocks of coenzyme A (CoA), an essential cofactor utilized in ~4% of primary metabolism and central to fatty acid, polyketide, and nonribosomal peptide synthases.	Disulfides	34-43	outer membrane porin F	Escherichia coli str. K-12 substr. MG1655	107-117
23550886-1	2013	Pantetheine and its corresponding disulfide pantethine play a key role in metabolism as building blocks of coenzyme A (CoA), an essential cofactor utilized in ~4% of primary metabolism and central to fatty acid, polyketide, and nonribosomal peptide synthases.	Disulfides	34-43	outer membrane porin F	Escherichia coli str. K-12 substr. MG1655	119-122
18537713-1	2008	An intermolecular disulfide bond serves as a thioredoxin-dependent redox-sensing switch for the regulation of the enzymatic activity of 3-mercaptopyruvate sulfurtransferase (MST, EC.2.8.1.2).	Disulfides	18-27	mercaptopyruvate sulfurtransferase	Homo sapiens	136-172
18057002-0	2008	The differential impact of disulfide bonds and N-linked glycosylation on the stability and function of CD14.	Disulfides	27-36	CD14 molecule	Homo sapiens	103-107
27174643-5	2016	To selectively disrupt this redox switch, we identified a catalytically fully active SUMO E2 enzyme variant (Ubc9 D100A) with strongly reduced propensity to maintain a disulfide with the E1 enzyme in vitro and in cells.	Disulfides	168-177	ubiquitin conjugating enzyme E2 I	Homo sapiens	109-113
18057002-7	2008	A differential impact is observed for the five disulfide bonds on CD14 folding, with the first two (Cys(6)-Cys(17) and Cys(15)-Cys(32)) being indispensable, the third and fourth (Cys(168)-Cys(198) and Cys(222)-Cys(253)) being important, and the last (Cys(287)-Cys(333)) being dispensable.	Disulfides	47-56	CD14 molecule	Homo sapiens	66-70
18057002-8	2008	A functional role is observed for the first disulfide bond because the C6A substitution severely reduces the ability of CD14 to confer lipopolysaccharide responsiveness to U373 cells.	Disulfides	44-53	CD14 molecule	Homo sapiens	120-124
18057002-11	2008	When mapped onto the crystal structure of mouse CD14, the first two disulfide bonds and Asn(132) are in close proximity to the initial beta strands of the leucine rich repeat domain.	Disulfides	68-77	CD14 antigen	Mus musculus	48-52
18057002-12	2008	Thus, disulfide bonds and N-linked glycosylation in the initial beta sheets of the inner concave surface of CD14 are crucial for structure and function.	Disulfides	6-15	CD14 molecule	Homo sapiens	108-112
17964057-2	2008	Elafin and SLPI are structurally related in that both have a fold with a four-disulfide core or whey acidic protein (WAP) domain responsible for inhibiting proteases.	Disulfides	78-87	peptidase inhibitor 3	Homo sapiens	0-6
23514737-5	2013	This finding was further confirmed when both beta2 integrins were activated by chemokines (fMLF or IL-8), divalent cations (Mg(2+) or Mn(2+)), or disulfide bond lockage on an HA state.	Disulfides	146-155	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	45-50
23354473-1	2013	In this study, we demonstrated the formation of gas-phase peptide perthiyl (RSS ) and thiyl (RS ) radical ions besides sulfinyl radical (RSO ) ions from atmospheric pressure (AP) ion/radical reactions of peptides containing inter-chain disulfide bonds.	Disulfides	236-245	Russell-Silver dwarfism	Homo sapiens	76-79
26894887-3	2016	The N-terminal region of IAPP contains a conserved disulfide bond between cysteines at position 2 and 7, which is important to hIAPP"s in vivo function and may play a role in in vitro aggregation.	Disulfides	51-60	islet amyloid polypeptide	Homo sapiens	25-29
18181226-1	2008	Insulin is a peptide hormone consisting of two peptide chains (A- and B-chain) that are cross-linked by two disulfide bonds.	Disulfides	108-117	INS	Equus caballus	0-7
17920929-5	2007	Here, we report the large-scale stable production of ILT1 D1D2 domains through engineering of site-directed mutagenesis (R142C) that introduces a cysteine at amino acid position 142 to form a disulfide bond with the spare cys132 without topological influences of the native protein based on the known structures of the homologous ILT 2/4/11.	Disulfides	192-201	leukocyte immunoglobulin like receptor A2	Homo sapiens	53-57
26894887-3	2016	The N-terminal region of IAPP contains a conserved disulfide bond between cysteines at position 2 and 7, which is important to hIAPP"s in vivo function and may play a role in in vitro aggregation.	Disulfides	51-60	islet amyloid polypeptide	Homo sapiens	127-132
17892489-5	2007	This includes a family of enzymes involved in catalyzing thiol-disulfide exchange in the endoplasmic reticulum, the protein disulfide isomerase (PDI) family.	Disulfides	63-72	prolyl 4-hydroxylase subunit beta	Homo sapiens	116-143
17892489-5	2007	This includes a family of enzymes involved in catalyzing thiol-disulfide exchange in the endoplasmic reticulum, the protein disulfide isomerase (PDI) family.	Disulfides	63-72	prolyl 4-hydroxylase subunit beta	Homo sapiens	145-148
23169770-6	2013	CS affected the formation of disulfide bonds through excessive posttranslational oxidation of protein disulfide isomerase (PDI).	Disulfides	29-38	prolyl 4-hydroxylase subunit beta	Homo sapiens	94-121
23169770-6	2013	CS affected the formation of disulfide bonds through excessive posttranslational oxidation of protein disulfide isomerase (PDI).	Disulfides	29-38	prolyl 4-hydroxylase subunit beta	Homo sapiens	123-126
23352894-5	2013	Furthermore, the recombinant LECT2 was found to be self-oligomerized by disulfide bonds in vitro, but this was suppressed by addition of zinc.	Disulfides	72-81	leukocyte cell-derived chemotaxin 2	Mus musculus	29-34
26894887-4	2016	The importance of the disulfide bond in this region was probed using a combination of ion mobility-based mass spectrometry experiments, molecular dynamics simulations, and high-resolution atomic force microscopy imaging on the wildtype 1-8 hIAPP fragment, a reduced fragment with no disulfide bond, and a fragment with both cysteines at positions 2 and 7 mutated to serine.	Disulfides	22-31	islet amyloid polypeptide	Homo sapiens	240-245
27145151-5	2016	Conformational flexibility in the body of SPLUNC1 is also involved in the bacteriostatic, surfactant, and LPS binding functions of the protein as revealed by disulfide mutants introduced into SPLUNC1.	Disulfides	158-167	BPI fold containing family A member 1	Homo sapiens	42-49
23247088-0	2013	Bacterial expression and purification of a heterodimeric adrenomedullin receptor extracellular domain complex using DsbC-assisted disulfide shuffling.	Disulfides	130-139	putative protein DsbC	Escherichia coli	116-120
23247088-5	2013	Co-expression of the RAMP2 ECD with the disulfide bond isomerase DsbC in the oxidizing cytoplasm of E. coli trxB gor enabled proper disulfide formation in vivo.	Disulfides	40-49	putative protein DsbC	Escherichia coli	65-69
23247088-5	2013	Co-expression of the RAMP2 ECD with the disulfide bond isomerase DsbC in the oxidizing cytoplasm of E. coli trxB gor enabled proper disulfide formation in vivo.	Disulfides	132-141	putative protein DsbC	Escherichia coli	65-69
17697113-2	2007	In vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase.	Disulfides	9-18	prolyl 4-hydroxylase subunit beta	Homo sapiens	57-84
17222592-6	2007	Thioredoxin, glutaredoxin (thioltransferase) and protein disulfide isomerase are the key enzymes in controlling cellular oxidative stress that catalyze reduction of glutathionyl protein disulfide bonds.	Disulfides	57-66	glutaredoxin	Homo sapiens	27-43
26993521-5	2016	Biophysical analysis of recombinant MUC5B COOH-terminus (CT5B; D4-B-C-CK) expressed in 293-EBNA cells showed that MUC5B dimerizes by disulfide linkage.	Disulfides	133-142	mucin 5B, oligomeric mucus/gel-forming	Homo sapiens	36-41
17513868-6	2007	Biochemical and biosynthesis analyses revealed that MT6-MMP displayed on the cell surface exists as a major form of 120 kDa that likely represents enzyme homodimers linked by disulfide bonds.	Disulfides	175-184	matrix metallopeptidase 25	Homo sapiens	52-59
23291178-7	2013	In addition, disulfide isomerase, DsbC, catalyzed the efficient shuffling of incorrectly formed disulfide bonds during the protein synthesis reaction.	Disulfides	13-22	putative protein DsbC	Escherichia coli	34-38
23221553-1	2013	The structure of the transmembrane subunit (TM) of the retroviral envelope glycoprotein (Env) is highly conserved among most retrovirus genera and includes a pair of cysteines that forms an intramolecular disulfide loop within the ectodomain.	Disulfides	205-214	endogenous retrovirus group K member 6, envelope	Homo sapiens	66-87
26993521-5	2016	Biophysical analysis of recombinant MUC5B COOH-terminus (CT5B; D4-B-C-CK) expressed in 293-EBNA cells showed that MUC5B dimerizes by disulfide linkage.	Disulfides	133-142	mucin 5B, oligomeric mucus/gel-forming	Homo sapiens	114-119
23221553-1	2013	The structure of the transmembrane subunit (TM) of the retroviral envelope glycoprotein (Env) is highly conserved among most retrovirus genera and includes a pair of cysteines that forms an intramolecular disulfide loop within the ectodomain.	Disulfides	205-214	endogenous retrovirus group K member 6, envelope	Homo sapiens	89-92
23221553-2	2013	Alpha-, gamma-, and deltaretroviruses have a third cysteine, adjacent to the loop, which forms a disulfide bond between TM and the surface subunit (SU) of Env, while lentiviruses, which have noncovalently associated subunits, lack this third cysteine.	Disulfides	97-106	endogenous retrovirus group K member 6, envelope	Homo sapiens	155-158
26961872-12	2016	Disulfide loading of cells by inhibition of GSSG reductase (bischoloronitrosourea) or thioredoxin reductase (auranofin) was effective in causing EOMA death as well.	Disulfides	0-9	peroxiredoxin 2	Mus musculus	86-107
23012103-3	2013	Lysosomal cysteine protease cathepsin S (CatS) contains disulfide bonds and mediates essential steps in MHC class II-restricted processing, including proteolysis of large polypeptides and cleavage of the invariant chain.	Disulfides	56-65	cathepsin S	Felis catus	28-39
17468103-10	2007	Glutaredoxin (GRx), which specifically catalyzes reduction of protein-SSG mixed disulfides, reversed inhibition of p65-NFkappaB DNA binding in extracts from cells treated with hypoxia plus NAC and restored NFkappaB activity.	Disulfides	80-90	glutaredoxin	Homo sapiens	0-12
17468103-10	2007	Glutaredoxin (GRx), which specifically catalyzes reduction of protein-SSG mixed disulfides, reversed inhibition of p65-NFkappaB DNA binding in extracts from cells treated with hypoxia plus NAC and restored NFkappaB activity.	Disulfides	80-90	glutaredoxin	Homo sapiens	14-17
23012103-3	2013	Lysosomal cysteine protease cathepsin S (CatS) contains disulfide bonds and mediates essential steps in MHC class II-restricted processing, including proteolysis of large polypeptides and cleavage of the invariant chain.	Disulfides	56-65	cathepsin S	Felis catus	41-45
26836020-9	2016	RESULTS: ICA512-RESP18HD possesses a strong tendency to aggregate and polymerize via intermolecular disulfide formation, particularly at pH&gt;4.5.	Disulfides	100-109	protein tyrosine phosphatase, receptor type, N	Rattus norvegicus	9-15
23012103-8	2013	GILT"s reductase active site was necessary for diminished CatS protein levels, and GILT expression decreased the half-life of CatS, suggesting that GILT-mediated reduction of protein disulfide bonds enhances CatS degradation.	Disulfides	183-192	cathepsin S	Felis catus	58-62
23012103-8	2013	GILT"s reductase active site was necessary for diminished CatS protein levels, and GILT expression decreased the half-life of CatS, suggesting that GILT-mediated reduction of protein disulfide bonds enhances CatS degradation.	Disulfides	183-192	cathepsin S	Felis catus	126-130
23012103-8	2013	GILT"s reductase active site was necessary for diminished CatS protein levels, and GILT expression decreased the half-life of CatS, suggesting that GILT-mediated reduction of protein disulfide bonds enhances CatS degradation.	Disulfides	183-192	cathepsin S	Felis catus	126-130
17525470-0	2007	The disulfide loop of gp41 is critical to the furin recognition site of HIV gp160.	Disulfides	4-13	furin, paired basic amino acid cleaving enzyme	Homo sapiens	46-51
17525470-0	2007	The disulfide loop of gp41 is critical to the furin recognition site of HIV gp160.	Disulfides	4-13	glutamyl aminopeptidase	Homo sapiens	76-81
17525470-7	2007	We suggest that the mutations have altered the interaction between gp120 C5 and the gp41 disulfide loop, resulting in decreased accessibility of the furin recognition site and implying that the interaction between the gp120 C5 and gp41 loop is a conformational requirement for gp160 processing.	Disulfides	89-98	furin, paired basic amino acid cleaving enzyme	Homo sapiens	149-154
17525470-7	2007	We suggest that the mutations have altered the interaction between gp120 C5 and the gp41 disulfide loop, resulting in decreased accessibility of the furin recognition site and implying that the interaction between the gp120 C5 and gp41 loop is a conformational requirement for gp160 processing.	Disulfides	89-98	glutamyl aminopeptidase	Homo sapiens	277-282
17355969-3	2007	IL-17F is a disulfide-linked dimer that contains a cysteine-knot motif.	Disulfides	12-21	interleukin 17F	Homo sapiens	0-6
23349893-10	2013	This similarity appears to enable the GBV-C E2 N-terminus to interact with the HIV-1 gp41 disulfide loop, a crucial domain involved in the gp120-gp41 interface.	Disulfides	90-99	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	139-144
23123197-2	2012	Here, we show that NPGPx is a newly identified stress sensor that transmits oxidative stress signals by forming the disulfide bond between its Cys57 and Cys86 residues.	Disulfides	116-125	glutathione peroxidase 7	Homo sapiens	19-24
26702061-4	2016	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a beta-sandwich topology formed by 2 sheets of antiparallel beta strands stabilized by the hallmark disulfide bond between the B and F strands.	Disulfides	193-202	immunoglobulin heavy locus	Homo sapiens	41-45
23041318-0	2012	Nucleocytoplasmic coagulation: an injury-induced aggregation event that disulfide crosslinks proteins and facilitates their removal by plasmin.	Disulfides	72-81	plasminogen	Homo sapiens	135-142
17514531-14	2007	These results indicate that both disulfide bond formation and protein unfolding are responsible for GR inactivation.	Disulfides	33-42	glutathione-disulfide reductase	Homo sapiens	100-102
17488621-7	2007	AFF-1 and EFF-1 differ in their fusogenic activity and expression patterns but share eight conserved predicted disulfide bonds in their ectodomains, including a putative TGF-beta-type-I-Receptor domain.	Disulfides	111-120	Epithelial Fusion Failure	Caenorhabditis elegans	10-15
26702055-4	2016	Through employing a combination of non-reducing SDS-PAGE, electrophysiology, and mass spectrometry we have identified the formation of subunit dimers carrying a stable intersubunit disulfide bond between Cys-258 and Cys-742 of human TRPV1 (hTRPV1).	Disulfides	181-190	transient receptor potential cation channel subfamily V member 1	Homo sapiens	233-238
26702055-4	2016	Through employing a combination of non-reducing SDS-PAGE, electrophysiology, and mass spectrometry we have identified the formation of subunit dimers carrying a stable intersubunit disulfide bond between Cys-258 and Cys-742 of human TRPV1 (hTRPV1).	Disulfides	181-190	transient receptor potential cation channel subfamily V member 1	Homo sapiens	240-246
26702055-5	2016	C258S and C742S hTRPV1 mutants have a decreased protein half-life, reflecting the role of the intersubunit disulfide bond in supporting channel stability.	Disulfides	107-116	transient receptor potential cation channel subfamily V member 1	Homo sapiens	16-22
17158226-6	2007	Penumbra is targeted to the cell surface and forms disulfide-bonded homodimers.	Disulfides	51-60	tetraspanin 33	Mus musculus	0-8
22634549-3	2012	Here, we show that restriction of the flexibility of the loop by a disulfide cross-linking between cysteines within the loop results in the inefficient formation of a stable GroEL-polypeptide-GroES ternary complex and inefficient folding.	Disulfides	67-76	heat shock protein family E (Hsp10) member 1	Homo sapiens	192-197
26702055-8	2016	Our results suggest that Cys-258 residues are heterogeneously modified in the hTRPV1 tetrameric complex and comprise Cys-258 with free thiol for oxidation sensing and Cys-258, which is involved in the disulfide bond for assisting subunit dimerization.	Disulfides	201-210	transient receptor potential cation channel subfamily V member 1	Homo sapiens	78-84
26647758-6	2016	This study found that when the disulfide bonds in PDI are reduced to thiols, the reduced PDI exhibits a smaller hydrodynamic diameter than the oxided PDI.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Homo sapiens	50-53
22704541-1	2012	Factor XI (FXI), a disulfide-linked covalent homodimer, circulates in plasma, and upon activation initiates the intrinsic/consolidation phase of coagulation.	Disulfides	19-28	coagulation factor XI	Homo sapiens	0-9
22704541-1	2012	Factor XI (FXI), a disulfide-linked covalent homodimer, circulates in plasma, and upon activation initiates the intrinsic/consolidation phase of coagulation.	Disulfides	19-28	coagulation factor XI	Homo sapiens	11-14
22704541-2	2012	We present evidence that disulfide bonds in FXI are reduced to free thiols by oxidoreductases thioredoxin-1 (TRX-1) and protein disulfide isomerase (PDI).	Disulfides	25-34	coagulation factor XI	Homo sapiens	44-47
17320038-1	2007	The structure of wild-type mouse prion protein mPrP(23-231) consists of two distinctive segments with approximately equal size, a disordered and flexible N-terminal domain encompassing residues 23-124 and a largely structured C-terminal domain containing about 40% of helical structure and stabilized by one disulfide bond (Cys(178)-Cys(213)).	Disulfides	308-317	prion protein	Mus musculus	47-51
17320038-4	2007	Oxidative folding of fully reduced mutant, mPrP(6C), generates one predominant 3-disulfide isomer, designated as N-mPrP(3SS), which comprises the native disulfide (Cys(178)-Cys(213)) and two non-native disulfide bonds (Cys(36)-Cys(134) and Cys(112)-Cys(169)) that covalently connect the N- and C-domains.	Disulfides	81-90	prion protein	Mus musculus	43-47
17320038-4	2007	Oxidative folding of fully reduced mutant, mPrP(6C), generates one predominant 3-disulfide isomer, designated as N-mPrP(3SS), which comprises the native disulfide (Cys(178)-Cys(213)) and two non-native disulfide bonds (Cys(36)-Cys(134) and Cys(112)-Cys(169)) that covalently connect the N- and C-domains.	Disulfides	81-90	prion protein	Mus musculus	115-119
17320038-4	2007	Oxidative folding of fully reduced mutant, mPrP(6C), generates one predominant 3-disulfide isomer, designated as N-mPrP(3SS), which comprises the native disulfide (Cys(178)-Cys(213)) and two non-native disulfide bonds (Cys(36)-Cys(134) and Cys(112)-Cys(169)) that covalently connect the N- and C-domains.	Disulfides	153-162	prion protein	Mus musculus	43-47
17320038-4	2007	Oxidative folding of fully reduced mutant, mPrP(6C), generates one predominant 3-disulfide isomer, designated as N-mPrP(3SS), which comprises the native disulfide (Cys(178)-Cys(213)) and two non-native disulfide bonds (Cys(36)-Cys(134) and Cys(112)-Cys(169)) that covalently connect the N- and C-domains.	Disulfides	153-162	prion protein	Mus musculus	115-119
22862303-9	2012	Experiments on K19 C322A PHFs further confirm the influence of disulfide bond formation on the core structure.	Disulfides	63-72	keratin 19	Homo sapiens	15-18
26647758-6	2016	This study found that when the disulfide bonds in PDI are reduced to thiols, the reduced PDI exhibits a smaller hydrodynamic diameter than the oxided PDI.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Homo sapiens	89-92
26647758-6	2016	This study found that when the disulfide bonds in PDI are reduced to thiols, the reduced PDI exhibits a smaller hydrodynamic diameter than the oxided PDI.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Homo sapiens	89-92
22869735-6	2012	Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57-Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer.	Disulfides	80-89	copper chaperone for superoxide dismutase	Homo sapiens	116-120
22869735-6	2012	Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57-Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer.	Disulfides	145-154	copper chaperone for superoxide dismutase	Homo sapiens	116-120
22651090-3	2012	During hSOD1 maturation, disulfide formation is catalysed by CCS1 (copper chaperone for SOD1).	Disulfides	25-34	copper chaperone CCS1	Saccharomyces cerevisiae S288C	61-65
22651090-6	2012	We demonstrate that hGrx1 (human Grx1) uses a monothiol mechanism to reduce the hSOD1 disulfide, and the GSH/hGrx1 system reduces ALS mutant SOD1 at a faster rate than WT (wild-type) hSOD1.	Disulfides	86-95	glutaredoxin	Homo sapiens	20-25
22651090-6	2012	We demonstrate that hGrx1 (human Grx1) uses a monothiol mechanism to reduce the hSOD1 disulfide, and the GSH/hGrx1 system reduces ALS mutant SOD1 at a faster rate than WT (wild-type) hSOD1.	Disulfides	86-95	glutaredoxin	Homo sapiens	21-25
22481091-4	2012	These reactions generate the production of reactive oxygen species (ROS) as a byproduct of thiol/disulfide exchange reaction among ER oxidoreductin 1 (Ero1), protein disulfide isomerase (PDI) and ER client proteins, during the formation of disulfide bonds in nascent or incorrectly folded proteins.	Disulfides	97-106	prolyl 4-hydroxylase subunit beta	Homo sapiens	158-185
22481091-4	2012	These reactions generate the production of reactive oxygen species (ROS) as a byproduct of thiol/disulfide exchange reaction among ER oxidoreductin 1 (Ero1), protein disulfide isomerase (PDI) and ER client proteins, during the formation of disulfide bonds in nascent or incorrectly folded proteins.	Disulfides	97-106	prolyl 4-hydroxylase subunit beta	Homo sapiens	187-190
22481091-4	2012	These reactions generate the production of reactive oxygen species (ROS) as a byproduct of thiol/disulfide exchange reaction among ER oxidoreductin 1 (Ero1), protein disulfide isomerase (PDI) and ER client proteins, during the formation of disulfide bonds in nascent or incorrectly folded proteins.	Disulfides	166-175	prolyl 4-hydroxylase subunit beta	Homo sapiens	187-190
17306253-1	2007	Lectin-like oxidized low-density lipoprotein (LDL) receptor (LOX-1) exists as a homodimer formed by an intermolecular disulfide bond.	Disulfides	118-127	oxidized low density lipoprotein receptor 1	Homo sapiens	61-66
17372204-2	2007	Pro-HGF acquires functional competence upon cleavage between R494 and V495, generating a disulfide-linked alpha/beta-heterodimer, where the beta-chain of HGF (HGF beta) has a serine protease fold that lacks enzymatic activity.	Disulfides	89-98	hepatocyte growth factor	Homo sapiens	4-7
17372204-2	2007	Pro-HGF acquires functional competence upon cleavage between R494 and V495, generating a disulfide-linked alpha/beta-heterodimer, where the beta-chain of HGF (HGF beta) has a serine protease fold that lacks enzymatic activity.	Disulfides	89-98	hepatocyte growth factor	Homo sapiens	154-157
17372204-2	2007	Pro-HGF acquires functional competence upon cleavage between R494 and V495, generating a disulfide-linked alpha/beta-heterodimer, where the beta-chain of HGF (HGF beta) has a serine protease fold that lacks enzymatic activity.	Disulfides	89-98	hepatocyte growth factor	Homo sapiens	159-167
17444035-4	2007	The research in thioltransferase (TTase) and thioredoxin (Trx) system show TTase can specifically dithiolate protein-S-S-glutathione and restore protein free SH groups for proper enzymatic or protein functions; Trx system can dithiolate protein disulfides and thus is an extremely important regulator for redox homeostasis in the cells.	Disulfides	245-255	glutaredoxin	Homo sapiens	16-32
17444035-4	2007	The research in thioltransferase (TTase) and thioredoxin (Trx) system show TTase can specifically dithiolate protein-S-S-glutathione and restore protein free SH groups for proper enzymatic or protein functions; Trx system can dithiolate protein disulfides and thus is an extremely important regulator for redox homeostasis in the cells.	Disulfides	245-255	glutaredoxin	Homo sapiens	34-39
17444035-4	2007	The research in thioltransferase (TTase) and thioredoxin (Trx) system show TTase can specifically dithiolate protein-S-S-glutathione and restore protein free SH groups for proper enzymatic or protein functions; Trx system can dithiolate protein disulfides and thus is an extremely important regulator for redox homeostasis in the cells.	Disulfides	245-255	glutaredoxin	Homo sapiens	75-80
26601956-4	2016	Here we show that the active site Cys residues of Prx2 form stable mixed disulfides with glutathione (GSH).	Disulfides	73-83	peroxiredoxin 2	Mus musculus	50-54
17283341-0	2007	Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones.	Disulfides	0-9	heat shock protein family E (Hsp10) member 1	Homo sapiens	51-56
17283341-3	2007	Here, we have monitored topology employing disulfide bond formation of a secretory protein, trypsinogen (TG), that behaves in vitro as a stringent, GroEL-GroES-requiring substrate.	Disulfides	43-52	heat shock protein family E (Hsp10) member 1	Homo sapiens	154-159
17283341-4	2007	Inside the long-lived cis chamber formed by SR1, a single-ring version of GroEL, complexed with GroES, we observed an ordered formation of disulfide bonds.	Disulfides	139-148	heat shock protein family E (Hsp10) member 1	Homo sapiens	96-101
22609432-5	2012	In this study, we showed that, in the mouse heart, and in cultured cardiac myocytes, ATF6 induced the protein disulfide isomerase associated 6 (PDIA6) gene, which encodes an ER enzyme that catalyzes protein disulfide bond formation.	Disulfides	110-119	activating transcription factor 6	Mus musculus	85-89
22609432-5	2012	In this study, we showed that, in the mouse heart, and in cultured cardiac myocytes, ATF6 induced the protein disulfide isomerase associated 6 (PDIA6) gene, which encodes an ER enzyme that catalyzes protein disulfide bond formation.	Disulfides	110-119	protein disulfide isomerase associated 6	Mus musculus	144-149
26646753-1	2016	To develop safe and effective macromolecular MRI contrast agents, a macromolecular contrast agent (mCA) containing biocleavable disulfide bonds in the main chain and oligolysine in the side chain is prepared, and its applicability as a MRI contrast agent is demonstrated both in vitro and in vivo.	Disulfides	128-137	radial spoke head 1 homolog (Chlamydomonas)	Mus musculus	99-102
22627700-4	2012	Protein disulfide isomerase (PDI) is a member of the thioredoxin superfamily and is believed to accelerate the folding of disulfide-bonded proteins in the luminal space of the endoplasmic reticulum.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
22577146-9	2012	MMP-2 formed a homodimer through an intermolecular disulfide bond between Cys(102) and the neighboring Cys(102).	Disulfides	51-60	matrix metallopeptidase 2	Homo sapiens	0-5
17260971-8	2007	Bulk expression of fully processed, glycosylated clusterin in mammalian cells is difficult, often producing inappropriately disulfide-bonded high molecular weight aggregates; this has hampered previous studies aimed at identifying those regions of the molecule important in its chaperone action.	Disulfides	124-133	clusterin	Homo sapiens	49-58
26554721-0	2016	Inhibition of murine breast cancer growth and metastasis by survivin-targeted siRNA using disulfide cross-linked linear PEI.	Disulfides	90-99	baculoviral IAP repeat-containing 5	Mus musculus	60-68
17074504-2	2007	Here we describe a procedure utilizing isotope-coded affinity tag (ICAT) technology and mass spectrometry that quantitates relative changes in the dynamic thiol and disulfide states of human PDI.	Disulfides	165-174	prolyl 4-hydroxylase subunit beta	Homo sapiens	191-194
16962657-2	2007	To utilize a reducing microenvironment of cellular plasma membrane as a potential trigger, LbL films are assembled to contain both DNA and the TAT-based polypeptide (PTAT) with reducible disulfide bonds in the backbone.	Disulfides	187-196	tyrosine aminotransferase	Homo sapiens	143-146
17467674-0	2006	The interchain disulfide linkage is not a prerequisite but enhances CD28 costimulatory function.	Disulfides	15-24	CD28 molecule	Homo sapiens	68-72
17467674-2	2006	In this study we address the biological relevance of the disulfide-linked dimeric structure of CD28.	Disulfides	57-66	CD28 molecule	Homo sapiens	95-99
17212778-0	2006	Aberrant interchain disulfide bridge of tissue-nonspecific alkaline phosphatase with an Arg433--&gt;Cys substitution associated with severe hypophosphatasia.	Disulfides	20-29	alkaline phosphatase, biomineralization associated	Homo sapiens	40-79
17212778-4	2006	In contrast to an 80 kDa mature form of the wild-type and TNSALP(R433H), a unique disulfide-bonded 160 kDa molecular species appeared on the cell surface of the cells expressing TNSALP(R433C).	Disulfides	82-91	alkaline phosphatase, biomineralization associated	Homo sapiens	178-184
17212778-5	2006	Sucrose density gradient centrifugation demonstrated that TNSALP(R433C) forms a disulfide-bonded dimer, instead of being noncovalently assembled like the wild-type.	Disulfides	80-89	alkaline phosphatase, biomineralization associated	Homo sapiens	58-64
17212778-7	2006	Replacement of Cys102 with serine did not affect the dimerization state of TNSALP(R433C), implying that TNSALP(R433C) forms a disulfide bridge between the cysteine residues at position 433 on each subunit.	Disulfides	126-135	alkaline phosphatase, biomineralization associated	Homo sapiens	104-110
17212778-12	2006	Thus, loss of function resulting from the interchain disulfide bridge is the molecular basis for the lethal hypophosphatasia associated with TNSALP(R433C).	Disulfides	53-62	alkaline phosphatase, biomineralization associated	Homo sapiens	141-147
22593621-11	2012	Disulfide-dependent B27 H chain dimers and multimers are stronger ligands for LILRB2 than HLA class I heterotrimers and H chains.	Disulfides	0-9	leukocyte immunoglobulin like receptor B2	Homo sapiens	78-84
22671587-6	2012	Interestingly, this phosphorylation hotspot is localized in an unstructured region close to the ZO-1 binding site, and a cysteine residue which is involved in intermolecular disulfide-bond formation thus contributing to occludin dimerization.	Disulfides	174-183	occludin	Homo sapiens	220-228
21826650-3	2012	ActA and ActB consist of two disulfide-linked Inhibin (Inh)beta subunits, InhbetaA and InhbetaB, respectively.	Disulfides	29-38	actin, beta	Rattus norvegicus	9-13
22474296-2	2012	Alkyl hydroperoxide reductase Ahp1 belongs to the Prx5 subfamily and is a two-cysteine (2-Cys) Prx that forms an intermolecular disulfide bond.	Disulfides	128-137	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	30-34
22474296-8	2012	An intermolecular C(P)-C(R) disulfide bond crossing the A-type dimer interface distinguishes Ahp1 from other typical 2-Cys Prxs.	Disulfides	28-37	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	93-97
26779479-6	2015	Protein Disulfide Isomerase (PDI) is an ER chaperone induced during ER stress that is responsible for the formation of disulfide bonds in proteins.	Disulfides	119-128	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
22569138-7	2012	We have further engineered a major improvement by integrating into its chromosome a signal sequenceless disulfide bond isomerase, DsbC.	Disulfides	104-113	putative protein DsbC	Escherichia coli	130-134
22569138-8	2012	We probed the redox state of DsbC in the oxidizing cytoplasm and evaluated its role in assisting the formation of correctly folded multi-disulfide bonded proteins.	Disulfides	137-146	putative protein DsbC	Escherichia coli	29-33
17021265-6	2006	This report now shows that PKCdelta forms disulfide bonds specifically with cystine that is released from lysosomes in cultured fibroblasts and renal proximal tubule epithelial cells during apoptosis.	Disulfides	42-51	protein kinase C delta	Homo sapiens	27-35
22401853-6	2012	PDI is a converging hub for pathways of disulfide bond introduction into ER-processed proteins, via hydrogen peroxide-generating mechanisms involving the oxidase Ero1alpha, as well as hydrogen peroxide-consuming reactions involving peroxiredoxin IV and the novel peroxidases Gpx7/8.	Disulfides	40-49	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
26779479-6	2015	Protein Disulfide Isomerase (PDI) is an ER chaperone induced during ER stress that is responsible for the formation of disulfide bonds in proteins.	Disulfides	119-128	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
16787389-2	2006	We expressed the C-terminal cysteine-rich part of the human MUC5AC mucin in CHO-K1 cells (Chinese-hamster ovary K1 cells) where it formed disulfide-linked dimers in the ER (endoplasmic reticulum).	Disulfides	138-147	LOC100508689	Homo sapiens	67-72
22406321-7	2012	Similarly, a more reduced redox state of the cytosol, but not of the ER, is observed during oxidative protein folding in the ER without UPR induction, as demonstrated by overexpressing genes of disulfide bond-rich secretory proteins such as porcine trypsinogen or protein disulfide isomerase (PDI1) and ER oxidase (ERO1).	Disulfides	194-203	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	293-297
27819029-0	2016	Combining biophysical methods to analyze the disulfide bond in SH2 domain of C-terminal Src kinase.	Disulfides	45-54	C-terminal Src kinase	Homo sapiens	77-98
16849325-9	2006	Molecular modeling of hPreP based on the crystal structure at 2.1 A resolution of AtPreP allowed us to identify Cys(90) and Cys(527) that form disulfide bridges under oxidized conditions and might be involved in redox regulation of the enzyme.	Disulfides	143-152	prolyl endopeptidase	Homo sapiens	22-27
27819029-2	2016	The SH2 domain of C-terminal Src kinase (Csk) contains a single disulfide bond, which is unusual for most SH2 domains.	Disulfides	64-73	C-terminal Src kinase	Homo sapiens	18-39
27819029-2	2016	The SH2 domain of C-terminal Src kinase (Csk) contains a single disulfide bond, which is unusual for most SH2 domains.	Disulfides	64-73	C-terminal Src kinase	Homo sapiens	41-44
16880213-4	2006	When both copper pathways were blocked, wild type SOD1 stably accumulated in yeast cells with a reduced disulfide, whereas ALS SOD1 mutants A4V, G93A, and G37R were degraded.	Disulfides	104-113	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	50-54
16880213-5	2006	We describe here an unprecedented role for the thiol oxidoreductase glutaredoxin in reducing the SOD1 disulfide and destabilizing ALS mutants.	Disulfides	102-111	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	97-101
22200620-6	2012	Moreover, dimerization of the MUC1-C subunit in cancer cells was blocked by reducing agents and increased by oxidative stress, supporting involvement of the CQC motif in forming disulfide bonds.	Disulfides	178-187	mucin 1, cell surface associated	Homo sapiens	30-34
16880213-6	2006	Specifically, the major cytosolic glutaredoxin of yeast was seen to reduce the intramolecular disulfide of ALS SOD1 mutant A4V SOD1 in vivo and in vitro.	Disulfides	94-103	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	111-115
26719247-0	2015	Native Conformation and Canonical Disulfide Bond Formation Are Interlinked Properties of HIV-1 Env Glycoproteins.	Disulfides	34-43	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	95-98
16880213-6	2006	Specifically, the major cytosolic glutaredoxin of yeast was seen to reduce the intramolecular disulfide of ALS SOD1 mutant A4V SOD1 in vivo and in vitro.	Disulfides	94-103	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	127-131
16880213-7	2006	By comparison, glutaredoxin was less reactive toward the disulfide of wild type SOD1.	Disulfides	57-66	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	80-84
22142231-6	2012	CRITICAL ISSUES: The precise molecular mechanism by which a dedicated PDI family member disrupts the disulfide bonds in the misfolded ER proteins and pathogens, as well as how they act to unfold these substrates to promote their ER-to-cytosol membrane transport, remain poorly characterized.	Disulfides	101-110	prolyl 4-hydroxylase subunit beta	Homo sapiens	70-73
22142231-8	2012	What physical characteristics surrounding a substrate"s disulfide bond instruct PDI that it is mispaired or native?	Disulfides	56-65	prolyl 4-hydroxylase subunit beta	Homo sapiens	80-83
22398258-0	2012	Synthesis and evaluation of disulfide bond mimetics of amylin-(1-8) as agents to treat osteoporosis.	Disulfides	28-37	islet amyloid polypeptide	Homo sapiens	55-61
22398258-4	2012	Our own animal studies demonstrated the anabolic potential of the small but unstable octapeptide fragment of amylin-(1-37), namely amylin-(1-8) containing one disulfide bridge (Cys/2 and Cys/7) [Am.	Disulfides	159-168	islet amyloid polypeptide	Homo sapiens	109-115
22398258-4	2012	Our own animal studies demonstrated the anabolic potential of the small but unstable octapeptide fragment of amylin-(1-37), namely amylin-(1-8) containing one disulfide bridge (Cys/2 and Cys/7) [Am.	Disulfides	159-168	islet amyloid polypeptide	Homo sapiens	131-137
22398258-8	2012	Herein, we describe the synthesis of amylin-(1-8) octapeptide and seven analogues thereof wherein the disulfide bridge is modified either via insertion of different linkers or bridges of a different nature in order to improve the stability and/or bone anabolic activity of the parent peptide.	Disulfides	102-111	islet amyloid polypeptide	Homo sapiens	37-43
16876116-0	2006	Disulfide bond formation in NGR fiber-modified adenovirus is essential for retargeting to aminopeptidase N.	Disulfides	0-9	alanyl aminopeptidase, membrane	Homo sapiens	90-106
16876116-5	2006	Finally, we show evidence that disulfide bond formation within an Ad bearing the CDCNGRCFC sequence is essential for retargeting to APN, suggesting that this sequence does indeed assume a cyclic structure which facilitates NGR binding to APN.	Disulfides	31-40	alanyl aminopeptidase, membrane	Homo sapiens	132-135
16876116-5	2006	Finally, we show evidence that disulfide bond formation within an Ad bearing the CDCNGRCFC sequence is essential for retargeting to APN, suggesting that this sequence does indeed assume a cyclic structure which facilitates NGR binding to APN.	Disulfides	31-40	alanyl aminopeptidase, membrane	Homo sapiens	238-241
16849316-7	2006	We observed that a portion of peroxynitrite-induced phospho-p38alpha is associated with an approximately 85-kDa disulfide complex in wild-type MEF cells.	Disulfides	112-121	mitogen-activated protein kinase 14	Mus musculus	60-68
16849316-8	2006	Peroxynitrite-induced phosphorylation of p38alpha in the approximately 85-kDa complex is independent from MKK3/6 because only phospho-p38alpha not associated with the disulfide complex was diminished in MKK3/6 DKO cells.	Disulfides	167-176	mitogen-activated protein kinase 14	Mus musculus	41-49
26458166-6	2015	Inhibition of lysis by gp120 mAb 2G12, which binds at the base of the V3 loop, as well as disulfide mutational effects, argued that PTT-induced disruption of the gp120 disulfide cluster at the base of the V3 loop is an important step in lytic inactivation of HIV-1.	Disulfides	168-177	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	162-167
16936091-9	2006	WDNM1-like protein was cloned and confirmed as a member of the four-disulfide core family.	Disulfides	68-77	WAP four-disulfide core domain 18	Rattus norvegicus	0-5
22404596-6	2012	Subsequent folding with concomitant formation of the native disulfide bond afforded correctly folded homogeneous glycosyl-interferon-beta.	Disulfides	60-69	interferon beta 1	Homo sapiens	122-137
16507315-6	2006	We found that the ability of thioredoxin to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 Env gp120 and that thioredoxin also reduces disulfide bonds in gp120 directly in the absence of CD4.	Disulfides	158-167	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	177-182
26458166-9	2015	The dependence of lysis activity on thiol-disulfide interaction may be related to intrinsic disulfide exchange susceptibility in gp120 that has been reported previously to play a role in HIV-1 cell infection.	Disulfides	42-51	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	129-134
26458166-9	2015	The dependence of lysis activity on thiol-disulfide interaction may be related to intrinsic disulfide exchange susceptibility in gp120 that has been reported previously to play a role in HIV-1 cell infection.	Disulfides	92-101	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	129-134
22406901-10	2012	The decreased free sulfhydryl content of glycinin indicated that the oxidation of free sulfhydryls and the formation of disulfide bonds occurred when the extraction time was prolonged.	Disulfides	120-129	LOC732636	Glycine max	41-49
26459573-3	2015	The p.Gly97Arg was absent in 800 ethnically matched chromosomes and 1400 in-house exome dataset, and was located in the first of the two highly conserved disulfide bonded loop of secreted phosphoprotein 2 (Spp-24) encoded by SPP2.	Disulfides	154-163	secreted phosphoprotein 2	Danio rerio	179-204
22442221-4	2012	PPD6 is unique among the PsbP family of proteins in that it contains a conserved disulfide bond which can be reduced in vitro by thioredoxin.	Disulfides	81-90	thioredoxin H-type 1	Arabidopsis thaliana	129-140
16715370-5	2006	RESULTS: Western blotting indicated that ABCG2 was expressed as a glycosylated disulfide-linked complex in the mouse retina and in peripheral tissues, including liver, kidney, and small intestine.	Disulfides	79-88	ATP binding cassette subfamily G member 2 (Junior blood group)	Mus musculus	41-46
26459573-3	2015	The p.Gly97Arg was absent in 800 ethnically matched chromosomes and 1400 in-house exome dataset, and was located in the first of the two highly conserved disulfide bonded loop of secreted phosphoprotein 2 (Spp-24) encoded by SPP2.	Disulfides	154-163	secreted phosphoprotein 2	Danio rerio	225-229
16448670-1	2006	IL-12 is a 75 kDa heterodimer (IL12p70) comprised of independently regulated disulfide-linked 40 kDa (p40) and 35 kDa (p35) subunits.	Disulfides	77-86	interleukin 9	Homo sapiens	102-105
26278353-7	2015	Similarly, Cys-112 of GSTA1-1, which lies outside the active site and is known to form disulfides with GSH, does not react with EdAG.	Disulfides	87-97	glutathione S-transferase alpha 1	Homo sapiens	22-29
16771671-2	2006	In the major pathway, the membrane-associated flavoprotein Ero1 generates disulfide bonds for transfer to protein disulfide isomerase (PDI), which is responsible for directly introducing disulfide bonds into secretory proteins.	Disulfides	74-83	prolyl 4-hydroxylase subunit beta	Homo sapiens	106-133
22207754-0	2012	Identification of in vivo disulfide conformation of TRPA1 ion channel.	Disulfides	26-35	transient receptor potential cation channel subfamily A member 1	Homo sapiens	52-57
22207754-3	2012	Here, we present a comprehensive mass spectrometry investigation of the in vivo disulfide bonding conformation and in vitro reactivity of 30 of the 31 cysteine residues in the TRPA1 ion channel.	Disulfides	80-89	transient receptor potential cation channel subfamily A member 1	Homo sapiens	176-181
22207754-4	2012	Four disulfide bonds were detected in the in vivo TRPA1 structure: Cys-666-Cys-622, Cys-666-Cys-463, Cys-622-Cys-609, and Cys-666-Cys-193.	Disulfides	5-14	transient receptor potential cation channel subfamily A member 1	Homo sapiens	50-55
22207754-7	2012	These results indicate that the activation mechanism of TRPA1 may involve N-terminal conformation changes and disulfide bonding between critical cysteine residues.	Disulfides	110-119	transient receptor potential cation channel subfamily A member 1	Homo sapiens	56-61
22013897-9	2012	We conclude that PDI regulates thrombin-induced shedding of N60 and exposure of the TEM5 RGD motif by catalysing the reduction of crucial disulfide bonds of TEM5 on the cell surface.	Disulfides	138-147	prolyl 4-hydroxylase subunit beta	Homo sapiens	17-20
25911448-2	2015	The BPA detection probe, a recombinant protein (LacI-BPA), was constructed by fusing a disulfide-constrained high affinity BPA binding peptide (CKSLENSYC) to the C-terminus of Lac repressor (LacI).	Disulfides	87-96	tissue factor pathway inhibitor	Homo sapiens	48-52
22190736-5	2012	Through the use of a yeast expression system for apolipoprotein B (ApoB), which is disulfide rich, we discovered that Pdi1 interacts with ApoB and facilitates degradation through its chaperone activity.	Disulfides	83-92	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	118-122
22190736-6	2012	In contrast, Pdi1"s redox activity was required for the ERAD of CPY* (a misfolded version of carboxypeptidase Y that has five disulfide bonds).	Disulfides	126-135	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	13-17
22291921-4	2012	A CD4-mimetic miniprotein, miniCD4 (M64U1-SH), was produced and covalently complexed to recombinant, trimeric gp140 envelope glycoprotein (gp140) using site-specific disulfide linkages.	Disulfides	166-175	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	116-137
16605247-1	2006	Human glutaredoxin (GRx), also known as thioltransferase, is a 12 kDa thiol-disulfide oxidoreductase that is highly selective for reduction of glutathione-containing mixed disulfides.	Disulfides	172-182	glutaredoxin	Homo sapiens	6-18
16605247-1	2006	Human glutaredoxin (GRx), also known as thioltransferase, is a 12 kDa thiol-disulfide oxidoreductase that is highly selective for reduction of glutathione-containing mixed disulfides.	Disulfides	172-182	glutaredoxin	Homo sapiens	20-23
16605247-1	2006	Human glutaredoxin (GRx), also known as thioltransferase, is a 12 kDa thiol-disulfide oxidoreductase that is highly selective for reduction of glutathione-containing mixed disulfides.	Disulfides	172-182	glutaredoxin	Homo sapiens	40-56
16605247-9	2006	The effects of the mutations on the interaction energy between the adducted glutathionyl moiety and GRx were roughly estimated from the van der Waals and electrostatic energies between the glutathionyl moiety and proximal protein residues in a mixed disulfide adduct of GRx and glutathione, i.e., the GRx-SSG intermediate.	Disulfides	250-259	glutaredoxin	Homo sapiens	100-103
16608220-7	2006	Differential scanning calorimetry analysis of whole muscle samples revealed that at ambient pressure the unfolding of myosin was completed at 60 degrees C, unlike actin, which completely denatured only above 70 degrees C. With simultaneous pressure treatment at &gt;200 MPa, myosin and actin unfolded at 20 degrees C. Unfolding of myosin and actin could be induced in extracted myofibrillar protein with simultaneous treatment at 200 MPa and 40 degrees C. Electrophoretic analysis indicated high pressure/temperature regimens induced disulfide bonding between myosin chains.	Disulfides	534-543	myosin, heavy chain 15	Gallus gallus	118-124
16686937-4	2006	RESULTS: To create a disulfide bond that could increase the stability of the Drosophila melanogaster acetylcholinesterase, we selected seven positions taking into account first the distance between Cbeta of two residues, in which newly introduced cysteines will form the new disulfide bond and second the conservation of the residues in the cholinesterase family.	Disulfides	275-284	Acetylcholine esterase	Drosophila melanogaster	101-121
26203189-6	2015	Thus, our data demonstrate that the bundle of GP Ibbeta and GP IX TMDs instead of their individual CTs is the structural element that mediates the beta/IX complex localization to the membrane GEMs, which through the alpha/beta disulfide linkage brings GP Ibalpha into the GEMs.	Disulfides	227-236	glycoprotein IX platelet	Homo sapiens	60-65
16406209-6	2006	We have found that the use of 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) or dimethyl sulfoxide (DMSO) significantly improves disulfide formation and purification of highly aggregation-prone IAPP sequences.	Disulfides	123-132	islet amyloid polypeptide	Homo sapiens	188-192
16406209-9	2006	Formation of the intramolecular disulfide using DMSO was found to be the most effective method for IAPP oxidation, reducing the reaction time from 24 to 5 h. Aggregated IAPP can be resolubilized by HFIP or DMSO and recovered by HPLC with very good yield.	Disulfides	32-41	islet amyloid polypeptide	Homo sapiens	99-103
16406209-9	2006	Formation of the intramolecular disulfide using DMSO was found to be the most effective method for IAPP oxidation, reducing the reaction time from 24 to 5 h. Aggregated IAPP can be resolubilized by HFIP or DMSO and recovered by HPLC with very good yield.	Disulfides	32-41	islet amyloid polypeptide	Homo sapiens	169-173
22033478-1	2011	Tick-derived protease inhibitor (TdPI) is a tight-binding Kunitz-related inhibitor of human tryptase beta with a unique structure and disulfide-bond pattern.	Disulfides	134-143	tryptase beta 2	Homo sapiens	92-105
21968397-0	2011	A disulfide-free single-domain V(L) intrabody with blocking activity towards huntingtin reveals a novel mode of epitope recognition.	Disulfides	2-11	huntingtin	Homo sapiens	77-87
21968397-1	2011	We present the crystal structure and biophysical characterization of a human V(L) [variable domain immunoglobulin (Ig) light chain] single-domain intrabody that binds to the huntingtin (Htt) protein and has been engineered for antigen recognition in the absence of its intradomain disulfide bond, otherwise conserved in the Ig fold.	Disulfides	281-290	huntingtin	Homo sapiens	174-184
21968397-1	2011	We present the crystal structure and biophysical characterization of a human V(L) [variable domain immunoglobulin (Ig) light chain] single-domain intrabody that binds to the huntingtin (Htt) protein and has been engineered for antigen recognition in the absence of its intradomain disulfide bond, otherwise conserved in the Ig fold.	Disulfides	281-290	huntingtin	Homo sapiens	186-189
26214018-7	2015	The concept of the oxidative folding pathway was first proposed on the basis of folding and import data for the small Tim proteins that have conserved cysteine motifs and must adopt intramolecular disulfides after import so that they are retained in the organelle.	Disulfides	197-207	Rho guanine nucleotide exchange factor 5	Homo sapiens	118-121
21983541-5	2011	We have determined the crystal structure of AMIGO-1 at 2.0 A resolution, which reveals a typical cell surface LRR domain arrangement with N- and C-terminal capping domains with disulfide bridges, followed by a C2-type Ig domain.	Disulfides	177-186	adhesion molecule with Ig like domain 1	Homo sapiens	44-51
16537584-7	2006	These results suggest the existence in African swine fever virus of a system for the formation of disulfide bonds constituted at least by proteins pB119L and pA151R and identify protein pE248R as a possible final substrate of this pathway.	Disulfides	98-107	pB119L	African swine fever virus	147-153
16677073-1	2006	Disulfide bonds are formed in the endoplasmic reticulum (ER) by sequential interchange reactions: Ero1alpha and Ero1beta transfer oxidative equivalents to protein disulfide isomerase (PDI), which in turn oxidizes cargo proteins.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	155-182
16677073-1	2006	Disulfide bonds are formed in the endoplasmic reticulum (ER) by sequential interchange reactions: Ero1alpha and Ero1beta transfer oxidative equivalents to protein disulfide isomerase (PDI), which in turn oxidizes cargo proteins.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	184-187
16677074-1	2006	Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds, a process which in vivo is one of the rate limiting steps of protein folding and which is facilitated by the enzyme protein disulfide isomerase (PDI).	Disulfides	94-103	prolyl 4-hydroxylase subunit beta	Homo sapiens	227-254
16677074-1	2006	Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds, a process which in vivo is one of the rate limiting steps of protein folding and which is facilitated by the enzyme protein disulfide isomerase (PDI).	Disulfides	94-103	prolyl 4-hydroxylase subunit beta	Homo sapiens	256-259
16677077-4	2006	The formation and rearrangement of disulfide bonds is modulated by a family of enzymes known as the thiol isomerases, which include protein disulfide isomerase (PDI), ERp5, ERp57, and ERp72.	Disulfides	35-44	prolyl 4-hydroxylase subunit beta	Homo sapiens	132-159
16677077-4	2006	The formation and rearrangement of disulfide bonds is modulated by a family of enzymes known as the thiol isomerases, which include protein disulfide isomerase (PDI), ERp5, ERp57, and ERp72.	Disulfides	35-44	prolyl 4-hydroxylase subunit beta	Homo sapiens	161-164
16515838-6	2006	In addition, manipulation of endogenous levels of glutaredoxin-1 via RNAi, or overexpression resulted in altered sensitivity to H2O2 induced formation of glutathione mixed disulfides.	Disulfides	172-182	glutaredoxin	Homo sapiens	50-64
21745122-3	2011	Protein disulfide isomerase (PDI) is a member of the thioredoxin superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
21745122-3	2011	Protein disulfide isomerase (PDI) is a member of the thioredoxin superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum.	Disulfides	122-131	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
21745122-3	2011	Protein disulfide isomerase (PDI) is a member of the thioredoxin superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum.	Disulfides	122-131	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
21825095-3	2011	The only known selective blocker of ASIC1a is pi-TRTX-Pc1a (PcTx1), a disulfide-rich 40-residue peptide isolated from spider venom.	Disulfides	70-79	acid-sensing (proton-gated) ion channel 1	Mus musculus	36-42
16455490-5	2006	This is due to direct and reversible inhibition of SUMO conjugating enzymes through the formation of (a) disulfide bond(s) involving the catalytic cysteines of the SUMO E1 subunit Uba2 and the E2-conjugating enzyme Ubc9.	Disulfides	105-114	ubiquitin conjugating enzyme E2 I	Homo sapiens	215-219
26218428-5	2015	Sequence analysis of zebrafish ca10a and ca10b reveals strongly predicted signal peptides, N-glycosylation sites, and a potential disulfide, all of which are conserved, suggesting that all of CARP X and XI are secretory proteins and potentially dimeric.	Disulfides	130-139	carbonic anhydrase Xa	Danio rerio	31-36
16457775-8	2006	However, results obtained using diamide treatment to covalently link the AtAOX1a subunits by the disulfide bond indicated that Cys(I) must be in the reduced state for activation at Cys(II) to occur.	Disulfides	97-106	alternative oxidase 1A	Arabidopsis thaliana	73-80
16444599-1	2006	Our work has identified a cancer-specific, cell surface and growth-related quinol oxidase with both NADH oxidase and protein disulfide-thiol interchange activities, a member of the ECTO-NOX protein family designated tNOX.	Disulfides	125-134	tripartite motif containing 33	Homo sapiens	181-185
21936829-1	2011	SLPI (secretory leucoprotease inhibitor) and elafin represent the archetypal members of the WFDC [WAP (whey acidic protein) four disulfide core] family of proteins, and were originally characterized as protease inhibitors but have since been shown to possess a wider repertoire of activities.	Disulfides	129-138	peptidase inhibitor 3	Homo sapiens	45-51
21661057-0	2011	Mechanistic insight of photo-induced aggregation of chicken egg white lysozyme: the interplay between hydrophobic interactions and formation of intermolecular disulfide bonds.	Disulfides	159-168	lysozyme (renal amyloidosis)	Gallus gallus	60-78
26119103-4	2015	The consequences of beta1-beta2 contacts are evaluated by disulfide engineering, biophysical techniques, and cell viability assays.	Disulfides	58-67	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	26-31
25861801-18	2015	In contrast to TLR4- and TLR2-binding lipopolysaccharide used as a positive control, disulfide-HMGB1 did not stimulate proinflammatory cytokines.	Disulfides	85-94	high mobility group box 1	Homo sapiens	95-100
21540283-3	2011	Here we find that PDX1 is a direct transcriptional regulator of ER oxidoreductin-1-like beta (Ero1lbeta), which maintains the oxidative environment of the ER to facilitate disulfide bond formation.	Disulfides	172-181	pancreatic and duodenal homeobox 1	Mus musculus	18-22
16401067-14	2006	We conclude that reactivation of oxidized 1-Cys Prx by GST pi occurs by heterodimerization of 1-Cys Prx and GST pi harboring bound GSH, followed by glutathionylation of 1-Cys Prx and then formation of an intersubunit disulfide.	Disulfides	217-226	peroxiredoxin 6	Homo sapiens	42-51
16401067-15	2006	Finally, the GSH-mediated reduction of the disulfide regenerates the reduced active-site sulfhydryl of 1-Cys Prx.	Disulfides	43-52	peroxiredoxin 6	Homo sapiens	103-112
21507943-6	2011	Thus, for the first time, we demonstrated that GP Ibbeta/GP IX mediates the disulfide-linked GP Ibalpha localization to the GEMs, which is critical for vWf interaction at high shear.	Disulfides	76-85	glycoprotein IX platelet	Homo sapiens	57-62
26039939-3	2015	A proposed reaction scheme involves the peptide-channel complex stabilized by a disulfide bond formed via thiol-disulfide exchange between Cys24 of the peptide and a Cys residue at neurotoxin receptor site 8 in the pore module of the channel (specifically, Cys910 of rat NaV1.2).	Disulfides	80-89	sodium voltage-gated channel alpha subunit 2	Rattus norvegicus	271-277
21270431-7	2011	ProMBP specifically forms disulfide-mediated, covalent complexes with the metzincin metalloproteinase pregnancy-associated plasma protein A (PAPPA) and the prohormone angiotensinogen (AGT).	Disulfides	26-35	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	0-6
21270431-7	2011	ProMBP specifically forms disulfide-mediated, covalent complexes with the metzincin metalloproteinase pregnancy-associated plasma protein A (PAPPA) and the prohormone angiotensinogen (AGT).	Disulfides	26-35	pappalysin 1	Homo sapiens	141-146
16257458-0	2006	Disruption of disulfide bond formation alters the trafficking of prothyrotropin releasing hormone (proTRH)-derived peptides.	Disulfides	14-23	thyrotropin releasing hormone	Homo sapiens	99-105
16257458-3	2006	We show here that a disulfide bond in the carboxy-terminus of proTRH plays an important role in the trafficking of this prohormone.	Disulfides	20-29	thyrotropin releasing hormone	Homo sapiens	62-68
16257458-4	2006	Recombinant proTRH was observed to migrate faster on a native gel when treated with dithiothreitol (DTT) suggesting the presence of a disulfide bond.	Disulfides	134-143	thyrotropin releasing hormone	Homo sapiens	12-18
16257458-8	2006	These data suggest that the proposed disulfide bond of proTRH is involved in sorting of proTRH-derived peptides and in their retention within maturing secretory granules.	Disulfides	37-46	thyrotropin releasing hormone	Homo sapiens	55-61
16257458-8	2006	These data suggest that the proposed disulfide bond of proTRH is involved in sorting of proTRH-derived peptides and in their retention within maturing secretory granules.	Disulfides	37-46	thyrotropin releasing hormone	Homo sapiens	88-94
26039939-3	2015	A proposed reaction scheme involves the peptide-channel complex stabilized by a disulfide bond formed via thiol-disulfide exchange between Cys24 of the peptide and a Cys residue at neurotoxin receptor site 8 in the pore module of the channel (specifically, Cys910 of rat NaV1.2).	Disulfides	112-121	sodium voltage-gated channel alpha subunit 2	Rattus norvegicus	271-277
16860661-3	2006	In particular, NKG2D is a type II transmembrane-anchored glycoprotein expressed as a disulfide-linked homodimer on the surface of all mouse and human natural killer cells (NK cells).	Disulfides	85-94	killer cell lectin-like receptor subfamily K, member 1	Mus musculus	15-20
17065740-2	2006	Based on its amino acid and gene sequences data, disulfide bond (2 bonds) assignment secondary structure predictions, and chemical properties, a model for J-chain folding has been proposed.	Disulfides	49-58	joining chain of multimeric IgA and IgM	Homo sapiens	155-162
17192673-4	2006	ColQ characterizes the collagen-tailed forms (Aforms) of AChE and butyrylcholinesterase (BChE), which are localized in the basal lamina at neuromuscular junctions (NMJs) of vertebrates (Krejci et al., 1999); in these molecules (A4, A8, A12), one, two, or three tetramers of catalytic subunits are disulfide-linked to the strands of a triple helix of ColQ collagen.	Disulfides	297-306	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	0-4
21481187-7	2011	Here, we show, by MALDI-TOF/TOF MS, a direct interaction of bacitracin with PDI, involving disulfide bond formation between an open thiol form of the bacitracin thiazoline ring and cysteines in the substrate-binding domain of PDI.	Disulfides	91-100	prolyl 4-hydroxylase subunit beta	Homo sapiens	76-79
21481187-7	2011	Here, we show, by MALDI-TOF/TOF MS, a direct interaction of bacitracin with PDI, involving disulfide bond formation between an open thiol form of the bacitracin thiazoline ring and cysteines in the substrate-binding domain of PDI.	Disulfides	91-100	prolyl 4-hydroxylase subunit beta	Homo sapiens	226-229
21378161-8	2011	In a heterologous expression system, CTRP13 is secreted as a disulfide-linked oligomeric protein.	Disulfides	61-70	C1q-like 3	Mus musculus	37-43
21357685-9	2011	PDI catalyzes the reduction of the PABP disulfide bond resulting in specific binding of PABP to the insulin 5" UTR.	Disulfides	40-49	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
25529346-1	2015	Human chorionic gonadotropin (hCG) is a glycoprotein hormone that exists as a heterodimer with a alpha subunit and beta subunit assembled together with disulfide bridges.	Disulfides	152-161	glycoprotein hormones, alpha polypeptide	Homo sapiens	30-33
21428412-1	2011	The disulfides in three monoclonal antibodies (mAb), the anti-HER2, anti-CD11a, and GLP-1 with IgG4-Fc fusion protein, were completely mapped by LC-MS with the combination of electron-transfer dissociation (ETD) and collision induced dissociation (CID) fragmentation.	Disulfides	4-14	integrin subunit alpha L	Homo sapiens	73-78
21428412-1	2011	The disulfides in three monoclonal antibodies (mAb), the anti-HER2, anti-CD11a, and GLP-1 with IgG4-Fc fusion protein, were completely mapped by LC-MS with the combination of electron-transfer dissociation (ETD) and collision induced dissociation (CID) fragmentation.	Disulfides	4-14	glucagon like peptide 1 receptor	Homo sapiens	84-89
16721657-4	2006	Based on homology modeling and upon comparison of its structure with human G6PDH, it was predicted that cysteine 184 of one subunit could form a disulfide bond with cysteine 352 of the other subunit resulting in reinforced intersubunit interactions that hold the dimer together.	Disulfides	145-154	hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase	Homo sapiens	75-80
26101955-7	2015	SA suppresses both the chemoattractant activity of fully reduced HMGB1 and the increased expression of proinflammatory cytokine genes and cyclooxygenase 2 (COX-2) induced by disulfide HMGB1.	Disulfides	174-183	high mobility group box 1	Homo sapiens	184-189
16342937-13	2005	Partial disulfide bond assignment indicates that the intramolecular disulfide patterns in rat ZP1, ZP2, and ZP3 are identical to those of their corresponding mouse counterparts.	Disulfides	8-17	zona pellucida glycoprotein 1	Rattus norvegicus	94-97
21285457-8	2011	This is because cysteine-rich domain 3 (CRD3) of CD40 has a disulfide bridge in an unusual position that alters the direction of the ladder-like structure of CD40.	Disulfides	60-69	CD40 molecule	Homo sapiens	49-53
21285457-8	2011	This is because cysteine-rich domain 3 (CRD3) of CD40 has a disulfide bridge in an unusual position that alters the direction of the ladder-like structure of CD40.	Disulfides	60-69	CD40 molecule	Homo sapiens	158-162
16342937-13	2005	Partial disulfide bond assignment indicates that the intramolecular disulfide patterns in rat ZP1, ZP2, and ZP3 are identical to those of their corresponding mouse counterparts.	Disulfides	68-77	zona pellucida glycoprotein 1	Rattus norvegicus	94-97
25877331-4	2015	All the corresponding recombinant proteins form various types of covalent oligomers linked by intermolecular disulfide bonds that are reduced in vitro by the thioredoxin (TRX) and/or glutathione/glutaredoxin (GRX) systems.	Disulfides	109-118	glutaredoxin	Homo sapiens	183-207
16234242-3	2005	Activation of CuZn-SODs in eukaryotic cells occurs post-translationally and is generally dependent on the copper chaperone for SOD1 (CCS), which inserts the catalytic copper cofactor and catalyzes the oxidation of a conserved disulfide bond that is essential for activity.	Disulfides	226-235	copper chaperone for superoxide dismutase	Homo sapiens	133-136
16234242-8	2005	Our investigation of the cysteine residues that form the disulfide bond in wSOD-1 suggests that the ability of wSODs to readily form this disulfide bond may be the key to obtaining high levels of activation through the CCS-independent pathway.	Disulfides	57-66	copper chaperone for superoxide dismutase	Homo sapiens	219-222
21387408-4	2011	Disulfide formation at either of two positions (R48C/T77C or V49C/E99C) involving a specific surface loop (44-55) increased the protein melting temperature by ~5 C compared with RTA1-33/44-198 and by ~13 C compared with RTA.	Disulfides	0-9	RNA binding fox-1 homolog 2	Homo sapiens	178-181
16234242-8	2005	Our investigation of the cysteine residues that form the disulfide bond in wSOD-1 suggests that the ability of wSODs to readily form this disulfide bond may be the key to obtaining high levels of activation through the CCS-independent pathway.	Disulfides	138-147	copper chaperone for superoxide dismutase	Homo sapiens	219-222
25724691-8	2015	A mechanism has been proposed for GPx7 involving two Cys residues, in which an intramolecular disulfide of the CP is formed with an alleged resolving Cys (CR) located in the strongly conserved FPCNQ motif (C86 in humans), a noncanonical position in GPxs.	Disulfides	94-103	glutathione peroxidase 7	Homo sapiens	34-38
16316452-2	2005	Theoretical models predict that the disulfide cross-linked, N- and C-terminal domains of SP-B fold as charged amphipathic helices, and suggest that these adjacent helices participate in critical surfactant activities.	Disulfides	36-45	surfactant protein B	Homo sapiens	89-93
16260597-0	2005	Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.	Disulfides	6-15	thyroglobulin	Homo sapiens	46-59
16260597-0	2005	Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.	Disulfides	6-15	prolyl 4-hydroxylase subunit beta	Homo sapiens	121-148
16260597-1	2005	We present the first identification of transient folding intermediates of endogenous thyroglobulin (Tg; a large homodimeric secretory glycoprotein of thyrocytes), which include mixed disulfides with endogenous oxidoreductases servicing Tg folding needs.	Disulfides	183-193	thyroglobulin	Homo sapiens	85-98
16260597-1	2005	We present the first identification of transient folding intermediates of endogenous thyroglobulin (Tg; a large homodimeric secretory glycoprotein of thyrocytes), which include mixed disulfides with endogenous oxidoreductases servicing Tg folding needs.	Disulfides	183-193	thyroglobulin	Homo sapiens	100-102
16260597-2	2005	Formation of disulfide-linked Tg adducts with endoplasmic reticulum (ER) oxidoreductases begins cotranslationally.	Disulfides	13-22	thyroglobulin	Homo sapiens	30-32
16184766-1	2005	Endoplasmic reticulum (ER)p61, ERp72, and protein disulfide isomerase (PDI), which are members of the PDI family protein, are ubiquitously present in mammalian cells and are thought to participate in disulfide bond formation and isomerization.	Disulfides	50-59	prolyl 4-hydroxylase subunit beta	Homo sapiens	71-74
16184766-1	2005	Endoplasmic reticulum (ER)p61, ERp72, and protein disulfide isomerase (PDI), which are members of the PDI family protein, are ubiquitously present in mammalian cells and are thought to participate in disulfide bond formation and isomerization.	Disulfides	50-59	prolyl 4-hydroxylase subunit beta	Homo sapiens	102-105
21199866-0	2011	Conserved intramolecular disulfide bond is critical to trafficking and fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea receptor 1 (SUR1)/ABCC8.	Disulfides	25-34	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	79-99
21199866-0	2011	Conserved intramolecular disulfide bond is critical to trafficking and fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea receptor 1 (SUR1)/ABCC8.	Disulfides	25-34	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	101-104
21199866-0	2011	Conserved intramolecular disulfide bond is critical to trafficking and fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea receptor 1 (SUR1)/ABCC8.	Disulfides	25-34	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	119-124
21199866-0	2011	Conserved intramolecular disulfide bond is critical to trafficking and fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea receptor 1 (SUR1)/ABCC8.	Disulfides	25-34	ATP binding cassette subfamily C member 8	Homo sapiens	129-152
21199866-0	2011	Conserved intramolecular disulfide bond is critical to trafficking and fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea receptor 1 (SUR1)/ABCC8.	Disulfides	25-34	ATP binding cassette subfamily C member 8	Homo sapiens	154-158
21199866-0	2011	Conserved intramolecular disulfide bond is critical to trafficking and fate of ATP-binding cassette (ABC) transporters ABCB6 and sulfonylurea receptor 1 (SUR1)/ABCC8.	Disulfides	25-34	ATP binding cassette subfamily C member 8	Homo sapiens	160-165
21199866-13	2011	These results suggest that for ABC transporters the propensity to form a disulfide bond in the ER defines a unique checkpoint that determines whether a protein is ER-retained.	Disulfides	73-82	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	31-34
21143193-0	2011	Two dileucine motifs mediate late endosomal/lysosomal targeting of transmembrane protein 192 (TMEM192) and a C-terminal cysteine residue is responsible for disulfide bond formation in TMEM192 homodimers.	Disulfides	156-165	transmembrane protein 192	Homo sapiens	184-191
16184766-3	2005	We hypothesized that each PDI family protein might have different modes of enzymatic activity in disulfide bond formation and isomerization.	Disulfides	97-106	prolyl 4-hydroxylase subunit beta	Homo sapiens	26-29
25849895-4	2015	While the role of the additional N-terminal residues of HO2 is not yet understood, the HRMs have been proposed to reversibly form a thiol/disulfide redox switch that modulates the affinity of HO2 for ferric heme as a function of cellular redox poise.	Disulfides	138-147	heme oxygenase 2	Homo sapiens	192-195
16142915-11	2005	The variant, which is a poor catalyst of disulfide bond reduction and dithiol oxidation, retains virtually all of the activity of wild-type PDI in catalysis of disulfide bond isomerization.	Disulfides	160-169	prolyl 4-hydroxylase subunit beta	Homo sapiens	140-143
21143193-2	2011	Subsequently, localization in late endosomes/lysosomes has been confirmed for overexpressed and endogenous TMEM192, and homodimers of TMEM192 linked by disulfide bonds have been reported.	Disulfides	152-161	transmembrane protein 192	Homo sapiens	134-141
21143193-7	2011	Mutation of Cys266 abolished disulfide bridge formation between TMEM192 molecules, indicating that TMEM192 dimers are linked by a disulfide bridge between their C-terminal tails.	Disulfides	29-38	transmembrane protein 192	Homo sapiens	64-71
21143193-7	2011	Mutation of Cys266 abolished disulfide bridge formation between TMEM192 molecules, indicating that TMEM192 dimers are linked by a disulfide bridge between their C-terminal tails.	Disulfides	29-38	transmembrane protein 192	Homo sapiens	99-106
21143193-7	2011	Mutation of Cys266 abolished disulfide bridge formation between TMEM192 molecules, indicating that TMEM192 dimers are linked by a disulfide bridge between their C-terminal tails.	Disulfides	130-139	transmembrane protein 192	Homo sapiens	99-106
16142915-13	2005	We conclude that catalysis of disulfide bond isomerization by PDI does not necessarily involve a cycle of substrate reduction/oxidation.	Disulfides	30-39	prolyl 4-hydroxylase subunit beta	Homo sapiens	62-65
25853617-2	2015	Previous studies using the soluble form of human HO2 spanning residues 1-288 (HO2sol) have shown that a disulfide bond forms between Cys265 and Cys282 and that, in this oxidized state, heme binds to the catalytic site of HO2sol via His45.	Disulfides	104-113	heme oxygenase 2	Homo sapiens	49-52
25853617-2	2015	Previous studies using the soluble form of human HO2 spanning residues 1-288 (HO2sol) have shown that a disulfide bond forms between Cys265 and Cys282 and that, in this oxidized state, heme binds to the catalytic site of HO2sol via His45.	Disulfides	104-113	heme oxygenase 2	Homo sapiens	78-81
25770093-0	2015	A role for whey acidic protein four-disulfide-core 12 (WFDC12) in the regulation of the inflammatory response in the lung.	Disulfides	36-45	WAP four-disulfide core domain 12	Homo sapiens	55-61
16000300-8	2005	This suggests that formation of an intrachain disulfide bond is required for SPC-mediated cleavage and that SPC-mediated cleavage is essential to protein function.	Disulfides	46-55	urocortin 3	Homo sapiens	77-80
21168482-10	2011	Taken together, these findings strongly suggest that TNSALP (A116T) fails to fold properly and forms disulfide-bonded aggregates, though it is indeed capable of interacting with the wild-type and reaching the cell surface, therefore explaining its dominant transmission.	Disulfides	101-110	alkaline phosphatase, biomineralization associated	Homo sapiens	53-59
25885774-11	2015	The predictive power of MAESTRO for single point mutations and stabilizing disulfide bonds is comparable to similar methods.	Disulfides	75-84	maestro	Homo sapiens	24-31
16212239-0	2005	Reductive depolymerization of bovine thyroglobulin multimers via enzymatic reduction of protein disulfide and glutathionylated mixed disulfide linkages.	Disulfides	96-105	thyroglobulin	Bos taurus	37-50
16212239-0	2005	Reductive depolymerization of bovine thyroglobulin multimers via enzymatic reduction of protein disulfide and glutathionylated mixed disulfide linkages.	Disulfides	133-142	thyroglobulin	Bos taurus	37-50
16212239-4	2005	The PDI/GSH-induced depolymerization of the Tg multimers, which were generated from either partially unfolded Tg or partially unfolded/reduced Tg, required the simultaneous inclusion of glutathione reductase, which is capable of reducing glutathionylated mixed disulfide (PSSG).	Disulfides	261-270	prolyl 4-hydroxylase subunit beta	Bos taurus	4-7
16212239-4	2005	The PDI/GSH-induced depolymerization of the Tg multimers, which were generated from either partially unfolded Tg or partially unfolded/reduced Tg, required the simultaneous inclusion of glutathione reductase, which is capable of reducing glutathionylated mixed disulfide (PSSG).	Disulfides	261-270	glutathione-disulfide reductase	Bos taurus	186-207
16212239-7	2005	Overall, under the net GSH condition, the depolymerization of Tg multimers might be mediated by PDI, which is assisted by other reductive enzymes, and the mechanism for depolymerizing the Tg multimers differs according to the type of Tg multimer containing different degrees and types of disulfide linkages.	Disulfides	288-297	prolyl 4-hydroxylase subunit beta	Bos taurus	96-99
16102752-7	2005	Our study further revealed that both mini-PDX peptides inactivate furin in a slow tight binding manner, with disulfide-bridged cyclic form being slightly more potent.	Disulfides	109-118	furin, paired basic amino acid cleaving enzyme	Homo sapiens	66-71
21359175-4	2011	Mature ERp90 contains 10 cysteine residues, of which at least some form intramolecular disulfides.	Disulfides	87-97	thioredoxin domain containing 16	Homo sapiens	7-12
21282613-3	2011	Using a combination of biochemical and biophysical techniques both in vitro and in live cells, we show that the R9C mutation increases the stability of the PLN pentameric assembly via disulfide bridge formation, preventing its binding to Ca(2+)-ATPase as well as phosphorylation by protein kinase A.	Disulfides	184-193	phospholamban	Homo sapiens	156-159
25769921-9	2015	We conclude that HpGroES, in which a unique conformational structure, domain B, is generated by these two disulfide bonds, induces IL-8 secretion via a TLR4-dependent mechanism.	Disulfides	106-115	chemokine (C-X-C motif) ligand 15	Mus musculus	131-135
25713137-1	2015	RNase A is the prototype of an extensive family of divergent proteins whose members share a unique disulfide-bonded tertiary structure, conserved catalytic motifs, and the ability to hydrolyze polymeric RNA.	Disulfides	99-108	ribonuclease, RNase A family, 1 (pancreatic)	Mus musculus	0-7
21123168-0	2011	Thiol-disulfide redox dependence of heme binding and heme ligand switching in nuclear hormone receptor rev-erb{beta}.	Disulfides	6-15	nuclear receptor subfamily 1 group D member 2	Homo sapiens	103-115
16029046-8	2005	Alternatively, thiol-decorated (nonderivatized) micelles are prepared and show improved mucoadhesion through the formation of disulfide bonds with mucin.	Disulfides	126-135	LOC100508689	Homo sapiens	147-152
21168353-2	2011	In this study attempts have been made to develop a functional model for the catechol binding site of the human dopamine D(2) receptor, with two primary models being postulated based on the presence of a disulfide bridge in the second extracellular loop.	Disulfides	203-212	dopamine receptor D2	Homo sapiens	111-133
25793542-0	2015	Cysteine specific targeting of the functionally distinct peroxiredoxin and glutaredoxin proteins by the investigational disulfide BNP7787.	Disulfides	120-129	glutaredoxin	Homo sapiens	75-87
15893506-0	2005	Disulfide-linked dimers of human adrenaline synthesizing enzyme PNMT are catalytically active.	Disulfides	0-9	phenylethanolamine N-methyltransferase	Homo sapiens	64-68
15893506-1	2005	The crystal structure of human phenylethanolamine N-methyltransferase (hPNMT) reveals a disulfide-linked dimer, despite the presence of reducing agent in the crystallisation conditions.	Disulfides	88-97	phenylethanolamine N-methyltransferase	Homo sapiens	31-69
15893506-1	2005	The crystal structure of human phenylethanolamine N-methyltransferase (hPNMT) reveals a disulfide-linked dimer, despite the presence of reducing agent in the crystallisation conditions.	Disulfides	88-97	phenylethanolamine N-methyltransferase	Homo sapiens	71-76
21074623-6	2011	In the very recently published first monomeric structure of human cystatin C (hCC-stab1), dimerization was abrogated due to clasping of the beta-strands from the swapping domains by an engineered disulfide bridge.	Disulfides	196-205	cystatin C	Homo sapiens	66-76
21074623-6	2011	In the very recently published first monomeric structure of human cystatin C (hCC-stab1), dimerization was abrogated due to clasping of the beta-strands from the swapping domains by an engineered disulfide bridge.	Disulfides	196-205	HCC	Homo sapiens	78-81
25554517-3	2015	The Tat pathway is a promising alternative means of export, because it preferentially exports correctly folded proteins; however, the reducing cytoplasm of standard strains has been predicted to preclude export by Tat of proteins that contain disulfide bonds in the native state because, in the reduced state, they are sensed as misfolded and rejected.	Disulfides	243-252	tyrosine aminotransferase	Homo sapiens	4-7
21117647-8	2011	E3330 was also found to increase the extent of disulfide bond formation involving redox critical Cys residues in APE1 as assessed by liquid chromatography and tandem mass spectrometry, suggesting a basis for its inhibitory effects on APE1"s redox activity.	Disulfides	47-56	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	113-117
15893506-6	2005	Furthermore, the solution dimer of hPNMT incorporates disulfide bonds, since this form is sensitive to reducing agent.	Disulfides	54-63	phenylethanolamine N-methyltransferase	Homo sapiens	35-40
15893506-7	2005	The C48A and C139A mutants of hPNMT, which are incapable of forming the disulfide bond observed in the crystal structure, have a decreased propensity to form dimer in solution.	Disulfides	72-81	phenylethanolamine N-methyltransferase	Homo sapiens	30-35
25554517-3	2015	The Tat pathway is a promising alternative means of export, because it preferentially exports correctly folded proteins; however, the reducing cytoplasm of standard strains has been predicted to preclude export by Tat of proteins that contain disulfide bonds in the native state because, in the reduced state, they are sensed as misfolded and rejected.	Disulfides	243-252	tyrosine aminotransferase	Homo sapiens	214-217
25554517-4	2015	Here, we have tested a series of disulfide-bond containing biopharmaceuticals for export by the Tat pathway in CyDisCo strains that do enable disulfide bond formation in the cytoplasm.	Disulfides	33-42	tyrosine aminotransferase	Homo sapiens	96-99
15820220-7	2005	In contrast, the TAP counterpart (Cys5-Cys15, Cys33-Cys55, Cys39-Cys59) represents only 5% of the total TAP intermediates; (b) three isomers of TAP sharing a stable non-native disulfide bond Cys15-Cys33 are shown to act as kinetic traps of TAP folding.	Disulfides	176-185	tracheal antimicrobial peptide	Bos taurus	17-20
25554517-4	2015	Here, we have tested a series of disulfide-bond containing biopharmaceuticals for export by the Tat pathway in CyDisCo strains that do enable disulfide bond formation in the cytoplasm.	Disulfides	142-151	tyrosine aminotransferase	Homo sapiens	96-99
15829265-1	2005	We recently showed that oligomerization of CD40 molecules on cell surface leads to disulfide-linked CD40/CD40 dimer formation, an event that is necessary for CD40-induced B7-2 expression in human B cells.	Disulfides	83-92	CD40 molecule	Homo sapiens	43-47
21875564-2	2011	PDI has multiple roles, acting as a chaperone, a binding partner of other proteins, and a hormone reservoir as well as a disulfide isomerase in the formation of disulfide bonds.	Disulfides	121-130	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
15829265-1	2005	We recently showed that oligomerization of CD40 molecules on cell surface leads to disulfide-linked CD40/CD40 dimer formation, an event that is necessary for CD40-induced B7-2 expression in human B cells.	Disulfides	83-92	CD40 molecule	Homo sapiens	100-104
25554517-5	2015	We show that interferon alpha2b, human growth hormone (hGH) and two antibody fragments are exported with high efficiency; surprisingly, however, they are efficiently exported even in the absence of cytoplasmic disulfide formation.	Disulfides	210-219	interferon alpha 2	Homo sapiens	13-31
15829265-1	2005	We recently showed that oligomerization of CD40 molecules on cell surface leads to disulfide-linked CD40/CD40 dimer formation, an event that is necessary for CD40-induced B7-2 expression in human B cells.	Disulfides	83-92	CD40 molecule	Homo sapiens	100-104
15829265-1	2005	We recently showed that oligomerization of CD40 molecules on cell surface leads to disulfide-linked CD40/CD40 dimer formation, an event that is necessary for CD40-induced B7-2 expression in human B cells.	Disulfides	83-92	CD40 molecule	Homo sapiens	100-104
15829265-3	2005	Disulfide bonds mediate the formation of CD40/CD40 homodimers in CD40-activated cells.	Disulfides	0-9	CD40 molecule	Homo sapiens	41-45
15829265-3	2005	Disulfide bonds mediate the formation of CD40/CD40 homodimers in CD40-activated cells.	Disulfides	0-9	CD40 molecule	Homo sapiens	46-50
15829265-3	2005	Disulfide bonds mediate the formation of CD40/CD40 homodimers in CD40-activated cells.	Disulfides	0-9	CD40 molecule	Homo sapiens	46-50
15829265-6	2005	In contrast to cells expressing CD40-WT protein, disulfide-linked CD40/CD40 dimer formation was completely abolished in HEK 293 cells expressing CD40-C6Q proteins.	Disulfides	49-58	CD40 molecule	Homo sapiens	66-70
15829265-6	2005	In contrast to cells expressing CD40-WT protein, disulfide-linked CD40/CD40 dimer formation was completely abolished in HEK 293 cells expressing CD40-C6Q proteins.	Disulfides	49-58	CD40 molecule	Homo sapiens	66-70
15829265-6	2005	In contrast to cells expressing CD40-WT protein, disulfide-linked CD40/CD40 dimer formation was completely abolished in HEK 293 cells expressing CD40-C6Q proteins.	Disulfides	49-58	CD40 molecule	Homo sapiens	66-70
15829265-7	2005	Abolishment of disulfide-linked CD40/CD40 dimers in these transfected cells was sufficient to inhibit CD40-induced mRNA expression and secretion of IL-8.	Disulfides	15-24	CD40 molecule	Homo sapiens	32-36
15829265-7	2005	Abolishment of disulfide-linked CD40/CD40 dimers in these transfected cells was sufficient to inhibit CD40-induced mRNA expression and secretion of IL-8.	Disulfides	15-24	CD40 molecule	Homo sapiens	37-41
15829265-7	2005	Abolishment of disulfide-linked CD40/CD40 dimers in these transfected cells was sufficient to inhibit CD40-induced mRNA expression and secretion of IL-8.	Disulfides	15-24	CD40 molecule	Homo sapiens	37-41
20880254-5	2011	FXIII-B is a glycoprotein consisting of 10 repetitive sushi domains each held together by two internal disulfide bonds.	Disulfides	103-112	coagulation factor XIII B chain	Homo sapiens	0-7
25554517-7	2015	Tat-dependent export of hGH proceeds even when the disulfide bonds are removed by substitution of the Cys residues involved, suggesting that these substrates adopt tertiary structures that are accepted as fully-folded by the Tat machinery.	Disulfides	51-60	tyrosine aminotransferase	Homo sapiens	0-3
21278127-2	2011	Protein disulfide isomerase (PDI) family oxidoreductase PDIL2;3, an ortholog of human P5, contains a conserved structural disulfide in the redox-inactive thioredoxin-like (TRX) domain and was efficiently targeted to the surface of PB-I in a redox active site-dependent manner, whereas PDIL1;1, an ortholog of human PDI, was localized in the ER lumen.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
21278127-2	2011	Protein disulfide isomerase (PDI) family oxidoreductase PDIL2;3, an ortholog of human P5, contains a conserved structural disulfide in the redox-inactive thioredoxin-like (TRX) domain and was efficiently targeted to the surface of PB-I in a redox active site-dependent manner, whereas PDIL1;1, an ortholog of human PDI, was localized in the ER lumen.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	56-59
25678063-1	2015	During thermal treatment of soymilk, a rapid incorporation of Kunitz trypsin inhibitor (KTI) into protein aggregates by covalent (disulfide bond, SS) and/or noncovalent interactions with other proteins is responsible for its fast inactivation of trypsin inhibitor activity (TIA).	Disulfides	130-139	cysteine rich secretory protein LCCL domain containing 2	Homo sapiens	69-86
22140547-8	2011	We also showed that both endogenous and secreted GOLPH2 exist as a disulfide-bonded dimer, and the coiled-coil domain was sufficient for dimerization.	Disulfides	67-76	golgi membrane protein 1	Homo sapiens	49-55
15743766-0	2005	Disulfide linkage controls the affinity and stoichiometry of IgE Fcepsilon3-4 binding to FcepsilonRI.	Disulfides	0-9	Fc epsilon receptor Ia	Homo sapiens	89-100
25717100-6	2015	Targeting mucin disulfide cross-links using current thiol-amino structures such as N-acetylcysteine (NAC) requires high drug concentrations to have mucolytic effects.	Disulfides	16-25	LOC100508689	Homo sapiens	10-15
15695509-1	2005	Disulfide bonds and protein-protein interactions in the MAM and TRAF domains.	Disulfides	0-9	sarcoglycan gamma	Homo sapiens	56-59
15695509-5	2005	Three symmetrical intersubunit disulfide bonds were identified in the noncatalytic interaction domains; two in the MAM (meprin, A-5 protein, protein-tyrosine phosphatase mu) domain and one in the TRAF (tumor necrosis factor receptor-associated factor) domain.	Disulfides	31-40	sarcoglycan gamma	Homo sapiens	115-118
20880849-7	2010	The structure also explains a requirement for the Cys(105)-Cys(137) disulfide bond in CRT/CNX for efficient carbohydrate binding.	Disulfides	68-77	calnexin	Homo sapiens	90-93
25595776-1	2015	Endoplasmic reticulum disulfide oxidase ERO1-alpha plays a role in the formation of disulfide bonds in collaboration with protein disulfide isomerase.	Disulfides	22-31	endoplasmic reticulum oxidoreductase 1 alpha	Mus musculus	40-50
21087088-8	2010	In summary, these observations provide a model of how phosphorylation, a disulfide bridge and proteolytic cleavage are involved in HDGF secretion.	Disulfides	73-82	heparin binding growth factor	Homo sapiens	131-135
15695509-9	2005	The MAM domain also had one intradomain disulfide bond and one free cysteine.	Disulfides	40-49	sarcoglycan gamma	Homo sapiens	4-7
16511065-2	2005	Five glutaredoxin genes have been identified in Saccharomyces cerevisiae; however, Grx2 is responsible for the majority of oxidoreductase activity in the cell, suggesting that its primary function may be the detoxification of mixed disulfides generated by reactive oxygen species (ROS).	Disulfides	232-242	dithiol glutaredoxin GRX2	Saccharomyces cerevisiae S288C	83-87
15647258-0	2005	Proteinase inhibition by proform of eosinophil major basic protein (pro-MBP) is a multistep process of intra- and intermolecular disulfide rearrangements.	Disulfides	129-138	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	36-66
20615094-2	2010	The spp24 BMP-2-binding/transforming growth factor receptor II homology-1 (TRH1) domain is a highly conserved N-to-C terminally disulfide-bonded 19-amino acid residue loop similar to those in fetuin and the BMP receptor II.	Disulfides	128-137	secreted phosphoprotein 2	Bos taurus	4-9
25595776-8	2015	In addition, production of G-CSF and CXCL1/2, which have intramolecular disulfide bonds, from KD cells was significantly decreased compared with that from SCR cells.	Disulfides	72-81	peripheral blood stem cell response to granulocyte colony stimulating factor 1	Mus musculus	27-32
15647258-0	2005	Proteinase inhibition by proform of eosinophil major basic protein (pro-MBP) is a multistep process of intra- and intermolecular disulfide rearrangements.	Disulfides	129-138	myelin basic protein	Homo sapiens	72-75
15647258-2	2005	The proteolytic activity of PAPP-A is inhibited by the proform of eosinophil major basic protein (pro-MBP), which forms a covalent 2:2 proteinase-inhibitor complex based on disulfide bonds.	Disulfides	173-182	pappalysin 1	Homo sapiens	28-34
25595776-8	2015	In addition, production of G-CSF and CXCL1/2, which have intramolecular disulfide bonds, from KD cells was significantly decreased compared with that from SCR cells.	Disulfides	72-81	chemokine (C-X-C motif) ligand 12	Mus musculus	37-44
15647258-2	2005	The proteolytic activity of PAPP-A is inhibited by the proform of eosinophil major basic protein (pro-MBP), which forms a covalent 2:2 proteinase-inhibitor complex based on disulfide bonds.	Disulfides	173-182	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	66-96
15647258-2	2005	The proteolytic activity of PAPP-A is inhibited by the proform of eosinophil major basic protein (pro-MBP), which forms a covalent 2:2 proteinase-inhibitor complex based on disulfide bonds.	Disulfides	173-182	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	98-105
15647258-2	2005	The proteolytic activity of PAPP-A is inhibited by the proform of eosinophil major basic protein (pro-MBP), which forms a covalent 2:2 proteinase-inhibitor complex based on disulfide bonds.	Disulfides	173-182	endogenous retrovirus group K member 18	Homo sapiens	135-145
15647258-4	2005	A comparison of the disulfide structure of the reactants with the known disulfide structure of the PAPP-A.pro-MBP complex reveals that six cysteine residues of the pro-MBP subunit (Cys-51, Cys-89, Cys-104, Cys-107, Cys-128, and Cys-169) and two cysteine residues of the PAPP-A subunit (Cys-381 and Cys-652) change their status from the uncomplexed to the complexed states.	Disulfides	72-81	pappalysin 1	Homo sapiens	99-105
15647258-4	2005	A comparison of the disulfide structure of the reactants with the known disulfide structure of the PAPP-A.pro-MBP complex reveals that six cysteine residues of the pro-MBP subunit (Cys-51, Cys-89, Cys-104, Cys-107, Cys-128, and Cys-169) and two cysteine residues of the PAPP-A subunit (Cys-381 and Cys-652) change their status from the uncomplexed to the complexed states.	Disulfides	72-81	myelin basic protein	Homo sapiens	110-113
15647258-4	2005	A comparison of the disulfide structure of the reactants with the known disulfide structure of the PAPP-A.pro-MBP complex reveals that six cysteine residues of the pro-MBP subunit (Cys-51, Cys-89, Cys-104, Cys-107, Cys-128, and Cys-169) and two cysteine residues of the PAPP-A subunit (Cys-381 and Cys-652) change their status from the uncomplexed to the complexed states.	Disulfides	72-81	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	106-113
15647258-5	2005	Upon complex formation, three disulfide bonds of pro-MBP, which connect the acidic propiece with the basic, mature portion, are disrupted.	Disulfides	30-39	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	49-56
15647258-6	2005	In the PAPP-A.pro-MBP complex, two of these form the basis of both two interchain disulfide bonds between the PAPP-A and the pro-MBP subunits and two disulfide bonds responsible for pro-MBP dimerization, respectively.	Disulfides	82-91	pappalysin 1	Homo sapiens	7-13
15647258-6	2005	In the PAPP-A.pro-MBP complex, two of these form the basis of both two interchain disulfide bonds between the PAPP-A and the pro-MBP subunits and two disulfide bonds responsible for pro-MBP dimerization, respectively.	Disulfides	82-91	myelin basic protein	Homo sapiens	18-21
15647258-6	2005	In the PAPP-A.pro-MBP complex, two of these form the basis of both two interchain disulfide bonds between the PAPP-A and the pro-MBP subunits and two disulfide bonds responsible for pro-MBP dimerization, respectively.	Disulfides	82-91	pappalysin 1	Homo sapiens	110-116
21174348-4	2010	The ayu hepcidin mature peptide sequence contained 25 amino acids with eight cysteines that formed four disulfide bonds.	Disulfides	104-113	hepcidin	Salmo salar	8-16
21059944-4	2010	The disulfide bond (C125-C127) at the tip of Loop3 is important for determining the unique topology of Loop3, and docking E126 close to RANKL, which was supported by the inability of C127A or E126A mutants of RANK to bind to RANKL.	Disulfides	4-13	TNF receptor superfamily member 11a	Homo sapiens	136-140
25604073-8	2015	Oxidation induced cross-linking via disulfide bonds hindered the unfolding of rod, particularly in PM myosin.	Disulfides	36-45	myosin, heavy chain 15	Gallus gallus	102-108
21045303-10	2010	The preliminary electron-density map shows a large conformational change of the C-terminal domain of NDPK-A induced by a novel disulfide bond that is formed under oxidative conditions.	Disulfides	127-136	NME/NM23 nucleoside diphosphate kinase 1	Homo sapiens	101-107
15736974-0	2005	Diversity of human insulin-like growth factor (IGF) binding protein-2 fragments in plasma: primary structure, IGF-binding properties, and disulfide bonding pattern.	Disulfides	138-147	insulin like growth factor binding protein 2	Homo sapiens	19-69
15466936-1	2005	Formation and rearrangement of disulfide bonds during the correct folding of nascent proteins is modulated by a family of enzymes known as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERP5), and ERP57.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Homo sapiens	171-198
15466936-1	2005	Formation and rearrangement of disulfide bonds during the correct folding of nascent proteins is modulated by a family of enzymes known as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERP5), and ERP57.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Homo sapiens	200-203
26075280-4	2015	Herein, the hydrophobic ADR was successfully linked to the biocompatible human serum albumin (HSA) by disulfide bond 3-(2-pyridyldithio) propionyl hydrazide (PDPH), resulting in amphiphilic HSA-ADR.	Disulfides	102-111	albumin	Mus musculus	79-92
15665090-2	2005	In the present study, we found that the GWD enzyme is inactive in the oxidized form, which is accompanied by the formation of a specific intramolecular disulfide bond as determined by disulfide-linked peptide mapping.	Disulfides	152-161	alpha-glucan water dikinase, chloroplastic	Solanum tuberosum	40-43
15665090-2	2005	In the present study, we found that the GWD enzyme is inactive in the oxidized form, which is accompanied by the formation of a specific intramolecular disulfide bond as determined by disulfide-linked peptide mapping.	Disulfides	184-193	alpha-glucan water dikinase, chloroplastic	Solanum tuberosum	40-43
20935509-7	2010	Moreover, the intramolecular disulfide bridge (C23/45) of HMGB1 is required for binding to Beclin 1 and sustaining autophagy.	Disulfides	29-38	high mobility group box 1	Homo sapiens	58-63
20657012-0	2010	The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1alpha.	Disulfides	43-53	prolyl 4-hydroxylase subunit beta	Homo sapiens	63-90
24911456-12	2015	These studies are the first to demonstrate that lung cancer chemotherapy agents increase procoagulant activity on endothelial cells and A549 cells by tissue factor decryption through a disulfide bond formation in a PDI-dependent mechanism.	Disulfides	185-194	prolyl 4-hydroxylase subunit beta	Homo sapiens	215-218
20657012-1	2010	Disulfide formation in newly synthesized proteins entering the mammalian endoplasmic reticulum is catalyzed by protein disulfide isomerase (PDI), which is itself thought to be directly oxidized by Ero1alpha.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	111-138
20657012-1	2010	Disulfide formation in newly synthesized proteins entering the mammalian endoplasmic reticulum is catalyzed by protein disulfide isomerase (PDI), which is itself thought to be directly oxidized by Ero1alpha.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	140-143
20657012-7	2010	These results demonstrate that the specificity of Ero1alpha toward the active sites of PDI requires the presence of the regulatory disulfides.	Disulfides	131-141	prolyl 4-hydroxylase subunit beta	Homo sapiens	87-90
20657012-8	2010	In addition, the rate of PDI oxidation is limited by the reduction potential of the PDI active site disulfide.	Disulfides	100-109	prolyl 4-hydroxylase subunit beta	Homo sapiens	25-28
20657012-8	2010	In addition, the rate of PDI oxidation is limited by the reduction potential of the PDI active site disulfide.	Disulfides	100-109	prolyl 4-hydroxylase subunit beta	Homo sapiens	84-87
20657012-9	2010	The inability of Ero1alpha to oxidize PDI efficiently likely reflects the requirement for PDI to act as both an oxidase and an isomerase during the formation of native disulfides in proteins entering the secretory pathway.	Disulfides	168-178	prolyl 4-hydroxylase subunit beta	Homo sapiens	90-93
20599662-8	2010	Alkylation of cysteine residues in C terminus of PrP121-231, which breaks a disulfide bond and disrupts the structure, had diminished the reactivity.	Disulfides	76-85	prion protein	Mus musculus	49-52
15711751-2	2005	Pm-VEGF, a novel member ofVEGF family from the venom gland of Taiwan habu (Protobothrops mucrosquamatu), is a disulfide-linked homodimer with 119 amino acid residues.	Disulfides	110-119	vascular endothelial growth factor A	Gallus gallus	3-7
15475357-1	2005	Protein disulfide isomerase (PDI) is the archetypal enzyme involved in the formation and reshuffling of disulfide bonds in the endoplasmic reticulum (ER).	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
16333982-2	2005	ERp72, a protein disulfide isomerase (PDI) family member, possesses 3 thioredoxin homology domains, but the participation of each domain in disulfide-bond formation and isomerization remains to be determined.	Disulfides	17-26	prolyl 4-hydroxylase subunit beta	Homo sapiens	38-41
15501515-1	2004	Granulysin is a disulfide rich 9 kDa human tumoricidal protein produced by cytolytic cells.	Disulfides	16-25	granulysin	Homo sapiens	0-10
25561977-5	2015	Immunoblots showed early, intense and transient presence of IL-1beta, IFN-gamma, and both the all-thiol and disulfide forms of HMGB1 in the NTAT of non-tumor bearing mice.	Disulfides	108-117	high mobility group box 1	Mus musculus	127-132
20819940-7	2010	Moreover, the intramolecular disulfide bridge (C23/45) of HMGB1 is required for binding to Beclin1 and sustaining autophagy.	Disulfides	29-38	high mobility group box 1	Homo sapiens	58-63
25434589-3	2015	Prokineticins (PKs), which include PK1 and PK2, represent a novel family of chemokines characterized by a unique structural motif comprising five disulfide bonds.	Disulfides	146-155	prokineticin 2	Mus musculus	43-46
20399532-6	2010	Redox titrations demonstrated that the four conserved cysteines of each CP12 isoform could form two internal disulfide bridges with different midpoint redox potentials (E(m,7.9) -326 mV and -350 mV in both CP12-1 and CP12-2; E(m,7.9) -332 mV and -373 mV in CP12-3).	Disulfides	109-118	CP12 domain-containing protein 1	Arabidopsis thaliana	206-212
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	377-386	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	38-43
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	377-386	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	169-174
20538591-6	2010	We show that 2dCD4-S60C binds HIV-1 gp120 with a significantly higher affinity than wild-type protein under conditions that facilitate disulfide exchange and that this translates into a corresponding increase in the efficacy of CD4-mediated viral entry inhibition.	Disulfides	135-144	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	36-41
20538591-7	2010	We propose that targeted redox exchange between conserved gp120 disulfides and nucleophilic moieties positioned strategically on CD4 (or CD4-like scaffolds) conceptualizes a new strategy in the development of high affinity HIV-1 Env ligands, with important implications for therapy and vaccine development.	Disulfides	64-74	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	58-63
20538591-7	2010	We propose that targeted redox exchange between conserved gp120 disulfides and nucleophilic moieties positioned strategically on CD4 (or CD4-like scaffolds) conceptualizes a new strategy in the development of high affinity HIV-1 Env ligands, with important implications for therapy and vaccine development.	Disulfides	64-74	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	229-232
25218089-1	2014	Glutaredoxin (Grx) is a major redox enzyme that reduces disulfide bonds using glutathione (GSH) as an electron donor.	Disulfides	56-65	glutaredoxin	Homo sapiens	0-12
20507993-5	2010	Upon oxidative folding of equimolar amounts of the alpha1, alpha2, and alpha3 chains of NC2, a stable heterotrimer with a disulfide bridge between alpha1 and alpha3 chains is formed.	Disulfides	122-131	down-regulator of transcription 1	Homo sapiens	88-91
25218089-1	2014	Glutaredoxin (Grx) is a major redox enzyme that reduces disulfide bonds using glutathione (GSH) as an electron donor.	Disulfides	56-65	glutaredoxin	Homo sapiens	14-17
24968724-7	2014	Mia40 was in the oxidized, functional state, while SOD1 disulfide bond formation was promoted by increasing the level of the SOD1 chaperone, CCS, in the IMS.	Disulfides	56-65	copper chaperone for superoxide dismutase	Homo sapiens	141-144
24094148-5	2014	Conversely, the disulfide-containing form of HMGB1 dose dependently enhanced NMDA-induced Ca(2+) increase in neuronal cell bodies.	Disulfides	16-25	high mobility group box 1	Mus musculus	45-50
20603018-5	2010	Introducing two long-range disulfide bonds into DM-MBP reduces the entropic folding barrier of this intermediate and strongly accelerates native state formation.	Disulfides	27-36	myelin basic protein	Homo sapiens	51-54
24094148-8	2014	Disulfide HMGB1 effect on NMDA-induced Ca(2+) influx was prevented by 3-O-methylsphingomyelin (3-O-MS) and 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo [3,4-d] pyrimidine, (PP2) selective inhibitors of neutral sphingomyelinase and Src-family Tyr kinases, respectively.	Disulfides	0-9	high mobility group box 1	Mus musculus	10-15
24094148-9	2014	Disulfide HMGB1, but not 3S-HMGB1, increased Tyr(1472) phosphorylation of the NR2B subunit of the NMDAR, which is known to increase Ca(2+) channel permeability.	Disulfides	0-9	high mobility group box 1	Mus musculus	10-15
20417731-1	2010	Yeast glutaredoxins Grx1 and Grx2 catalyze the reduction of both inter- and intra-molecular disulfide bonds using glutathione (GSH) as the electron donor.	Disulfides	92-101	glutaredoxin	Homo sapiens	20-24
24094148-10	2014	Similarly, disulfide HMGB1 increased NMDA-induced neuronal cell death in vitro and enhanced kainate-induced seizures in vivo.	Disulfides	11-20	high mobility group box 1	Mus musculus	21-26
25122773-10	2014	These results indicate that BPA, a widely distributed and potentially harmful chemical, inhibits Ero1-PDI-mediated disulfide bond formation.	Disulfides	115-124	prolyl 4-hydroxylase subunit beta	Homo sapiens	102-105
20427280-4	2010	Here we describe a thiol/disulfide redox switch in the human BK channel and biochemical experiments of heme, CO, and HO2 binding to a 134-residue region within the cytoplasmic domain of the channel.	Disulfides	25-34	heme oxygenase 2	Homo sapiens	117-120
24920800-6	2014	In the context of cell surface-expressed JRFL Env, introduction of a previously reported additional disulfide between residues A501 and T605 perturbs the native conformation, though this effect is partially alleviated by furin coexpression.	Disulfides	100-109	furin, paired basic amino acid cleaving enzyme	Homo sapiens	221-226
20348090-7	2010	In particular, the amino-terminal domain of Pdi1p preferentially formed mixed disulfides with Ero1p in vivo, and we observed synthetic lethality between a temperature-sensitive Ero1p variant and mutant Pdi1p lacking the amino-terminal active-site disulfide.	Disulfides	78-87	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	44-49
24905701-11	2014	The recombinant HMGB1 utilized in this study shows properties that are similar to disulfide-HMGB1.	Disulfides	82-91	high mobility group box 1	Homo sapiens	16-21
24905701-11	2014	The recombinant HMGB1 utilized in this study shows properties that are similar to disulfide-HMGB1.	Disulfides	82-91	high mobility group box 1	Homo sapiens	92-97
24863694-2	2014	The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress.	Disulfides	126-136	glutaredoxin	Homo sapiens	26-38
24894009-7	2014	Inhibiting the formation of CD40 disulfide-bound-homodimers, a process required for some CD40 signaling, further enhances Rituximab-induced cell death.	Disulfides	33-42	CD40 molecule	Homo sapiens	28-32
24894009-7	2014	Inhibiting the formation of CD40 disulfide-bound-homodimers, a process required for some CD40 signaling, further enhances Rituximab-induced cell death.	Disulfides	33-42	CD40 molecule	Homo sapiens	89-93
24758166-1	2014	Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as PDI (protein disulfide-isomerase) and a mechanism to form disulfides de novo.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	121-124
24758166-1	2014	Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as PDI (protein disulfide-isomerase) and a mechanism to form disulfides de novo.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	126-153
24758166-1	2014	Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as PDI (protein disulfide-isomerase) and a mechanism to form disulfides de novo.	Disulfides	86-95	prolyl 4-hydroxylase subunit beta	Homo sapiens	121-124
24758166-1	2014	Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as PDI (protein disulfide-isomerase) and a mechanism to form disulfides de novo.	Disulfides	86-95	prolyl 4-hydroxylase subunit beta	Homo sapiens	126-153
24758166-1	2014	Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as PDI (protein disulfide-isomerase) and a mechanism to form disulfides de novo.	Disulfides	179-189	prolyl 4-hydroxylase subunit beta	Homo sapiens	121-124
24758166-1	2014	Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as PDI (protein disulfide-isomerase) and a mechanism to form disulfides de novo.	Disulfides	179-189	prolyl 4-hydroxylase subunit beta	Homo sapiens	126-153
24758166-8	2014	Further studies showed that both active sites of PDI contribute to the formation of regulatory disulfides in Ero1alpha and that the PDI substrate-binding domain is crucial to allow electron transfer between the two enzymes.	Disulfides	95-105	prolyl 4-hydroxylase subunit beta	Homo sapiens	49-52
24515870-2	2014	Here, we surprisingly found that a fraction of KLRG1 molecules expressed in the murine A5 T-cell line and in IL-2-activated NK cells forms disulfide-linked heteromers with the transferrin receptor (TfR).	Disulfides	139-148	transferrin receptor	Mus musculus	198-201
24855952-0	2014	Interaction of circadian clock proteins CRY1 and PER2 is modulated by zinc binding and disulfide bond formation.	Disulfides	87-96	clock circadian regulator	Homo sapiens	25-30
24634211-1	2014	We report a new function for Escherichia coli DsbC, a protein best known for disulfide bond isomerization in the periplasm.	Disulfides	77-86	putative protein DsbC	Escherichia coli	46-50
24634211-4	2014	DsbC, unlike the homologous protein DsbG, reduces the intermolecular disulfide, restoring AraF binding properties.	Disulfides	69-78	putative protein DsbC	Escherichia coli	0-4
24954595-7	2014	Functional assay showed that the full-length of SlVKOR with Trx-like domain without the transit peptide could catalyze the formation of disulfide bonds.	Disulfides	136-145	vitamin K epoxide reductase	Solanum lycopersicum	48-54
24616105-7	2014	An unexpected disulfide bond between Cys-230 and Cys-267 is crucial for the selective binding of Alkbh5 to single-stranded RNA/DNA by bringing a "flipping" motif toward the central beta-helix fold.	Disulfides	14-23	alkB homolog 5, RNA demethylase	Homo sapiens	97-103
24497506-7	2014	The susceptibility of rNaV1.2 to GVIIJSSG was significantly altered by treating the channels with thiol-oxidizing or disulfide-reducing agents.	Disulfides	117-126	sodium voltage-gated channel alpha subunit 2	Rattus norvegicus	22-29
24338014-5	2014	From the crystal structure of plasminogen, we propose that plasmin ligands such as phosphoglycerate kinase induce a conformational change in reduced kringle 5 that leads to attack by the Cys(541) thiolate anion on the Cys(536) sulfur atom of the Cys(512)-Cys(536) disulfide bond, resulting in reduction of the bond by thiol/disulfide exchange.	Disulfides	264-273	plasminogen	Homo sapiens	30-37
24338014-5	2014	From the crystal structure of plasminogen, we propose that plasmin ligands such as phosphoglycerate kinase induce a conformational change in reduced kringle 5 that leads to attack by the Cys(541) thiolate anion on the Cys(536) sulfur atom of the Cys(512)-Cys(536) disulfide bond, resulting in reduction of the bond by thiol/disulfide exchange.	Disulfides	324-333	plasminogen	Homo sapiens	30-37
24397493-6	2014	Molecular dynamics trajectories of the VanA ligase of Enterococcus faecium with or without a disulfide bridge distant from the catalytic site revealed differences in the catalytic site conformations with a slight opening.	Disulfides	93-102	Vancomycin Teicoplanin A-type resistance protein VanA / D-alanine--D-alanine ligase	Enterococcus faecium	39-43
24216109-5	2014	Cytochrome c6A from Arabidopsis thaliana was identified as a protein responsible for disulfide bond formation in response to intracellular redox state changes and c550 is well known element of photosystem II.	Disulfides	85-94	Cytochrome c	Arabidopsis thaliana	0-14
24465374-1	2014	In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (oxidative folding).	Disulfides	91-100	prolyl 4-hydroxylase subunit beta	Homo sapiens	112-115
24041990-1	2014	BACKGROUND: Glutaredoxin 1 (Grx1), a small protein belonging to the thioredoxin family, is involved in redox-regulation since it catalyzes the reduction of protein disulfides and that of mixed disulfides.	Disulfides	164-174	glutaredoxin	Homo sapiens	12-26
24041990-1	2014	BACKGROUND: Glutaredoxin 1 (Grx1), a small protein belonging to the thioredoxin family, is involved in redox-regulation since it catalyzes the reduction of protein disulfides and that of mixed disulfides.	Disulfides	164-174	glutaredoxin	Homo sapiens	28-32
24041990-1	2014	BACKGROUND: Glutaredoxin 1 (Grx1), a small protein belonging to the thioredoxin family, is involved in redox-regulation since it catalyzes the reduction of protein disulfides and that of mixed disulfides.	Disulfides	193-203	glutaredoxin	Homo sapiens	12-26
24041990-1	2014	BACKGROUND: Glutaredoxin 1 (Grx1), a small protein belonging to the thioredoxin family, is involved in redox-regulation since it catalyzes the reduction of protein disulfides and that of mixed disulfides.	Disulfides	193-203	glutaredoxin	Homo sapiens	28-32
24253198-8	2014	Nevertheless, both NRX1 and NRX2 have disulfide reduction capacities, although NRX1 alone can be reduced by the thioredoxin reductase NTRA.	Disulfides	38-47	protein kinase C-like zinc finger protein	Arabidopsis thaliana	28-32
24174618-4	2013	Based on deglycosylation and nonreduced/reduced two-dimensional SDS-PAGE, we detected CL-K1 and CL-L1 in disulfide bridge-stabilized complexes.	Disulfides	105-114	collectin subfamily member 10	Homo sapiens	96-101
20361855-7	2010	Reversible oxidation of thiols in serine threonine protein phosphatase PP2A and in protein tyrosin phosphatases SHP1, SHP2 and CD45 leads to their inactivation generally by formation of intramolecular disulfides.	Disulfides	201-211	nuclear receptor subfamily 0 group B member 2	Homo sapiens	112-116
24490732-2	2013	The ability of both AGR2 and ERp57/GRP58 to catalyze the formation of disulfide bonds in proteins is the parameter most important for assigning them to a PDI family.	Disulfides	70-79	prolyl 4-hydroxylase subunit beta	Homo sapiens	154-157
24037759-2	2013	The current model for insulin receptor activation is that two distinct surfaces of insulin monomer engage sequentially with two distinct binding sites on the extracellular surface of the insulin receptor, which is itself a disulfide-linked (alphabeta)2 homodimer.	Disulfides	223-232	insulin receptor	Homo sapiens	22-38
24037759-2	2013	The current model for insulin receptor activation is that two distinct surfaces of insulin monomer engage sequentially with two distinct binding sites on the extracellular surface of the insulin receptor, which is itself a disulfide-linked (alphabeta)2 homodimer.	Disulfides	223-232	insulin receptor	Homo sapiens	187-203
24043621-2	2013	The folding mechanism of type I procollagen has been well characterized, and protein disulfide isomerase (PDI) has been suggested as a key player in the formation of the correct disulfide bonds in the noncollagenous carboxyl-terminal and amino-terminal propeptides.	Disulfides	85-94	prolyl 4-hydroxylase subunit beta	Homo sapiens	106-109
23902771-6	2013	These interactions are controlled by a redox-sensitive amino acid, cysteine 10 of Pex5, which is essential for the formation of disulfide bond-linked Pex5 forms, for high affinity cargo binding, and for receptor recycling.	Disulfides	128-137	peroxisomal biogenesis factor 5	Homo sapiens	82-86
23902771-6	2013	These interactions are controlled by a redox-sensitive amino acid, cysteine 10 of Pex5, which is essential for the formation of disulfide bond-linked Pex5 forms, for high affinity cargo binding, and for receptor recycling.	Disulfides	128-137	peroxisomal biogenesis factor 5	Homo sapiens	150-154
23902771-7	2013	Disulfide bond-linked Pex5 showed the highest affinity for PTS1 cargo.	Disulfides	0-9	peroxisomal biogenesis factor 5	Homo sapiens	22-26
23902771-8	2013	Upon reduction of the disulfide bond by dithiothreitol, Pex5 transitioned to a noncovalent dimer, concomitant with the partial release of PTS1 cargo.	Disulfides	22-31	peroxisomal biogenesis factor 5	Homo sapiens	56-60
24023779-4	2013	These studies employed a construct of SP-B, SP-B (1-25,63-78), also called Super Mini-B, which is a 41-residue peptide with internal disulfide bonds comprising the N-terminal 7-residue insertion sequence and the N- and C-terminal helices of SP-B.	Disulfides	133-142	surfactant protein B	Homo sapiens	38-42
24023779-4	2013	These studies employed a construct of SP-B, SP-B (1-25,63-78), also called Super Mini-B, which is a 41-residue peptide with internal disulfide bonds comprising the N-terminal 7-residue insertion sequence and the N- and C-terminal helices of SP-B.	Disulfides	133-142	surfactant protein B	Homo sapiens	44-48
24023779-4	2013	These studies employed a construct of SP-B, SP-B (1-25,63-78), also called Super Mini-B, which is a 41-residue peptide with internal disulfide bonds comprising the N-terminal 7-residue insertion sequence and the N- and C-terminal helices of SP-B.	Disulfides	133-142	surfactant protein B	Homo sapiens	44-48
23615222-1	2013	Thioredoxin (Trx) is a key player in redox homeostasis in various cells, modulating the functions of target proteins by catalyzing a thiol-disulfide exchange reaction.	Disulfides	139-148	thioredoxin H-type 1	Arabidopsis thaliana	0-11
23615222-1	2013	Thioredoxin (Trx) is a key player in redox homeostasis in various cells, modulating the functions of target proteins by catalyzing a thiol-disulfide exchange reaction.	Disulfides	139-148	thioredoxin H-type 1	Arabidopsis thaliana	13-16
23446148-4	2013	Firstly, the cytokine-stimulating activity of HMGB1 requires C23 and C45 to be in a disulfide linkage, at the same time that C106 must remain in its reduced form as a thiol.	Disulfides	84-93	high mobility group box 1	Homo sapiens	46-51
23446148-4	2013	Firstly, the cytokine-stimulating activity of HMGB1 requires C23 and C45 to be in a disulfide linkage, at the same time that C106 must remain in its reduced form as a thiol.	Disulfides	84-93	nucleolin	Homo sapiens	61-64
23444301-5	2013	Proteins forming mixed-disulfide intermediates with the mutated Trx were identified by proteomic approaches.	Disulfides	23-32	thioredoxin H-type 1	Arabidopsis thaliana	64-67
23486466-4	2013	Here, we show that the mutation abolishes secretion of IRBP and results in formation of insoluble high molecular weight complexes via disulfide bonds.	Disulfides	134-143	retinol binding protein 3	Homo sapiens	55-59
23486466-5	2013	Co-expression of protein disulfide isomerase A2 that regulates disulfide bond formation or introduction of double Cys-to-Ala substitutions at positions 304 and 1175 in D1080N IRBP promoted secretion of the mutated IRBP.	Disulfides	25-34	retinol binding protein 3	Homo sapiens	175-179
23486466-5	2013	Co-expression of protein disulfide isomerase A2 that regulates disulfide bond formation or introduction of double Cys-to-Ala substitutions at positions 304 and 1175 in D1080N IRBP promoted secretion of the mutated IRBP.	Disulfides	25-34	retinol binding protein 3	Homo sapiens	214-218
23530257-5	2013	PDI engages with a range of clients as the direct catalyst of disulfide bond formation, isomerization or reduction.	Disulfides	62-71	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
23315166-7	2013	This rapid and potent mechanism of cellular TF activation represents a novel connection between the complement system and cell surface PDI-mediated thiol-disulfide exchange.	Disulfides	154-163	prolyl 4-hydroxylase subunit beta	Homo sapiens	135-138
23497318-5	2013	RESULTS: We provided evidence for the presence of the NTD-CTD interface in HIV-1 particles by engineering intersubunit NTD-CTD disulfide crosslinks, resulting in accumulation of disulfide-linked oligomers up to hexamers.	Disulfides	127-136	fuzzy planar cell polarity protein	Homo sapiens	54-57
23497318-5	2013	RESULTS: We provided evidence for the presence of the NTD-CTD interface in HIV-1 particles by engineering intersubunit NTD-CTD disulfide crosslinks, resulting in accumulation of disulfide-linked oligomers up to hexamers.	Disulfides	127-136	fuzzy planar cell polarity protein	Homo sapiens	119-122
23497318-5	2013	RESULTS: We provided evidence for the presence of the NTD-CTD interface in HIV-1 particles by engineering intersubunit NTD-CTD disulfide crosslinks, resulting in accumulation of disulfide-linked oligomers up to hexamers.	Disulfides	178-187	fuzzy planar cell polarity protein	Homo sapiens	54-57
20429571-0	2010	Effect of the disulfide bond on the monomeric structure of human amylin studied by combined Hamiltonian and temperature replica exchange molecular dynamics simulations.	Disulfides	14-23	islet amyloid polypeptide	Homo sapiens	65-71
20429571-4	2010	However, the effect of the disulfide bond on the intrinsic structural properties of monomeric hIAPP is yet to be determined.	Disulfides	27-36	islet amyloid polypeptide	Homo sapiens	94-99
23497318-5	2013	RESULTS: We provided evidence for the presence of the NTD-CTD interface in HIV-1 particles by engineering intersubunit NTD-CTD disulfide crosslinks, resulting in accumulation of disulfide-linked oligomers up to hexamers.	Disulfides	178-187	fuzzy planar cell polarity protein	Homo sapiens	119-122
23283984-6	2013	Tim22 forms a disulfide-bonded intermediate with Mia40 upon import into mitochondria.	Disulfides	14-23	translocase of inner mitochondrial membrane 22	Homo sapiens	0-5
20429571-7	2010	On the basis of a total simulation time of 28 mus, we find that, although native hIAPP (in the presence of a disulfide bond) essentially adopts a disordered conformation in solution, consistent with the signal measured by ultraviolet-circular dichroism (UV-CD) spectroscopy, it also transiently samples alpha-helical structure for residues 5-16.	Disulfides	109-118	islet amyloid polypeptide	Homo sapiens	81-86
20429571-10	2010	Implications of the stabilization of N-terminal helical structure by disulfide bond on the initialization of hIAPP amyloid formation are discussed.	Disulfides	69-78	islet amyloid polypeptide	Homo sapiens	109-114
20332089-8	2010	Neither GCL activation, nor the formation of holoenzyme, required a covalent intermolecular disulfide bridge between GCLC and GCLM.	Disulfides	92-101	glutamate-cysteine ligase catalytic subunit	Homo sapiens	117-121
20458450-2	2010	Previous studies suggest the cell surface protein disulfide isomerase (PDI) might interact with disulfide bond(s) of gp120 and thus facilitate HIV-1 entry.	Disulfides	50-59	prolyl 4-hydroxylase subunit beta	Homo sapiens	71-74
20458450-2	2010	Previous studies suggest the cell surface protein disulfide isomerase (PDI) might interact with disulfide bond(s) of gp120 and thus facilitate HIV-1 entry.	Disulfides	50-59	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	117-122
20144905-6	2010	Together our results showed for the first time that AKR1B10"s enzymatic activity and inhibitor sensitivity are modulated by thiol/disulfide exchanges.	Disulfides	130-139	aldo-keto reductase family 1 member B10	Homo sapiens	52-59
23283984-8	2013	We propose that Mia40 not only is responsible for disulfide bond formation, but also assists the Tim22 protein in its integration into the inner membrane of mitochondria.	Disulfides	50-59	translocase of inner mitochondrial membrane 22	Homo sapiens	97-102
23537207-2	2013	Disulfide-rich peptides that antagonize the growth factor receptors neuropilin-1 and neuropilin-2 were developed using bacterial display libraries.	Disulfides	0-9	neuropilin 1	Homo sapiens	68-80
20147294-7	2010	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.	Disulfides	59-68	adenosine deaminase 2	Homo sapiens	125-129
23537207-3	2013	Peptide ligands specific for the VEGFA binding site on neuropilin-1 were identified by screening a library of disulfide-rich peptides derived from the thermostable, protease-resistant cyclotide kalata B1.	Disulfides	110-119	neuropilin 1	Homo sapiens	55-67
20230797-1	2010	The conserved disulfide-bonded region (DSR) of the human immunodeficiency virus type 1 (HIV-1) fusion glycoprotein, gp41, mediates association with the receptor-binding glycoprotein, gp120.	Disulfides	14-23	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	183-188
22885023-6	2013	Disulfide bridges in native gamma3-hordein were almost the same as those found in wheat gamma46-gliadin, except the bridge involving the cysteine included in the glycosylation site.	Disulfides	0-9	LOC102682035	Hordeum vulgare	28-42
20209080-1	2010	BACKGROUND: Protein Disulfide Isomerase (PDI) in the endoplasmic reticulum of all cells catalyzes the rearrangement of disulfide bridges during folding of membrane and secreted proteins.	Disulfides	119-128	prolyl 4-hydroxylase subunit beta	Bos taurus	12-39
20209080-1	2010	BACKGROUND: Protein Disulfide Isomerase (PDI) in the endoplasmic reticulum of all cells catalyzes the rearrangement of disulfide bridges during folding of membrane and secreted proteins.	Disulfides	119-128	prolyl 4-hydroxylase subunit beta	Bos taurus	41-44
22920903-4	2013	Disulfide forming/ isomerizing enzymes like thioredoxin (Trx), protein disulfide isomerase (PDI), which are chaperone proteins, are implicated into transnitrosation reactions, which are the transfer of  NO from one cysteine residue to another one.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	63-90
20070606-9	2010	We also show that PDI binds to TAP in a tapasin-independent manner, but forms disulfide-linked conjugates with soluble tapasin.	Disulfides	78-87	prolyl 4-hydroxylase subunit beta	Homo sapiens	18-21
20097158-1	2010	Protein disulfide isomerase (PDI), the chief endoplasmic reticulum (ER) resident oxidoreductase chaperone that catalyzes maturation of disulfide-bond-containing proteins is involved in the pathogenesis of both Parkinson"s (PD) and Alzheimer"s (AD) diseases.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
22920903-4	2013	Disulfide forming/ isomerizing enzymes like thioredoxin (Trx), protein disulfide isomerase (PDI), which are chaperone proteins, are implicated into transnitrosation reactions, which are the transfer of  NO from one cysteine residue to another one.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	92-95
22990208-4	2013	A disulfide-linked immunoconjugate of a 5-amino-modified 24 mer phosphorothioate anti-sense E2A-PBX1 oligonucleotide (AON) with a mAb specific for a CD19 receptor (alphaCD19-AON) was prepared as a CD19-directed and leukemia-specific biotherapeutic agent against E2A-PBX1(+) B-lineage ALL.	Disulfides	2-11	CD19 molecule	Homo sapiens	149-153
19916574-9	2010	When the disulfide bonds are absent, the N-terminal beta- strand unfolds by 20 ns but beta-strands are observed in the C-terminal region of HNP-3.	Disulfides	9-18	defensin alpha 3	Homo sapiens	140-145
22990208-4	2013	A disulfide-linked immunoconjugate of a 5-amino-modified 24 mer phosphorothioate anti-sense E2A-PBX1 oligonucleotide (AON) with a mAb specific for a CD19 receptor (alphaCD19-AON) was prepared as a CD19-directed and leukemia-specific biotherapeutic agent against E2A-PBX1(+) B-lineage ALL.	Disulfides	2-11	CD19 molecule	Homo sapiens	169-173
22530666-1	2012	SIGNIFICANCE: Glutaredoxin (Grx) is the primary enzyme responsible for catalysis of deglutathionylation of protein-mixed disulfides with glutathione (GSH) (protein-SSG).	Disulfides	121-131	glutaredoxin	Homo sapiens	14-26
19896952-7	2010	Furthermore, the presence of a disulfide bond in amylin allows IDE to cut at an additional site in the middle of the peptide (amino acids 18-19).	Disulfides	31-40	islet amyloid polypeptide	Homo sapiens	49-55
19896952-8	2010	Our amylin-bound IDE structure offers insight into how the structural constraint from a disulfide bond in amylin can alter IDE cleavage sites.	Disulfides	88-97	islet amyloid polypeptide	Homo sapiens	4-10
22530666-1	2012	SIGNIFICANCE: Glutaredoxin (Grx) is the primary enzyme responsible for catalysis of deglutathionylation of protein-mixed disulfides with glutathione (GSH) (protein-SSG).	Disulfides	121-131	glutaredoxin	Homo sapiens	28-31
19896952-8	2010	Our amylin-bound IDE structure offers insight into how the structural constraint from a disulfide bond in amylin can alter IDE cleavage sites.	Disulfides	88-97	islet amyloid polypeptide	Homo sapiens	106-112
23045530-0	2012	Engineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair.	Disulfides	11-20	mutS homolog 2	Homo sapiens	129-133
23045530-4	2012	An engineered disulfide bond within this region prevented the ATP-driven conformational change and resulted in an Msh2-Msh6 complex that bound mispaired bases but could not form sliding clamps or bind Mlh1-Pms1.	Disulfides	14-23	mutS homolog 2	Homo sapiens	114-118
22988091-1	2012	Protein disulfide isomerase (PDI), an endoplasmic reticulum chaperone protein, catalyzes disulfide bond breakage, formation, and rearrangement.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
20062808-5	2010	A role for disulfide bonds in stabilizing the ETR1 protein complex was demonstrated by use of reducing agents and mutation of Cys4 and Cys6 of ETR1.	Disulfides	11-20	Cystatin/monellin superfamily protein	Arabidopsis thaliana	126-130
21513117-2	2010	DsbA and Dsbc interact with unfolded proteins to catalyze disulfide bond formation or isomerisation, respectively.	Disulfides	58-67	putative protein DsbC	Escherichia coli	9-13
15351291-1	2004	In eukaryotic cells the enzyme protein disulfide isomerase (PDI) is responsible for the formation and reshuffling of disulfide bonds in secretory proteins.	Disulfides	39-48	prolyl 4-hydroxylase subunit beta	Homo sapiens	60-63
15351291-10	2004	These aspects should make substrates of this type generally applicable for assaying PDI and other thiol-disulfide exchange enzymes.	Disulfides	104-113	prolyl 4-hydroxylase subunit beta	Homo sapiens	84-87
20029959-4	2010	CANX along with ERP-57 promotes the formation of disulfide bond bridges in nascent proteins.	Disulfides	49-58	calnexin	Homo sapiens	0-4
23085174-5	2012	Since denaturation of disulfide bonds of envelope glycoprotein (gp) 120 is a key step in the prevention of the spread of HIV-1, the development of the proposed study is promised to HIV-1 research field.	Disulfides	22-31	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	41-71
20029959-5	2010	The human GnRH receptor (hGnRHR) is stabilized by two disulfide bond bridges (C(14)-C(200) and C(114)-C(196)), that, when broken, lead to a decrease in receptor expression at the plasma membrane.	Disulfides	54-63	gonadotropin releasing hormone receptor	Homo sapiens	10-23
20029959-5	2010	The human GnRH receptor (hGnRHR) is stabilized by two disulfide bond bridges (C(14)-C(200) and C(114)-C(196)), that, when broken, lead to a decrease in receptor expression at the plasma membrane.	Disulfides	54-63	gonadotropin releasing hormone receptor	Homo sapiens	25-31
19878651-3	2009	IL-4 disulfides were in vitro reduced by thioredoxin 1 (Trx1) and protein disulfide isomerase (PDI).	Disulfides	5-15	prolyl 4-hydroxylase subunit beta	Homo sapiens	66-93
19878651-3	2009	IL-4 disulfides were in vitro reduced by thioredoxin 1 (Trx1) and protein disulfide isomerase (PDI).	Disulfides	5-15	prolyl 4-hydroxylase subunit beta	Homo sapiens	95-98
19878651-4	2009	Reduction of IL-4 disulfides by the cell surface of HeLa cells was inhibited by auranofin, an inhibitor of thioredoxin reductase that is an electron donor to both Trx1 and PDI.	Disulfides	18-28	prolyl 4-hydroxylase subunit beta	Homo sapiens	172-175
15357668-1	2004	We have previously described a disulfide-linked cyclic nonapeptide (inhibitory peptide-01, IP01), with the sequence CLLRMRSIC, which binds to intercellular adhesion molecule-1 (ICAM-1), and blocks binding to its counter-structure, the integrin alphaLbeta2 (leukocyte functional antigen-1, LFA-1) (Sillerud et al., J. Peptide Res.	Disulfides	31-40	intercellular adhesion molecule 1	Mus musculus	142-175
15357668-1	2004	We have previously described a disulfide-linked cyclic nonapeptide (inhibitory peptide-01, IP01), with the sequence CLLRMRSIC, which binds to intercellular adhesion molecule-1 (ICAM-1), and blocks binding to its counter-structure, the integrin alphaLbeta2 (leukocyte functional antigen-1, LFA-1) (Sillerud et al., J. Peptide Res.	Disulfides	31-40	intercellular adhesion molecule 1	Mus musculus	177-183
22789914-1	2012	In chloroplasts, the ferredoxin/thioredoxin pathway regulates enzyme activity in response to light by reduction of regulatory disulfides in target enzymes, ensuring coordination between photosynthesis and diurnal metabolism.	Disulfides	126-136	thioredoxin H-type 1	Arabidopsis thaliana	32-43
15166248-3	2004	hCG is stabilized by a strand of its beta-subunit that has been likened to a "seatbelt" because it surrounds alpha-subunit loop 2 and its end is "latched" by an intrasubunit disulfide bond to the beta-subunit core.	Disulfides	174-183	glycoprotein hormones, alpha polypeptide	Homo sapiens	0-3
15166248-7	2004	hCG assembly appears to be limited by the need to disrupt the disulfide that stabilizes the small seatbelt loop prior to threading.	Disulfides	62-71	glycoprotein hormones, alpha polypeptide	Homo sapiens	0-3
19878651-5	2009	Both Trx1 and PDI have been shown to be located at the cell surface and our data suggests that these enzymes are involved in catalyzing reduction of IL-4 disulfides.	Disulfides	154-164	prolyl 4-hydroxylase subunit beta	Homo sapiens	14-17
22572242-4	2012	PDI catalyzes dithiol/disulfide interchange reactions, and the cysteine residues in PDI proteins are very important.	Disulfides	22-31	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
19697117-5	2009	Wild type and both mutants containing N-terminal cysteines catalyzed the reduction of disulfides in a coupled system with GSH, NADPH, and glutathione reductase.	Disulfides	86-96	glutathione-disulfide reductase	Homo sapiens	138-159
15070828-8	2004	Bovine TKDP-2 had a P1 lysine and the three conserved disulfides, but it possessed an unusual residue (Asp) at P2.	Disulfides	54-64	trophoblast Kunitz domain protein 2	Bos taurus	7-13
19712047-8	2009	HRG fragments, generated by plasmin cleavage, are held together by disulfide linkages and are not released from the molecule under non-reducing conditions.	Disulfides	67-76	plasminogen	Homo sapiens	28-35
22572242-12	2012	Thus, CYO1 may accelerate the folding of cysteine residue--containing PSI and PSII subunits by repeatedly breaking and creating disulfide bonds.	Disulfides	128-137	protein disulfide isomerase	Arabidopsis thaliana	6-10
15307920-1	2004	The HIV-1 envelope glycoprotein complex (Env) can be stabilized by the introduction of a disulfide bond between the gp120 and gp41 subunits.	Disulfides	89-98	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	41-44
15307920-1	2004	The HIV-1 envelope glycoprotein complex (Env) can be stabilized by the introduction of a disulfide bond between the gp120 and gp41 subunits.	Disulfides	89-98	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	116-121
22648419-5	2012	GSH alone is sufficient to reduce the disulfide, restoring the ability of Atox1 to bind copper; glutaredoxin 1 facilitates this reaction when GSH is low.	Disulfides	38-47	glutaredoxin	Homo sapiens	96-110
15212484-2	2004	HRGS treatment of myofibrils caused cross-linking of myosin heavy chains (MHC) via disulfide bonding, an increase in Ca-ATPase activity, and a decrease in K-ATPase activity, suggesting that thiol groups of myosin including those at the active site were modified.	Disulfides	83-92	myosin, heavy chain 15	Gallus gallus	53-59
19604149-1	2009	PDI (protein disulfide-isomerase) catalyses the formation of native disulfide bonds of secretory proteins in the endoplasmic reticulum.	Disulfides	13-22	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
22616859-7	2012	Recent studies with HO2 (haem oxygenase-2), a K+ ion channel (the BK channel) and a nuclear receptor (Rev-Erb) demonstrate that this mode of regulation involves a thiol-disulfide redox switch that regulates haem binding and that gas signalling molecules (CO and NO) modulate the effect of haem.	Disulfides	169-178	heme oxygenase 2	Homo sapiens	20-23
19706676-0	2009	Ligand-independent signaling by disulfide-crosslinked dimers of the p75 neurotrophin receptor.	Disulfides	32-41	PC4 and SFRS1 interacting protein 1	Homo sapiens	68-71
19706676-3	2009	The p75 neurotrophin receptor (p75(NTR)) forms disulfide-linked dimers at the cell surface independently of ligand binding through Cys257 in its transmembrane domain.	Disulfides	47-56	PC4 and SFRS1 interacting protein 1	Homo sapiens	4-7
15186099-3	2004	The purified glycinin from soybean in the adverse conditions was associated with a significant amount of sugar and showed reductions in hydrophobic interactions after 3 months; the total free sulfhydryl content in glycinin decreased, but the intramolecular disulfide bonds increased; the alpha-helix content of secondary structure slightly increased, but the beta-sheet content decreased.	Disulfides	257-266	LOC732636	Glycine max	13-21
22616859-7	2012	Recent studies with HO2 (haem oxygenase-2), a K+ ion channel (the BK channel) and a nuclear receptor (Rev-Erb) demonstrate that this mode of regulation involves a thiol-disulfide redox switch that regulates haem binding and that gas signalling molecules (CO and NO) modulate the effect of haem.	Disulfides	169-178	heme oxygenase 2	Homo sapiens	25-41
15158710-4	2004	This review focuses specifically on one of these folding assistants, protein disulfide isomerase (PDI), an enzyme that catalyzes disulfide formation and isomerization and a chaperone that inhibits aggregation.	Disulfides	77-86	prolyl 4-hydroxylase subunit beta	Homo sapiens	98-101
19706676-3	2009	The p75 neurotrophin receptor (p75(NTR)) forms disulfide-linked dimers at the cell surface independently of ligand binding through Cys257 in its transmembrane domain.	Disulfides	47-56	neurotensin receptor 1	Homo sapiens	31-39
19706676-5	2009	The activity profiles of different disulfide-crosslinked p75(NTR) mutants were similar but not identical, suggesting that different configurations of p75(NTR) dimers might be endowed with different functions.	Disulfides	35-44	PC4 and SFRS1 interacting protein 1	Homo sapiens	57-60
19706676-5	2009	The activity profiles of different disulfide-crosslinked p75(NTR) mutants were similar but not identical, suggesting that different configurations of p75(NTR) dimers might be endowed with different functions.	Disulfides	35-44	neurotensin receptor 1	Homo sapiens	61-64
19706676-5	2009	The activity profiles of different disulfide-crosslinked p75(NTR) mutants were similar but not identical, suggesting that different configurations of p75(NTR) dimers might be endowed with different functions.	Disulfides	35-44	PC4 and SFRS1 interacting protein 1	Homo sapiens	150-153
19706676-5	2009	The activity profiles of different disulfide-crosslinked p75(NTR) mutants were similar but not identical, suggesting that different configurations of p75(NTR) dimers might be endowed with different functions.	Disulfides	35-44	neurotensin receptor 1	Homo sapiens	154-157
15109915-2	2004	Here we test the hypothesis that glutaredoxin-1 (Grx-1), a member of the oxidoreductase family of enzymes, may be a critical component of redox-sensitive molecular switches by mediating reversible protein S-glutathionylation and enzymatic catalysis of thiol/disulfide exchange.	Disulfides	258-267	glutaredoxin	Homo sapiens	33-47
22489915-1	2012	BACKGROUND: Ligation of the platelet-specific collagen receptor, GPVI/FcRgamma, causes rapid, transient disulfide-dependent homodimerization, and the production of intracellular reactive oxygen species (ROS) generated by the NADPH oxidase, linked to GPVI via TRAF4.	Disulfides	104-113	Fc epsilon receptor Ig	Homo sapiens	70-78
15109915-2	2004	Here we test the hypothesis that glutaredoxin-1 (Grx-1), a member of the oxidoreductase family of enzymes, may be a critical component of redox-sensitive molecular switches by mediating reversible protein S-glutathionylation and enzymatic catalysis of thiol/disulfide exchange.	Disulfides	258-267	glutaredoxin	Homo sapiens	49-54
15133840-3	2004	RESULTS: The N-terminal deletions of the clusterin gene and the appearance of a 50-53 ku nuclear clusterin, an uncleaved, nonglycosylated, and disulfide-linked isoform, were the major alterations in cancer cells of esophagus.	Disulfides	143-152	clusterin	Homo sapiens	41-50
19651040-0	2009	Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2-B unique sequence.	Disulfides	39-48	titin	Homo sapiens	14-19
19651040-0	2009	Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2-B unique sequence.	Disulfides	39-48	titin	Homo sapiens	72-77
19651040-3	2009	Additional modulatory effects on titin stiffness may arise from disulfide bonding under oxidant stress, as many immunoglobulin-like (Ig-)domains in titin"s spring region have a potential for S-S formation.	Disulfides	64-73	titin	Homo sapiens	33-38
19651040-5	2009	However, we demonstrate that the human N2-B-unique sequence (N2-B(us)), a cardiac-specific, physiologically extensible titin segment comprising 572 amino-acid residues, contains up to three disulfide bridges under oxidizing conditions.	Disulfides	190-199	titin	Homo sapiens	119-124
15133840-3	2004	RESULTS: The N-terminal deletions of the clusterin gene and the appearance of a 50-53 ku nuclear clusterin, an uncleaved, nonglycosylated, and disulfide-linked isoform, were the major alterations in cancer cells of esophagus.	Disulfides	143-152	clusterin	Homo sapiens	97-106
22489915-1	2012	BACKGROUND: Ligation of the platelet-specific collagen receptor, GPVI/FcRgamma, causes rapid, transient disulfide-dependent homodimerization, and the production of intracellular reactive oxygen species (ROS) generated by the NADPH oxidase, linked to GPVI via TRAF4.	Disulfides	104-113	TNF receptor associated factor 4	Homo sapiens	259-264
22220984-6	2012	A specific protein-protein interaction between either isoform and protein disulfide isomerase (PDI) facilitates the propagation of disulfides from Ero1 via PDI to nascent polypeptides, and inbuilt oxidative shutdown mechanisms in Ero1alpha and Ero1beta prevent excessive oxidation of PDI.	Disulfides	131-141	prolyl 4-hydroxylase subunit beta	Homo sapiens	66-93
14729662-0	2004	Hierarchical formation of disulfide bonds in the immunoglobulin Fc fragment is assisted by protein-disulfide isomerase.	Disulfides	26-35	prolyl 4-hydroxylase subunit beta	Homo sapiens	91-118
14729662-11	2004	Our results indicate that the two domains of the Fc fragment fold independently, with a precise hierarchy of disulfide formation in which the disulfide bond, especially, of the C(H)2 domain requires catalysis by PDI.	Disulfides	109-118	prolyl 4-hydroxylase subunit beta	Homo sapiens	212-215
14729662-11	2004	Our results indicate that the two domains of the Fc fragment fold independently, with a precise hierarchy of disulfide formation in which the disulfide bond, especially, of the C(H)2 domain requires catalysis by PDI.	Disulfides	142-151	prolyl 4-hydroxylase subunit beta	Homo sapiens	212-215
19473966-0	2009	Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state.	Disulfides	56-65	heme oxygenase 2	Homo sapiens	26-42
19473966-5	2009	In HO-2, the C-terminal HRMs constitute a thiol/disulfide redox switch that regulates affinity of the enzyme for heme (Yi, L., and Ragsdale, S. W. (2007) J. Biol.	Disulfides	48-57	heme oxygenase 2	Homo sapiens	3-7
22220984-6	2012	A specific protein-protein interaction between either isoform and protein disulfide isomerase (PDI) facilitates the propagation of disulfides from Ero1 via PDI to nascent polypeptides, and inbuilt oxidative shutdown mechanisms in Ero1alpha and Ero1beta prevent excessive oxidation of PDI.	Disulfides	131-141	prolyl 4-hydroxylase subunit beta	Homo sapiens	95-98
19473966-8	2009	Here, we demonstrate that the thiol/disulfide switch in human HO-2 is physiologically relevant.	Disulfides	36-45	heme oxygenase 2	Homo sapiens	62-66
14656938-6	2004	The PKCdelta stimulatory response in COS7-PKCdelta cells was triggered only by the disulfide agent and not by its reduced thiol counterpart, providing evidence for an oxidative mechanism.	Disulfides	83-92	protein kinase C delta	Homo sapiens	4-12
22220984-6	2012	A specific protein-protein interaction between either isoform and protein disulfide isomerase (PDI) facilitates the propagation of disulfides from Ero1 via PDI to nascent polypeptides, and inbuilt oxidative shutdown mechanisms in Ero1alpha and Ero1beta prevent excessive oxidation of PDI.	Disulfides	131-141	prolyl 4-hydroxylase subunit beta	Homo sapiens	156-159
14656938-6	2004	The PKCdelta stimulatory response in COS7-PKCdelta cells was triggered only by the disulfide agent and not by its reduced thiol counterpart, providing evidence for an oxidative mechanism.	Disulfides	83-92	protein kinase C delta	Homo sapiens	42-50
19473966-13	2009	Thus, the thiol/disulfide switch in HO-2 responds to cellular oxidative stress and reductive conditions, representing a paradigm for how HRMs can integrate heme homeostasis with CO signaling and redox regulation of cellular metabolism.	Disulfides	16-25	heme oxygenase 2	Homo sapiens	36-40
19393216-4	2009	The disulfide bridge pattern of recombinant homodimeric rGDF5 was recently elucidated by X-ray diffraction.	Disulfides	4-13	growth differentiation factor 5	Rattus norvegicus	56-61
19393216-6	2009	The cystine knot of homodimeric rGDF5 exhibits the pattern Cys1-Cys5, Cys2-Cys6, and Cys3-Cys7 (three intrachain disulfide bonds), and the monomers are connected by a single interchain disulfide bridge (Cys4-Cys4) in accordance with other members of the TGF-beta superfamily.	Disulfides	113-122	growth differentiation factor 5	Rattus norvegicus	32-37
19393216-6	2009	The cystine knot of homodimeric rGDF5 exhibits the pattern Cys1-Cys5, Cys2-Cys6, and Cys3-Cys7 (three intrachain disulfide bonds), and the monomers are connected by a single interchain disulfide bridge (Cys4-Cys4) in accordance with other members of the TGF-beta superfamily.	Disulfides	185-194	growth differentiation factor 5	Rattus norvegicus	32-37
14656938-8	2004	Demonstration of oxidative regulation of cellular PKCdelta and PKCepsilon by disulfides in this report provides evidence that redox-regulatory sites in PKCdelta and PKCepsilon may offer novel targets for development of cancer preventive or therapeutic agents that selectively inactivate PKCepsilon or stimulate PKCdelta.	Disulfides	77-87	protein kinase C delta	Homo sapiens	50-58
14656938-8	2004	Demonstration of oxidative regulation of cellular PKCdelta and PKCepsilon by disulfides in this report provides evidence that redox-regulatory sites in PKCdelta and PKCepsilon may offer novel targets for development of cancer preventive or therapeutic agents that selectively inactivate PKCepsilon or stimulate PKCdelta.	Disulfides	77-87	protein kinase C delta	Homo sapiens	152-160
14656938-8	2004	Demonstration of oxidative regulation of cellular PKCdelta and PKCepsilon by disulfides in this report provides evidence that redox-regulatory sites in PKCdelta and PKCepsilon may offer novel targets for development of cancer preventive or therapeutic agents that selectively inactivate PKCepsilon or stimulate PKCdelta.	Disulfides	77-87	protein kinase C delta	Homo sapiens	152-160
15028751-7	2004	We demonstrate further that torsinA forms different disulfide-linked complexes that may be linked functionally to subcellular localization in the NE versus cytoplasmic ER.	Disulfides	52-61	torsin family 1, member A	Rattus norvegicus	28-35
22220984-6	2012	A specific protein-protein interaction between either isoform and protein disulfide isomerase (PDI) facilitates the propagation of disulfides from Ero1 via PDI to nascent polypeptides, and inbuilt oxidative shutdown mechanisms in Ero1alpha and Ero1beta prevent excessive oxidation of PDI.	Disulfides	131-141	prolyl 4-hydroxylase subunit beta	Homo sapiens	156-159
19382745-0	2009	The cataract-associated R14C mutant of human gamma D-crystallin shows a variety of intermolecular disulfide cross-links: a Raman spectroscopic study.	Disulfides	98-107	crystallin gamma D	Homo sapiens	45-63
22401853-6	2012	PDI is a converging hub for pathways of disulfide bond introduction into ER-processed proteins, via hydrogen peroxide-generating mechanisms involving the oxidase Ero1alpha, as well as hydrogen peroxide-consuming reactions involving peroxiredoxin IV and the novel peroxidases Gpx7/8.	Disulfides	40-49	glutathione peroxidase 7	Homo sapiens	275-281
14766672-4	2004	Samples from the H(2)O(2) group electrophoresed under nonreducing conditions and probed with actin, desmin, or tropomyosin monoclonal antibodies showed high-molecular mass complexes indicative of disulfide cross-bridges along with splitting and thickening of tropomyosin and actin bands, respectively.	Disulfides	196-205	desmin	Rattus norvegicus	100-106
19038358-0	2009	Human glutaredoxin-1 catalyzes the reduction of HIV-1 gp120 and CD4 disulfides and its inhibition reduces HIV-1 replication.	Disulfides	68-78	glutaredoxin	Homo sapiens	6-20
22270372-7	2012	A disulfide mutation that locks the N-domain to D1 in a coplanar position reversibly abrogates ATPase activity.	Disulfides	2-11	dynein axonemal heavy chain 8	Homo sapiens	95-101
19038358-1	2009	Reduction of intramolecular disulfides in the HIV-1 envelope protein gp120 occurs after its binding to the CD4 receptor.	Disulfides	28-38	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	69-74
19038358-2	2009	Protein disulfide isomerase (PDI) catalyzes the disulfide reduction in vitro and inhibition of this enzyme blocks viral entry.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
14592831-6	2004	We further find that PDI facilitates thiol/disulfide rearrangement in gp120 during conformational change, whereas inhibition of this redox shuffling prevents gp41 from assuming the fusogenic 6-helix bundle conformation.	Disulfides	43-52	prolyl 4-hydroxylase subunit beta	Homo sapiens	21-24
22230366-0	2012	Thioredoxin-1 and protein disulfide isomerase catalyze the reduction of similar disulfides in HIV gp120.	Disulfides	80-90	prolyl 4-hydroxylase subunit beta	Homo sapiens	18-45
14988014-2	2004	PAPP-A circulates in pregnancy as a proteolytically inactive complex, disulfide bound to the proform of eosinophil major basic protein (proMBP).	Disulfides	70-79	pappalysin 1	Homo sapiens	0-6
14988014-2	2004	PAPP-A circulates in pregnancy as a proteolytically inactive complex, disulfide bound to the proform of eosinophil major basic protein (proMBP).	Disulfides	70-79	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	104-134
14988014-2	2004	PAPP-A circulates in pregnancy as a proteolytically inactive complex, disulfide bound to the proform of eosinophil major basic protein (proMBP).	Disulfides	70-79	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	136-142
14988014-10	2004	We further conclude that proMBP inhibits PAPP-A in an unusual manner, not paralleled by other proteinase inhibitors of our knowledge, which requires proMBP to be covalently bound to PAPP-A by disulfide bonds.	Disulfides	192-201	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	25-31
14988014-10	2004	We further conclude that proMBP inhibits PAPP-A in an unusual manner, not paralleled by other proteinase inhibitors of our knowledge, which requires proMBP to be covalently bound to PAPP-A by disulfide bonds.	Disulfides	192-201	pappalysin 1	Homo sapiens	41-47
19038358-5	2009	We show that Grx1 efficiently catalyzes gp120, and CD4 disulfide reduction in vitro, even at low plasma levels of glutathione.	Disulfides	55-64	glutaredoxin	Homo sapiens	13-17
19821078-1	2009	Members of the protein disulfide isomerase (PDI) family play a critical role in catalyzing the formation of disulfide bonds in secretory proteins, and most of these enzymes have a wide tissue distribution.	Disulfides	23-32	prolyl 4-hydroxylase subunit beta	Homo sapiens	44-47
14988014-10	2004	We further conclude that proMBP inhibits PAPP-A in an unusual manner, not paralleled by other proteinase inhibitors of our knowledge, which requires proMBP to be covalently bound to PAPP-A by disulfide bonds.	Disulfides	192-201	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	149-155
22230366-3	2012	Previous studies indicate that protein disulfide isomerase (PDI), thioredoxin-1 (Trx1), and glutaredoxin-1 (Grx1) catalyze gp120 reduction, but their specific disulfide targets are not known.	Disulfides	39-48	prolyl 4-hydroxylase subunit beta	Homo sapiens	60-63
14988014-10	2004	We further conclude that proMBP inhibits PAPP-A in an unusual manner, not paralleled by other proteinase inhibitors of our knowledge, which requires proMBP to be covalently bound to PAPP-A by disulfide bonds.	Disulfides	192-201	pappalysin 1	Homo sapiens	182-188
19150607-1	2009	Protein disulfide isomerase (PDI) and its homologs are catalysts of the formation of disulfide bonds in secretory proteins, and they also serve as molecular chaperones.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
19233841-1	2009	Pdi1p (protein-disulfide isomerase) is a folding assistant of the endoplasmic reticulum (ER) that catalyzes disulfide formation and the isomerization of incorrect disulfides.	Disulfides	15-24	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	0-5
19233841-1	2009	Pdi1p (protein-disulfide isomerase) is a folding assistant of the endoplasmic reticulum (ER) that catalyzes disulfide formation and the isomerization of incorrect disulfides.	Disulfides	163-173	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	0-5
15017976-6	2004	In this review, through a comparative analysis of the oxidation process of Yap1 and PTPs, we propose the mechanism of disulfide bond formation in the PTPs.	Disulfides	118-127	Yes1 associated transcriptional regulator	Homo sapiens	75-79
14743430-7	2004	On the other hand, we find that preservation of disulfide bonds in the N-terminal extracellular domain of mGluRs is essential for stimulation by Ca2+(o) as well as glutamate.	Disulfides	48-57	glutamate metabotropic receptor 1	Homo sapiens	106-112
22230366-3	2012	Previous studies indicate that protein disulfide isomerase (PDI), thioredoxin-1 (Trx1), and glutaredoxin-1 (Grx1) catalyze gp120 reduction, but their specific disulfide targets are not known.	Disulfides	39-48	glutaredoxin	Homo sapiens	108-112
19122201-4	2009	However, other PTPRJ complexes, dependent on the formation of disulfide bonds, are detected by treatment with the oxidant agent H(2)O(2) or by a mutation Asp872Cys, located in the eighth fibronectin type III domain of PTPRJ.	Disulfides	62-71	protein tyrosine phosphatase receptor type J	Homo sapiens	15-20
19122201-4	2009	However, other PTPRJ complexes, dependent on the formation of disulfide bonds, are detected by treatment with the oxidant agent H(2)O(2) or by a mutation Asp872Cys, located in the eighth fibronectin type III domain of PTPRJ.	Disulfides	62-71	protein tyrosine phosphatase receptor type J	Homo sapiens	218-223
19122201-5	2009	A deletion in the eighth fibronectin domain of PTPRJ impairs its dimerization in the plasma membrane and increases the formation of PTPRJ complexes dependent on disulfide bonds that remain trapped in the cytoplasm.	Disulfides	161-170	protein tyrosine phosphatase receptor type J	Homo sapiens	47-52
19122201-5	2009	A deletion in the eighth fibronectin domain of PTPRJ impairs its dimerization in the plasma membrane and increases the formation of PTPRJ complexes dependent on disulfide bonds that remain trapped in the cytoplasm.	Disulfides	161-170	protein tyrosine phosphatase receptor type J	Homo sapiens	132-137
22230366-4	2012	Here, it was demonstrated that PDI and Trx1 have similar gp120 disulfide targets as determined by labeling after reduction, but with some pattern differences, including overall stronger labeling with Trx1 than with PDI.	Disulfides	63-72	prolyl 4-hydroxylase subunit beta	Homo sapiens	31-34
22247548-6	2012	The role of thioltransferase and glutathione reductase in the cellular reduction of disulfides and other oxidized forms of thiols was clarified.	Disulfides	84-94	glutaredoxin	Homo sapiens	12-28
19241374-6	2009	Comparison of the disulfide bond connectivities and the tertiary structures with those of other CRDs revealed that the Fn14 CRD is similar to the fourth CRD of TNF receptor 1 (A1-C2 module type), but not to the CRD of B-cell maturation antigen and the second CRD of transmembrane activator and CAML (calcium modulator and cyclophilin ligand) interactor (A1-D2 module type).	Disulfides	18-27	TNF receptor superfamily member 12A	Homo sapiens	119-123
19111842-1	2009	Human ATP-binding cassette (ABC) transporter ABCG2 (BCRP/MXR/ABCP) is a plasma membrane protein carrying intra- and inter-molecular disulfide bonds and an N-linked glycan.	Disulfides	132-141	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	6-26
19111842-1	2009	Human ATP-binding cassette (ABC) transporter ABCG2 (BCRP/MXR/ABCP) is a plasma membrane protein carrying intra- and inter-molecular disulfide bonds and an N-linked glycan.	Disulfides	132-141	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	28-31
14713336-1	2004	Most cells contain high levels of glutathione and multiple glutaredoxins, which utilize the reducing power of glutathione to catalyze disulfide reductions in the presence of NADPH and glutathione reductase (the glutaredoxin system).	Disulfides	134-143	glutathione-disulfide reductase	Homo sapiens	184-205
14713336-1	2004	Most cells contain high levels of glutathione and multiple glutaredoxins, which utilize the reducing power of glutathione to catalyze disulfide reductions in the presence of NADPH and glutathione reductase (the glutaredoxin system).	Disulfides	134-143	glutaredoxin	Homo sapiens	59-71
22247548-6	2012	The role of thioltransferase and glutathione reductase in the cellular reduction of disulfides and other oxidized forms of thiols was clarified.	Disulfides	84-94	glutathione-disulfide reductase	Homo sapiens	33-54
14730967-5	2004	The structure shows that two novel disulfide bonds found in FGF19, one of which appears to be conserved among several of the other FGFs, stabilize extended loops.	Disulfides	35-44	fibroblast growth factor 19	Homo sapiens	60-65
22340500-3	2012	Here, we show that Furin and SKI-1 combine with autocatalytic cleavage and a disulfide bridge to generate four membrane-bound and three soluble forms of the repulsive guidance molecule (RGMa).	Disulfides	77-86	furin, paired basic amino acid cleaving enzyme	Homo sapiens	19-24
15603510-3	2004	The mature, active form of human cystatin C is a single non-glycosylated polypeptide chain consisting of 120 amino acid residues, with a molecular mass of 13,343-13,359 Da, and containing four characteristic disulfide-paired cysteine residues.	Disulfides	208-217	cystatin C	Homo sapiens	33-43
18996119-2	2008	We have carried out quantitative investigations of the redox chemistry involving Cys22 and Cys44 of the HMGB1 A-domain, which form an intramolecular disulfide bond.	Disulfides	149-158	high mobility group box 1	Homo sapiens	104-109
22057392-7	2012	By contrast copper, which on its own activates MTF-1 only weakly in the cell lines tested, stabilizes the dimer by inducing intermolecular disulfide bond formation and synergizes with zinc to boost MTF-1 dependent transcription.	Disulfides	139-148	metal regulatory transcription factor 1	Homo sapiens	47-52
18842719-6	2008	Here, we provide evidence that A26 forms a disulfide-bonded complex with A27 that is anchored to the MV through a noncovalent interaction with the A17 transmembrane protein.	Disulfides	43-52	immunoglobulin kappa variable 3-20	Homo sapiens	73-76
15663362-1	2004	Ly-49 receptors are lectin-like type II transmembrane disulfide-bonded homodimers expressed on natural killer (NK) cells and some T-cell subsets.	Disulfides	54-63	killer cell lectin like receptor A1, pseudogene	Homo sapiens	0-5
14563687-0	2003	An atomic detail model for the human ATP binding cassette transporter P-glycoprotein derived from disulfide cross-linking and homology modeling.	Disulfides	98-107	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	37-57
22148505-6	2012	Disulfide bond formation upon oxidation of APE1 was analyzed by proteolysis of the protein followed by mass spectrometry analysis.	Disulfides	0-9	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	43-47
12939140-7	2003	Measurements of backbone (15)N relaxation times and interpretation of these by the model-free formalism with axial diffusional anisotropy further reveal significant ms to micros time scale motions centered about two of the conserved disulfide bonds and in several residues that comprise the TGFbeta binding surface.	Disulfides	233-242	transforming growth factor beta 3	Homo sapiens	291-298
18973303-2	2008	Curiously, the disordered, disulfide-null variant of mouse alpha-defensin cryptdin-4 (Crp4), termed (6C/A)-Crp4, has bactericidal activity equal to or greater than that of the native peptide, providing a rationale for comparing the mechanisms by which the peptides interact with and disrupt phospholipid vesicles of defined composition.	Disulfides	27-36	defensin, alpha, 4	Mus musculus	86-90
18973303-2	2008	Curiously, the disordered, disulfide-null variant of mouse alpha-defensin cryptdin-4 (Crp4), termed (6C/A)-Crp4, has bactericidal activity equal to or greater than that of the native peptide, providing a rationale for comparing the mechanisms by which the peptides interact with and disrupt phospholipid vesicles of defined composition.	Disulfides	27-36	defensin, alpha, 4	Mus musculus	107-111
18937500-2	2008	This work investigates how QSOX and protein disulfide isomerase (PDI) cooperate in vitro to generate native pairings in two unfolded reduced proteins: ribonuclease A (RNase, four disulfide bonds and 105 disulfide isomers of the fully oxidized protein) and avian riboflavin binding protein (RfBP, nine disulfide bonds and more than 34 million corresponding disulfide pairings).	Disulfides	44-53	prolyl 4-hydroxylase subunit beta	Homo sapiens	65-68
19020352-0	2008	Structure of the F-spondin reeler domain reveals a unique beta-sandwich fold with a deformable disulfide-bonded loop.	Disulfides	95-104	spondin 1	Homo sapiens	17-26
12919322-2	2003	Together with maurotoxin, Pi1, Pi7 and HsTx1, Pi4 belongs to the alpha KTX6 subfamily of short four-disulfide-bridged scorpion toxins acting on K+ channels.	Disulfides	100-109	Pancreas inflammation QTL 1	Rattus norvegicus	26-29
12919325-2	2003	The disulfide structure of the CRIPTO/FRL-1/CRYPTIC (CFC) domain of human Cripto protein was determined by a combination of enzymatic and chemical fragmentation, followed by chromatographic separation of the fragments, and characterization by mass spectrometry and N-terminal sequencing.	Disulfides	4-13	teratocarcinoma-derived growth factor 1 pseudogene 3	Homo sapiens	31-37
12919325-2	2003	The disulfide structure of the CRIPTO/FRL-1/CRYPTIC (CFC) domain of human Cripto protein was determined by a combination of enzymatic and chemical fragmentation, followed by chromatographic separation of the fragments, and characterization by mass spectrometry and N-terminal sequencing.	Disulfides	4-13	teratocarcinoma-derived growth factor 1 pseudogene 3	Homo sapiens	74-80
12919325-4	2003	Protein database searching and molecular modeling revealed that the pattern of disulfide linkages in the CFC domain of Cripto is the same as that in PARS intercerebralis major Peptide C (PMP-C), a serine protease inhibitor, and that the EGF-CFC domains of Cripto are predicted to be structurally homologous to the EGF-VWFC domains of the C-terminal extracellular portions of Jagged 1 and Jagged 2.	Disulfides	79-88	teratocarcinoma-derived growth factor 1 pseudogene 3	Homo sapiens	119-125
22148505-8	2012	Disulfide-bonded APE1 or APE1-TRX species were further characterized by size exclusion chromatography and found to form large complexes.	Disulfides	0-9	apurinic/apyrimidinic endodeoxyribonuclease 1	Homo sapiens	17-21
12930796-0	2003	Sodium channel beta4, a new disulfide-linked auxiliary subunit with similarity to beta2.	Disulfides	28-37	tubulin beta 3 class III	Homo sapiens	15-20
12930796-0	2003	Sodium channel beta4, a new disulfide-linked auxiliary subunit with similarity to beta2.	Disulfides	28-37	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	82-87
22505815-9	2012	The complex formation accompanied by distortion of disulfide bond within MsrB1 facilitates the reduction of oxidized MsrB1 as it is evidenced by the obtained data.	Disulfides	51-60	methionine sulfoxide reductase B1	Homo sapiens	73-78
12878193-9	2003	In addition, the analyses of porcine ZPB and ZPC fragments revealed that disulfide bonds within the ZP domains are divided into two groups, suggesting that the ZP domain consists of two subdomains.	Disulfides	73-82	zona pellucida glycoprotein 3	Homo sapiens	45-48
18846282-6	2008	We confirmed the thioredoxin-dependent reduction of a disulfide bond in CHLI2 and thiol-modulation of its ATPase activity.	Disulfides	54-63	thioredoxin H-type 1	Arabidopsis thaliana	17-28
22505815-9	2012	The complex formation accompanied by distortion of disulfide bond within MsrB1 facilitates the reduction of oxidized MsrB1 as it is evidenced by the obtained data.	Disulfides	51-60	methionine sulfoxide reductase B1	Homo sapiens	117-122
21842374-4	2012	We observed that wild-type calnexin as well as the P-domain double cysteine mutant contained an intramolecular disulfide bond which is lost when the N-domain cysteines are mutated.	Disulfides	111-120	calnexin	Homo sapiens	27-35
18809725-5	2008	Biochemical assays demonstrate that Ero1L is required for formation of disulfide bonds of three Lin12-Notch repeats (LNRs) present in the extracellular domain of Notch.	Disulfides	71-80	Endoplasmic reticulum oxidoreductin-1-like	Drosophila melanogaster	36-41
12885904-9	2003	Additionally, we show that the Cys(71) residue is required for intermolecular disulfide bond formation and describe the properties of a virus expressing an allele of A14 that cannot form disulfide-linked dimers.	Disulfides	187-196	immunoglobulin kappa variable 6D-41 (non-functional)	Homo sapiens	166-169
22645657-0	2012	Interleukin-2 signalling is modulated by a labile disulfide bond in the CD132 chain of its receptor.	Disulfides	50-59	interleukin 2 receptor subunit gamma	Homo sapiens	72-77
18710262-2	2008	The 37-residue, C-terminally amidated human amylin peptide derives from a proprotein that undergoes disulfide bond formation in the endoplasmic reticulum and is then subjected to four enzymatic processing events in the immature secretory granule.	Disulfides	100-109	islet amyloid polypeptide	Homo sapiens	44-50
22645657-3	2012	Recent studies have shown that a wide range of membrane proteins have labile disulfide bonds including CD132, the common gamma chain of the receptors for several cytokines including interleukin-2 and interleukin-4 (IL-2 and IL-4).	Disulfides	77-86	interleukin 2 receptor subunit gamma	Homo sapiens	103-108
12746437-1	2003	Retinoschisin is a 24-kDa discoidin domain-containing protein that is secreted from photoreceptor and bipolar cells as a large disulfide-linked multisubunit complex.	Disulfides	127-136	retinoschisin 1	Homo sapiens	0-13
22645657-4	2012	The Cys(183)-Cys(232) disulfide bond in mouse CD132 is susceptible to reduction by enzymes such as thioredoxin (TRX), gamma interferon-inducible lysosomal thiolreductase and protein disulfide isomerase, which are commonly secreted during immune activation.	Disulfides	22-31	interleukin 2 receptor, gamma chain	Mus musculus	46-51
22645657-6	2012	Conditions that lead to the reduction of the Cys(183)-Cys(232) disulfide bond in CD132 inhibit proliferation of an IL-2-dependent T cell clone and concomitant inhibition of the STAT-5 signalling pathway.	Disulfides	63-72	interleukin 2 receptor subunit gamma	Homo sapiens	81-86
22645657-8	2012	We postulate that reduction of the Cys(183)-Cys(232) disulfide in CD132 inhibits IL-2 binding to the receptor complex.	Disulfides	53-62	interleukin 2 receptor subunit gamma	Homo sapiens	66-71
22645657-9	2012	Published data show that the Cys(183)-Cys(232) disulfide bond is exposed at the surface of CD132 and in close contact with IL-2 and IL-4 in their respective receptor complexes.	Disulfides	47-56	interleukin 2 receptor subunit gamma	Homo sapiens	91-96
12672481-3	2003	The AChE dimers were converted into monomers by reducing the disulfide bond which links the enzyme subunits.	Disulfides	61-70	acetylcholinesterase	Mus musculus	4-8
18693759-7	2008	We conclude that the second disulfide bridge, which according to the beta2-adrenergic structure will form a covalent link across the entrance to the main ligand binding pocket, serves to dampen GPR39 activation.	Disulfides	28-37	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	69-74
22442689-6	2012	SD2 reveals a new protein fold made of loops connected by four disulfide bridges.	Disulfides	63-72	sd-2	Drosophila melanogaster	0-3
18593714-7	2008	Furthermore, we observed the exclusive formation of a thiosulfinate linkage between Prx and Srx (k = 1.4 min(-1)) that collapses to the disulfide-bonded Srx-Prx species (k = 0.14 min(-1)).	Disulfides	136-145	sulfiredoxin 1	Homo sapiens	92-95
18593714-7	2008	Furthermore, we observed the exclusive formation of a thiosulfinate linkage between Prx and Srx (k = 1.4 min(-1)) that collapses to the disulfide-bonded Srx-Prx species (k = 0.14 min(-1)).	Disulfides	136-145	sulfiredoxin 1	Homo sapiens	153-156
12819769-1	2003	The cell death-inducing serine protease granzyme A (GzmA) has a unique disulfide-linked quaternary structure.	Disulfides	71-80	granzyme A	Homo sapiens	40-50
12819769-1	2003	The cell death-inducing serine protease granzyme A (GzmA) has a unique disulfide-linked quaternary structure.	Disulfides	71-80	granzyme A	Homo sapiens	52-56
12819770-2	2003	In contrast to the related granzyme B (GzmB), GzmA forms a stable disulfide-linked homodimer and triggers target-cell death in a caspase-independent way.	Disulfides	66-75	granzyme A	Homo sapiens	46-50
21909944-1	2011	Protein disulfide isomerase (PDI) is a thiodisulfide oxidoreductase that catalyzes the formation, reduction and rearrangement of disulfide bonds in proteins of eukaryotes.	Disulfides	8-17	protein disulfide isomerase	Arabidopsis thaliana	29-32
12560222-5	2003	Cys97Ser and Cys175Ser mutants of the P2Y(12) receptor did not express when transfected into Chinese hamster ovary (CHO-K1) cells, indicating the essential nature of a disulfide bridge between these residues.	Disulfides	168-177	purinergic receptor P2Y12	Homo sapiens	38-45
12560222-11	2003	We speculate that the active metabolites of clopidogrel and CS-747 form disulfide bridges with both Cys17 and Cys270 in the P2Y(12) receptor, and thereby inactivate the receptor.	Disulfides	72-81	purinergic receptor P2Y12	Homo sapiens	124-131
18676877-1	2008	Protein disulfide isomerase (PDI) oxidizes, reduces, and isomerizes disulfide bonds, modulates redox responses, and chaperones proteins.	Disulfides	8-17	protein disulfide isomerase	Arabidopsis thaliana	29-32
18511416-9	2008	Complexes with PQ or with PRiMA contained heavy components, which migrated abnormally in SDS-PAGE but probably resulted from disulfide bonding of four AChE(T) subunits with the four upstream cysteines of the associated protein.	Disulfides	125-134	proline rich membrane anchor 1	Homo sapiens	26-31
21715714-4	2011	The ZP module is divided in two related immunoglobulin-like domains, ZP-N and ZP-C, that contain characteristic disulfide bond patterns and, in the case of ZP-C, also incorporate the EHP.	Disulfides	112-121	zona pellucida glycoprotein 3	Homo sapiens	78-82
18657506-4	2008	ROS-generating compounds, e.g., the environmental toxins menadione and beta-lapachone (in vivo IC(50) = 0.45 muM) also cause intermolecular disulfide crosslinking of SMN.	Disulfides	140-149	survival of motor neuron 1, telomeric	Homo sapiens	166-169
12522011-2	2003	Recent results with an adhesion blocking antibody (RAM.1) against GPIb beta, which is disulfide linked to GPIb alpha, have suggested a novel function of this subunit in regulating VWF-mediated platelet adhesion, possibly involving its intracellular face.	Disulfides	86-95	von Willebrand factor	Cricetulus griseus	180-183
21715714-6	2011	The structures explain several apparently contradictory observations by reconciling the variable disulfide bond patterns found in different homologues of ZP3 as well as the multiple ZP3 determinants alternatively involved in gamete interaction.	Disulfides	97-106	zona pellucida glycoprotein 3	Homo sapiens	154-157
18513323-4	2008	Furthermore, this transition seems to involve a thermodynamic equilibrium between XDH and XO; disulfide bond formation or proteolysis can then lock the enzyme in the XO form.	Disulfides	94-103	xanthine dehydrogenase	Homo sapiens	82-85
21755988-6	2011	Previous work has shown that apo-nNOS can be activated by thiol-disulfide exchange, and we show substantial activation with a small molecule dithiol modeled on the active motifs of thioredoxin and protein disulfide isomerase.	Disulfides	64-73	nitric oxide synthase 1	Homo sapiens	33-37
18480461-1	2008	Human T-cell leukemia virus (HTLV-1) Env carries a typical disulfide isomerization motif, C(225)XXC, in the C-terminal domain SU.	Disulfides	59-68	env	Human T-cell leukemia virus type I	37-40
18480461-4	2008	Next, we constructed a secreted Env ectodomain and showed that it underwent incubation-dependent intersubunit disulfide isomerization on target cells.	Disulfides	110-119	env	Human T-cell leukemia virus type I	32-35
12700266-2	2003	VirB7 assembles as a disulfide cross-linked homodimer that associates with the T pilus and a VirB7-VirB9 heterodimer that stabilizes other VirB proteins during biogenesis of the secretion machine.	Disulfides	21-30	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	0-5
21628455-0	2011	Increasing hydrophobicity or disulfide bridging at the factor VIII A1 and C2 domain interface enhances procofactor stability.	Disulfides	29-38	coagulation factor VIII	Homo sapiens	55-66
12717017-1	2003	Protein disulfide isomerase (PDI, EC 5.3.4.1), an enzyme and chaperone, catalyses disulfide bond formation and rearrangements in protein folding.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Bos taurus	29-32
20849374-3	2011	Pathways that form disulfide bonds have now been unraveled in the bacterial periplasm (disulfide bond protein A [DsbA], DsbB, DsbC, DsbG, and DsbD), the endoplasmic reticulum (protein disulfide isomerase and Ero1), and the mitochondrial intermembrane space (Mia40 and Erv1).	Disulfides	19-28	prolyl 4-hydroxylase subunit beta	Homo sapiens	176-203
12556467-2	2003	Glutaredoxin (GRx, thioltransferase) is implicated in cellular redox regulation, and it is known for specific and efficient catalysis of reduction of protein-S-S-glutathione-mixed disulfides (protein-SSG) because of its remarkably low thiol pK(a) ( approximately 3.5) and its ability to stabilize a catalytic S-glutathionyl intermediate (GRx-SSG).	Disulfides	180-190	glutaredoxin	Homo sapiens	0-12
12556467-2	2003	Glutaredoxin (GRx, thioltransferase) is implicated in cellular redox regulation, and it is known for specific and efficient catalysis of reduction of protein-S-S-glutathione-mixed disulfides (protein-SSG) because of its remarkably low thiol pK(a) ( approximately 3.5) and its ability to stabilize a catalytic S-glutathionyl intermediate (GRx-SSG).	Disulfides	180-190	glutaredoxin	Homo sapiens	14-17
12556467-2	2003	Glutaredoxin (GRx, thioltransferase) is implicated in cellular redox regulation, and it is known for specific and efficient catalysis of reduction of protein-S-S-glutathione-mixed disulfides (protein-SSG) because of its remarkably low thiol pK(a) ( approximately 3.5) and its ability to stabilize a catalytic S-glutathionyl intermediate (GRx-SSG).	Disulfides	180-190	glutaredoxin	Homo sapiens	19-35
12556467-2	2003	Glutaredoxin (GRx, thioltransferase) is implicated in cellular redox regulation, and it is known for specific and efficient catalysis of reduction of protein-S-S-glutathione-mixed disulfides (protein-SSG) because of its remarkably low thiol pK(a) ( approximately 3.5) and its ability to stabilize a catalytic S-glutathionyl intermediate (GRx-SSG).	Disulfides	180-190	glutaredoxin	Homo sapiens	338-341
12582170-2	2003	The hemagglutinin (HA) tag of wild type RPTP alpha and of constitutively dimeric, active RPTP alpha-F135C with a disulfide bond in the extracellular domain was not accessible for antibody, whereas the HA tag of constitutively dimeric, inactive RPTP alpha-P137C was.	Disulfides	113-122	protein tyrosine phosphatase receptor type A	Homo sapiens	89-99
18645017-7	2008	By two-dimensional nonreduced/reduced SDS-PAGE analysis, we also found that TUBB3 protein in vivo forms protein complexes through intermolecular disulfide bridges.	Disulfides	145-154	tubulin beta 3 class III	Homo sapiens	76-81
18600557-1	2008	Mammalian xanthine oxidoreductase can be converted from the dehydrogenase to the oxidase form, either reversibly by formation of disulfide bridges or irreversibly by proteolytic cleavage within the xanthine oxidoreductase protein molecule.	Disulfides	129-138	xanthine dehydrogenase	Homo sapiens	10-33
18331351-9	2008	The formation of the PDI-alpha(V)beta(3) stoichiometric complex was further demonstrated by surface plasmon resonance analysis, which showed that the initial reversible binding of PDI becomes irreversible in the presence of Mn(2+), probably mediated by disulfide bonds.	Disulfides	253-262	prolyl 4-hydroxylase subunit beta	Homo sapiens	21-24
18331351-9	2008	The formation of the PDI-alpha(V)beta(3) stoichiometric complex was further demonstrated by surface plasmon resonance analysis, which showed that the initial reversible binding of PDI becomes irreversible in the presence of Mn(2+), probably mediated by disulfide bonds.	Disulfides	253-262	prolyl 4-hydroxylase subunit beta	Homo sapiens	180-183
12582170-2	2003	The hemagglutinin (HA) tag of wild type RPTP alpha and of constitutively dimeric, active RPTP alpha-F135C with a disulfide bond in the extracellular domain was not accessible for antibody, whereas the HA tag of constitutively dimeric, inactive RPTP alpha-P137C was.	Disulfides	113-122	protein tyrosine phosphatase receptor type A	Homo sapiens	89-99
12582175-4	2003	Here we report that two subunits of mammalian GPI transamidase, GPI8 and PIG-T, form a functionally important disulfide bond between conserved cysteine residues.	Disulfides	110-119	phosphatidylinositol glycan anchor biosynthesis class K	Sus scrofa	46-62
12582175-9	2003	Furthermore trypanosome GPI8 forms a similar intermolecular disulfide bond via its conserved cysteine residue, suggesting that the trypanosome GPI transamidase is also a multimeric complex likely containing the orthologue of PIG-T.	Disulfides	60-69	phosphatidylinositol glycan anchor biosynthesis class K	Sus scrofa	143-159
12680754-8	2003	The effects of intermolecular disulfide bond formation in the SP-B(1-25) dimer were also investigated.	Disulfides	30-39	surfactant protein B	Homo sapiens	62-66
12680754-9	2003	The experiments suggest that the SP-B helix A has to rotate at an angle to form a disulfide bond with the neighboring cysteine, which makes the hydrophobic sides of the amphipathic helices face each other, thus forming a hydrophobic domain.	Disulfides	82-91	surfactant protein B	Homo sapiens	33-37
17936362-1	2008	Cell surface and growth-related NADH oxidases with protein disulfide-thiol interchange activity, ECTO-NOX, exhibit copper-dependent, clock-related, temperature-independent and entrainable patterns of regular oscillations in the rate of oxidation of NAD(P)H as do aqueous solutions of copper salts.	Disulfides	59-68	tripartite motif containing 33	Homo sapiens	97-101
20919935-5	2011	In PTPs, the initially generated sulfenic acid residues have the potential to undergo secondary reactions with a neighboring amide nitrogen or cysteine thiol residue to yield a sulfenyl amide or disulfide, respectively.	Disulfides	195-204	6-pyruvoyltetrahydropterin synthase	Homo sapiens	3-7
21553912-4	2011	To gain such insights into the disulfide-less GLTP fold, we investigated the effect of a change in pH on the fungal HET-C2 GLTP fold by taking advantage of its two tryptophans and four tyrosines (compared to three tryptophans and 10 tyrosines in human GLTP).	Disulfides	31-40	glycolipid transfer protein	Homo sapiens	46-50
17692377-2	2008	It contains three genetically distinct subunits; C8alpha and C8gamma form a disulfide-linked C8alpha-gamma heterodimer that is noncovalently associated with C8beta.	Disulfides	76-85	complement C8 beta chain	Homo sapiens	157-163
17956189-3	2008	The protein disulfide isomerase (PDI) is the eukaryotic factor that catalyzes oxidative protein folding in the endoplasmic reticulum; by contrast, in prokaryotes, a family of disulfide bond (Dsb) proteins have an equivalent outcome in the bacterial periplasm.	Disulfides	12-21	prolyl 4-hydroxylase subunit beta	Homo sapiens	33-36
12667078-3	2003	Expression of LEKTI in Sf9 cells showed the presence of disulfide bonds, suggesting the maintenance of the tertiary protein structure.	Disulfides	56-65	serine peptidase inhibitor Kazal type 5	Homo sapiens	14-19
12538003-0	2003	The design of potent hydrazones and disulfides as cathepsin S inhibitors.	Disulfides	36-46	cathepsin S	Homo sapiens	50-61
21553912-4	2011	To gain such insights into the disulfide-less GLTP fold, we investigated the effect of a change in pH on the fungal HET-C2 GLTP fold by taking advantage of its two tryptophans and four tyrosines (compared to three tryptophans and 10 tyrosines in human GLTP).	Disulfides	31-40	glycolipid transfer protein	Homo sapiens	123-127
21553912-4	2011	To gain such insights into the disulfide-less GLTP fold, we investigated the effect of a change in pH on the fungal HET-C2 GLTP fold by taking advantage of its two tryptophans and four tyrosines (compared to three tryptophans and 10 tyrosines in human GLTP).	Disulfides	31-40	glycolipid transfer protein	Homo sapiens	123-127
21435343-1	2011	Protein disulfide isomerase (PDI) has an essential role in the process of disulfide bond formation, where it catalyzes disulfide bond formation, reduction, and isomerization.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
12486139-0	2003	Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase.	Disulfides	56-65	prolyl 4-hydroxylase subunit beta	Homo sapiens	83-110
12486139-1	2003	Protein-disulfide isomerase (PDI) catalyzes the formation and isomerization of disulfides during oxidative protein folding.	Disulfides	79-89	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
12486139-1	2003	Protein-disulfide isomerase (PDI) catalyzes the formation and isomerization of disulfides during oxidative protein folding.	Disulfides	79-89	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
12486139-7	2003	Escape also reduces the substrate, and if it is invoked frequently, disulfide isomerization will involve cycles of reduction and reoxidation in preference to intramolecular isomerization of the PDI-bound substrate.	Disulfides	68-77	prolyl 4-hydroxylase subunit beta	Homo sapiens	194-197
12486139-11	2003	These rapid cycles of PDI oxidation and reduction suggest that PDI catalyzes isomerization by trial and error, reducing disulfides and oxidizing them in a different configuration.	Disulfides	120-130	prolyl 4-hydroxylase subunit beta	Homo sapiens	22-25
12486139-11	2003	These rapid cycles of PDI oxidation and reduction suggest that PDI catalyzes isomerization by trial and error, reducing disulfides and oxidizing them in a different configuration.	Disulfides	120-130	prolyl 4-hydroxylase subunit beta	Homo sapiens	63-66
17961071-5	2008	For example, protein disulfide isomerase (PDI) can provide neuroprotection from misfolded proteins or endoplasmic reticulum stress through its molecular chaperone and thiol-disulfide oxidoreductase activities.	Disulfides	21-30	prolyl 4-hydroxylase subunit beta	Homo sapiens	42-45
17959606-6	2007	This work provides in situ validation of the concept that thioredoxin-dependent reduction of the gamma-subunit regulatory disulfide modulates the proton electrochemical potential energy requirement for activation of the chloroplast ATP synthase and that the activation state of the ATP synthase can limit leaf level photosynthesis.	Disulfides	122-131	thioredoxin H-type 1	Arabidopsis thaliana	58-69
12486139-13	2003	In the absence of a redox buffer, these steady-state reduction-oxidation cycles can balance the redox state of PDI and support effective catalysis of disulfide isomerization.	Disulfides	150-159	prolyl 4-hydroxylase subunit beta	Homo sapiens	111-114
21435343-1	2011	Protein disulfide isomerase (PDI) has an essential role in the process of disulfide bond formation, where it catalyzes disulfide bond formation, reduction, and isomerization.	Disulfides	74-83	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
12589762-2	2003	Native RC-RNase 4 (RNase 4), consisting of 106 residues linked with four disulfide bridges, is a cytotoxic ribonuclease isolated from oocytes of bullfrog Rana catesbeiana.	Disulfides	73-82	ribonuclease A family member 4	Bos taurus	10-17
12589762-2	2003	Native RC-RNase 4 (RNase 4), consisting of 106 residues linked with four disulfide bridges, is a cytotoxic ribonuclease isolated from oocytes of bullfrog Rana catesbeiana.	Disulfides	73-82	ribonuclease A family member 4	Bos taurus	19-26
17931362-5	2007	Our data suggest that oligomerization of occludin involves disulfide bond formation within transmembrane regions, and that assembly of the TJ oligomeric protein complex is facilitated by an oligomeric caveolin scaffold.	Disulfides	59-68	occludin	Rattus norvegicus	41-49
17958379-0	2007	Transporter-to-trap conversion: a disulfide bond formation in cellular retinoic acid binding protein I mutant triggered by retinoic acid binding irreversibly locks the ligand inside the protein.	Disulfides	34-43	cellular retinoic acid binding protein 1	Homo sapiens	62-102
17958379-4	2007	We designed and expressed a CRABP I mutant (A35C/T57C), in which a small-scale conformational switch caused by the ligand binding event triggers formation of a disulfide bond in the portal region, thereby arresting structural fluctuations and effectively locking the ligand inside the binding cavity.	Disulfides	160-169	cellular retinoic acid binding protein 1	Homo sapiens	28-35
21435343-1	2011	Protein disulfide isomerase (PDI) has an essential role in the process of disulfide bond formation, where it catalyzes disulfide bond formation, reduction, and isomerization.	Disulfides	74-83	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
17702751-5	2007	In general view, the folding of proteins with nonconsecutive disulfides requires the protein disulfide isomerase DsbC.	Disulfides	61-71	putative protein DsbC	Escherichia coli	113-117
12565167-1	2003	ECTO-NOX protein"s are cell surface-associated and growth-related hydroquinone oxidases with both protein disulfide-thiol interchange activity and the capacity to oxidize NAD(P)H. The activities of these ECTO-NOX proteins are not steady state but fluctuate to create a repeating pattern of oscillations.	Disulfides	106-115	tripartite motif containing 33	Homo sapiens	0-4
12565167-1	2003	ECTO-NOX protein"s are cell surface-associated and growth-related hydroquinone oxidases with both protein disulfide-thiol interchange activity and the capacity to oxidize NAD(P)H. The activities of these ECTO-NOX proteins are not steady state but fluctuate to create a repeating pattern of oscillations.	Disulfides	106-115	tripartite motif containing 33	Homo sapiens	204-208
17702751-10	2007	Under the more oxidizing conditions of dsb(-) strains, DsbC becomes necessary to correct non-native disulfides, but it cannot substitute for DsbA.	Disulfides	100-110	putative protein DsbC	Escherichia coli	55-59
21435343-2	2011	It is thought that the major route for oxidizing dithiols in folding proteins to disulfides is via Ero1-mediated oxidation of PDI.	Disulfides	81-91	prolyl 4-hydroxylase subunit beta	Homo sapiens	126-129
17666395-6	2007	We found that Dorfin ubiquitylated mutant SOD1 by recognizing the Cys(6)- and Cys(111)-disulfide cross-linked form and targeted it for proteasomal degradation.	Disulfides	87-96	ring finger protein 19A	Mus musculus	14-20
21435343-8	2011	The data generated here on the rapid reactivity of PDI towards glutathione suggest that reevaluation is required for several aspects of the field of catalyzed disulfide bond formation, including the potential physiological role of glutathione.	Disulfides	159-168	prolyl 4-hydroxylase subunit beta	Homo sapiens	51-54
21266296-9	2011	Conversely, hIAPP is highly disordered in the C-terminal region, presenting transient isolated beta-strand conformations, particularly at higher temperatures and when the natural disulfide bond is present.	Disulfides	179-188	islet amyloid polypeptide	Homo sapiens	12-17
17713902-9	2007	Oxygenation of the copper(I) complex derived from BIT(OMe,SCPh3) ligand 12 produces a novel dinuclear disulfide complex, [(BIT(OMe,S)2Cu2(mu-OH)2](PF6)2 (17), which is structurally characterized.	Disulfides	102-111	sperm associated antigen 17	Homo sapiens	147-150
12600944-6	2003	The sensing of both stresses requires two cysteine residues within the HSF1 DNA-binding domain that are engaged in redox-sensitive disulfide bonds.	Disulfides	131-140	heat shock transcription factor 1	Homo sapiens	71-75
12547204-5	2003	The ease with which the hPrP structure can accommodate a variety of locations for a second disulfide bond within the presumed protein X-binding epitope suggests a functional role for the extensive perturbation by a natural second disulfide bond of the corresponding region in the human doppel protein.	Disulfides	91-100	prion like protein doppel	Homo sapiens	286-292
21634027-3	2011	During episodes of crisis, ISCs accumulate C284-C373 intramolecularly disulfide bonded actin, which reduces actin filament dynamics.	Disulfides	70-79	NFS1 cysteine desulfurase	Homo sapiens	27-31
21569239-7	2011	The unique feature of F-spondin FS domain is the presence of three disulfide bonds associated with the N- and C-termini of the domain and a highly conserved N-linked glycosylation site.	Disulfides	67-76	spondin 1	Homo sapiens	22-31
12421832-3	2003	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.	Disulfides	74-83	pappalysin 1	Homo sapiens	0-6
12421832-3	2003	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.	Disulfides	74-83	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	130-160
12421832-3	2003	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.	Disulfides	74-83	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	162-169
12421832-3	2003	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.	Disulfides	74-83	pappalysin 1	Homo sapiens	228-234
17540777-3	2007	The integrin recognizes a tripeptide motif in a small disulfide-bonded loop at the N terminus of the lectin head region of CD23, centered around Arg(172), Lys(173), and Cys(174) (RKC).	Disulfides	54-63	Fc epsilon receptor II	Homo sapiens	123-127
12421832-9	2003	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.	Disulfides	56-65	pappalysin 1	Homo sapiens	24-30
21398518-0	2011	Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI).	Disulfides	39-48	prolyl 4-hydroxylase subunit beta	Homo sapiens	97-124
12421832-9	2003	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.	Disulfides	100-110	myelin basic protein	Homo sapiens	76-79
12421832-9	2003	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.	Disulfides	100-110	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	72-79
12421832-9	2003	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.	Disulfides	100-109	myelin basic protein	Homo sapiens	76-79
12498799-0	2003	DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo.	Disulfides	67-76	putative protein DsbC	Escherichia coli	9-13
12498799-6	2003	DsbC catalyzes folding of RBI under all redox conditions in vitro, but is particularly efficient in rearranging buried, non-native disulfide bonds formed under oxidizing conditions.	Disulfides	131-140	putative protein DsbC	Escherichia coli	0-4
12498799-11	2003	This shows that DsbC is the bacterial enzyme of choice for improving the periplasmic folding yields of proteins with very complex disulfide bond patterns.	Disulfides	130-139	putative protein DsbC	Escherichia coli	16-20
17540772-7	2007	Oxidized HO-2, which contains an intramolecular disulfide bond linking Cys(265) of HRM1 and Cys(282) of HRM2, binds heme tightly.	Disulfides	48-57	heme oxygenase 2	Homo sapiens	9-13
17540772-10	2007	Because HO-2 plays a key role in CO generation and heme homeostasis, reduction of the disulfide bond would be expected to increase intracellular free heme and decrease CO concentrations.	Disulfides	86-95	heme oxygenase 2	Homo sapiens	8-12
17540772-11	2007	Thus, we propose that the HRMs in HO-2 constitute a thiol/disulfide redox switch that regulates the myriad physiological functions of HO-2, including its involvement in the hypoxic response in the carotid body, which involves interactions with a Ca(2+)-activated potassium channel.	Disulfides	58-67	heme oxygenase 2	Homo sapiens	34-38
17540772-11	2007	Thus, we propose that the HRMs in HO-2 constitute a thiol/disulfide redox switch that regulates the myriad physiological functions of HO-2, including its involvement in the hypoxic response in the carotid body, which involves interactions with a Ca(2+)-activated potassium channel.	Disulfides	58-67	heme oxygenase 2	Homo sapiens	134-138
17580966-2	2007	One of these, cysteine 85 that could form intermolecular disulfide bonds, is present in SP-A1 (Cys85) and absent in SP-A2 (Arg85).	Disulfides	57-66	surfactant protein A1	Homo sapiens	88-93
21398518-0	2011	Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI).	Disulfides	39-48	prolyl 4-hydroxylase subunit beta	Homo sapiens	126-129
21398518-5	2011	ERO1alpha associated preferentially with reduced PDI, explaining the stepwise disulfide shuttle mechanism, first from ERO1alpha to PDI and then from oxidized PDI to an unfolded polypeptide bound to its hydrophobic pocket.	Disulfides	78-87	prolyl 4-hydroxylase subunit beta	Homo sapiens	49-52
19636846-1	2007	Protein disulfide isomerase (PDI) participates in protein folding and catalyses formation of disulfide bonds.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
21398518-5	2011	ERO1alpha associated preferentially with reduced PDI, explaining the stepwise disulfide shuttle mechanism, first from ERO1alpha to PDI and then from oxidized PDI to an unfolded polypeptide bound to its hydrophobic pocket.	Disulfides	78-87	prolyl 4-hydroxylase subunit beta	Homo sapiens	131-134
21398518-5	2011	ERO1alpha associated preferentially with reduced PDI, explaining the stepwise disulfide shuttle mechanism, first from ERO1alpha to PDI and then from oxidized PDI to an unfolded polypeptide bound to its hydrophobic pocket.	Disulfides	78-87	prolyl 4-hydroxylase subunit beta	Homo sapiens	131-134
12507971-2	2003	Furthermore, some partially degraded forms of hCG and its subunits have become of potential clinical importance, e.g., "nicked" forms of hCG (hCGn) and hCGbeta (hCGbetan), which contain cuts in the peptide backbone between amino acids 44-45 or 47-48 in hCGbeta, and a fragment of hCGbeta (hCGbetacf) consisting of amino acids 6-40 and 55-92 bound together by disulfide bridges.	Disulfides	359-368	glycoprotein hormones, alpha polypeptide	Homo sapiens	46-49
21277937-7	2011	The Tyr108Cys mutant forms an aberrant disulfide bridge that prevents formation of the required Cys14-Cys200 bridge essential for GnRHR plasma membrane expression.	Disulfides	39-48	gonadotropin releasing hormone receptor	Homo sapiens	130-135
12507971-2	2003	Furthermore, some partially degraded forms of hCG and its subunits have become of potential clinical importance, e.g., "nicked" forms of hCG (hCGn) and hCGbeta (hCGbetan), which contain cuts in the peptide backbone between amino acids 44-45 or 47-48 in hCGbeta, and a fragment of hCGbeta (hCGbetacf) consisting of amino acids 6-40 and 55-92 bound together by disulfide bridges.	Disulfides	359-368	glycoprotein hormones, alpha polypeptide	Homo sapiens	137-140
12507971-2	2003	Furthermore, some partially degraded forms of hCG and its subunits have become of potential clinical importance, e.g., "nicked" forms of hCG (hCGn) and hCGbeta (hCGbetan), which contain cuts in the peptide backbone between amino acids 44-45 or 47-48 in hCGbeta, and a fragment of hCGbeta (hCGbetacf) consisting of amino acids 6-40 and 55-92 bound together by disulfide bridges.	Disulfides	359-368	cingulin	Homo sapiens	142-146
17604546-2	2007	SOSIP gp140 is a soluble, proteolytically mature form of the HIV-1 envelope wherein gp120-gp41 interactions are stabilized via a disulfide bond and gp41 contains an additional trimer-stabilizing point mutation.	Disulfides	129-138	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	84-89
12485997-1	2002	Protein disulfide isomerase (PDI) is a multifunctional protein catalysing the formation of disulfide bonds, acting as a molecular chaperone and being a component of the enzymes prolyl 4-hydroxylase (P4H) and microsomal triglyceride transfer protein.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
17399679-1	2007	The cardiac hormone B-type natriuretic peptide (BNP) is synthesized as a prepro 134 residue molecule which is further proteolytically processed into a 76 residue fragment termed N-terminal proBNP (NT-proBNP) and the active portion of this hormone, a 32-residue disulfide-linked peptide (BNP-32).	Disulfides	261-270	natriuretic peptide B	Homo sapiens	20-46
21544205-3	2011	Here we studied the organization of the amino terminal domain (ATD) of the rat GluN1/GluN2A and GluN1/GluN2B NMDA receptors by cysteine-directed, disulfide bond-mediated cross-linking.	Disulfides	146-155	glutamate ionotropic receptor NMDA type subunit 1	Rattus norvegicus	79-84
17399679-1	2007	The cardiac hormone B-type natriuretic peptide (BNP) is synthesized as a prepro 134 residue molecule which is further proteolytically processed into a 76 residue fragment termed N-terminal proBNP (NT-proBNP) and the active portion of this hormone, a 32-residue disulfide-linked peptide (BNP-32).	Disulfides	261-270	natriuretic peptide B	Homo sapiens	48-51
12450397-4	2002	Under oxidizing conditions, C(N)- and C(N)C(C)-apoC-II formed a highly tangled network of fibrils, suggesting that the addition of an N-terminal cysteine to apoC-II promotes interfibril disulfide cross-links.	Disulfides	186-195	apolipoprotein C2	Homo sapiens	47-54
12450397-4	2002	Under oxidizing conditions, C(N)- and C(N)C(C)-apoC-II formed a highly tangled network of fibrils, suggesting that the addition of an N-terminal cysteine to apoC-II promotes interfibril disulfide cross-links.	Disulfides	186-195	apolipoprotein C2	Homo sapiens	157-164
21544205-3	2011	Here we studied the organization of the amino terminal domain (ATD) of the rat GluN1/GluN2A and GluN1/GluN2B NMDA receptors by cysteine-directed, disulfide bond-mediated cross-linking.	Disulfides	146-155	glutamate ionotropic receptor NMDA type subunit 1	Rattus norvegicus	96-101
12239218-8	2002	The formation of at least one of the disulfide bonds in the CD1d heavy chain is coupled to its glucose trimming-dependent association with ERp57, calnexin, and calreticulin.	Disulfides	37-46	calnexin	Homo sapiens	146-154
12361711-4	2002	The method is based on the specific reduction of mixed disulfides by glutaredoxin, their reaction with N-ethylmaleimide-biotin, affinity purification of tagged proteins, and identification by proteomic analysis.	Disulfides	55-65	glutaredoxin	Homo sapiens	69-81
17475865-6	2007	The main isoform of C4BP contains seven identical alpha-chains and one beta-chain linked together with disulfide bridges.	Disulfides	103-112	complement component 4 binding protein, alpha	Rattus norvegicus	20-24
21544205-4	2011	We found that GluN1 ATDs and GluN2 ATDs spontaneously formed disulfide bond-mediated dimers after introducing cysteines into the L1 interface of GluN2A or GluN2B ATD.	Disulfides	61-70	glutamate ionotropic receptor NMDA type subunit 1	Rattus norvegicus	14-19
17379186-2	2007	In our recent study, the reduced nonessential disulfide (-CESC-), which is structurally homologous to the active-site motif (-CGPC-) of thioredoxin, was shown to have thioredoxin-like activity.	Disulfides	46-55	thioredoxin	Bos taurus	136-147
21355578-3	2011	Two cysteine residues in HMGB1 domain A form a reversible disulfide bond under mildly oxidizing conditions.	Disulfides	58-67	high mobility group box 1	Homo sapiens	25-30
17379186-2	2007	In our recent study, the reduced nonessential disulfide (-CESC-), which is structurally homologous to the active-site motif (-CGPC-) of thioredoxin, was shown to have thioredoxin-like activity.	Disulfides	46-55	thioredoxin	Bos taurus	167-178
17385906-8	2007	Although formation of the disulfide dimer takes place only for Ca2+-loaded recoverin, accumulation of the oxidized monomer proceeds more effectively for apo-recoverin.	Disulfides	26-35	recoverin	Homo sapiens	75-84
12393260-6	2002	Moreover, it was secreted into the medium and then was cleaved to form disulfide-linked fragments, one of which was 30 kDa, similar to C1s, suggesting its processing in the extracellular space.	Disulfides	71-80	complement C1s	Rattus norvegicus	135-138
12359323-1	2002	Apolipoprotein(a) (Apo(a)) is a glycoprotein that is linked by a disulfide bond to apolipoprotein B on low density lipoprotein particles to form lipoprotein(a) (Lp(a)).	Disulfides	65-74	lipoprotein(a)	Homo sapiens	0-17
12359323-1	2002	Apolipoprotein(a) (Apo(a)) is a glycoprotein that is linked by a disulfide bond to apolipoprotein B on low density lipoprotein particles to form lipoprotein(a) (Lp(a)).	Disulfides	65-74	lipoprotein(a)	Homo sapiens	19-25
12359323-1	2002	Apolipoprotein(a) (Apo(a)) is a glycoprotein that is linked by a disulfide bond to apolipoprotein B on low density lipoprotein particles to form lipoprotein(a) (Lp(a)).	Disulfides	65-74	lipoprotein(a)	Homo sapiens	3-17
12359323-1	2002	Apolipoprotein(a) (Apo(a)) is a glycoprotein that is linked by a disulfide bond to apolipoprotein B on low density lipoprotein particles to form lipoprotein(a) (Lp(a)).	Disulfides	65-74	lipoprotein(a)	Homo sapiens	161-166
21355578-5	2011	The binding affinities of singly and doubly mutated HMGB1 domain A, respectively deficient in one or both cysteine residues that form the disulfide bond, are unaffected by changes in external redox conditions.	Disulfides	138-147	high mobility group box 1	Homo sapiens	52-57
12270713-4	2002	This enzyme catalyzes the formation of disulfide bonds in CNX and CRT-bound glycoprotein substrates.	Disulfides	39-48	calnexin	Homo sapiens	58-61
17301129-7	2007	Further characterization showed the intermonomer disulfide bond to be a target for PDI processing.	Disulfides	49-58	prolyl 4-hydroxylase subunit beta	Homo sapiens	83-86
21355578-6	2011	The redox-dependent nature of the binding of HMGB1 domain A to cisplatin-modified DNA suggests that formation of the intradomain disulfide bond induces a conformational change that disfavors binding to cisplatin-modified DNA.	Disulfides	129-138	high mobility group box 1	Homo sapiens	45-50
21238616-0	2011	Both PDI and PDIp can attack the native disulfide bonds in thermally-unfolded RNase and form stable disulfide-linked complexes.	Disulfides	40-49	prolyl 4-hydroxylase subunit beta	Homo sapiens	5-8
21238616-0	2011	Both PDI and PDIp can attack the native disulfide bonds in thermally-unfolded RNase and form stable disulfide-linked complexes.	Disulfides	100-109	prolyl 4-hydroxylase subunit beta	Homo sapiens	5-8
21238616-1	2011	Protein disulfide isomerase (PDI) and its pancreatic homolog (PDIp) are folding catalysts for the formation, reduction, and/or isomerization of disulfide bonds in substrate proteins.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
12214861-2	2002	The oligomerization of bovine Tg are intermolecular reactions that occur through oxidative processes, such as disulfide and dityrosine formation, as well as isopeptide formation; disulfide formation is primarily responsible for Tg oligomerization.	Disulfides	110-119	thyroglobulin	Bos taurus	30-32
17255099-0	2007	Engineering a disulfide bond to stabilize the calcium-binding loop of activated protein C eliminates its anticoagulant but not its protective signaling properties.	Disulfides	14-23	APC regulator of WNT signaling pathway	Homo sapiens	70-89
21238616-2	2011	However, the question as to whether PDI and PDIp can directly attack the native disulfide bonds in substrate proteins is still not answered, which is the subject of the present study.	Disulfides	80-89	prolyl 4-hydroxylase subunit beta	Homo sapiens	36-39
12214861-2	2002	The oligomerization of bovine Tg are intermolecular reactions that occur through oxidative processes, such as disulfide and dityrosine formation, as well as isopeptide formation; disulfide formation is primarily responsible for Tg oligomerization.	Disulfides	179-188	thyroglobulin	Bos taurus	30-32
12214861-2	2002	The oligomerization of bovine Tg are intermolecular reactions that occur through oxidative processes, such as disulfide and dityrosine formation, as well as isopeptide formation; disulfide formation is primarily responsible for Tg oligomerization.	Disulfides	179-188	thyroglobulin	Bos taurus	228-230
21238616-5	2011	The alkylated PDI and PDIp, which are devoid of enzymatic activities, cannot inactivate RNase, suggesting that the inactivation of RNase results from the disruption of its native disulfide bonds catalyzed by the enzymatic activities of PDI/PDIp.	Disulfides	179-188	prolyl 4-hydroxylase subunit beta	Homo sapiens	14-17
12214861-10	2002	Based on these results, it is proposed that PDI catalyzes the oligomerization of Tg through the disulfide linkage and its deoligomerization in the molecular fate, and this process may require a specific molecular form of Tg, optimally unfolded/reduced, in a proper redox state.	Disulfides	96-105	prolyl 4-hydroxylase subunit beta	Bos taurus	44-47
12214861-10	2002	Based on these results, it is proposed that PDI catalyzes the oligomerization of Tg through the disulfide linkage and its deoligomerization in the molecular fate, and this process may require a specific molecular form of Tg, optimally unfolded/reduced, in a proper redox state.	Disulfides	96-105	thyroglobulin	Bos taurus	81-83
21238616-6	2011	In support of this suggestion, we show that both PDI and PDIp form stable disulfide-linked complexes only with thermally-unfolded RNase, and RNase in the complexes can be released and reactivated dependently of the redox conditions used.	Disulfides	74-83	prolyl 4-hydroxylase subunit beta	Homo sapiens	49-52
17196658-4	2007	Sea bass IL-12 p40 and p35 conserve most cysteines involved in the intra-chain disulfide bonds of human IL-12 subunits as well as the important structural residues for human IL-12 heterodimerization.	Disulfides	79-88	interleukin 9	Homo sapiens	15-18
21238616-8	2011	These data indicate that PDI and PDIp can perform thiol-disulfide exchange reactions with native disulfide bonds in unfolded RNase via formation of stable disulfide-linked complexes, and from these complexes RNase is further released.	Disulfides	56-65	prolyl 4-hydroxylase subunit beta	Homo sapiens	25-28
17135266-8	2007	Then Cys(202) forms a disulfide bond with the second recycling cysteine Cys(196) that is preferentially reduced by thioredoxin.	Disulfides	22-31	thioredoxin	Bos taurus	115-126
12011044-4	2002	Scrambled RNase A (scRNase A), a misfolded protein, only slowly refolds spontaneously into an active form because of the rate-limiting unfolding of misfolded disulfide isomers.	Disulfides	158-167	ribonuclease A family member 1, pancreatic	Homo sapiens	10-17
12119363-3	2002	Dissection of the degradation process revealed that upon release from calnexin, extensively oxidized BACE457 transiently entered in disulfide-bonded complexes associated with the lumenal chaperones BiP and protein disulfide isomerase (PDI) before unfolding and dislocation into the cytosol for degradation.	Disulfides	132-141	prolyl 4-hydroxylase subunit beta	Homo sapiens	206-233
21238616-8	2011	These data indicate that PDI and PDIp can perform thiol-disulfide exchange reactions with native disulfide bonds in unfolded RNase via formation of stable disulfide-linked complexes, and from these complexes RNase is further released.	Disulfides	97-106	prolyl 4-hydroxylase subunit beta	Homo sapiens	25-28
17137590-0	2007	A novel disulfide bond in the SH2 Domain of the C-terminal Src kinase controls catalytic activity.	Disulfides	8-17	C-terminal Src kinase	Homo sapiens	48-69
17137590-1	2007	The SH2 domain of the C-terminal Src kinase [Csk] contains a unique disulfide bond that is not present in other known SH2 domains.	Disulfides	68-77	C-terminal Src kinase	Homo sapiens	22-43
21238616-8	2011	These data indicate that PDI and PDIp can perform thiol-disulfide exchange reactions with native disulfide bonds in unfolded RNase via formation of stable disulfide-linked complexes, and from these complexes RNase is further released.	Disulfides	97-106	prolyl 4-hydroxylase subunit beta	Homo sapiens	25-28
17137590-1	2007	The SH2 domain of the C-terminal Src kinase [Csk] contains a unique disulfide bond that is not present in other known SH2 domains.	Disulfides	68-77	C-terminal Src kinase	Homo sapiens	45-48
21242306-4	2011	Exposure of U2OS osteosarcoma cells with low levels of intrinsic ROS to hydrogen peroxide (H(2)O(2)) induces thiol-reversible disulfide bond-mediated oligomerization of NS.	Disulfides	126-135	G protein nucleolar 3	Homo sapiens	169-171
17137590-3	2007	The kinase activity of full-length Csk decreases by an order of magnitude upon formation of the disulfide bond in the distal SH2 domain.	Disulfides	96-105	C-terminal Src kinase	Homo sapiens	35-38
17098255-4	2007	Like other CysGPxs with thioredoxin peroxidase activity, Drosophila melanogaster (Dm)GPx oxidized by H(2)O(2) contained an intra-molecular disulfide bridge between the active-site cysteine (C45; C(P)) and C91.	Disulfides	139-148	PHGPx	Drosophila melanogaster	14-17
11914370-5	2002	Size exclusion chromatography showed that disulfide bond formation reduced the hydrodynamic volume of the enzyme, and two-dimensional gel electrophoresis of chymotrypsin-digested XO showed significant, disulfide bond-mediated, conformational heterogeneity in the N-terminal third of the enzyme but no evidence of disulfide bonds between the N-terminal and C-terminal regions or between XOR subunits.	Disulfides	42-51	xanthine dehydrogenase	Homo sapiens	386-389
11914370-5	2002	Size exclusion chromatography showed that disulfide bond formation reduced the hydrodynamic volume of the enzyme, and two-dimensional gel electrophoresis of chymotrypsin-digested XO showed significant, disulfide bond-mediated, conformational heterogeneity in the N-terminal third of the enzyme but no evidence of disulfide bonds between the N-terminal and C-terminal regions or between XOR subunits.	Disulfides	202-211	xanthine dehydrogenase	Homo sapiens	386-389
11914370-5	2002	Size exclusion chromatography showed that disulfide bond formation reduced the hydrodynamic volume of the enzyme, and two-dimensional gel electrophoresis of chymotrypsin-digested XO showed significant, disulfide bond-mediated, conformational heterogeneity in the N-terminal third of the enzyme but no evidence of disulfide bonds between the N-terminal and C-terminal regions or between XOR subunits.	Disulfides	202-211	xanthine dehydrogenase	Homo sapiens	386-389
11914370-6	2002	These results indicate that intrasubunit disulfide bond formation leads to a global conformational change in XOR that results in the exposure of the region surrounding Phe560.	Disulfides	41-50	xanthine dehydrogenase	Homo sapiens	109-112
12009892-5	2002	Gel electrophoretic studies on LRAT in the presence of SDS and disulfide reducing agents show the expected 25 kDa monomer.	Disulfides	63-72	lecithin retinol acyltransferase	Homo sapiens	31-35
12009892-9	2002	The experiments suggest that LRAT monomers interact in membranes and form functional homodimers through protein-protein interactions and disulfide bond formation.	Disulfides	137-146	lecithin retinol acyltransferase	Homo sapiens	29-33
21210651-8	2011	Furthermore, the intramolecular linkage C199-C210 reveals itself as a correct disulfide pairing in the precursor protein, the finding not inferred from closely related family members IGFBP-4 and -6.	Disulfides	78-87	insulin-like growth factor binding protein 4	Rattus norvegicus	183-197
11982363-1	2002	RNase A, a model protein for oxidative folding studies, has four native disulfide bonds.	Disulfides	72-81	ribonuclease A family member 1, pancreatic	Homo sapiens	0-7
11982363-6	2002	The application of this method enabled us to populate and, in turn, study the key intermediates with two native disulfide bonds on the oxidative folding pathway of RNase A; it also facilitated the isolation of des [58-110] and des [26-84], the other two native-like structured des species whose isolation had thus far not been possible.	Disulfides	112-121	ribonuclease A family member 1, pancreatic	Homo sapiens	164-171
17028145-2	2007	Here, we engineer single disulfide bonds into four different locations of the human cardiac titin module (I27) to control the contour length while keeping the distance to the transition state unchanged.	Disulfides	25-34	titin	Homo sapiens	92-97
20812781-5	2011	We review recent results that define a mechanism for how thiol/disulfide redox switches that control heme binding can regulate the activities of an enzyme, heme oxygenase-2, and an ion channel, the BK potassium channel.	Disulfides	63-72	heme oxygenase 2	Homo sapiens	156-172
17507765-4	2007	Here, we show that the mouse homologue of ARMET is an 18-kDa soluble ER protein that is mature after cleavage of a signal sequence and has four intramolecular disulfide bonds, including two in CXXC sequences.	Disulfides	159-168	mesencephalic astrocyte-derived neurotrophic factor	Mus musculus	42-47
17059431-1	2007	BACKGROUND: Genetically engineered disulfide bonds in B-domain-deleted factor (F) VIII variants (C662-C1828 FVIII and C664-C1826 FVIII) improve FVIIIa stability by blocking A2 domain dissociation because the new disulfide covalently links the A2 and A3 domains in FVIIIa.	Disulfides	35-44	coagulation factor VIII	Homo sapiens	108-113
17059431-1	2007	BACKGROUND: Genetically engineered disulfide bonds in B-domain-deleted factor (F) VIII variants (C662-C1828 FVIII and C664-C1826 FVIII) improve FVIIIa stability by blocking A2 domain dissociation because the new disulfide covalently links the A2 and A3 domains in FVIIIa.	Disulfides	35-44	coagulation factor VIII	Homo sapiens	129-134
17059431-1	2007	BACKGROUND: Genetically engineered disulfide bonds in B-domain-deleted factor (F) VIII variants (C662-C1828 FVIII and C664-C1826 FVIII) improve FVIIIa stability by blocking A2 domain dissociation because the new disulfide covalently links the A2 and A3 domains in FVIIIa.	Disulfides	212-221	coagulation factor VIII	Homo sapiens	108-113
17059431-1	2007	BACKGROUND: Genetically engineered disulfide bonds in B-domain-deleted factor (F) VIII variants (C662-C1828 FVIII and C664-C1826 FVIII) improve FVIIIa stability by blocking A2 domain dissociation because the new disulfide covalently links the A2 and A3 domains in FVIIIa.	Disulfides	212-221	coagulation factor VIII	Homo sapiens	129-134
17059431-6	2007	The two disulfide bond-stabilized FVIII variants and WT FVIII had comparable clotting times at all studied concentrations.	Disulfides	8-17	coagulation factor VIII	Homo sapiens	34-39
17059431-9	2007	Measurement of the endogenous thrombin potential in FVIII-deficient plasma supplemented with these FVIII variants confirmed that the disulfide bond-stabilized variants supported high levels of thrombin generation at lower concentrations than did WT FVIII.	Disulfides	133-142	coagulation factor VIII	Homo sapiens	52-57
17059431-9	2007	Measurement of the endogenous thrombin potential in FVIII-deficient plasma supplemented with these FVIII variants confirmed that the disulfide bond-stabilized variants supported high levels of thrombin generation at lower concentrations than did WT FVIII.	Disulfides	133-142	coagulation factor VIII	Homo sapiens	99-104
17059431-9	2007	Measurement of the endogenous thrombin potential in FVIII-deficient plasma supplemented with these FVIII variants confirmed that the disulfide bond-stabilized variants supported high levels of thrombin generation at lower concentrations than did WT FVIII.	Disulfides	133-142	coagulation factor VIII	Homo sapiens	99-104
17109834-8	2006	Both glutathione reductase and glutaredoxin that reduce oxidized glutathione and protein glutathione mixed disulfides, respectively, were constitutively expressed at higher levels in females.	Disulfides	107-117	glutathione reductase	Mus musculus	5-26
11805097-9	2002	Punctin contains disulfide bonds based on antibody accessibility and electrophoretic migration under reducing versus nonreducing conditions.	Disulfides	17-26	ADAMTS like 1	Homo sapiens	0-7
11985604-13	2002	Interestingly, the position of the insert of PAPP-Ai, within the proteolytic domain, lies in close proximity to the cysteine residue, which in human PAPP-A forms a disulfide bond with the proform of eosinophil major basic protein (proMBP).	Disulfides	164-173	pappalysin 1	Homo sapiens	45-51
11985604-13	2002	Interestingly, the position of the insert of PAPP-Ai, within the proteolytic domain, lies in close proximity to the cysteine residue, which in human PAPP-A forms a disulfide bond with the proform of eosinophil major basic protein (proMBP).	Disulfides	164-173	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	199-229
11985604-13	2002	Interestingly, the position of the insert of PAPP-Ai, within the proteolytic domain, lies in close proximity to the cysteine residue, which in human PAPP-A forms a disulfide bond with the proform of eosinophil major basic protein (proMBP).	Disulfides	164-173	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	231-237
11855837-0	2002	Characterization of a Kunitz trypsin inhibitor with one disulfide bridge purified from Swartzia pickellii.	Disulfides	56-65	cysteine rich secretory protein LCCL domain containing 2	Homo sapiens	29-46
21310150-3	2011	Based on the analysis of sequence conservation we propose intra-molecular disulfide bridges and the inter-membrane space localization of three Cx(9)C-containing subunits in human: NDUFS5, NDUFB7 and NDUFA8.	Disulfides	74-83	NADH:ubiquinone oxidoreductase subunit S5	Homo sapiens	180-186
17096689-6	2006	These finding suggest that GPX isoenzymes may function to detoxify H2O2 and organic hydroperoxides using thioredoxin in vivo and may also be involved in regulation of the cellular redox homeostasis by maintaining the thiol/disulfide or NADPH/NADP balance.	Disulfides	223-232	thioredoxin H-type 1	Arabidopsis thaliana	105-116
17163439-1	2006	Thioredoxin (TRX) is a small multifunctional protein with a disulfide active site involved in redox regulation.	Disulfides	60-69	thioredoxin H-type 1	Arabidopsis thaliana	0-11
12677211-3	2002	In a first step, specific kringle IV domains in apo(a), mainly T-6 and T-7, bind to circulating low-density lipoproteins, followed by a second step in which stabilization of the newly formed Lp(a) complex is achieved by a disulfide bridge.	Disulfides	222-231	lipoprotein(a)	Homo sapiens	191-196
17163439-1	2006	Thioredoxin (TRX) is a small multifunctional protein with a disulfide active site involved in redox regulation.	Disulfides	60-69	thioredoxin H-type 1	Arabidopsis thaliana	13-16
21310150-4	2011	We experimentally confirm the localization of the latter two, while our data are consistent with disulfide bridges in NDUFA8.	Disulfides	97-106	NADH:ubiquinone oxidoreductase subunit A8	Homo sapiens	118-124
21198639-6	2011	Dimerization of STEP(61) involves intermolecular disulfide bond formation between two cysteine residues (Cys 65 and Cys 76 respectively) present in the hydrophobic region at the N-terminus specific to STEP(61).	Disulfides	49-58	protein tyrosine phosphatase non-receptor type 5	Homo sapiens	16-24
16930137-1	2006	Interleukin (IL)-12 is a 70-kDa cytokine comprised of two disulfide-linked proteins (p35 and p40) and is essential for the initiation of effective immune response.	Disulfides	58-67	interleukin 9	Homo sapiens	93-96
16880213-3	2006	Oxidation of the human SOD1 disulfide in vivo was found to involve both the copper chaperone for SOD1 (CCS) and the CCS-independent pathway for copper activation.	Disulfides	28-37	copper chaperone for superoxide dismutase	Homo sapiens	103-106
16880213-3	2006	Oxidation of the human SOD1 disulfide in vivo was found to involve both the copper chaperone for SOD1 (CCS) and the CCS-independent pathway for copper activation.	Disulfides	28-37	copper chaperone for superoxide dismutase	Homo sapiens	116-119
11859118-4	2002	In this study, we demonstrate that swapping the disulfide-linked CPNKEKEC sequence (residues 169-176) in the beta(2) I domain with a corresponding beta(3) sequence, or mutating Lys(174) to Thr, constitutively activates alpha(L)beta(2) binding to ICAM-1.	Disulfides	48-57	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	109-116
11859118-4	2002	In this study, we demonstrate that swapping the disulfide-linked CPNKEKEC sequence (residues 169-176) in the beta(2) I domain with a corresponding beta(3) sequence, or mutating Lys(174) to Thr, constitutively activates alpha(L)beta(2) binding to ICAM-1.	Disulfides	48-57	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	227-234
21198639-6	2011	Dimerization of STEP(61) involves intermolecular disulfide bond formation between two cysteine residues (Cys 65 and Cys 76 respectively) present in the hydrophobic region at the N-terminus specific to STEP(61).	Disulfides	49-58	protein tyrosine phosphatase non-receptor type 5	Homo sapiens	201-209
21123168-2	2011	Here, we demonstrate that a thiol-disulfide redox switch controls the interaction between heme and the ligand-binding domain of Rev-erbbeta.	Disulfides	34-43	nuclear receptor subfamily 1 group D member 2	Homo sapiens	128-139
11851405-9	2002	HSF1 with a single cysteine to serine mutation at either the C4 or C5 position gave different ox-HSF1 conformers in the presence of diamide, suggesting that C3 could be disulfide cross-linked to either C4 or C5.	Disulfides	169-178	heat shock transcription factor 1	Homo sapiens	0-4
21123168-3	2011	The reduced dithiol state of Rev-erbbeta binds heme 5-fold more tightly than the oxidized disulfide state.	Disulfides	90-99	nuclear receptor subfamily 1 group D member 2	Homo sapiens	29-40
16959886-3	2006	The surface-accessible, extracellular Cys186-Cys209 disulfide bond of TF is critical for coagulation, and protein disulfide isomerase (PDI) disables coagulation by targeting this disulfide.	Disulfides	114-123	prolyl 4-hydroxylase subunit beta	Homo sapiens	135-138
21123168-4	2011	By means of site-directed mutagenesis and by UV-visible and EPR spectroscopy, we also show that the ferric heme of reduced (dithiol) Rev-erbbeta can undergo a redox-triggered switch from imidazole/thiol ligation (via His-568 and Cys-384, based on a prior crystal structure) to His/neutral residue ligation upon oxidation to the disulfide form.	Disulfides	328-337	nuclear receptor subfamily 1 group D member 2	Homo sapiens	133-144
16690750-4	2006	One of these proteins, protein disulfide isomerase (PDI), has two distinct functions: acting as a molecular chaperone to maintain properly folded proteins and regulating the redox state of proteins by catalyzing the thiol-disulfide exchange reaction through two thioredoxin-like domains.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Homo sapiens	52-55
11741940-0	2002	Disulfide bond assignments of secreted Frizzled-related protein-1 provide insights about Frizzled homology and netrin modules.	Disulfides	0-9	secreted frizzled related protein 1	Homo sapiens	30-65
11741940-3	2002	In this study, the disulfide linkages of recombinant sFRP-1 were determined.	Disulfides	19-28	secreted frizzled related protein 1	Homo sapiens	53-59
11741940-4	2002	Numbering sFRP-1 cysteines sequentially from the N terminus, the five disulfide linkages in the Fz domain are 1-5, 2-4, 3-8, 6-10, and 7-9, consistent with the disulfide pattern determined for homologous domains of several other proteins.	Disulfides	70-79	secreted frizzled related protein 1	Homo sapiens	10-16
11741940-4	2002	Numbering sFRP-1 cysteines sequentially from the N terminus, the five disulfide linkages in the Fz domain are 1-5, 2-4, 3-8, 6-10, and 7-9, consistent with the disulfide pattern determined for homologous domains of several other proteins.	Disulfides	160-169	secreted frizzled related protein 1	Homo sapiens	10-16
11741940-6	2002	This latter set of assignments provides experimental verification of one of the disulfide patterns proposed for netrin (NTR) modules and thereby supports the prediction that the C-terminal heparin-binding domain of sFRP-1 is an NTR-type domain.	Disulfides	80-89	secreted frizzled related protein 1	Homo sapiens	215-221
11741940-7	2002	Interestingly, two subsets of sFRPs appear to have alternate disulfide linkage patterns compared with sFRP-1, one of which involves the loss of a disulfide due to deletion of a single cysteine from the NTR module, whereas the remaining cysteine may pair with a new cysteine introduced in the Fz domain of the protein.	Disulfides	146-155	secreted frizzled related protein 1	Homo sapiens	102-108
21114338-5	2011	Our results demonstrate that the disulfide connectivity in the N-terminal region of CON-S gp140 DeltaCFI is different from the disulfide bonding previously reported in the monomeric form of gp120 HIV-1 Env.	Disulfides	33-42	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	202-205
11752205-8	2002	Molecular dynamics (MD) simulations suggested that CGRP(1-7) exhibited a relatively rigid ring structure imparted by the disulfide bridge between Cys(2) and Cys(7).	Disulfides	121-130	calcitonin-related polypeptide alpha	Rattus norvegicus	51-55
16893192-0	2006	Catalysis of covalent Lp(a) assembly: evidence for an extracellular enzyme activity that enhances disulfide bond formation.	Disulfides	98-107	lipoprotein(a)	Homo sapiens	22-27
16893192-1	2006	The assembly of lipoprotein(a) (Lp(a)) particles occurs via a two-step mechanism in which noncovalent interactions between apolipoprotein(a) (apo(a)) and the apolipoproteinB-100 component of low density lipoprotein precede the formation of a single disulfide bond.	Disulfides	249-258	lipoprotein(a)	Homo sapiens	16-30
16893192-1	2006	The assembly of lipoprotein(a) (Lp(a)) particles occurs via a two-step mechanism in which noncovalent interactions between apolipoprotein(a) (apo(a)) and the apolipoproteinB-100 component of low density lipoprotein precede the formation of a single disulfide bond.	Disulfides	249-258	lipoprotein(a)	Homo sapiens	32-37
16893192-1	2006	The assembly of lipoprotein(a) (Lp(a)) particles occurs via a two-step mechanism in which noncovalent interactions between apolipoprotein(a) (apo(a)) and the apolipoproteinB-100 component of low density lipoprotein precede the formation of a single disulfide bond.	Disulfides	249-258	lipoprotein(a)	Homo sapiens	123-140
16893192-1	2006	The assembly of lipoprotein(a) (Lp(a)) particles occurs via a two-step mechanism in which noncovalent interactions between apolipoprotein(a) (apo(a)) and the apolipoproteinB-100 component of low density lipoprotein precede the formation of a single disulfide bond.	Disulfides	249-258	lipoprotein(a)	Homo sapiens	142-148
16893192-9	2006	In this way, the putative Lp(a) oxidase may be functionally analogous to protein disulfide isomerase, which exhibits a similar mechanism during the catalysis of disulfide bond formation during protein folding, although we have ruled out a role for this enzyme in Lp(a) assembly.	Disulfides	81-90	lipoprotein(a)	Homo sapiens	26-31
16893192-9	2006	In this way, the putative Lp(a) oxidase may be functionally analogous to protein disulfide isomerase, which exhibits a similar mechanism during the catalysis of disulfide bond formation during protein folding, although we have ruled out a role for this enzyme in Lp(a) assembly.	Disulfides	81-90	lipoprotein(a)	Homo sapiens	263-268
11717130-4	2001	In mature spermatozoa the p43 and p97 fragments exist as disulfide-bonded dimers.	Disulfides	57-66	melanotransferrin	Oryctolagus cuniculus	34-37
21114338-5	2011	Our results demonstrate that the disulfide connectivity in the N-terminal region of CON-S gp140 DeltaCFI is different from the disulfide bonding previously reported in the monomeric form of gp120 HIV-1 Env.	Disulfides	127-136	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	190-195
16780799-1	2006	Thioredoxin reductase catalyzes the NADPH-dependent reduction of the catalytic disulfide bond of thioredoxin.	Disulfides	79-88	Thioredoxin reductase 1	Caenorhabditis elegans	0-21
21114338-5	2011	Our results demonstrate that the disulfide connectivity in the N-terminal region of CON-S gp140 DeltaCFI is different from the disulfide bonding previously reported in the monomeric form of gp120 HIV-1 Env.	Disulfides	127-136	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	202-205
21035571-2	2011	LOX-1 exists as a disulfide-linked homodimer on the cell surface, which contains a pair of the ligand-binding domains (CTLD; C-type lectin-like domain).	Disulfides	18-27	oxidized low density lipoprotein receptor 1	Homo sapiens	0-5
16815443-7	2006	We therefore suggest that the role of cytochrome c6A is to use its disulfide group to oxidize dithiol/disulfide groups of other proteins of the thylakoid lumen, followed by internal electron transfer from the dithiol to the heme, and re-oxidation of the heme by another thylakoid oxidant.	Disulfides	67-76	Cytochrome c	Arabidopsis thaliana	38-52
11746222-6	2001	In this model, larger solenoid modules formed from PLEC repeats can be disulfide-bridged via conserved cysteines.	Disulfides	71-80	plectin	Homo sapiens	51-55
16815443-7	2006	We therefore suggest that the role of cytochrome c6A is to use its disulfide group to oxidize dithiol/disulfide groups of other proteins of the thylakoid lumen, followed by internal electron transfer from the dithiol to the heme, and re-oxidation of the heme by another thylakoid oxidant.	Disulfides	102-111	Cytochrome c	Arabidopsis thaliana	38-52
21236356-6	2011	These data suggest a key role for C107 and C184 in both receptor structure/stability and function and is consistent with the presence of a conserved disulfide bond between C107 and C184 in mouse EP3 that is required for normal receptor expression and function.	Disulfides	149-158	prostaglandin E receptor 3 (subtype EP3)	Mus musculus	195-198
16807147-3	2006	Secretory Leucocyte Protease Inhibitor (SLPI) is a 107 amino acids protein with a high density of disulfide pairing (eight).	Disulfides	98-107	serpin family A member 13, pseudogene	Homo sapiens	20-38
11473128-10	2001	Under natural conditions, recombinant mouse neuroglobin occurs as a monomer with disulfide-dependent formation of dimers.	Disulfides	81-90	neuroglobin	Mus musculus	44-55
21297336-1	2011	Protein disulfide isomerase (PDI) is a multifunctional protein that catalyzes disulfide bond formation and assists protein folding, as well as being a structural subunit of microsomal triglyceride transfer protein (MTP) and prolyl 4-hydroxylase (P4HD), and an estrogen and thyroid hormone-binding protein.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
11580274-2	2001	Disulfides of both thiol compounds appear to be very effective as ALR2 thiolating agents.	Disulfides	0-10	lens aldose reductase pseudogene	Bos taurus	66-70
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Disulfides	127-136	lens aldose reductase pseudogene	Bos taurus	30-34
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Disulfides	127-136	lens aldose reductase pseudogene	Bos taurus	46-50
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Disulfides	127-136	lens aldose reductase pseudogene	Bos taurus	46-50
11574464-3	2001	Unexpectedly, the crystal structure of IL-17F reveals that IL-17 family members adopt a monomer fold typical of cystine knot growth factors, despite lacking the disulfide responsible for defining the canonical "knot" structure.	Disulfides	161-170	interleukin 17F	Homo sapiens	39-45
16698902-8	2006	Site-specific mutants showed that TR-BAMY oxidative inhibition depended on the formation of a disulfide bridge between Cys-32 and Cys-470.	Disulfides	94-103	beta-amylase 1	Arabidopsis thaliana	34-41
16634638-0	2006	Peptide binding and NMR analysis of the interaction between SAP97 PDZ2 and GluR-A: potential involvement of a disulfide bond.	Disulfides	110-119	discs large MAGUK scaffold protein 1	Homo sapiens	60-65
16634638-8	2006	A covalent disulfide-linked complex between SAP97(PDZ2) and the GluR-A peptide was seen in the binding assay and in the NMR experiments performed under oxidizing conditions.	Disulfides	11-20	discs large MAGUK scaffold protein 1	Homo sapiens	44-49
16672522-3	2006	NCL is a heterodimer composed of an N-glycosylated acidic subunit (NAS) and a basic subunit (NBS), which are conjugated by disulfide bonds.	Disulfides	123-132	nucleolin	Rattus norvegicus	0-3
16497834-0	2006	The chloroplast protein disulfide isomerase RB60 reacts with a regulatory disulfide of the RNA-binding protein RB47.	Disulfides	24-33	uncharacterized protein	Chlamydomonas reinhardtii	111-115
16497834-3	2006	Our present studies show that RB47 forms a single disulfide bridge that most probably involves Cys143 and Cys259.	Disulfides	50-59	uncharacterized protein	Chlamydomonas reinhardtii	30-34
16497834-4	2006	We found that RB60 reacts with high selectivity with the disulfide of RB47, suggesting that the redox states of these two redox partners are coupled.	Disulfides	57-66	uncharacterized protein	Chlamydomonas reinhardtii	70-74
11696186-0	2001	Reversible redox control of plant vacuolar H+-ATPase activity is related to disulfide bridge formation in subunit E as well as subunit A.	Disulfides	76-85	ATPase H+ transporting V1 subunit B2	Bos taurus	34-52
21062891-4	2011	Here we report a structural model of the p14   bulged duplex interaction based on a combination of X-ray crystallography of an adenine p14/SF3b155 peptide complex, biochemical comparison of a panel of disulfide cross-linked protein-RNA complexes, and small-angle X-ray scattering (SAXS).	Disulfides	201-210	splicing factor 3b subunit 1	Homo sapiens	139-146
11425856-9	2001	Analysis of the disulfide arrangement of bNT-CRFR1 revealed bonds between Cys(30) and Cys(54), Cys(44) and Cys(87), and Cys(68) and Cys(102).	Disulfides	16-25	corticotropin releasing hormone receptor 1	Homo sapiens	45-50
16507355-11	2006	The disulfide reduction and chaperone activity of 400 MPa-treated PDI were also recovered to be comparable to those of native one.	Disulfides	4-13	prolyl 4-hydroxylase subunit beta	Homo sapiens	66-69
20937841-1	2010	Hepatocyte growth factor (HGF) binds to its target receptor tyrosine kinase, Met, as a single-chain form (pro-HGF) or as a cleaved two-chain disulfide-linked alpha/beta-heterodimer.	Disulfides	141-150	hepatocyte growth factor	Homo sapiens	0-24
16055191-4	2006	Fugu IL-15 homologues also contain four conserved cysteines allowing the formation of two disulfide bridges along with four predicted alpha-helices.	Disulfides	90-99	interleukin 15	Danio rerio	5-10
11493705-1	2001	The correct formation of disulfide bonds in the periplasm of Escherichia coli involves Dsb proteins, including two related periplasmic disulfide-bond isomerases, DsbC and DsbG.	Disulfides	25-34	putative protein DsbC	Escherichia coli	162-166
11470158-6	2001	Computer searches revealed that human hepassocin as well as rat hepassocin has a characteristic disulfide structure close to that of fibrinogen-gamma.	Disulfides	96-105	fibrinogen like 1	Homo sapiens	38-48
20937841-1	2010	Hepatocyte growth factor (HGF) binds to its target receptor tyrosine kinase, Met, as a single-chain form (pro-HGF) or as a cleaved two-chain disulfide-linked alpha/beta-heterodimer.	Disulfides	141-150	hepatocyte growth factor	Homo sapiens	26-29
11470158-6	2001	Computer searches revealed that human hepassocin as well as rat hepassocin has a characteristic disulfide structure close to that of fibrinogen-gamma.	Disulfides	96-105	fibrinogen like 1	Homo sapiens	64-74
21170271-4	2010	ROS induce intermolecular disulfide bonds formation in MPYS homodimer and inhibit MPYS IFNbeta stimulatory activity.	Disulfides	26-35	stimulator of interferon response cGAMP interactor 1	Homo sapiens	55-59
11444984-0	2001	Identification and function of disulfide bridges in the extracellular domains of the angiotensin II type 2 receptor.	Disulfides	31-40	angiotensin II receptor type 2	Homo sapiens	85-115
11297543-5	2001	The human Grx2 sequence contains three characteristic regions of the glutaredoxin family: the dithiol/disulfide active site, CSYC, the GSH binding site, and a hydrophobic surface area.	Disulfides	102-111	glutaredoxin	Homo sapiens	69-81
16445295-10	2006	TAFI contains eight cysteine residues, of which two, Cys69 and Cys383, are not involved in disulfides and contain free sulfhydryl groups.	Disulfides	91-101	carboxypeptidase B2	Homo sapiens	0-4
16303761-3	2006	Stimulation of c-met requires two-chain, disulfide-linked HGF.	Disulfides	41-50	hepatocyte growth factor	Homo sapiens	58-61
21170271-4	2010	ROS induce intermolecular disulfide bonds formation in MPYS homodimer and inhibit MPYS IFNbeta stimulatory activity.	Disulfides	26-35	interferon beta 1	Homo sapiens	87-94
16257458-0	2006	Disruption of disulfide bond formation alters the trafficking of prothyrotropin releasing hormone (proTRH)-derived peptides.	Disulfides	14-23	thyrotropin releasing hormone	Homo sapiens	65-97
20849982-9	2010	Redox titrations for the separately-expressed Trx-motif containing C-domain also revealed the presence of a single two-electron couple with an E(m) value of approximately -260 mV at 20 C. The fact that these two E(m) values are identical, provides additional support for assignment of the redox couple to a disulfide/dithiol involving C304 and C307.	Disulfides	307-316	thioredoxin H-type 1	Arabidopsis thaliana	46-49
11335716-3	2001	Furthermore, the feasibility and desirability of introducing a disulfide bridge between CDR1 and CDR3 was investigated.	Disulfides	63-72	CDR3	Homo sapiens	97-101
21029072-0	2010	Effect of immunoglobulin G (IgG) interchain disulfide bond cleavage on efficacy of intravenous immunoglobulin for immune thrombocytopenic purpura (ITP).	Disulfides	44-53	immunoglobulin heavy variable V1-62	Mus musculus	28-31
11335716-5	2001	Mass spectrometric analyses indicated that CDR1-CDR3 disulfide formation was universal.	Disulfides	53-62	CDR3	Homo sapiens	48-52
11335716-6	2001	However, surface plasmon resonance and NMR data showed that the CDR3 constraint imposed by the disulfide bridge was not always desirable.	Disulfides	95-104	CDR3	Homo sapiens	64-68
11432744-2	2001	Folding of mPrP(23-231) involves formation of a single disulfide bond, Cys179-Cys214.	Disulfides	55-64	prion protein	Mus musculus	11-15
16368681-1	2006	Native disulfide bond formation in eukaryotes is dependent on protein-disulfide isomerase (PDI) and its homologs, which contain varying combinations of catalytically active and inactive thioredoxin domains.	Disulfides	7-16	prolyl 4-hydroxylase subunit beta	Homo sapiens	62-89
16368681-1	2006	Native disulfide bond formation in eukaryotes is dependent on protein-disulfide isomerase (PDI) and its homologs, which contain varying combinations of catalytically active and inactive thioredoxin domains.	Disulfides	7-16	prolyl 4-hydroxylase subunit beta	Homo sapiens	91-94
16368681-2	2006	However, the specific contribution of PDI to the formation of new disulfides versus reduction/rearrangement of non-native disulfides is poorly understood.	Disulfides	66-76	prolyl 4-hydroxylase subunit beta	Homo sapiens	38-41
16368681-3	2006	We analyzed the role of individual PDI domains in disulfide bond formation in a reaction driven by their natural oxidant, Ero1p.	Disulfides	50-59	prolyl 4-hydroxylase subunit beta	Homo sapiens	35-38
16368681-8	2006	These findings reveal how native disulfide folding is accomplished in the endoplasmic reticulum and provide a context for understanding the proliferation of PDI homologs with combinatorial arrangements of thioredoxin domains.	Disulfides	33-42	prolyl 4-hydroxylase subunit beta	Homo sapiens	157-160
16877880-3	2006	In addition, Lp(a) contains a unique hydrophilic, carbohydrate-rich protein, apo(a), linked to apoB through a single disulfide bond connecting the C-terminal regions of the two proteins.	Disulfides	117-126	lipoprotein(a)	Homo sapiens	13-18
21029072-4	2010	The interchain disulfide bond cleavage decreased the affinity much more for mouse FcgammaRIV than for mouse FcgammaRIIB.	Disulfides	15-24	Fc receptor, IgG, low affinity IV	Mus musculus	82-92
20721684-3	2010	Using different approaches, a disulfide pattern has been defined for the Tat protein and a specific DTT-dependent breaking order of disulfide bonds highlighted.	Disulfides	30-39	tyrosine aminotransferase	Homo sapiens	73-76
16257008-0	2005	Oligomerization and interacellular localization of the glycoprotein receptor ERGIC-53 is independent of disulfide bonds.	Disulfides	104-113	lectin, mannose binding 1	Homo sapiens	77-85
16257008-2	2005	Previous results have shown that ERGIC-53 is present as reduction-sensitive homo-oligomers, i.e. as a balanced mixture of disulfide-linked hexamers and dimers, with the two cysteine residues located close to the transmembrane domain playing a crucial role in oligomerization.	Disulfides	122-131	lectin, mannose binding 1	Homo sapiens	33-41
16087673-2	2005	DsbC, the primary disulfide isomerase, likely resolves incorrect disulfides.	Disulfides	65-75	putative protein DsbC	Escherichia coli	0-4
11454166-0	2001	Mapping the receptor binding regions of human chorionic gonadotropin (hCG) using disulfide peptides of its beta-subunit: possible involvement of the disulfide bonds Cys(9)-Cys(57) and Cys(23)-Cys(72) in receptor binding of the hormone.	Disulfides	81-90	chorionic gonadotropin subunit beta 5	Homo sapiens	46-74
11454166-0	2001	Mapping the receptor binding regions of human chorionic gonadotropin (hCG) using disulfide peptides of its beta-subunit: possible involvement of the disulfide bonds Cys(9)-Cys(57) and Cys(23)-Cys(72) in receptor binding of the hormone.	Disulfides	149-158	chorionic gonadotropin subunit beta 5	Homo sapiens	46-74
11454166-2	2001	The alpha- and beta-subunits of hCG are highly cross-linked internally by disulfide bonds which seem to stabilize the tertiary structures required for the noncovalent association of the subunits to generate hormonal activity.	Disulfides	74-83	chorionic gonadotropin subunit beta 5	Homo sapiens	32-35
11454166-4	2001	Six disulfide peptides incorporating each of the six disulfide bonds of hCGbeta were synthesized and screened, along with their linear counterparts, for their ability to competitively inhibit the binding of [125I] hCG to sheep ovarian corpora luteal LH/CG receptor.	Disulfides	4-13	chorionic gonadotropin subunit beta 5	Homo sapiens	72-75
11454166-4	2001	Six disulfide peptides incorporating each of the six disulfide bonds of hCGbeta were synthesized and screened, along with their linear counterparts, for their ability to competitively inhibit the binding of [125I] hCG to sheep ovarian corpora luteal LH/CG receptor.	Disulfides	4-13	chorionic gonadotropin subunit beta 5	Homo sapiens	73-75
11454166-4	2001	Six disulfide peptides incorporating each of the six disulfide bonds of hCGbeta were synthesized and screened, along with their linear counterparts, for their ability to competitively inhibit the binding of [125I] hCG to sheep ovarian corpora luteal LH/CG receptor.	Disulfides	53-62	chorionic gonadotropin subunit beta 5	Homo sapiens	72-75
11454166-5	2001	Disulfide peptide Cys (9-57) was found to be approximately 4-fold more potent than the most active of its linear counterparts in inhibiting radiolabeled hCG from binding to its receptor.	Disulfides	0-9	chorionic gonadotropin subunit beta 5	Homo sapiens	153-156
11454166-7	2001	The results suggest the involvement of the disulfide bonds Cys(9)-Cys(57) and Cys(23)-Cys(72) of the beta-subunit of hCG in receptor binding of the hormone.	Disulfides	43-52	chorionic gonadotropin subunit beta 5	Homo sapiens	117-120
11454166-8	2001	This study is the first of its kind to use disulfide peptides rather than linear peptides to map the receptor binding regions of hCG.	Disulfides	43-52	chorionic gonadotropin subunit beta 5	Homo sapiens	129-132
16087673-4	2005	Here we demonstrate that mutations in the entire DsbC disulfide isomerization pathway cause an increased sensitivity to the redox-active metal copper.	Disulfides	54-63	putative protein DsbC	Escherichia coli	49-53
16087673-5	2005	We find that copper catalyzes periplasmic disulfide bond formation under aerobic conditions and that copper catalyzes the formation of disulfide-bonded oligomers in vitro, which DsbC can resolve.	Disulfides	135-144	putative protein DsbC	Escherichia coli	178-182
16087673-6	2005	Our data suggest that the copper sensitivity of dsbC- strains arises from the inability of the cell to rearrange copper-catalyzed non-native disulfides in the absence of functional DsbC.	Disulfides	141-151	putative protein DsbC	Escherichia coli	48-52
16087673-9	2005	These findings lead us to a model in which DsbA may be significantly more accurate in disulfide oxidation than previously thought, and in which the primary role of DsbC may be to rearrange incorrect disulfide bonds that are formed during certain oxidative stresses.	Disulfides	199-208	putative protein DsbC	Escherichia coli	164-168
20721684-3	2010	Using different approaches, a disulfide pattern has been defined for the Tat protein and a specific DTT-dependent breaking order of disulfide bonds highlighted.	Disulfides	132-141	tyrosine aminotransferase	Homo sapiens	73-76
16142915-1	2005	Protein disulfide isomerase (PDI) catalyzes the rearrangement of nonnative disulfide bonds in the endoplasmic reticulum of eukaryotic cells, a process that often limits the rate at which polypeptide chains fold into a native protein conformation.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
20721684-7	2010	This is due to strong electrostatic and metal-binding interactions, whereas Tat dimerization involves metal-binding interactions as well as disulfide bond formation.	Disulfides	140-149	tyrosine aminotransferase	Homo sapiens	76-79
16142915-8	2005	Fluorescence resonance energy transfer from 280 to 465 nm increases by 28-fold upon isomerization of the disulfide bonds into their native state (which has a lower E(o") = -0.313 V than does PDI).	Disulfides	105-114	prolyl 4-hydroxylase subunit beta	Homo sapiens	191-194
16142915-10	2005	We find that wild-type PDI catalyzes the isomerization of the substrate with kcat/K(M) = 1.7 x 10(5) M(-1) s(-1), which is the largest value yet reported for catalysis of disulfide bond isomerization.	Disulfides	171-180	prolyl 4-hydroxylase subunit beta	Homo sapiens	23-26
16142915-11	2005	The variant, which is a poor catalyst of disulfide bond reduction and dithiol oxidation, retains virtually all of the activity of wild-type PDI in catalysis of disulfide bond isomerization.	Disulfides	41-50	prolyl 4-hydroxylase subunit beta	Homo sapiens	140-143
16014632-7	2005	Chemical shift perturbation analysis of the disulfide ubiquitin-Ubc1 complex by NMR spectroscopy reveals an ubiquitin-Ubc1 interface similar to that for the ubiquitin-E2 thioester.	Disulfides	44-53	ubiquitin	Saccharomyces cerevisiae S288C	54-63
16014632-7	2005	Chemical shift perturbation analysis of the disulfide ubiquitin-Ubc1 complex by NMR spectroscopy reveals an ubiquitin-Ubc1 interface similar to that for the ubiquitin-E2 thioester.	Disulfides	44-53	ubiquitin	Saccharomyces cerevisiae S288C	108-117
11274208-4	2001	Recombinant NC2/COL readily formed disulfide-bonded hexamers, each representing one antiparallel dimer of collagen VII.	Disulfides	35-44	down-regulator of transcription 1	Homo sapiens	12-15
11399772-8	2001	Specificity for the amidated disulfide cofactor partly can be explained by the substitution of Arg-37, shown by x-ray crystallographic data of the human glutathione reductase to hydrogen-bond one of the glutathione glycyl carboxylates, by the negatively charged Glu-21.	Disulfides	29-38	glutathione-disulfide reductase	Homo sapiens	153-174
16014632-7	2005	Chemical shift perturbation analysis of the disulfide ubiquitin-Ubc1 complex by NMR spectroscopy reveals an ubiquitin-Ubc1 interface similar to that for the ubiquitin-E2 thioester.	Disulfides	44-53	ubiquitin	Saccharomyces cerevisiae S288C	108-117
20956340-4	2010	Under nonreducing conditions, in gel permeation chromatography recombinant CL-11 forms disulfide-linked oligomers of 100 and 200 kDa.	Disulfides	87-96	collectin subfamily member 11	Homo sapiens	75-80
16014632-8	2005	In addition to the typical E2 catalytic domain, Ubc1 contains an ubiquitin-associated (UBA) domain, and we have utilized NMR spectroscopy to demonstrate that in this disulfide complex the UBA domain is freely accessible to non-covalently bind a second molecule of ubiquitin.	Disulfides	166-175	ubiquitin	Saccharomyces cerevisiae S288C	65-74
16014632-8	2005	In addition to the typical E2 catalytic domain, Ubc1 contains an ubiquitin-associated (UBA) domain, and we have utilized NMR spectroscopy to demonstrate that in this disulfide complex the UBA domain is freely accessible to non-covalently bind a second molecule of ubiquitin.	Disulfides	166-175	ubiquitin	Saccharomyces cerevisiae S288C	264-273
16002696-8	2005	Furthermore, the thiol oxidoreductase ERp57 was detected in FcRn-CNX complexes, suggesting its role in disulfide bond formation of the FcRn H chain.	Disulfides	103-112	calnexin	Homo sapiens	65-68
11279095-0	2001	Unique disulfide bond structures found in ST8Sia IV polysialyltransferase are required for its activity.	Disulfides	7-16	ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4	Homo sapiens	42-51
11279095-11	2001	These results combined indicate that the sterical structure formed by intramolecular disulfide bonds, which bring the sialylmotifs and the COOH terminus within close proximity, is critical for the catalytic activity of ST8Sia IV.	Disulfides	85-94	ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4	Homo sapiens	219-228
11297517-4	2001	The use of PAG mutants (C52S, C71S, and C173S) revealed that this association was significantly affected by C173S, but not C52S and C71S, indicating that a disulfide involving Cys(173) of PAG is responsible for the formation of MIF-PAG complex.	Disulfides	156-165	macrophage migration inhibitory factor	Homo sapiens	228-231
20692383-4	2010	Homology modeling results demonstrated that rLcn12 adopted an eight-stranded, antiparallel beta-barrel conformation containing a conserved disulfide bond between Cys98 and Cys203, which was in accordance with the physicochemical properties elucidated by a combination of mass, circular dichroism, and nuclear magnetic resonance spectrometry.	Disulfides	139-148	lipocalin 12	Rattus norvegicus	44-50
11369537-3	2001	The N-terminal domain of SP-A is required for disulfide-dependent protein oligomerization, and for binding and aggregation of phospholipids, but there is no evidence that this domain directly interacts with lipid membranes.	Disulfides	46-55	surfactant protein A1	Homo sapiens	25-29
15998247-1	2005	Glutaredoxins (Grxs) are small ubiquitous proteins of the thioredoxin (Trx) family, which catalyze dithiol-disulfide exchange reactions or reduce protein-mixed glutathione disulfides.	Disulfides	107-116	thioredoxin H-type 1	Arabidopsis thaliana	58-69
15998247-1	2005	Glutaredoxins (Grxs) are small ubiquitous proteins of the thioredoxin (Trx) family, which catalyze dithiol-disulfide exchange reactions or reduce protein-mixed glutathione disulfides.	Disulfides	107-116	thioredoxin H-type 1	Arabidopsis thaliana	71-74
20719953-5	2010	Since A56 contains three extracellular cysteines, we hypothesized that one of the cysteines may be unpaired and could therefore form a disulfide bridge with VCP.	Disulfides	135-144	valosin containing protein	Homo sapiens	157-160
15849182-7	2005	In the present study, we show that AIIt thiols are oxidized during the reduction of plasmin disulfides, establishing that AIIt directly participates in the reduction reaction.	Disulfides	92-102	plasminogen	Homo sapiens	84-91
11256994-7	2001	This was strong evidence for the involvement of all six Cys in the intrachain disulfide bonds required for proper folding, processing and transport of LOX-1.	Disulfides	78-87	oxidized low density lipoprotein receptor 1	Homo sapiens	151-156
20540164-6	2010	Various non-native intra-A (A20 with A6, A7, or A11), intra-B (between B7 and B19), and inter-A-B disulfide bonds were observed in the intermediates with two disulfide bonds.	Disulfides	158-167	CD80 molecule	Homo sapiens	71-81
20471426-0	2010	Conformational characterization of aberrant disulfide-linked HIV-1 gp120 dimers secreted from overexpressing cells.	Disulfides	44-53	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	67-72
11102453-6	2001	PFO(C190-C57) that was allowed to form the prepore prior to the reduction of the disulfide exhibited a dramatic increase in the rate of PFO-dependent hemolysis and the membrane insertion of its TMHs when compared with toxin that had the disulfide reduced prior mixing the toxin with membranes.	Disulfides	81-90	LHFPL tetraspan subfamily member 5	Homo sapiens	194-198
11102453-6	2001	PFO(C190-C57) that was allowed to form the prepore prior to the reduction of the disulfide exhibited a dramatic increase in the rate of PFO-dependent hemolysis and the membrane insertion of its TMHs when compared with toxin that had the disulfide reduced prior mixing the toxin with membranes.	Disulfides	237-246	LHFPL tetraspan subfamily member 5	Homo sapiens	194-198
11266655-1	2001	The susceptibility of recombinant human thiopurine methyltransferase (hTPMT) to thiol-disulfide exchange was investigated.	Disulfides	86-95	thiopurine S-methyltransferase	Homo sapiens	70-75
15769741-8	2005	In conclusion, proper oligomerization of Ang1 having at least four subunits by the intermolecular disulfide linkage involving cysteines 41 and 54 is critical for Tie2 binding and activation.	Disulfides	98-107	angiopoietin 1	Homo sapiens	41-45
15769741-8	2005	In conclusion, proper oligomerization of Ang1 having at least four subunits by the intermolecular disulfide linkage involving cysteines 41 and 54 is critical for Tie2 binding and activation.	Disulfides	98-107	TEK receptor tyrosine kinase	Homo sapiens	162-166
15848158-0	2005	Effect of EPS1 gene deletion in Saccharomyces cerevisiae on the secretion of foreign proteins which have disulfide bridges.	Disulfides	105-114	protein disulfide isomerase EPS1	Saccharomyces cerevisiae S288C	10-14
15848158-5	2005	These observations lead to the supposition that yeast cells deficient for the protein disulfide isomerase-family-member EPS1 locus secrete more of labile disulfide-containing model proteins.	Disulfides	86-95	protein disulfide isomerase EPS1	Saccharomyces cerevisiae S288C	120-124
15823038-7	2005	Since previous studies have shown that N-glycan-bound calnexin/calreticulin are also capable of recruiting ERp57, our results suggest that N-linked glycosylation and RAP can independently and cooperatively recruit oxidoreductases to facilitate protein folding and proper disulfide bond formation.	Disulfides	271-280	calnexin	Homo sapiens	54-62
15767043-4	2005	We found that some intersubunit disulfide crosslinks reduced the efficacies of hCG analogs lacking only the alpha2 oligosaccharide.	Disulfides	32-41	glycoprotein hormones, alpha polypeptide	Homo sapiens	79-82
11266655-4	2001	Activity measurements of the enzyme over time in these buffers at 30 degrees C indicated that thiol-disulfide exchange may be a part of the posttranslational modulation of hTPMT activity.	Disulfides	100-109	thiopurine S-methyltransferase	Homo sapiens	172-177
11266655-9	2001	Inspection of the model indicated that one of the protein thiols subject to slow thiol-disulfide exchange may be situated at the binding site of the co-substrate of the enzyme and thus be responsible for the glutathione/glutathione disulfide modulation of the activity of hTPMT.	Disulfides	87-96	thiopurine S-methyltransferase	Homo sapiens	272-277
12549186-2	2001	It is a disulfide-linked heterodimer composed of a 35 kD light chain (P35) and a 40 kD heavy chain (P40).	Disulfides	8-17	interleukin 9	Homo sapiens	100-103
20302941-2	2010	Here, a novel procedure is presented which allows fast and efficient production of biologically active BMP-2 via a TWO-STEP procedure: the conditions are designed such that the first step favors formation of monomeric species with the correct intramolecular disulfide bridges, the conditions of the second folding reaction stimulate the formation of the intermolecular disulfide bridge.	Disulfides	258-267	bone morphogenetic protein 2	Homo sapiens	103-108
16233046-0	2001	Disulfide bond formation in refolding of thermophilic fungal protein disulfide isomerase.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	61-88
16233046-1	2001	Disulfide bond formation in the refolding of thermophilic fungal protein disulfide isomerase (PDI) was investigated.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	65-92
16233046-1	2001	Disulfide bond formation in the refolding of thermophilic fungal protein disulfide isomerase (PDI) was investigated.	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	94-97
16233046-2	2001	It was revealed that (i) a disulfide bond buried inside the molecule is preferentially formed and contributes to the thermal stability and the isomerizing power of PDI, and (ii) formation of disulfide bonds in active sites located on the molecular surface causes deformation of the optimum conformation resulting in a decrease in the thermal stability.	Disulfides	27-36	prolyl 4-hydroxylase subunit beta	Homo sapiens	164-167
16233046-2	2001	It was revealed that (i) a disulfide bond buried inside the molecule is preferentially formed and contributes to the thermal stability and the isomerizing power of PDI, and (ii) formation of disulfide bonds in active sites located on the molecular surface causes deformation of the optimum conformation resulting in a decrease in the thermal stability.	Disulfides	191-200	prolyl 4-hydroxylase subunit beta	Homo sapiens	164-167
15794757-8	2005	SDS/PAGE and analysis by sucrose-density-gradient analysis indicated that TNSALP (1559delT) forms a disulfide-bonded high-molecular-mass aggregate.	Disulfides	100-109	alkaline phosphatase, biomineralization associated	Homo sapiens	74-80
20302941-2	2010	Here, a novel procedure is presented which allows fast and efficient production of biologically active BMP-2 via a TWO-STEP procedure: the conditions are designed such that the first step favors formation of monomeric species with the correct intramolecular disulfide bridges, the conditions of the second folding reaction stimulate the formation of the intermolecular disulfide bridge.	Disulfides	369-378	bone morphogenetic protein 2	Homo sapiens	103-108
20566629-3	2010	GRX1 is a thiol oxidoreductase that catalyzes the reversible reduction of GSH-mixed disulfides to their respective sulfhydryls (deglutathionylation).	Disulfides	84-94	glutaredoxin	Homo sapiens	0-4
15748721-7	2005	Twelve cysteine residues, forming six disulfide bonds within beta-subunit and two putative asparagine-linked glycosylation sites, are also conserved in the Chinese soft-shell turtle FSHbeta subunit.	Disulfides	38-47	follitropin subunit beta	Pelodiscus sinensis	182-189
11092861-0	2000	Proteome analysis of the effect of mucoid conversion on global protein expression in Pseudomonas aeruginosa strain PAO1 shows induction of the disulfide bond isomerase, dsbA.	Disulfides	143-152	thiol:disulfide interchange protein DsbA	Pseudomonas aeruginosa PAO1	169-173
15644328-0	2005	RS1, a discoidin domain-containing retinal cell adhesion protein associated with X-linked retinoschisis, exists as a novel disulfide-linked octamer.	Disulfides	123-132	retinoschisin 1	Homo sapiens	0-3
20550946-6	2010	Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER).	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
15644328-0	2005	RS1, a discoidin domain-containing retinal cell adhesion protein associated with X-linked retinoschisis, exists as a novel disulfide-linked octamer.	Disulfides	123-132	retinoschisin 1	Homo sapiens	81-103
15644328-6	2005	Our results indicate that RS1 exists as a novel octamer in which the eight subunits are joined together by Cys(59)-Cys(223) intermolecular disulfide bonds.	Disulfides	139-148	retinoschisin 1	Homo sapiens	26-29
15644328-10	2005	Because mutations that disrupt subunit assembly cause X-linked retinoschisis, the assembly of RS1 into a disulfide-linked homo-octamer appears to be critical for its function as a retinal cell adhesion protein.	Disulfides	105-114	retinoschisin 1	Homo sapiens	54-76
15644328-10	2005	Because mutations that disrupt subunit assembly cause X-linked retinoschisis, the assembly of RS1 into a disulfide-linked homo-octamer appears to be critical for its function as a retinal cell adhesion protein.	Disulfides	105-114	retinoschisin 1	Homo sapiens	94-97
15647258-0	2005	Proteinase inhibition by proform of eosinophil major basic protein (pro-MBP) is a multistep process of intra- and intermolecular disulfide rearrangements.	Disulfides	129-138	endogenous retrovirus group K member 18	Homo sapiens	0-10
11063595-4	2000	Dpl 24-152 was shown to contain two disulfide bonds (Cys94-Cys145 and Cys108-Cys140).	Disulfides	36-45	prion like protein doppel	Homo sapiens	0-3
10913121-8	2000	In human pregnancy, PAPP-A is known to circulate as a 500-kDa disulfide-bound 2:2 complex with the proform of eosinophil major basic protein (proMBP), PAPP-A/proMBP.	Disulfides	62-71	pappalysin 1	Homo sapiens	20-26
10913121-8	2000	In human pregnancy, PAPP-A is known to circulate as a 500-kDa disulfide-bound 2:2 complex with the proform of eosinophil major basic protein (proMBP), PAPP-A/proMBP.	Disulfides	62-71	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	110-140
10913121-8	2000	In human pregnancy, PAPP-A is known to circulate as a 500-kDa disulfide-bound 2:2 complex with the proform of eosinophil major basic protein (proMBP), PAPP-A/proMBP.	Disulfides	62-71	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	142-148
10913121-8	2000	In human pregnancy, PAPP-A is known to circulate as a 500-kDa disulfide-bound 2:2 complex with the proform of eosinophil major basic protein (proMBP), PAPP-A/proMBP.	Disulfides	62-71	pappalysin 1	Homo sapiens	151-157
10913121-8	2000	In human pregnancy, PAPP-A is known to circulate as a 500-kDa disulfide-bound 2:2 complex with the proform of eosinophil major basic protein (proMBP), PAPP-A/proMBP.	Disulfides	62-71	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	158-164
10913121-13	2000	Inhibition of PAPP-A by proMBP represents a novel inhibitory mechanism with the enzyme irreversibly bound to its inhibitor by disulfide bonds.	Disulfides	126-135	pappalysin 1	Homo sapiens	14-20
10913121-13	2000	Inhibition of PAPP-A by proMBP represents a novel inhibitory mechanism with the enzyme irreversibly bound to its inhibitor by disulfide bonds.	Disulfides	126-135	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	24-30
15843355-3	2005	HRI has 32 cysteine residues, and the oxidative formation of disulfide bonds from those cysteine residues is a rapid cooperative process that inactivates HRI.	Disulfides	61-70	eukaryotic translation initiation factor 2 alpha kinase 1	Homo sapiens	0-3
15843355-3	2005	HRI has 32 cysteine residues, and the oxidative formation of disulfide bonds from those cysteine residues is a rapid cooperative process that inactivates HRI.	Disulfides	61-70	eukaryotic translation initiation factor 2 alpha kinase 1	Homo sapiens	154-157
20550946-6	2010	Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER).	Disulfides	127-136	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
15537649-7	2005	Endoglin, a disulfide-linked homodimer, is an accessory component of the TGF-beta receptor complex and mainly expressed on endothelial cells.	Disulfides	12-21	endoglin	Rattus norvegicus	0-8
10974203-10	2000	In addition, the peptide of M(r) = 4821 observed in the Glu-C digestion of the disulfiram-treated ALDH reverted to M(r) = 4823 after treatment with DTT, which indicated that the disulfide bond was reduced.	Disulfides	178-187	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	98-102
20550946-6	2010	Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER).	Disulfides	127-136	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
20695529-2	2010	Disulfide-scrambling experiments suggested that rice LTP2 is more thermostable than rice LTP1 and identified multiple disulfide-scrambled isomers for LTP1 but only one for LTP2.	Disulfides	0-9	non-specific lipid-transfer protein Cw18	Triticum aestivum	53-57
11012661-3	2000	Glutaredoxins catalyze glutathione-disulfide oxidoreductions overlapping the functions of thioredoxins and using electrons from NADPH via glutathione reductase.	Disulfides	35-44	glutathione-disulfide reductase	Homo sapiens	138-159
15627473-7	2005	The possible role of gamma-cystathionase in generating sulfane sulfur from the disulfide-containing cysteine S-conjugates present in allium extracts, and the possible role of this sulfane sulfur in enzyme regulation, targeting of cancer cells and detoxification reactions is discussed.	Disulfides	79-88	cystathionine gamma-lyase	Rattus norvegicus	21-40
15628884-2	2005	To explore inherent structural and functional determinants within the amino acid sequence of mature SP-B, porcine SP-B has been subjected to extensive disulfide reduction under highly denaturing conditions and to cysteine carboxyamidomethylation, and the structure, lipid-protein interactions, and surface activity of this modified form have been characterized.	Disulfides	151-160	surfactant protein B	Homo sapiens	114-118
15628884-3	2005	Refolding of the reduced protein yielded a form (SP-Br) with secondary structure practically identical to that of the native disulfide-linked SP-B dimer.	Disulfides	125-134	surfactant protein B	Homo sapiens	49-53
20695529-2	2010	Disulfide-scrambling experiments suggested that rice LTP2 is more thermostable than rice LTP1 and identified multiple disulfide-scrambled isomers for LTP1 but only one for LTP2.	Disulfides	118-127	non-specific lipid-transfer protein Cw18	Triticum aestivum	53-57
10827185-0	2000	Inactivation of rabbit muscle creatine kinase by reversible formation of an internal disulfide bond induced by the fungal toxin gliotoxin.	Disulfides	85-94	creatine kinase M-type	Oryctolagus cuniculus	23-45
19958171-6	2010	Oxidized protein repair systems, thioredoxin/thioredoxin reductase or glutaredoxin/glutathione/glutathione reductase that catalytically reduce disulfide bridges or sulfenic acids, and methionine sulfoxide reductase that reverses methionine sulfoxide back to methionine within proteins, are present in the mitochondrial matrix.	Disulfides	143-152	glutaredoxin	Homo sapiens	70-82
15674109-2	2005	IL-12 is a heterodimeric protein comprising 2 disulfide-linked subunits designated p35 and p40.	Disulfides	46-55	interleukin 9	Homo sapiens	91-94
10903744-4	2000	The mutations Gly25--&gt;Asp and Gly28--&gt;Glu disrupt the disulfide-bonding arrangement of the protein and cause at least a 5-fold increase in the half-time of secretion of MBP compared with wild-type rat serum MBP.	Disulfides	60-69	myelin basic protein	Homo sapiens	175-178
19958171-6	2010	Oxidized protein repair systems, thioredoxin/thioredoxin reductase or glutaredoxin/glutathione/glutathione reductase that catalytically reduce disulfide bridges or sulfenic acids, and methionine sulfoxide reductase that reverses methionine sulfoxide back to methionine within proteins, are present in the mitochondrial matrix.	Disulfides	143-152	glutathione-disulfide reductase	Homo sapiens	95-116
20448108-3	2010	Recently, the protein disulfide isomerase (PDI) has been hypothesized to regulate TF decryption through the redox switch of an exposed disulfide in TF extracellular domain.	Disulfides	22-31	prolyl 4-hydroxylase subunit beta	Homo sapiens	43-46
11195969-6	2000	Based on our previous and present observations, we propose that at pH 8 there may be two kinds of incorrect interactions within and between prochymosin polypeptides leading to unproductive pathways: one prevents disulfide rearrangement, which can be avoided by high pH; the other interferes with acquisition of native conformation, which can be relieved by GroE and PDI.	Disulfides	212-221	prolyl 4-hydroxylase subunit beta	Homo sapiens	366-369
15596720-7	2004	This motif lies directly at the docking point of COX I helix 3 and cytochrome c, and modeling of bovine COX I suggests the possibility of an unprecedented helix-terminating disulfide bridge that could alter COX/cytochrome c dissociation kinetics.	Disulfides	173-182	LOC104968582	Bos taurus	67-79
15596720-7	2004	This motif lies directly at the docking point of COX I helix 3 and cytochrome c, and modeling of bovine COX I suggests the possibility of an unprecedented helix-terminating disulfide bridge that could alter COX/cytochrome c dissociation kinetics.	Disulfides	173-182	LOC104968582	Bos taurus	211-223
20516062-6	2010	Indeed, mutation of the disulfide in hbetac led to both a complete loss of high affinity binding with the human IL-3Ralpha SP2 isoform and of downstream signaling.	Disulfides	24-33	interleukin 3 receptor, alpha chain	Mus musculus	112-122
15358778-1	2004	Protein disulfide isomerase (PDI, EC 5.3.4.1) is a chaperone and catalyzes the formation and rearrangement of disulfide bonds in proteins.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
15526038-5	2004	Each WAT makes similar but unique interactions, consistent with an asymmetric pattern of disulfide linkages between the AChE tetramer subunits and ColQ.	Disulfides	89-98	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	147-151
10987366-0	2000	The thioredoxin boxes of thyroglobulin: possible implications for intermolecular disulfide bond formation in the follicle lumen.	Disulfides	81-90	thyroglobulin	Homo sapiens	25-38
10987366-2	2000	Human thyroglobulin (hTG) has been shown to multimerize mainly by intermolecular disulfide cross-links.	Disulfides	81-90	thyroglobulin	Homo sapiens	6-19
10852729-9	2000	Thus, both oxidation of NG to form intramolecular disulfides and phosphorylation of NG by PKC are effective in modulating the intracellular level of CaM.	Disulfides	50-60	calmodulin 1	Rattus norvegicus	149-152
20536384-5	2010	HGF is a disulfide-linked alpha/beta-heterodimer having a trypsin serine protease-like beta-chain.	Disulfides	9-18	hepatocyte growth factor	Homo sapiens	0-3
10852729-10	2000	These results indicate that modification of NG to form intramolecular disulfides outside the IQ domain provides an alternative mechanism for regulation of its binding affinity to CaM.	Disulfides	70-80	calmodulin 1	Rattus norvegicus	179-182
15475481-1	2004	Protein disulfide isomerase (PDI) plays a key role in protein folding by catalyzing rearrangements of disulfide bonds in substrate proteins following their synthesis in eukaryotic cells.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
20501611-5	2010	We found that MT6-MMP is present in the membrane, granules and nuclear/endoplasmic reticulum/Golgi fractions of PMNs where it is displayed as a disulfide-linked homodimer of 120 kDa.	Disulfides	144-153	matrix metallopeptidase 25	Homo sapiens	14-21
15388859-1	2004	Bikunin is a glycosylated protein that aggregates extensively during mammalian cell culture, resulting in loss of activity, loss of native secondary structure, and the formation of nonnative disulfide bonds.	Disulfides	191-200	alpha-1-microglobulin/bikunin precursor	Homo sapiens	0-7
15358240-4	2004	All eight cysteines are involved in disulfide bonds with the pattern consistent with that for the PSI domain from Sema4D.	Disulfides	36-45	semaphorin 4D	Homo sapiens	114-120
10841552-0	2000	Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase.	Disulfides	6-15	methionine sulfoxide reductase A	Bos taurus	75-105
10825441-3	2000	SP-B, in contrast to other saposins, is hydrophobic and a disulfide-linked dimer, and its mechanism of action is not known.	Disulfides	58-67	surfactant protein B	Homo sapiens	0-4
20689590-4	2010	METHODOLOGY/PRINCIPAL FINDINGS: By PCR directed mutagenesis we showed that disruption of a single disulfide bond induced MMP-2 epitope presentation.	Disulfides	98-107	matrix metallopeptidase 2	Homo sapiens	121-126
10825441-4	2000	A model of the three-dimensional structure of one SP-B subunit was generated from the structure of monomeric NK-lysin determined by nuclear magnetic resonance, and the SP-B dimer was formed by joining two subunits via the intersubunit disulfide bond Cys48-Cys48".	Disulfides	235-244	surfactant protein B	Homo sapiens	168-172
15284220-6	2004	Recombinant Ang3 and Ang4 formed disulfide-linked dimers.	Disulfides	33-42	angiogenin, ribonuclease A family, member 3	Mus musculus	12-16
10799583-6	2000	The SOS disulfide bond formed efficiently in gp140s containing a single loop deletion or a combination deletion of the V1 and V2 loops.	Disulfides	8-17	immunoglobulin kappa variable 1-5	Homo sapiens	119-128
20689590-5	2010	By Pulse-Chase experiment, we demonstrated that disulfide bonds stabilized MMP-2 and impeded its degradation.	Disulfides	48-57	matrix metallopeptidase 2	Homo sapiens	75-80
20568731-1	2010	Protein disulfide isomerase (PDI), the chief endoplasmic reticulum (ER) resident oxidoreductase chaperone, is known to catalyze the maturation of disulfide bond-containing proteins primarily through oxidation and isomerization functions.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
10801974-2	2000	In the oxidized enzyme, we demonstrated two nonflavin redox centers by chemical modification and peptide sequencing: one was a disulfide within the sequence -Cys(59)-Val-Asn-Val-Gly-Cys(64), identical to the active site of GR; the other was a selenenylsulfide formed from Cys(497)-SeCys(498) and confirmed by mass spectrometry.	Disulfides	127-136	glutathione-disulfide reductase	Homo sapiens	223-225
10825541-0	2000	The ecto-5"-nucleotidase subunits in dimers are not linked by disulfide bridges but by non-covalent bonds.	Disulfides	62-71	5'-nucleotidase ecto	Homo sapiens	4-24
10825541-1	2000	It has long been considered that ecto-5"-nucleotidase (eNT) dimers consist of subunits linked by disulfide bonds.	Disulfides	97-106	5'-nucleotidase ecto	Homo sapiens	33-53
10825541-1	2000	It has long been considered that ecto-5"-nucleotidase (eNT) dimers consist of subunits linked by disulfide bonds.	Disulfides	97-106	5'-nucleotidase ecto	Homo sapiens	55-58
15215895-0	2004	Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS.	Disulfides	50-59	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	29-33
15215895-1	2004	The antioxidant enzyme Cu,Zn-superoxide dismutase (SOD1) has the distinction of being one of the most abundant disulfide-containing protein known in the eukaryotic cytosol; however, neither catalytic nor physiological roles for the conserved disulfide are known.	Disulfides	111-120	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	51-55
15215895-1	2004	The antioxidant enzyme Cu,Zn-superoxide dismutase (SOD1) has the distinction of being one of the most abundant disulfide-containing protein known in the eukaryotic cytosol; however, neither catalytic nor physiological roles for the conserved disulfide are known.	Disulfides	242-251	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	51-55
15215895-2	2004	Here we show that the disulfide status of Saccharomyces cerevisiae SOD1 significantly affects the monomer-dimer equilibrium, the interaction with the copper chaperone CCS, and the activity of the enzyme itself.	Disulfides	22-31	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	67-71
15215895-3	2004	Disulfide formation in SOD1 by O2 is slow but is greatly accelerated by the Cu-bound form of CCS (Cu-CCS) in vivo and in vitro even in the presence of excess reductants; once formed, this disulfide is kinetically stable.	Disulfides	0-9	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	23-27
15215895-3	2004	Disulfide formation in SOD1 by O2 is slow but is greatly accelerated by the Cu-bound form of CCS (Cu-CCS) in vivo and in vitro even in the presence of excess reductants; once formed, this disulfide is kinetically stable.	Disulfides	188-197	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	23-27
10825541-4	2000	2S) and amphiphilic (2.6S) eNT monomers were obtained after reduction of disulfide bonds in dimers.	Disulfides	73-82	5'-nucleotidase ecto	Homo sapiens	27-30
10825541-7	2000	The results unambiguously demonstrate that the subunits in eNT dimers are not linked by disulfide bridges, but by non-covalent bonds, and that dissociation precedes inactivation and unfolding.	Disulfides	88-97	5'-nucleotidase ecto	Homo sapiens	59-62
15215895-6	2004	Thus Cu-CCS mediation of correct disulfide formation in SOD1 is important for regulation of enzyme activity and for prevention of misfolding or aggregation.	Disulfides	33-42	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	56-60
20348090-7	2010	In particular, the amino-terminal domain of Pdi1p preferentially formed mixed disulfides with Ero1p in vivo, and we observed synthetic lethality between a temperature-sensitive Ero1p variant and mutant Pdi1p lacking the amino-terminal active-site disulfide.	Disulfides	78-88	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	44-49
15136577-3	2004	Our results reveal that two essential cysteine triads (Cys85-Cys94-Cys99 and Cys391-Cys394-Cys397) cooperate in electron transfer, with Cys94 likely forming mixed disulfides with PDI.	Disulfides	163-173	prolyl 4-hydroxylase subunit beta	Homo sapiens	179-182
10809777-2	2000	The common glycoprotein hormone alpha-subunit (GPH-alpha) contains five intramolecular disulfide bonds, three of which form a cystine knot motif (10-60, 28-82, and 32-84).	Disulfides	87-96	glycoprotein hormones, alpha polypeptide	Homo sapiens	47-56
10863933-1	2000	The 52-residue alpha/beta chimera of the epidermal growth factor-like domain in neu differentiation factor (NDFealpha/beta) has been synthesized and folded to form a three disulfide bridge (Cys182-Cys196, Cys190-Cys210, Cys212-Cys221) containing peptide.	Disulfides	172-181	neuregulin 1	Homo sapiens	80-106
15222768-5	2004	Mass spectrometric analysis of wild-type Sml1p revealed an intermolecular disulfide bond involving the cysteine residue at position 14 of the primary sequence.	Disulfides	74-83	ribonucleotide reductase inhibiting protein SML1	Saccharomyces cerevisiae S288C	41-46
20479580-2	2010	Lp(a) contains a unique protein, apolipoprotein(a), which is linked to the Apo B-100 through a disulfide bond that gives it a great structural homology with plasminogen, and confers it atherogenic and atherothrombotic properties.	Disulfides	95-104	lipoprotein(a)	Homo sapiens	0-5
15234539-6	2004	PDI increased significantly in plasma-blasts and plasma cells, indicating its importance in the highly specialized immunoglobulin assembly-machinery, including disulfide-bond isomerization.	Disulfides	160-169	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
10769120-0	2000	Two critical cysteine residues implicated in disulfide bond formation and proper folding of Kir2.1.	Disulfides	45-54	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	92-98
10769120-10	2000	Taken together, these results suggest that intramolecular disulfide bond exists between C122 and C154 of Kir2.1 channel and this cross-link might be required for proper channel folding.	Disulfides	58-67	potassium inwardly rectifying channel subfamily J member 2	Homo sapiens	105-111
20147296-10	2010	This is the first study to demonstrate PPIase-assisted folding of conotoxins, small disulfide-rich peptides with unique structural properties.	Disulfides	84-93	peptidylprolyl isomerase like 3	Homo sapiens	39-45
15028721-0	2004	Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C: use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C.	Disulfides	114-123	cystatin C	Homo sapiens	84-94
15028721-4	2004	The present work describes the production of two variants of wild type and L68Q cystatin C with disulfide bridges at positions selected to inhibit domain swapping without affecting the biological function of the four cystatin C variants as cysteine protease inhibitors.	Disulfides	96-105	cystatin C	Homo sapiens	80-90
10772986-3	2000	Because the epitope recognized by CL3 has two cysteine residues that could potentially produce a disulfide loop in gp41, we analyzed binding of our monoclonal antibody to the cyclic and linear motif of the peptide sequence IWGCSGKLICTTAVP (residues 600-614).	Disulfides	97-106	adhesion G protein-coupled receptor L3	Homo sapiens	34-37
20219472-13	2010	Our data indicate that in vitro, HuR RRM1 and RRM1,2 homodimerization involves a disulfide bond at cysteine 13.	Disulfides	81-90	ribonucleotide reductase catalytic subunit M1	Homo sapiens	37-41
15159594-2	2004	In vitro, it is possible via a reaction with 5,5"-dithiobis-(2-nitrobenzoic acid) to make a stable mixed-disulfide complex between thioredoxin from Staphylococcus aureus and one of its substrates, oxidized pI258 arsenate reductase (ArsC) from S. aureus.	Disulfides	105-114	AT695_RS07555	Staphylococcus aureus	131-142
15159594-5	2004	In the adduct form, the TNB molecule is buried in a hydrophobic pocket and the disulfide bridge between TNB and Cys89 is sterically inaccessible to thioredoxin.	Disulfides	79-88	AT695_RS07555	Staphylococcus aureus	148-159
15159594-6	2004	In order to form a mixed disulfide between ArsC and thioredoxin, a change in the orientation of the TNB-Cys89 disulfide in the structure is necessary.	Disulfides	25-34	AT695_RS07555	Staphylococcus aureus	52-63
20219472-13	2010	Our data indicate that in vitro, HuR RRM1 and RRM1,2 homodimerization involves a disulfide bond at cysteine 13.	Disulfides	81-90	ribonucleotide reductase catalytic subunit M1	Homo sapiens	46-50
10754306-8	2000	We hypothesize that PAO-induced L-selectin shedding involves a regulatory molecule, such as protein disulfide isomerase (PDI), an enzyme that plays a role in the formation and rearrangement of disulfide bonds, contains PAO-binding, vicinal dithiol-active sites, and is expressed on the neutrophil surface.	Disulfides	100-109	prolyl 4-hydroxylase subunit beta	Homo sapiens	121-124
20052969-2	2010	Here we show that simple diselenides can also facilitate the conversion of dithiols to disulfides in vivo, functionally replacing one such oxidoreductase, DsbA, in the oxidative folding of diverse proteins.	Disulfides	87-97	hydroxysteroid 17-beta dehydrogenase 6	Homo sapiens	139-153
10753942-4	2000	Syncollin has intramolecular disulfide bonds and was accessible to water-soluble cross-linking and biotinylating reagents only when granules were lysed by sonication.	Disulfides	29-38	syncollin	Homo sapiens	0-9
15026000-6	2004	Furthermore, the relation of LEKTI domain 6 to Kazal-type inhibitors is confirmed by determining its disulfide bond pattern (1-4/2-3) and its P(1) site located after the second Cys residue of LD-6.	Disulfides	101-110	serine peptidase inhibitor Kazal type 5	Homo sapiens	29-34
14656938-2	2004	In this report, we show that the oxidative regulatory responses of purified PKCdelta and PKCepsilon to cystine are recapitulated in disulfide-treated cells.	Disulfides	132-141	protein kinase C delta	Homo sapiens	76-84
19679200-7	2010	Thus, two catalytic domains of CA IX associate to form a dimer, which is stabilized by the formation of an intermolecular disulfide bond.	Disulfides	122-131	carbonic anhydrase 9	Homo sapiens	31-36
14684740-1	2004	Disulfide bond formation in the endoplasmic reticulum of eukaryotes is catalyzed by the ubiquitously expressed enzyme protein disulfide isomerase (PDI).	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	118-145
14684740-1	2004	Disulfide bond formation in the endoplasmic reticulum of eukaryotes is catalyzed by the ubiquitously expressed enzyme protein disulfide isomerase (PDI).	Disulfides	0-9	prolyl 4-hydroxylase subunit beta	Homo sapiens	147-150
14684740-2	2004	The effectiveness of PDI as a catalyst of native disulfide bond formation in folding polypeptides depends on the ability to catalyze disulfide-dithiol exchange, to bind non-native proteins, and to trigger conformational changes in the bound substrate, allowing access to buried cysteine residues.	Disulfides	49-58	prolyl 4-hydroxylase subunit beta	Homo sapiens	21-24
14684740-2	2004	The effectiveness of PDI as a catalyst of native disulfide bond formation in folding polypeptides depends on the ability to catalyze disulfide-dithiol exchange, to bind non-native proteins, and to trigger conformational changes in the bound substrate, allowing access to buried cysteine residues.	Disulfides	133-142	prolyl 4-hydroxylase subunit beta	Homo sapiens	21-24
10734129-4	2000	PDI contains two active site dithiols/disulfides.	Disulfides	38-48	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
10734129-9	2000	These observations indicated that platelet activation triggered reduction of the active site disulfides of PDI and a conformational change in GP1balpha that resulted in exposure of a free thiol(s).	Disulfides	93-103	prolyl 4-hydroxylase subunit beta	Homo sapiens	107-110
10713099-1	2000	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded, homodimeric mucin ( approximately 250 kDa) on leukocytes that binds to P-selectin on platelets and endothelial cells during the initial steps in inflammation.	Disulfides	47-56	LOC100508689	Homo sapiens	77-82
10700276-0	2000	Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.	Disulfides	33-42	putative protein DsbC	Escherichia coli	59-63
10700276-1	2000	DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is thought to function as a disulfide bond isomerase during oxidative protein folding in the periplasm.	Disulfides	59-68	putative protein DsbC	Escherichia coli	0-4
10700276-1	2000	DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is thought to function as a disulfide bond isomerase during oxidative protein folding in the periplasm.	Disulfides	116-125	putative protein DsbC	Escherichia coli	0-4
10700276-3	2000	We report the 1.9 A resolution crystal structure of oxidized DsbC where both Cys-X-X-Cys active sites form disulfide bonds.	Disulfides	107-116	putative protein DsbC	Escherichia coli	61-65
15169554-0	2004	Evolution of the HIV-1 envelope glycoproteins with a disulfide bond between gp120 and gp41.	Disulfides	53-62	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	76-81
15169554-1	2004	BACKGROUND: We previously described the construction of an HIV-1 envelope glycoprotein complex (Env) that is stabilized by an engineered intermolecular disulfide bond (SOS) between gp120 and gp41.	Disulfides	152-161	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	96-99
15169554-1	2004	BACKGROUND: We previously described the construction of an HIV-1 envelope glycoprotein complex (Env) that is stabilized by an engineered intermolecular disulfide bond (SOS) between gp120 and gp41.	Disulfides	152-161	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	181-186
15169554-4	2004	RESULTS: An HIV-1 molecular clone containing the SOS Env gene was only minimally replication competent, suggesting that the engineered disulfide bond substantially impaired Env function.	Disulfides	135-144	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	53-56
15169554-4	2004	RESULTS: An HIV-1 molecular clone containing the SOS Env gene was only minimally replication competent, suggesting that the engineered disulfide bond substantially impaired Env function.	Disulfides	135-144	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	173-176
20084172-2	2010	The disulfide cross-linked, N- and C-terminal domains of SP-B have been theoretically predicted to fold as charged, amphipathic helices, suggesting their participation in surfactant activities.	Disulfides	4-13	surfactant protein B	Homo sapiens	57-61
14760511-6	2004	The hydrophobic signal peptide sequence and the presence of cysteines needed for the interchain disulfide bonds were found to be conserved between clone KK34 and mammalian IL-5 proteins.	Disulfides	96-105	interleukin 5	Homo sapiens	172-176
14676197-3	2004	In the present study, we demonstrated that Epstein-Barr virus-transformed B cells and CD40-transfected HEK 293 cells constitutively expressed disulfide-linked CD40/CD40 homodimers at low levels.	Disulfides	142-151	CD40 molecule	Homo sapiens	86-90
14676197-3	2004	In the present study, we demonstrated that Epstein-Barr virus-transformed B cells and CD40-transfected HEK 293 cells constitutively expressed disulfide-linked CD40/CD40 homodimers at low levels.	Disulfides	142-151	CD40 molecule	Homo sapiens	159-163
10677237-21	2000	The differences are largely due to the four disulfide bonds in RNase A, which stabilize adjacent structures.	Disulfides	44-53	ribonuclease A family member 1, pancreatic	Homo sapiens	63-70
10652328-2	2000	This study tested the hypothesis that the disulfide bond formed between cysteine residues 35 and 46 (residues 235 and 246 of the SP-B proprotein) is essential for proper function of SP-B.	Disulfides	42-51	surfactant protein B	Homo sapiens	129-133
14676197-3	2004	In the present study, we demonstrated that Epstein-Barr virus-transformed B cells and CD40-transfected HEK 293 cells constitutively expressed disulfide-linked CD40/CD40 homodimers at low levels.	Disulfides	142-151	CD40 molecule	Homo sapiens	159-163
10716178-6	2000	Comparing the structure of TAP in TAP-BPTI with TAP bound to factor Xa(Xa) suggests a massive reorganization in the N-terminal tetrapeptide and the first disulfide loop of TAP (Cys5T-Cys15T) upon binding to Xa.	Disulfides	154-163	tracheal antimicrobial peptide	Bos taurus	27-30
20084172-3	2010	Earlier structural studies with Mini-B, a disulfide-linked construct based on the N- and C-terminal regions of SP-B (i.e., approximately residues 8-25 and 63-78), confirmed that these neighboring domains are helical; moreover, Mini-B retains critical in vitro and in vivo surfactant functions of the native protein.	Disulfides	42-51	surfactant protein B	Homo sapiens	111-115
10716178-6	2000	Comparing the structure of TAP in TAP-BPTI with TAP bound to factor Xa(Xa) suggests a massive reorganization in the N-terminal tetrapeptide and the first disulfide loop of TAP (Cys5T-Cys15T) upon binding to Xa.	Disulfides	154-163	tracheal antimicrobial peptide	Bos taurus	34-37
10716178-6	2000	Comparing the structure of TAP in TAP-BPTI with TAP bound to factor Xa(Xa) suggests a massive reorganization in the N-terminal tetrapeptide and the first disulfide loop of TAP (Cys5T-Cys15T) upon binding to Xa.	Disulfides	154-163	tracheal antimicrobial peptide	Bos taurus	34-37
10716178-6	2000	Comparing the structure of TAP in TAP-BPTI with TAP bound to factor Xa(Xa) suggests a massive reorganization in the N-terminal tetrapeptide and the first disulfide loop of TAP (Cys5T-Cys15T) upon binding to Xa.	Disulfides	154-163	tracheal antimicrobial peptide	Bos taurus	34-37
14676197-4	2004	Oligomerization of CD40 leads to a rapid and significant increase in the disulfide-linked CD40/CD40 homodimer formation, a response that could be prevented using a thiol-alkylating agent.	Disulfides	73-82	CD40 molecule	Homo sapiens	19-23
14676197-4	2004	Oligomerization of CD40 leads to a rapid and significant increase in the disulfide-linked CD40/CD40 homodimer formation, a response that could be prevented using a thiol-alkylating agent.	Disulfides	73-82	CD40 molecule	Homo sapiens	90-94
14676197-4	2004	Oligomerization of CD40 leads to a rapid and significant increase in the disulfide-linked CD40/CD40 homodimer formation, a response that could be prevented using a thiol-alkylating agent.	Disulfides	73-82	CD40 molecule	Homo sapiens	90-94
19854896-1	2010	Thioredoxin reductase (encoded by trxB) protects Staphylococcus aureus against oxygen or disulfide stress and is indispensable for growth.	Disulfides	89-98	AT695_RS13830	Staphylococcus aureus	0-21
10670717-0	2000	Peptide map procedure using immobilized protease cartridges in tandem for disulfide linkage identification of neu differentiation factor epidermal growth factor domain.	Disulfides	74-83	neuregulin 1	Homo sapiens	110-136
10670717-1	2000	Immobilized proteolytic enzyme cartridges were used to rapidly digest neu differentiation factor EGF domain in order to obtain improved peptide maps useful for assignment of disulfide linkages.	Disulfides	174-183	neuregulin 1	Homo sapiens	70-96
10670717-3	2000	The entire process can be automated using a commercially available workstation; and the total time required for both proteolytic digestion and the HPLC separation can be shortened to within 1 h. Using these immobilized columns, we demonstrated that disulfide structure assignment of the EGF domains of recombinant human neu differentiation factor can be performed by isolation of individual disulfide-containing peptides followed by assignment of disulfide linkages with prompt fragmentation of peptides using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.	Disulfides	249-258	neuregulin 1	Homo sapiens	320-346
14733943-2	2004	We report that peroxynitrite-induced disulfides in porcine brain tubulin are repaired by the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH.	Disulfides	37-47	glutathione-disulfide reductase	Homo sapiens	135-156
14733943-3	2004	Reduction of disulfide bonds between the alpha- and beta-tubulin subunits by the glutathione reductase system was assessed by Western blot.	Disulfides	13-22	glutathione-disulfide reductase	Homo sapiens	81-102
14757749-2	2004	Rather than relying on small molecule oxidants like glutathione, it is now clear that disulfide formation is driven by a protein relay involving Ero1, a novel conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by molecular oxygen and in turn acts as a specific oxidant of PDI, which then directly oxidizes disulfide bonds in folding proteins.	Disulfides	86-95	prolyl 4-hydroxylase subunit beta	Homo sapiens	195-222
14757749-2	2004	Rather than relying on small molecule oxidants like glutathione, it is now clear that disulfide formation is driven by a protein relay involving Ero1, a novel conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by molecular oxygen and in turn acts as a specific oxidant of PDI, which then directly oxidizes disulfide bonds in folding proteins.	Disulfides	86-95	prolyl 4-hydroxylase subunit beta	Homo sapiens	224-227
10623829-1	2000	The T cell coreceptor CD8 exists on mature T cells as disulfide-linked homodimers of CD8 alpha polypeptide chains and heterodimers of CD8 alpha- and CD8 beta-chains.	Disulfides	54-63	CD8 antigen, alpha chain	Mus musculus	85-94
19835883-7	2009	The IL-17A is a disulfide-linked homodimer that is similar in structure to IL-17F, adopting a cystine-knot fold.	Disulfides	16-25	interleukin 17F	Homo sapiens	75-81
11094439-5	2000	The conformation of PR3 is stabilized by four disulfide bonds and, to a lesser extent, by asparagine-linked glycosylation.	Disulfides	46-55	proteinase 3	Homo sapiens	20-23
14757749-2	2004	Rather than relying on small molecule oxidants like glutathione, it is now clear that disulfide formation is driven by a protein relay involving Ero1, a novel conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by molecular oxygen and in turn acts as a specific oxidant of PDI, which then directly oxidizes disulfide bonds in folding proteins.	Disulfides	86-95	prolyl 4-hydroxylase subunit beta	Homo sapiens	309-312
14757749-2	2004	Rather than relying on small molecule oxidants like glutathione, it is now clear that disulfide formation is driven by a protein relay involving Ero1, a novel conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by molecular oxygen and in turn acts as a specific oxidant of PDI, which then directly oxidizes disulfide bonds in folding proteins.	Disulfides	203-212	prolyl 4-hydroxylase subunit beta	Homo sapiens	224-227
19956735-4	2009	We found that Cys109 in Nm23-H1 is oxidized to various oxidation states including intra- and inter-disulfide crosslinks, glutathionylation, and sulfonic acid formation in response to H(2)O(2) treatment both in vivo and in vitro.	Disulfides	99-108	NME/NM23 nucleoside diphosphate kinase 1	Homo sapiens	24-31
15000751-3	2004	Western blot analysis of cell lysates under nonreducing or reducing conditions revealed one clear immunoreactive species corresponding to the size of a putative receptor dimer or a monomer, respectively, consistent with the presence of disulfide-linked hLOX-1 complexes.	Disulfides	236-245	oxidized low density lipoprotein receptor 1	Homo sapiens	253-259
15000751-4	2004	Site-directed mutagenesis studies indicated that cysteine 140 has a key role in the formation of these disulfide-linked hLOX-1 dimers.	Disulfides	103-112	oxidized low density lipoprotein receptor 1	Homo sapiens	120-126
15000751-5	2004	Eliminating this intermolecular disulfide bond markedly impairs the recognition of Escherichia coli by hLOX-1.	Disulfides	32-41	oxidized low density lipoprotein receptor 1	Homo sapiens	103-109
10521264-0	1999	Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid.	Disulfides	86-96	cathepsin K	Cricetulus griseus	14-25
14729690-0	2004	Genetic analysis of disulfide isomerization in Escherichia coli: expression of DsbC is modulated by RNase E-dependent mRNA processing.	Disulfides	20-29	putative protein DsbC	Escherichia coli	79-83
19956735-7	2009	Oxidized Nm23 is a substrate of NADPH-TrxR1-thioredoxin shuttle system, and the disulfide crosslinking is reversibly reduced and the enzymatic activity is recovered by this system.	Disulfides	80-89	NME/NM23 nucleoside diphosphate kinase 1	Homo sapiens	9-13
14729690-9	2004	These results (i) confirm the central role of DsbC in disulfide bond isomerization in the bacterial periplasm and (ii) suggest a critical role for RNase E in regulating DsbC expression.	Disulfides	54-63	putative protein DsbC	Escherichia coli	46-50
19886835-6	2009	Cystamine is a small disulfide that gives rise to sulfane sulfur when it undergoes oxidation catalyzed by diamine oxidase (a ubiquitous enzyme in animals).	Disulfides	21-30	amine oxidase copper containing 1	Homo sapiens	106-121
14581473-1	2004	During lipoprotein(a) (Lp(a)) assembly, non-covalent interactions between apolipoprotein(a) (apo(a)) and low density lipoprotein precede specific disulfide bond formation.	Disulfides	146-155	lipoprotein(a)	Homo sapiens	23-28
10491631-10	1999	Similarities to members of the four-disulfide-core family suggest clues to ESP13.2 function.	Disulfides	36-45	beta-defensin 126	Macaca fascicularis	75-82
10441134-14	1999	In summary, these studies indicate that PDI functions to form disulfide-linked complexes of vitronectin with thrombin-AT.	Disulfides	62-71	prolyl 4-hydroxylase subunit beta	Homo sapiens	40-43
19756380-8	2009	This demonstrates, for the first time, that disulfide bridge formation of the domain is involved in the occludin dimerization.	Disulfides	44-53	occludin	Homo sapiens	104-112
10375435-9	1999	A comparative study of recombinant human lens TTase and GST (mu and pi) on their dethiolating abilities using lens crystallin-thiol mixed disulfides showed that the lens TTase is 60-70% more efficient in the dethiolation/repair process than GST.	Disulfides	138-148	glutaredoxin	Homo sapiens	46-51
10375435-9	1999	A comparative study of recombinant human lens TTase and GST (mu and pi) on their dethiolating abilities using lens crystallin-thiol mixed disulfides showed that the lens TTase is 60-70% more efficient in the dethiolation/repair process than GST.	Disulfides	138-148	glutaredoxin	Homo sapiens	170-175
10375435-10	1999	When TTase and GST were tested in conjunction for the dethiolation of thiol mixed disulfides, there was no significant enhancement of dethiolase activity.	Disulfides	82-92	glutaredoxin	Homo sapiens	5-10
14702300-0	2004	Transcriptional regulation of the Staphylococcus aureus thioredoxin and thioredoxin reductase genes in response to oxygen and disulfide stress.	Disulfides	126-135	AT695_RS07555	Staphylococcus aureus	56-67
14702300-0	2004	Transcriptional regulation of the Staphylococcus aureus thioredoxin and thioredoxin reductase genes in response to oxygen and disulfide stress.	Disulfides	126-135	AT695_RS07555	Staphylococcus aureus	72-83
19551705-10	2009	We then applied our protocol to human leukocyte antigen CD69, for which the disulfide bonding is known, but only for its monomeric form.	Disulfides	76-85	CD69 antigen	Mus musculus	56-60
15197303-4	2004	5,5"-dithiobis (2-nitrobenzoic acid) (DTNB) acts to regenerate disulfide bonds between the two Fabs, whereas o-phenylenedimaleimide (o-PDM) acts to form a thioether bond between the two Fabs.	Disulfides	63-72	dystrobrevin beta	Homo sapiens	38-42
10403184-0	1999	The disulfide bond pattern between fragments obtained by the limited proteolysis of bovine thyroglobulin.	Disulfides	4-13	thyroglobulin	Bos taurus	91-104
10403184-1	1999	The comparative analysis of the products of the limited proteolysis of bovine thyroglobulin with trypsin by SDS-polyacrylamide gel electrophoresis in non-reducing and reducing conditions revealed the presence of disulfide linkages between some of the fragments.	Disulfides	212-221	thyroglobulin	Bos taurus	78-91
10403184-2	1999	In order to define the disulfide bond pattern between the proteolytic fragments of thyroglobulin, these were isolated by SDS-polyacrylamide gel electrophoresis in non-reducing conditions and electrophoretic transfer onto polyvinylidene difluoride membranes.	Disulfides	23-32	thyroglobulin	Bos taurus	83-96
10403184-9	1999	On the base of these data, a model is presented in which distinct subsets of cysteine-rich repeats and the carboxy-terminal, acetylcholinesterase-similar domain of thyroglobulin form sequentially aligned subdomains with internal disulfide linkages.	Disulfides	229-238	thyroglobulin	Bos taurus	164-177
10087161-9	1999	Together these data support an inhibitory mechanism, whereby cysteine -SH groups within the p56(lck) catalytic domain react with the isothiazolone ring, leading to ring opening and disulfide bond formation with the p56(lck) enzyme.	Disulfides	181-190	cyclin dependent kinase like 2	Homo sapiens	92-95
14640681-9	2003	Ahp1 is unique among the D-type Prx"s in its ability to form an intermolecular disulfide.	Disulfides	79-88	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	0-4
14645097-2	2003	In platelet-type von Willebrand disease, two mutations, G233V and M239V, have been described within the Cys209-Cys248 disulfide loop of GPIbalpha that compromise hemostasis by increasing the affinity for vWF.	Disulfides	118-127	von Willebrand factor	Cricetulus griseus	204-207
19786553-7	2009	We report that whereas gp96 undergoes intermolecular disulfide bond formation via Cys(138), gp93 is unable to do so due to the absence of a cysteine near the same region.	Disulfides	53-62	heat shock protein 90, beta (Grp94), member 1	Mus musculus	23-27
14628104-4	2003	A cysteine residue in the second cytoplasmic domain in mammalian C5aR, required for formation of disulfide-linked dimers, is seen in trout C5aR but not in other similar rhodopsin-like receptors.	Disulfides	97-106	C5a anaphylatoxin chemotactic receptor 1	Oncorhynchus mykiss	139-143
14610200-3	2003	We have created a RV containing a chimeric HIV-1 Env protein, which contains introduced cysteine residues that give rise to an intermolecular disulfide bridge between gp120 and the ectodomain of gp41.	Disulfides	142-151	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	49-52
14610200-3	2003	We have created a RV containing a chimeric HIV-1 Env protein, which contains introduced cysteine residues that give rise to an intermolecular disulfide bridge between gp120 and the ectodomain of gp41.	Disulfides	142-151	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	167-172
10085135-0	1999	Angiostatin formation involves disulfide bond reduction and proteolysis in kringle 5 of plasmin.	Disulfides	31-40	plasminogen	Homo sapiens	88-95
10085135-4	1999	We present evidence that the Cys461-Cys540 and Cys511-Cys535 disulfide bonds in kringle 5 of plasmin were reduced by plasmin reductase.	Disulfides	61-70	plasminogen	Homo sapiens	93-100
10085135-4	1999	We present evidence that the Cys461-Cys540 and Cys511-Cys535 disulfide bonds in kringle 5 of plasmin were reduced by plasmin reductase.	Disulfides	61-70	plasminogen	Homo sapiens	117-124
19786553-8	2009	However, abrogation of disulfide bond formation by substituting C with A (C138A) in gp96 via site-directed mutagenesis did not compromise its chaperone function.	Disulfides	23-32	heat shock protein 90, beta (Grp94), member 1	Mus musculus	84-88
19786553-11	2009	Moreover, gp96 N-terminal disulfide bond formation is not critical for its function, underscoring the importance of N-terminal dimerization via non-disulfide bond-mediated interactions in client protein folding by gp96.	Disulfides	26-35	heat shock protein 90, beta (Grp94), member 1	Mus musculus	10-14
9986706-2	1999	The 2.1-A resolution crystal structure of GR inhibited by (E)-ajoene revealed a mixed disulfide between the active site Cys58 and the CH2=CH-CH2-SO-CH2-CH=CH-S moiety of ajoene.	Disulfides	86-95	glutathione-disulfide reductase	Homo sapiens	42-44
19583444-1	2009	The V3 loop of the HIV-1gp120 glycoprotein presenting 35-residue-long, frequently glycosylated, highly variable, and disulfide bonded structure plays the central role in the virus biology and forms the principal target for neutralizing antibodies and the major viral determinant for co-receptor binding.	Disulfides	117-126	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	24-29
9891011-0	1999	Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase.	Disulfides	42-52	prolyl 4-hydroxylase subunit beta	Homo sapiens	56-83
9891011-1	1999	Protein disulfide isomerase (PDI) facilitates proper folding and disulfide bonding of nascent proteins in the endoplasmic reticulum and is secreted by cells and associates with the cell surface.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
9891011-2	1999	We examined the consequence of over- or underexpression of PDI in HT1080 fibrosarcoma cells for the redox state of cell-surface protein thiols/disulfides.	Disulfides	143-153	prolyl 4-hydroxylase subunit beta	Homo sapiens	59-62
14624581-0	2003	Disulfide bond isomerization in basic pancreatic trypsin inhibitor: multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling.	Disulfides	0-9	cysteine rich secretory protein LCCL domain containing 2	Homo sapiens	49-66
12954617-3	2003	Candidate components of intersubunit disulfides (Cys213, Cys214, and Cys267) were identified using matrix-assisted laser desorption ionization time-of-flight spectroscopy of iodoacetamide-modified DmGCLM as well as examination of the evolutionary conservation of cysteines.	Disulfides	37-47	Glutamate-cysteine ligase modifier subunit	Drosophila melanogaster	197-203
9891011-11	1999	These findings indicated that secreted PDI was controlling the redox state of existing exofacial protein thiols or reactive disulfide bonds.	Disulfides	124-133	prolyl 4-hydroxylase subunit beta	Homo sapiens	39-42
19776277-3	2009	Crystallographic, biochemical, and functional studies suggest that GluR2 Cys mutants which form intermolecular disulfide cross-links between the lower D2 lobes of the ligand binding cores can be trapped in a conformation that represents the desensitized state.	Disulfides	111-120	glutamate ionotropic receptor AMPA type subunit 2	Homo sapiens	67-72
9852122-6	1998	The roles of the half-cystines in the CGLCG motifs in the assembly of disulfide-bonded multimers of mucin were also assessed.	Disulfides	70-79	LOC100508689	Homo sapiens	100-105
9852122-13	1998	It is possible that these motifs in mucins are engaged in the thiol-disulfide interchange reactions during the assembly of disulfide-bonded multimers of mucin.	Disulfides	68-77	LOC100508689	Homo sapiens	36-41
9852122-13	1998	It is possible that these motifs in mucins are engaged in the thiol-disulfide interchange reactions during the assembly of disulfide-bonded multimers of mucin.	Disulfides	123-132	LOC100508689	Homo sapiens	36-41
12750926-4	2003	One of the most important angiogenic factors is the vascular endothelial cell growth factor (VEGF), a glycosylated protein of 46-48 kDa composed of two disulfide-linked subunits.	Disulfides	152-161	vascular endothelial growth factor A	Ovis aries	52-91
12750926-4	2003	One of the most important angiogenic factors is the vascular endothelial cell growth factor (VEGF), a glycosylated protein of 46-48 kDa composed of two disulfide-linked subunits.	Disulfides	152-161	vascular endothelial growth factor A	Ovis aries	93-97
19766572-5	2009	Prdx1 activates GDE2 through reduction of an intramolecular disulfide bond that bridges its intracellular N- and C-terminal domains.	Disulfides	60-69	glycerophosphodiester phosphodiesterase domain containing 5	Homo sapiens	16-20
14598324-2	2003	We have shown previously that thiol reducing agents, such as dithiothreitol, activate EP 24.15 by mediating the conversion of inactive multimeric forms to active monomers and that this conversion involves the disruption of intermolecular disulfide bonds involving cysteine residues 246, 248, and 253.	Disulfides	238-247	thimet oligopeptidase 1	Homo sapiens	86-94
14523092-5	2003	After expression in HEK 293 cells of such modified P2X2 or P2X4 subunits, the disulfide bond formation is evident because an ATP-evoked channel opening requires previous reduction with dithiothreitol.	Disulfides	78-87	purinergic receptor P2X 4	Homo sapiens	59-63
12957712-1	2003	Several cyclic disulfide alpha-melanocyte stimulating hormone (alpha-MSH) analogues containing the aromatic fluorescent amino acid beta-(2-naphthyl)-D-alanine (D-Nal) have high affinity and selectivity for the melanocortin (MC)-4 receptor.	Disulfides	15-24	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	131-138
12941038-5	2003	Structural analysis of the FVIII A domain homology model allowed us to identify residues 664 and 1826 as a potential disulfide bond pair.	Disulfides	117-126	coagulation factor VIII	Homo sapiens	27-32
9878517-3	1998	Immunoblots of human control and rat brain tissues with and without reduction show that human DRPLA protein forms more disulfide-bond complexes than rat DRPLA protein.	Disulfides	119-128	atrophin 1	Homo sapiens	94-99
9860827-2	1998	TTase acts as a potent and specific reducing agent for protein-S-S-glutathione mixed disulfides (protein-SSG) likely formed during oxidative stress or as redox intermediates in signal transduction pathways.	Disulfides	85-95	glutaredoxin	Homo sapiens	0-5
19766572-6	2009	GDE2 variants incapable of disulfide bond formation acquire independence from Prdx1 and are potent inducers of motor neuron differentiation.	Disulfides	27-36	glycerophosphodiester phosphodiesterase domain containing 5	Homo sapiens	0-4
9839241-2	1998	kappa-Casein is also involved in thiol-catalyzed disulfide interchange reactions with the whey proteins during heat treatments and, after rennet cleavage, in the facilitation of micelle coagulation.	Disulfides	49-58	casein kappa	Homo sapiens	0-12
19710473-4	2009	The ectodomain of FIBCD1 is characterized by a coiled-coil region, a polycationic region and C-terminal fibrinogen-related domain that by disulfide linkage assembles the protein into tetramers.	Disulfides	138-147	fibrinogen C domain containing 1	Homo sapiens	18-24
9760253-6	1998	Data are presented which indicate that the Cu-induced protein modification responsible for the inactivation of ALR2 is the generation on the enzyme of an intramolecular disulfide bond.	Disulfides	169-178	lens aldose reductase pseudogene	Bos taurus	111-115
12911312-7	2003	The shortest isoform of selenoprotein P, which terminates at residue 244, was analyzed for selenide-sulfide and disulfide linkages.	Disulfides	112-121	selenoprotein P	Rattus norvegicus	24-39
9760253-7	1998	GSH significantly interferes with the Cu-dependent inactivation of ALR2 and induces, through its oxidation to GSSG, the generation of an enzyme form linked to a glutathionyl residue by a disulfide bond.	Disulfides	187-196	lens aldose reductase pseudogene	Bos taurus	67-71
19361571-1	2009	PDI enzymes are oxidoreductases that catalyze oxidation, reduction and isomerization of disulfide bonds in polypeptide substrates.	Disulfides	88-97	prolyl 4-hydroxylase subunit beta	Bos taurus	0-3
9808198-3	1998	In this study we describe the epitope of the mAb H52 which has been mapped to a predicted disulfide-bonded loop (C386 and C400) in the beta2 integrin subunit.	Disulfides	90-99	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	135-140
12867999-1	2003	Clusterin is a heterodimeric, disulfide-linked 70-80 kDa glycoprotein that is induced during regression of most, if not all, hormone-dependent epithelial tissues.	Disulfides	30-39	clusterin	Homo sapiens	0-9
12867999-5	2003	This leads to the appearance of a 50-53 kDa uncleaved, nonglycosylated, disulfide-linked isoform of clusterin that accumulates in the nucleus.	Disulfides	72-81	clusterin	Homo sapiens	100-109
12846582-0	2003	G3 domains of aggrecan and PG-M/versican form intermolecular disulfide bonds that stabilize cell-matrix interaction.	Disulfides	61-70	versican	Homo sapiens	32-40
12846582-5	2003	Here, we demonstrated for the first time that the G3 domains of aggrecan and another proteoglycan, PG-M/versican, formed intermolecular disulfide bonds, and all subdomains were involved.	Disulfides	136-145	versican	Homo sapiens	104-112
19722646-4	2009	Analytical ultracentrifugation and equilibrium disulfide interchange show that the stability of MS1 is greatest when Gly is at each "a" position of the heptad repeat (MS1-Gly), followed by Ala &gt; Val &gt; Ile.	Disulfides	47-56	MS	Homo sapiens	96-99
12846582-9	2003	Furthermore, disruption of disulfide bonds also reduced the role of PG-M/versican G3 domain in mediating cell adhesion.	Disulfides	27-36	versican	Homo sapiens	73-81
9737954-2	1998	PDI introduces disulfide bonds into newly synthesized proteins and catalyzes disulfide bond isomerizations.	Disulfides	15-24	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
9737954-2	1998	PDI introduces disulfide bonds into newly synthesized proteins and catalyzes disulfide bond isomerizations.	Disulfides	77-86	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
9737954-3	1998	We have synthesized a library of disulfide-linked fluorescence-quenched peptides, individually linked to resin beads, for two purposes: 1) to probe PDI specificity, and 2) to identify simple, sensitive peptide substrates of PDI.	Disulfides	33-42	prolyl 4-hydroxylase subunit beta	Homo sapiens	148-151
9737954-3	1998	We have synthesized a library of disulfide-linked fluorescence-quenched peptides, individually linked to resin beads, for two purposes: 1) to probe PDI specificity, and 2) to identify simple, sensitive peptide substrates of PDI.	Disulfides	33-42	prolyl 4-hydroxylase subunit beta	Homo sapiens	224-227
12944372-6	2003	TNSALP (D289V) exhibited no alkaline phosphatase activity and mainly formed a disulfide-linked high molecular mass aggregate.	Disulfides	78-87	alkaline phosphatase, biomineralization associated	Homo sapiens	0-6
19542232-1	2009	Eukaryotic Cu,Zn-superoxide dismutases (SOD1s) are generally thought to acquire the essential copper cofactor and intramolecular disulfide bond through the action of the CCS copper chaperone.	Disulfides	129-138	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	40-44
12707279-1	2003	The sequencing of the genome of Arabidopsis thaliana revealed that this plant contained numerous isoforms of thioredoxin (Trx), a protein involved in thiol-disulfide exchanges.	Disulfides	156-165	thioredoxin H-type 1	Arabidopsis thaliana	109-120
12707279-1	2003	The sequencing of the genome of Arabidopsis thaliana revealed that this plant contained numerous isoforms of thioredoxin (Trx), a protein involved in thiol-disulfide exchanges.	Disulfides	156-165	thioredoxin H-type 1	Arabidopsis thaliana	122-125
9814841-12	1998	This finding suggests that nitroaromatics may bind close to the thioredoxin-binding site at the catalytic disulfide domain of TR, and induce a conformational change of enzymes (S.B.	Disulfides	106-115	thioredoxin H-type 1	Arabidopsis thaliana	64-75
19542232-1	2009	Eukaryotic Cu,Zn-superoxide dismutases (SOD1s) are generally thought to acquire the essential copper cofactor and intramolecular disulfide bond through the action of the CCS copper chaperone.	Disulfides	129-138	copper chaperone for superoxide dismutase	Homo sapiens	170-173
9724519-4	1998	When WT-PLB was denatured in guanidine at pH 8.1, all three cysteines reacted, disrupting the pentamer, which was restored upon cleavage of the disulfide bonds with DTT.	Disulfides	144-153	phospholamban	Homo sapiens	8-11
19542232-6	2009	The two pathways, however, strongly diverge when assayed for the SOD1 disulfide.	Disulfides	70-79	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	65-69
9668062-10	1998	This insoluble MUC2 mucin was recovered by immunoprecipitation after reduction of disulfide bonds.	Disulfides	82-91	LOC100508689	Homo sapiens	20-25
9653033-10	1998	Importantly, further physiological relevance of the disulfide motif was obtained by examining the mutants and alkylated MIF in an immunological assay that involved the macrophage-activating properties of MIF.	Disulfides	52-61	macrophage migration inhibitory factor	Homo sapiens	120-123
9653033-10	1998	Importantly, further physiological relevance of the disulfide motif was obtained by examining the mutants and alkylated MIF in an immunological assay that involved the macrophage-activating properties of MIF.	Disulfides	52-61	macrophage migration inhibitory factor	Homo sapiens	204-207
12795589-5	2003	It is shown here that there is a 10-fold increase in the propensity of the unfolded reduced forms of RNase A to form the native set of disulfides directly, compared to the propensity under strongly denaturing conditions (4-6 M GdnHCl).	Disulfides	135-145	ribonuclease A family member 1, pancreatic	Homo sapiens	101-108
12745250-1	2003	Oxidoreductases such as glutaredoxin are a major class of enzymes that reversibly catalyze thiol-disulfide exchange reactions.	Disulfides	97-106	glutaredoxin	Homo sapiens	24-36
19542232-7	2009	SOD1 molecules that are activated without CCS exhibit disulfide oxidation in vivo without oxygen and under copper-depleted conditions.	Disulfides	54-63	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	0-4
9648890-3	1998	Manipulation of the disulfide bonds in POMC and proPC2 blocked their transport to the trans-Golgi network and strongly inhibited their processing.	Disulfides	20-29	proopiomelanocortin L homeolog	Xenopus laevis	39-43
19542232-7	2009	SOD1 molecules that are activated without CCS exhibit disulfide oxidation in vivo without oxygen and under copper-depleted conditions.	Disulfides	54-63	copper chaperone for superoxide dismutase	Homo sapiens	42-45
19542232-8	2009	The strict requirement for copper, oxygen, and CCS in disulfide bond oxidation appears exclusive to yeast SOD1, and we find that a unique proline at position 144 in yeast SOD1 is responsible for this disulfide effect.	Disulfides	54-63	copper chaperone for superoxide dismutase	Homo sapiens	47-50
12796815-3	2003	Computer modeling of the alpha-helical coiled-coil domains of the HSF1 monomer and trimer showed that the alignment of the N- and C-terminal hydrophobic repeats of HSF1 monomer could bring C(3)(Cys(153))close to C(4) and C(5)(Cys(373) and Cys(378), respectively), in positions permissible for disulfide bond formation under appropriate experimental conditions.	Disulfides	293-302	heat shock transcription factor 1	Homo sapiens	66-70
12796815-3	2003	Computer modeling of the alpha-helical coiled-coil domains of the HSF1 monomer and trimer showed that the alignment of the N- and C-terminal hydrophobic repeats of HSF1 monomer could bring C(3)(Cys(153))close to C(4) and C(5)(Cys(373) and Cys(378), respectively), in positions permissible for disulfide bond formation under appropriate experimental conditions.	Disulfides	293-302	heat shock transcription factor 1	Homo sapiens	164-168
19542232-8	2009	The strict requirement for copper, oxygen, and CCS in disulfide bond oxidation appears exclusive to yeast SOD1, and we find that a unique proline at position 144 in yeast SOD1 is responsible for this disulfide effect.	Disulfides	54-63	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	106-110
12796815-4	2003	The results suggest that redox-dependent thiol-disulfide exchange can provide a mechanism for regulation the conformation and activity of hHSF1.	Disulfides	47-56	heat shock transcription factor 1	Homo sapiens	138-143
9618260-6	1998	Interestingly, this TNSALP mutant was found to form a disulfide-bonded high-molecular-mass aggregate and was rapidly degraded within the cell, though the mutant protein was modified by glycosylphosphatidylinositol (GPI).	Disulfides	54-63	alkaline phosphatase, biomineralization associated	Homo sapiens	20-26
19542232-8	2009	The strict requirement for copper, oxygen, and CCS in disulfide bond oxidation appears exclusive to yeast SOD1, and we find that a unique proline at position 144 in yeast SOD1 is responsible for this disulfide effect.	Disulfides	54-63	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	171-175
19542232-8	2009	The strict requirement for copper, oxygen, and CCS in disulfide bond oxidation appears exclusive to yeast SOD1, and we find that a unique proline at position 144 in yeast SOD1 is responsible for this disulfide effect.	Disulfides	200-209	copper chaperone for superoxide dismutase	Homo sapiens	47-50
19542232-8	2009	The strict requirement for copper, oxygen, and CCS in disulfide bond oxidation appears exclusive to yeast SOD1, and we find that a unique proline at position 144 in yeast SOD1 is responsible for this disulfide effect.	Disulfides	200-209	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	171-175
12791251-4	2003	We show that binding to F-actin induces a conformational change in plectin that is inhibited by an engineered interdomain disulfide bridge.	Disulfides	122-131	plectin	Homo sapiens	67-74
19588927-3	2009	To identify the interface regions that mediate oligomerization of Ste2, a set of 73 different mutants with Cys residues substituted near the extracellular ends of the transmembrane domains were screened for the ability to form intermolecular disulfide bonds.	Disulfides	242-251	alpha-factor pheromone receptor STE2	Saccharomyces cerevisiae S288C	66-70
12639955-7	2003	To show that this transition underlies the thermal regulation of the chaperone system, we introduced an intersubunit disulfide bond into the paired long helices of the GrpE dimer.	Disulfides	117-126	GrpE like 1, mitochondrial	Homo sapiens	168-172
9578571-3	1998	Previous studies revealed some of the structural features of Ang that underlie its catalytic inefficiency: Gln-117 blocks the space corresponding to the pyrimidine binding site of RNase A and Ang lacks the disulfide loop 65-72 that forms most of the purine binding site of RNase A.	Disulfides	206-215	angiogenin	Homo sapiens	61-64
12639955-8	2003	The transition was absent in disulfide-linked GrpE R40C but was restored by reduction.	Disulfides	29-38	GrpE like 1, mitochondrial	Homo sapiens	46-50
19588927-4	2009	Disulfide bonds formed between Cys residues at six positions in Ste2.	Disulfides	0-9	alpha-factor pheromone receptor STE2	Saccharomyces cerevisiae S288C	64-68
12639955-9	2003	With disulfide-stabilized GrpE, the rate of ADP/ATP exchange and conversion of DnaK from its ADP-liganded high affinity R state to the ATP-liganded low affinity T state continuously increased with increasing temperature.	Disulfides	5-14	GrpE like 1, mitochondrial	Homo sapiens	26-30
9578571-3	1998	Previous studies revealed some of the structural features of Ang that underlie its catalytic inefficiency: Gln-117 blocks the space corresponding to the pyrimidine binding site of RNase A and Ang lacks the disulfide loop 65-72 that forms most of the purine binding site of RNase A.	Disulfides	206-215	ribonuclease A family member 1, pancreatic	Homo sapiens	180-187
9578571-3	1998	Previous studies revealed some of the structural features of Ang that underlie its catalytic inefficiency: Gln-117 blocks the space corresponding to the pyrimidine binding site of RNase A and Ang lacks the disulfide loop 65-72 that forms most of the purine binding site of RNase A.	Disulfides	206-215	ribonuclease A family member 1, pancreatic	Homo sapiens	273-280
19583593-1	2009	Protein disulfide isomerase (PDI) and other PDI family proteins are members of the thioredoxin superfamily and are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum (ER).	Disulfides	8-17	thioredoxin	Glycine max	83-94
19571123-6	2009	We inferred the locations of the two beta 4 transmembrane (TM) helices TM1 and TM2 relative to the seven alpha TM helices, S0-S6, from the extent of disulfide bond formation between cysteines substituted in the extracellular flanks of these TM helices.	Disulfides	149-158	tropomyosin 1, alpha	Mus musculus	79-82
9593640-6	1998	In other tissues, an enzyme, thioltransferase (TTase), has been shown to be responsible for thiol/disulfide regulation.	Disulfides	98-107	glutaredoxin	Homo sapiens	29-45
9531277-3	1998	However, a large proportion of Qa-1b was found to be disulfide linked to gp44 without any detectable beta 2m.	Disulfides	53-62	histocompatibility 2, T region locus 23	Mus musculus	31-36
9560003-1	1998	Ten overlapping 15-mer peptides, spanning the entire inner disulfide loop of human C-reactive protein (residues 36-97), were used to isolate a potent inhibitor of the enzymes human leukocyte elastase and human leukocyte cathepsin G, which are associated with chronic inflammatory tissue damage.	Disulfides	59-68	elastase, neutrophil expressed	Homo sapiens	181-199
12719560-1	2003	We previously described a human immunodeficiency virus type 1 (HIV-1) envelope mutant that introduces a disulfide bridge between the gp120 surface proteins and gp41 transmembrane proteins (J. M. Binley, R. W. Sanders, B. Clas, N. Schuelke, A.	Disulfides	104-113	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	133-138
12719576-0	2003	Human immunodeficiency virus type 1 Env with an intersubunit disulfide bond engages coreceptors but requires bond reduction after engagement to induce fusion.	Disulfides	61-70	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	36-39
12719576-1	2003	A mutant human immunodeficiency virus (HIV) envelope protein (Env) with an engineered disulfide bond between the gp120 and gp41 subunits (SOS-Env) was expressed on cell surfaces.	Disulfides	86-95	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	62-65
12566443-1	2003	Lipoprotein(a) (Lp(a)) assembly proceeds via a two-step mechanism in which initial non-covalent interactions between apolipoprotein(a) (apo(a)) and low density lipoprotein precede disulfide bond formation.	Disulfides	180-189	lipoprotein(a)	Homo sapiens	0-14
12566443-1	2003	Lipoprotein(a) (Lp(a)) assembly proceeds via a two-step mechanism in which initial non-covalent interactions between apolipoprotein(a) (apo(a)) and low density lipoprotein precede disulfide bond formation.	Disulfides	180-189	lipoprotein(a)	Homo sapiens	16-21
12747729-7	2003	Further, upon disulfide formation, dixanthogens are reduced by glutathione reductase to a redox active xanthate.	Disulfides	14-23	glutathione-disulfide reductase	Homo sapiens	63-84
9506953-4	1998	Here we have analyzed the receptor binding and activating properties of several cysteine mutants of VEGF-C including those (Cys156 and Cys165), which in other platelet-derived growth factor/VEGF family members mediate interchain disulfide bonding.	Disulfides	229-238	vascular endothelial growth factor C	Bos taurus	100-106
19038358-6	2009	Grx1 catalyzes the reduction of two disulfide bridges in gp120 in a similar manner as PDI.	Disulfides	36-45	glutaredoxin	Homo sapiens	0-4
19038358-9	2009	Our findings suggest that Grx1 activity is important for HIV-1 entry and that Grx1 and the gp120 intramolecular disulfides are novel pharmacological targets for rational drug development.	Disulfides	112-122	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	91-96
12562843-0	2003	Apolipoprotein[a] secretion from hepatoma cells is regulated in a size-dependent manner by alterations in disulfide bond formation.	Disulfides	106-115	lipoprotein(a)	Homo sapiens	0-16
9430691-8	1998	[14C]Iodoacetamide labeling of free thiols of cysteine residues in mutant connexin-43s showed that two pairs of intramolecular disulfide bonds are formed between Cys54 and Cys192 and between Cys187 and Cys198.	Disulfides	127-136	gap junction protein alpha 1	Homo sapiens	74-85
19244249-5	2009	The first four residues in the structure are constrained to form a hairpin loop by the single disulfide bond in amylin.	Disulfides	94-103	islet amyloid polypeptide	Homo sapiens	112-118
9430691-9	1998	These results suggest that intercellular Ca2+ signaling takes place in cultured cells expressing connexin-43, leading to their own synchronization and that the extracellular disulfide bonds of connexin-43 are crucial for this process.	Disulfides	174-183	gap junction protein alpha 1	Homo sapiens	97-108
9430691-9	1998	These results suggest that intercellular Ca2+ signaling takes place in cultured cells expressing connexin-43, leading to their own synchronization and that the extracellular disulfide bonds of connexin-43 are crucial for this process.	Disulfides	174-183	gap junction protein alpha 1	Homo sapiens	193-204
9407058-7	1997	While in gel filtration the protein is eluted with a molecular mass of congruent with900 kDa, gel electrophoresis using nondenaturing, nonreducing conditions revealed that PTX3 forms multimers predominantly of 440 kDa apparent molecular mass, corresponding to decamers, and that disulfide bonds are required for multimer formation.	Disulfides	279-288	pentraxin-related protein PTX3	Cricetulus griseus	172-176
9407058-14	1997	Thus, as predicted on the basis of computer modeling, the prototypic long pentraxin PTX3 forms multimers, which differ from those formed by classical pentraxins in terms of protomer composition and requirement for disulfide bonds, and does not recognize CRP/SAP ligands.	Disulfides	214-223	pentraxin-related protein PTX3	Cricetulus griseus	84-88
12605606-4	2003	The effects on disulfide bond formation in the peptide by Zn (II) and Co (II) ions were also examined for this analog.	Disulfides	15-24	cytochrome c oxidase II, mitochondrial	Rattus norvegicus	70-77
19273600-0	2009	Intramolecular disulfide bonds of the prolactin receptor short form are required for its inhibitory action on the function of the long form of the receptor.	Disulfides	15-24	prolactin receptor	Homo sapiens	38-56
12595265-7	2003	The helix alpha3 is shortened by more than two turns when compared with alpha3 of hPrP, which is enforced by the positioning of the second disulfide bond in hDpl.	Disulfides	139-148	prion like protein doppel	Homo sapiens	157-161
9407136-8	1997	The corresponding half-cystine residue in human prepro-von Willebrand factor is also involved in interchain disulfide bond formation, which is consistent with the sequence identity of the half-cystine residues in norrin and part of the half-cystine residues in a disulfide-rich domain of von Willebrand factor.	Disulfides	108-117	norrin cystine knot growth factor NDP	Homo sapiens	213-219
9407136-8	1997	The corresponding half-cystine residue in human prepro-von Willebrand factor is also involved in interchain disulfide bond formation, which is consistent with the sequence identity of the half-cystine residues in norrin and part of the half-cystine residues in a disulfide-rich domain of von Willebrand factor.	Disulfides	263-272	norrin cystine knot growth factor NDP	Homo sapiens	213-219
9407136-11	1997	These studies suggest that norrin is a secreted protein that forms disulfide-bonded oligomers that are associated with the extracellular matrix upon secretion from cells.	Disulfides	67-76	norrin cystine knot growth factor NDP	Homo sapiens	27-33
9407136-12	1997	Moreover, the disulfide-rich motif of norrin and prepro-von Willebrand factor promotes interchain disulfide bond formation among polypeptides in which it is found.	Disulfides	14-23	norrin cystine knot growth factor NDP	Homo sapiens	38-44
19404536-7	2009	Surface-associated PDI has been previously shown to catalyse two distinct functions: transnitrosation with subsequent release of intracellular nitric oxide and disulfide bond rearrangement during platelet integrin ligation.	Disulfides	160-169	prolyl 4-hydroxylase subunit beta	Homo sapiens	19-22
9407136-12	1997	Moreover, the disulfide-rich motif of norrin and prepro-von Willebrand factor promotes interchain disulfide bond formation among polypeptides in which it is found.	Disulfides	98-107	norrin cystine knot growth factor NDP	Homo sapiens	38-44
9395456-2	1997	Enteropeptidase is synthesized as a single-chain protein, whereas purified enteropeptidase contains a approximately 47-kDa serine protease domain (light chain) and a disulfide-linked approximately 120-kDa heavy chain.	Disulfides	166-175	transmembrane serine protease 15	Bos taurus	75-90
12715890-4	2003	By addition of N-terminal cysteine residues we have generated a disulfide-conjugated CP1B with the cell-penetrating 16-mer peptide penetratin derived from the third helix of the Antennapedia homeodomain protein.	Disulfides	64-73	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	85-89
12770769-9	2003	To rationalize our results we postulate that platelet alpha6FucT is folded through disulfide bonds that bring together donor/acceptor-binding- and cysteine- and lysine-rich, presumably acceptor substrate binding sites, thus creating a catalytic center of the enzyme.	Disulfides	83-92	fucosyltransferase 8	Homo sapiens	54-64
12421832-9	2003	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.	Disulfides	100-109	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	72-79
12421832-12	2003	The large number of disulfide bonds of the PAPP-A.pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.	Disulfides	20-29	pappalysin 1	Homo sapiens	43-49
12421832-12	2003	The large number of disulfide bonds of the PAPP-A.pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.	Disulfides	20-29	myelin basic protein	Homo sapiens	54-57
9392417-1	1997	Lipoprotein[a], Lp[a], represents a class of lipoprotein particles that have as a protein moiety apoB-100 linked by a disulfide bridge to a multi-kringle structure, apolipoprotein[a], or apo[a].	Disulfides	118-127	lipoprotein(a)	Homo sapiens	16-20
19852088-6	2009	In this Account, we describe our studies of AlkB, ABH2, and ABH3, including our development of a general strategy to trap homogeneous protein-DNA complexes through active-site disulfide cross-linking.	Disulfides	176-185	alkB homolog 2, alpha-ketoglutarate dependent dioxygenase	Homo sapiens	50-54
9368610-4	1997	Analysis by flow cytometry and surface labeling with 125I showed that the recombinant MAFA (rMAFA) was expressed as a monomeric and disulfide-linked homodimeric glycoprotein in the membrane of the insect cells, and both forms exhibited the same epitopes as the protein isolated from RBL-2H3 cells.	Disulfides	132-141	killer cell lectin like receptor G1	Rattus norvegicus	86-90
9368610-4	1997	Analysis by flow cytometry and surface labeling with 125I showed that the recombinant MAFA (rMAFA) was expressed as a monomeric and disulfide-linked homodimeric glycoprotein in the membrane of the insect cells, and both forms exhibited the same epitopes as the protein isolated from RBL-2H3 cells.	Disulfides	132-141	MAF bZIP transcription factor A	Rattus norvegicus	92-97
12421832-12	2003	The large number of disulfide bonds of the PAPP-A.pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.	Disulfides	135-144	pappalysin 1	Homo sapiens	156-162
12421832-12	2003	The large number of disulfide bonds of the PAPP-A.pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.	Disulfides	135-144	pappalysin 1	Homo sapiens	156-162
14616057-4	2003	Furthermore, different stresses can result in distinct modifications to the same protein; in OxyR it seems that distinct modifications can occur at the same cysteine, and in Yap1 a partner protein ensures that the disulfide bond induced by peroxide stress is different from the disulfide bond induced by other stresses.	Disulfides	214-223	Yes1 associated transcriptional regulator	Homo sapiens	174-178
14616057-4	2003	Furthermore, different stresses can result in distinct modifications to the same protein; in OxyR it seems that distinct modifications can occur at the same cysteine, and in Yap1 a partner protein ensures that the disulfide bond induced by peroxide stress is different from the disulfide bond induced by other stresses.	Disulfides	278-287	Yes1 associated transcriptional regulator	Homo sapiens	174-178
19852088-6	2009	In this Account, we describe our studies of AlkB, ABH2, and ABH3, including our development of a general strategy to trap homogeneous protein-DNA complexes through active-site disulfide cross-linking.	Disulfides	176-185	alkB homolog 3, alpha-ketoglutarate dependent dioxygenase	Homo sapiens	60-64
9287313-2	1997	Human CD69 contains only a single consensus sequence for N-linked oligosaccharide addition within its extracellular domain (Asn-Val-Thr), yet exists as two distinct glycoforms that are assembled together into disulfide-linked homodimers and heterodimers.	Disulfides	209-218	CD69 molecule	Homo sapiens	6-10
19336037-6	2009	We propose that Vanabin2 forms a possible electron transfer cascade from the electron donor, NADPH, via glutathione reductase, glutathione, and Vanabin2 to the acceptor, and vanadium ions conjugated through thiol-disulfide exchange reactions.	Disulfides	213-222	glutathione-disulfide reductase	Homo sapiens	104-125
9315320-6	1997	Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione.	Disulfides	49-58	glutaredoxin	Homo sapiens	0-12
9315320-6	1997	Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione.	Disulfides	49-58	glutaredoxin	Homo sapiens	14-17
9315320-6	1997	Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione.	Disulfides	93-102	glutaredoxin	Homo sapiens	0-12
9315320-6	1997	Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione.	Disulfides	93-102	glutaredoxin	Homo sapiens	14-17
9268305-1	1997	trans-4,5-Dihydroxy-1,2-dithiane, the intramolecular disulfide form of dithiothreitol (DTTox) transcriptionally activates the stress-responsive genes gadd153(chop) and grp78.	Disulfides	53-62	heat shock protein family A (Hsp70) member 5	Sus scrofa	168-173
12395426-1	2002	The human p8(MTCP1) protein is constituted by an original disulfide bridged alpha-hairpin motif, and a third hydrophilic helix that appeared mobile and independent in NMR analysis.	Disulfides	58-67	mature T cell proliferation 1	Homo sapiens	13-18
19309163-1	2009	The oxidative folding pathways of two four-disulfide proteins of the ribonuclease family, ONC and RNase A, which have similar three-dimensional folds but only 30% sequence homology, are compared.	Disulfides	43-52	ribonuclease A family member 1, pancreatic	Homo sapiens	98-105
12377051-3	2002	Both with and without dipic the reaction has the stoichiometry 2[Mo(CN)(8)](3-) + 2TGA --&gt; 2[Mo(CN)(8)](4-) + RSSR, where RSSR is the disulfide derived from formal oxidative dimerization of TGA.	Disulfides	137-146	T-box transcription factor 1	Homo sapiens	83-86
12356317-4	2002	Despite the loss of a stabilizing disulfide bond in domain 1 (D1) of CD2, adhesive failure occurs abruptly with no evidence of partial protein unfolding during detachment.	Disulfides	34-43	CD2 antigen	Mus musculus	69-72
9242665-8	1997	However, addition of low amounts of the disulfide-reducing agent 2-ME during the binding assay revealed formation of a complex between IRP1 and IRE.	Disulfides	40-49	aconitase 1	Homo sapiens	135-139
9444979-6	1997	Reduction and subsequent alkylation of disulfide bridges of defensins greatly decreased the C1q binding ability but complement activation (C4b binding) remained high.	Disulfides	39-48	complement C4B (Chido blood group)	Homo sapiens	139-142
19274343-9	2009	These results suggest that ERp18 has a reduction role on disulfide bonds in wild-type hGnRHR folding.	Disulfides	57-66	gonadotropin releasing hormone receptor	Homo sapiens	86-92
9273886-2	1997	It is a 31-residue polypeptide reticulated by three disulfide bridges, i.e. Cys3-Cys21, Cys8-Cys26 and Cys12-Cys28.	Disulfides	52-61	cystathionase (cystathionine gamma-lyase)	Mus musculus	76-80
9273886-5	1997	The NMR studies reveal a three-dimensional structure identical with the native toxin for the analog lacking disulfide bridge Cys3-Cys21 and a loss of organized structure for another analog lacking disulfide bridge Cys12-Cys28.	Disulfides	108-117	cystathionase (cystathionine gamma-lyase)	Mus musculus	125-129
12097589-1	2002	We describe the further properties of a protein, designated SOS gp140, wherein the association of the gp120 and gp41 subunits of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein is stabilized by an intersubunit disulfide bond.	Disulfides	232-241	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	102-107
18992757-10	2009	We hypothesize that the substitutions of Ser23 and Gln52 in yGrx1 by Ala23 and Glu52 in yGrx2 modify the capability of the active-site C-terminal cysteine to attack the mixed disulfide between the N-terminal active-site cysteine and the glutathione molecule.	Disulfides	175-184	dithiol glutaredoxin GRX2	Saccharomyces cerevisiae S288C	88-93
12036872-9	2002	Replacing the N-terminal disulfide loops of GPIb beta (amino acids 1-14) with the corresponding disulfide loops of GPIX (amino acids 1-22) resulted in surface expression of coexpressed wildtype GPIX.	Disulfides	25-34	glycoprotein IX platelet	Homo sapiens	194-198
12036872-9	2002	Replacing the N-terminal disulfide loops of GPIb beta (amino acids 1-14) with the corresponding disulfide loops of GPIX (amino acids 1-22) resulted in surface expression of coexpressed wildtype GPIX.	Disulfides	96-105	glycoprotein IX platelet	Homo sapiens	115-119
12036872-9	2002	Replacing the N-terminal disulfide loops of GPIb beta (amino acids 1-14) with the corresponding disulfide loops of GPIX (amino acids 1-22) resulted in surface expression of coexpressed wildtype GPIX.	Disulfides	96-105	glycoprotein IX platelet	Homo sapiens	194-198
9195947-9	1997	Antibody studies suggest that MUC6 in its native form exists as a disulfide-bonded multimer.	Disulfides	66-75	mucin 6, oligomeric mucus/gel-forming	Homo sapiens	30-34
18985675-1	2009	We recently isolated a protein disulfide isomerase (PDI) from the Rubiaceae (coffee family) plant Oldenlandia affinis (OaPDI) and demonstrated that it facilitates the production of disulfide-knotted defense proteins called cyclotides.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Homo sapiens	52-55
9182589-1	1997	The region between the 10th and 12th cysteine (Cys88-Cys105 in human thyroid-stimulating hormone beta-subunit (hTSHbeta)) of the glycoprotein hormone beta-subunits corresponds to the disulfide-linked seat-belt region.	Disulfides	183-192	thyroid stimulating hormone subunit beta	Homo sapiens	111-119
9188699-9	1997	Sequencing of both native rat SP-A and human SP-A also revealed isoforms with disulfide-forming NH2-terminal extensions.	Disulfides	78-87	surfactant protein A1	Homo sapiens	45-49
12071705-8	2002	Purified B7-2 binds tightly to bacterially expressed monomeric and disulfide-linked homodimeric human CTLA-4 as shown by gel-filtration chromatography and native PAGE.	Disulfides	67-76	CD86 molecule	Homo sapiens	9-13
19777571-3	2009	Enhanced biomimicry of SP-B"s disulfide-bonded structure has been previously attempted via disulfide-mediated dimerization of SP-B(1-25) and other peptide mimics, which improved surface activity relative to the monomers.	Disulfides	30-39	surfactant protein B	Homo sapiens	23-27
12034449-0	2002	In vitro folding, functional characterization, and disulfide pattern of the extracellular domain of human GLP-1 receptor.	Disulfides	51-60	glucagon like peptide 1 receptor	Homo sapiens	106-120
9236773-2	1997	The homeodomain in the C-terminal region of Mat alpha 2 functions as a DNA-binding domain and the N-terminal region, containing two cysteine residues at positions 33 and 34, is thought to be involved in formation of Mat alpha 2 homodimers via disulfide bonds.	Disulfides	243-252	homeodomain mating type protein alpha2	Saccharomyces cerevisiae S288C	44-55
19777571-3	2009	Enhanced biomimicry of SP-B"s disulfide-bonded structure has been previously attempted via disulfide-mediated dimerization of SP-B(1-25) and other peptide mimics, which improved surface activity relative to the monomers.	Disulfides	30-39	surfactant protein B	Homo sapiens	126-130
19777571-3	2009	Enhanced biomimicry of SP-B"s disulfide-bonded structure has been previously attempted via disulfide-mediated dimerization of SP-B(1-25) and other peptide mimics, which improved surface activity relative to the monomers.	Disulfides	91-100	surfactant protein B	Homo sapiens	23-27
19777571-3	2009	Enhanced biomimicry of SP-B"s disulfide-bonded structure has been previously attempted via disulfide-mediated dimerization of SP-B(1-25) and other peptide mimics, which improved surface activity relative to the monomers.	Disulfides	91-100	surfactant protein B	Homo sapiens	126-130
9082998-1	1997	During oxidative protein folding, efficient catalysis of disulfide rearrangements by protein-disulfide isomerase is found to involve an escape mechanism that prevents the enzyme from becoming trapped in covalent complexes with substrates that fail to rearrange in a timely fashion.	Disulfides	57-66	prolyl 4-hydroxylase subunit beta	Homo sapiens	85-112
19053265-4	2008	We conclude that HNO produces a disulfide bond that alters the conformation of PLN, relieving inhibition of the Ca(2+) pump.	Disulfides	32-41	phospholamban	Homo sapiens	79-82
11854276-7	2002	First, among the six disulfide bonds, only SS1 in loop E (Gly(142)-Leu(155)) and SS6 in loop G (Ser(185)-Gly(197)) were necessary for the catalytic efficiency of neuropsin.	Disulfides	21-30	opsin 5	Mus musculus	162-171
19007166-3	2008	More disulfide bonds that associated acidic and basic polypeptides of glycinin broke as the sodium bisulfite concentration increased.	Disulfides	5-14	LOC732636	Glycine max	70-78
11897673-3	2002	In pregnancy serum, PAPP-A circulates as a disulfide-bound complex with the precursor form of major basic protein (pro-MBP), and in this complex PAPP-A"s proteolytic activity is not evident.	Disulfides	43-52	pappalysin 1	Homo sapiens	20-26
11897673-3	2002	In pregnancy serum, PAPP-A circulates as a disulfide-bound complex with the precursor form of major basic protein (pro-MBP), and in this complex PAPP-A"s proteolytic activity is not evident.	Disulfides	43-52	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	76-113
11897673-3	2002	In pregnancy serum, PAPP-A circulates as a disulfide-bound complex with the precursor form of major basic protein (pro-MBP), and in this complex PAPP-A"s proteolytic activity is not evident.	Disulfides	43-52	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	115-122
11724803-2	2002	Similar to furin-like proprotein convertases, MT1-MMP directly processes a single chain precursor of alpha(v) integrin subunit (pro-alpha(v)) into the heavy and light alpha-chains connected by a disulfide bridge.	Disulfides	195-204	matrix metallopeptidase 14	Homo sapiens	46-53
9227279-0	1997	Disulfide bond formation of cysteine-37 and cysteine-66 of beta B2 crystallin during cataractogenesis of the human lens.	Disulfides	0-9	crystallin beta B2	Homo sapiens	59-77
9227279-6	1997	Based upon previous knowledge of the three dimensional structure of beta B2 crystallin, formation of this disulfide bond suggests that significant denaturation of the beta B2 crystallin molecule has occurred during the process of human lens opacification.	Disulfides	106-115	crystallin beta B2	Homo sapiens	68-86
9227279-6	1997	Based upon previous knowledge of the three dimensional structure of beta B2 crystallin, formation of this disulfide bond suggests that significant denaturation of the beta B2 crystallin molecule has occurred during the process of human lens opacification.	Disulfides	106-115	crystallin beta B2	Homo sapiens	167-185
19007166-6	2008	Sodium bisulfite-induced disulfide bond cleavage increased the surface hydrophobicity of modified glycinin.	Disulfides	25-34	LOC732636	Glycine max	98-106
12061835-1	2002	IL-12 is a 75 kDa heterodimeric cytokine composed of two disulfide-linked subunits, p35 and p40, which plays an important role in the regulation of the immune response.	Disulfides	57-66	interleukin 9	Homo sapiens	92-95
18849342-7	2008	These interactions were required for the efficient maturation of NA as it prematurely formed intramolecular disulfides and aggregated when calnexin and calreticulin interactions were abolished.	Disulfides	108-118	neuraminidase 1	Homo sapiens	65-67
9138023-0	1997	The interchain disulfide bond between TCR alpha beta heterodimers on human T cells is not required for TCR-CD3 membrane expression and signal transduction.	Disulfides	15-24	T cell receptor alpha constant	Homo sapiens	38-47
9138023-5	1997	This result was supported by the finding that the interchain disulfide bond between TCR alpha and beta chains is not required for membrane expression or transmembrane signal transduction of TCR alpha beta-CD3 complexes.	Disulfides	61-70	T cell receptor alpha constant	Homo sapiens	84-93
18849342-10	2008	A subset of NA formed intermolecular disulfides and oligomerized cotranslationally.	Disulfides	37-47	neuraminidase 1	Homo sapiens	12-14
11969158-3	2002	It was shown that, in Caf1M-Hg (a derivative in which the disulfide bond is replaced by an S-Hg-S bond), the first to melt is the N-domain.	Disulfides	58-67	F1 capsule protein	Yersinia pestis	22-27
18849342-12	2008	NA dimerization also occurred for an NA mutant lacking the critical large loop disulfide bond, indicating that dimerization did not require proper NA oxidation.	Disulfides	79-88	neuraminidase 1	Homo sapiens	0-2
18849342-12	2008	NA dimerization also occurred for an NA mutant lacking the critical large loop disulfide bond, indicating that dimerization did not require proper NA oxidation.	Disulfides	79-88	neuraminidase 1	Homo sapiens	37-39
18849342-12	2008	NA dimerization also occurred for an NA mutant lacking the critical large loop disulfide bond, indicating that dimerization did not require proper NA oxidation.	Disulfides	79-88	neuraminidase 1	Homo sapiens	37-39
19216714-1	2008	Among the key antioxidant enzymes, thioredoxin and glutaredoxin systems play an important role in cell defense against oxidative stress and maintenance of redox homeostasis owing to the regulation of thiol-disulfide exchange.	Disulfides	206-215	glutaredoxin	Homo sapiens	51-63
11896678-10	2002	As revealed by spectrophotometry, mass spectrometry, and gel electrophoresis, the exceptionally strong inhibition by Cu(II) was associated with Fhit dimerization through formation of a disulfide bond.	Disulfides	185-194	fragile histidine triad diadenosine triphosphatase	Homo sapiens	144-148
11851405-1	2002	We present here evidence that redox-dependent thiol-disulfide exchange can provide a mechanism regulating the conformation and activity of the human heat shock transcription factor 1 (HSF1).	Disulfides	52-61	heat shock transcription factor 1	Homo sapiens	149-182
11851405-1	2002	We present here evidence that redox-dependent thiol-disulfide exchange can provide a mechanism regulating the conformation and activity of the human heat shock transcription factor 1 (HSF1).	Disulfides	52-61	heat shock transcription factor 1	Homo sapiens	184-188
11851405-5	2002	We showed that preincubation of the latent HSF1 monomer with diamide inhibited the in vitro heat-induced activation and trimerization of HSF1 and caused the formation of ox-hHSF1, a compact, disulfide cross-linked HSF1 conformer detectable in immuno-Western blot assay.	Disulfides	191-200	heat shock transcription factor 1	Homo sapiens	43-47
11851405-5	2002	We showed that preincubation of the latent HSF1 monomer with diamide inhibited the in vitro heat-induced activation and trimerization of HSF1 and caused the formation of ox-hHSF1, a compact, disulfide cross-linked HSF1 conformer detectable in immuno-Western blot assay.	Disulfides	191-200	heat shock transcription factor 1	Homo sapiens	173-178
11851405-7	2002	Cysteine site-specific mutants of HSF1 were constructed and used to determine which of the five cysteine residues may be engaged in disulfide cross-link.	Disulfides	132-141	heat shock transcription factor 1	Homo sapiens	34-38
11705998-2	2002	The crystal structure of modified human GR at 1.9-A resolution provides the first picture of protein inactivation by peroxynitrite and reveals that this is due to the exclusive nitration of 2 Tyr residues (residues 106 and 114) at the glutathione disulfide-binding site.	Disulfides	247-256	glutathione-disulfide reductase	Homo sapiens	40-42
11705998-4	2002	By oxidizing the catalytic dithiol to a disulfide, peroxynitrite itself can act as a substrate of unmodified and bisnitrated P. falciparum glutathione reductase.	Disulfides	40-49	glutathione-disulfide reductase	Homo sapiens	139-160
11694508-1	2002	Protein-disulfide isomerase (PDI) catalyzes the formation, rearrangement, and breakage of disulfide bonds and is capable of binding peptides and unfolded proteins in a chaperone-like manner.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
11694508-7	2002	The present results suggest that PDI is acting both as an isomerase and as a chaperone during folding and disulfide bond formation of proinsulin.	Disulfides	106-115	prolyl 4-hydroxylase subunit beta	Homo sapiens	33-36
11754565-0	2002	Heat-induced covalent complex between casein micelles and beta-lactoglobulin from goat"s milk: identification of an involved disulfide bond.	Disulfides	125-134	beta-lactoglobulin	Capra hircus	58-76
11928826-1	2002	Apolipoprotein(a) [apo(a)] is the distinctive glycoprotein of lipoprotein Lp(a), which is disulfide linked to the apo B100 of a low density lipoprotein particle.	Disulfides	90-99	lipoprotein(a)	Homo sapiens	0-17
11928826-1	2002	Apolipoprotein(a) [apo(a)] is the distinctive glycoprotein of lipoprotein Lp(a), which is disulfide linked to the apo B100 of a low density lipoprotein particle.	Disulfides	90-99	lipoprotein(a)	Homo sapiens	62-79
16233282-1	2002	DsbC, which catalyzes disulfide isomerization, was overproduced in the periplasm of Escherichia coli and purified from the periplasmic fraction by osmotic shock and anion-exchange chromatography.	Disulfides	22-31	putative protein DsbC	Escherichia coli	0-4
16233282-4	2002	Ox-DsbC facilitated the refolding of proteins with multiple disulfide bonds in both oxidative and reductive environments, while red-DsbC facilitated refolding only in the former.	Disulfides	60-69	putative protein DsbC	Escherichia coli	3-7
11752709-6	2002	They further suggest that the formation of an intrachain disulfide bond between the two cysteine residues of the sigmaC polypeptide has a negative effect on oligomer stability.	Disulfides	57-66	sigma-C protein	Avian orthoreovirus	113-119
12031340-5	2002	We suggest that the ratio between free sulfhydryl groups and disulfide bonds of the cysteine residues of VR1 pre-sets sensitivity of primary nociceptors to algogens and may represent a new target for treating some pain states in humans.	Disulfides	61-70	transient receptor potential cation channel subfamily V member 1	Homo sapiens	105-108
16245126-6	2002	CF(1) is a latent ATPase, activated additively by the high-energy state of the thylakoids, and by reduction of a disulfide bond on the gamma subunit.	Disulfides	113-122	dynein axonemal heavy chain 8	Homo sapiens	18-24
11595747-2	2001	The bacterial expression of the MBP/gp21 chimeras resulted in soluble trimers containing intramonomer disulfide bonds.	Disulfides	102-111	myelin basic protein	Homo sapiens	32-35
11679578-2	2001	Intermolecular disulfide bonds involve Cys(39) and probably Cys(147) of two adjacent cofilin units.	Disulfides	15-24	cofilin 1	Homo sapiens	85-92
11679578-9	2001	However, stabilization of cofilin oligomers in cytoplasm is probably achieved not by disulfide bonds but by a local increase in cofilin concentration and/or binding of regulatory proteins.	Disulfides	85-94	cofilin 1	Homo sapiens	26-33
11747440-4	2001	Introducing a disulfide bond between partner hinges within a dimer via the mutation V52C results in a protein that has increased affinity for O(1) operator DNA compared to wild-type LacI and abolishes allosteric response to inducer [Falcon, C. M., Swint-Kruse, L., and Matthews, K. S. (1997) J. Biol.	Disulfides	14-23	tissue factor pathway inhibitor	Homo sapiens	182-186
11747440-7	2001	We have established that this high affinity is maintained for the disulfide-linked protein even when symmetry and half-site spacing within the operator region are altered, whereas binding by the reduced protein, as for wild-type LacI, is severely diminished by these alterations.	Disulfides	66-75	tissue factor pathway inhibitor	Homo sapiens	229-233
11747440-9	2001	Temperature studies demonstrate that the presence of the disulfide alters the thermodynamics of the protein-DNA interaction, with a DeltaC(p) of significantly smaller magnitude compared to wild-type LacI.	Disulfides	57-66	tissue factor pathway inhibitor	Homo sapiens	199-203
11735395-5	2001	The overall fold of CR7 is similar to those of CR3 and CR8 from the LRP and LB5 from the LDL receptor, though the low degree of sequence homology of residues not involved in calcium coordination or in disulfide formation results in a distinct pattern of surface residues for each domain, including CR7.	Disulfides	201-210	teratocarcinoma-derived growth factor 1 pseudogene 3	Homo sapiens	47-50
11826952-6	2001	On the other hand, a single intrachain disulfide bond could be identified from ovalbumins of five species using a combination of peptide mapping and N-terminal amino acid sequencing analysis under reduced and non-reduced conditions, in which the intrachain disulfide bond was like that of hen ovalbumin (Cys73-Cys120).	Disulfides	39-48	ovalbumin	Anas platyrhynchos	79-88
11826952-6	2001	On the other hand, a single intrachain disulfide bond could be identified from ovalbumins of five species using a combination of peptide mapping and N-terminal amino acid sequencing analysis under reduced and non-reduced conditions, in which the intrachain disulfide bond was like that of hen ovalbumin (Cys73-Cys120).	Disulfides	257-266	ovalbumin	Anas platyrhynchos	79-88
11555655-5	2001	The addition of a non-native disulfide bond to ERDD RNase 1 not only increases the conformational stability of the enzyme but also increases its cytotoxicity such that its IC(50) value is only 8-fold greater than that of Onconase.	Disulfides	29-38	ribonuclease A family member 1, pancreatic	Homo sapiens	52-59
11705695-11	2001	The fact that GS-Pt inhibits the mammalian Trx as well as Grx systems shows that CDDP may exert effects at several stages of its metabolism, including after conjugation with GSH, which are intimately linked with the cellular disulfide/dithiol redox regulatory systems.	Disulfides	225-234	glutaredoxin	Homo sapiens	58-61
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	Disulfides	174-183	lens aldose reductase pseudogene	Bos taurus	42-46
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	Disulfides	174-183	lens aldose reductase pseudogene	Bos taurus	58-62
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	Disulfides	174-183	lens aldose reductase pseudogene	Bos taurus	58-62
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	Disulfides	174-183	lens aldose reductase pseudogene	Bos taurus	119-126
11580274-8	2001	A pathway of thiol/disulfide interconversion for bovine lens ALR2 induced, in oxidative conditions, by physiological thiol compounds is proposed.	Disulfides	19-28	lens aldose reductase pseudogene	Bos taurus	61-65
11473115-1	2001	We have previously shown that lipoprotein(a) (Lp(a)) assembly involves an initial noncovalent interaction between sequences within apolipoprotein(a) (apo(a)) kringle IV types 5-8 and the amino terminus of apolipoprotein B-100 (sequences between amino acids 680 and 781 in apoB-100), followed by formation of a disulfide bond.	Disulfides	310-319	lipoprotein(a)	Homo sapiens	30-44
11473115-1	2001	We have previously shown that lipoprotein(a) (Lp(a)) assembly involves an initial noncovalent interaction between sequences within apolipoprotein(a) (apo(a)) kringle IV types 5-8 and the amino terminus of apolipoprotein B-100 (sequences between amino acids 680 and 781 in apoB-100), followed by formation of a disulfide bond.	Disulfides	310-319	lipoprotein(a)	Homo sapiens	46-51
11473115-1	2001	We have previously shown that lipoprotein(a) (Lp(a)) assembly involves an initial noncovalent interaction between sequences within apolipoprotein(a) (apo(a)) kringle IV types 5-8 and the amino terminus of apolipoprotein B-100 (sequences between amino acids 680 and 781 in apoB-100), followed by formation of a disulfide bond.	Disulfides	310-319	lipoprotein(a)	Homo sapiens	131-148
11473115-1	2001	We have previously shown that lipoprotein(a) (Lp(a)) assembly involves an initial noncovalent interaction between sequences within apolipoprotein(a) (apo(a)) kringle IV types 5-8 and the amino terminus of apolipoprotein B-100 (sequences between amino acids 680 and 781 in apoB-100), followed by formation of a disulfide bond.	Disulfides	310-319	lipoprotein(a)	Homo sapiens	150-156
11524675-5	2001	This domain is linked to SOD1 by an intermolecular disulfide bond that may facilitate or regulate copper delivery.	Disulfides	51-60	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	25-29
11397793-1	2001	A thiol/disulfide oxidoreductase component of the GSH system, glutaredoxin (Grx), is involved in the reduction of GSH-based mixed disulfides and participates in a variety of cellular redox pathways.	Disulfides	130-140	glutaredoxin	Homo sapiens	62-74
11397793-1	2001	A thiol/disulfide oxidoreductase component of the GSH system, glutaredoxin (Grx), is involved in the reduction of GSH-based mixed disulfides and participates in a variety of cellular redox pathways.	Disulfides	130-140	glutaredoxin	Homo sapiens	76-79
11413331-0	2001	Functional analysis of the disulfide-bonded loop/chain reversal region of human immunodeficiency virus type 1 gp41 reveals a critical role in gp120-gp41 association.	Disulfides	27-36	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	142-147
11413331-7	2001	We now report that in contrast to our findings with HTLV-1, conservative substitutions in the HIV-1 gp41 disulfide-bonded loop/chain reversal region abolished association with gp120.	Disulfides	105-114	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	176-181
11413331-11	2001	The HIV-1 gp41 disulfide-bonded loop/chain reversal region is a critical gp120 contact site; therefore, it is also likely to play a central role in fusion activation by linking CD4 plus chemokine receptor-induced conformational changes in gp120 to gp41 fusogenicity.	Disulfides	15-24	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	73-78
11413331-11	2001	The HIV-1 gp41 disulfide-bonded loop/chain reversal region is a critical gp120 contact site; therefore, it is also likely to play a central role in fusion activation by linking CD4 plus chemokine receptor-induced conformational changes in gp120 to gp41 fusogenicity.	Disulfides	15-24	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	239-244
11313344-9	2001	We propose that Erv2p functions in the generation of microsomal disulfide bonds acting in parallel with Ero1p, the essential, FAD-dependent oxidase of protein disulfide isomerase.	Disulfides	64-73	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	16-21
11320084-6	2001	The disulfide cross-linked ox-hHSF1 was monomeric and resistant to the in vitro heat-induced trimerization and activation.	Disulfides	4-13	heat shock transcription factor 1	Homo sapiens	30-35
11375523-2	2001	The disulfide-linked homodimer of the extracellular segment of human CTLA-4 and the receptor-binding domain of human B7-2 were purified and cocrystallized.	Disulfides	4-13	CD86 molecule	Homo sapiens	117-121
11699729-2	2001	Lp(a) is, however, distinguishable from LDL by the presence of an additional glycoprotein apolipoprotein(a) [apo(a)], which is covalently attached to apo B-100 by a single disulfide bond.	Disulfides	172-181	lipoprotein(a)	Homo sapiens	0-5
11699729-2	2001	Lp(a) is, however, distinguishable from LDL by the presence of an additional glycoprotein apolipoprotein(a) [apo(a)], which is covalently attached to apo B-100 by a single disulfide bond.	Disulfides	172-181	lipoprotein(a)	Homo sapiens	90-107
11395930-6	2001	The finding that an intersubunit disulfide restored some of the activity lost by replacing alpha Lys51 suggests that this residue is not crucial for receptor binding or signaling and also that hCG and related hormones may be particularly sensitive to mutations that alter interactions between their subunits.	Disulfides	33-42	chorionic gonadotropin subunit beta 5	Homo sapiens	193-196
11371529-7	2001	Both the exocellular and cellular forms of VirB7 migrated as disulfide-cross-linked dimers and monomers when samples were electrophoresed under nonreducing conditions.	Disulfides	61-70	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	43-48
11371529-8	2001	A mutant synthesizing VirB7 with a Ser substitution of the lipid-modified Cys15 residue failed to elaborate the T pilus, whereas a mutant synthesizing VirB7 with a Ser substitution for the disulfide-reactive Cys24 residue produced very low levels of T pilus.	Disulfides	189-198	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	22-27
11371529-8	2001	A mutant synthesizing VirB7 with a Ser substitution of the lipid-modified Cys15 residue failed to elaborate the T pilus, whereas a mutant synthesizing VirB7 with a Ser substitution for the disulfide-reactive Cys24 residue produced very low levels of T pilus.	Disulfides	189-198	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	151-156
11371529-9	2001	Together, these findings establish that the VirB7 lipoprotein localizes exocellularly, it associates with the T pilus, and both VirB7 lipid modification and disulfide cross-linking are important for T-pilus assembly.	Disulfides	157-166	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	44-49
11279016-3	2001	We now report that overexpression of Dsb proteins known to catalyze formation and isomerization of disulfide bonds can substantially enhance periplasmic production of NGF.	Disulfides	99-108	nerve growth factor	Rattus norvegicus	167-170
11274477-2	2001	MGP is a 10.6-kD protein (84 amino acids) containing five gamma-carboxyglutamic acid (Gla) residues and one disulfide bond.	Disulfides	108-117	matrix Gla protein	Homo sapiens	0-3
11237737-1	2001	Reduction of disulfide bonds in human melanocortin 1 receptor (hMC1R) with increasing concentrations of DTT (dithiothreitol) resulted in a decrease in the binding of [125I]-ACTH (adrenocorticotropic hormone, L-isomer) in an uniphasic manner and a decrease in [125I]-NDP-MSH ([Nle(4),D-Phe(7)]-alpha-melanocyte stimulating hormone; D-isomer) binding in a biphasic manner.	Disulfides	13-22	norrin cystine knot growth factor NDP	Homo sapiens	266-269
11310611-3	2001	The methylenedithioether analogues displayed good binding affinities to rat liver AT1 receptors although in most cases somewhat lower than their disulfide counterparts.	Disulfides	145-154	angiotensin II receptor, type 1a	Rattus norvegicus	82-85
11297032-9	2001	Our present observation of a decreased disulfide bridge formation between GPIb alpha and GPIb beta shows that GPIX is not only needed for the correct assembly of the complex but might also be needed for the disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	39-48	glycoprotein IX platelet	Homo sapiens	110-114
11297032-9	2001	Our present observation of a decreased disulfide bridge formation between GPIb alpha and GPIb beta shows that GPIX is not only needed for the correct assembly of the complex but might also be needed for the disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	207-216	glycoprotein IX platelet	Homo sapiens	110-114
11260522-4	2001	The mutation responsible for 83% of HH (C260Y) results in the failure of HFE to form a critical disulfide bond, bind beta2 microglobulin, bind TfR, and traffic to the cell surface.	Disulfides	96-105	homeostatic iron regulator	Homo sapiens	73-76
11182766-0	2001	Expression, purification and characterization of the structure and disulfide linkages of insulin-like growth factor binding protein-4.	Disulfides	67-76	insulin-like growth factor binding protein 4	Rattus norvegicus	89-133
11276368-2	2001	Because chemokines have four conserved cysteines forming two intramolecular disulfide bridges, we decided to investigate their contribution in the biological activity of rIP-10.	Disulfides	76-85	C-X-C motif chemokine ligand 10	Rattus norvegicus	170-176
9065459-12	1997	Holo-P450BM-3 appears to dimerize via interactions that do not involve disulfide bond formation, whereas the reductase and FAD domains form intermolecular disulfides.	Disulfides	155-165	presenilin 1	Homo sapiens	123-126
9115997-1	1997	The apparent pKa for the active site thiol of human thioltransferase (TTase) is about 3.5, but the pH dependence of TTase-catalyzed rates of glutathione (GSH)-dependent reduction of disulfide substrates displays an inflection point near pH 8.5.	Disulfides	182-191	glutaredoxin	Homo sapiens	52-68
9115997-1	1997	The apparent pKa for the active site thiol of human thioltransferase (TTase) is about 3.5, but the pH dependence of TTase-catalyzed rates of glutathione (GSH)-dependent reduction of disulfide substrates displays an inflection point near pH 8.5.	Disulfides	182-191	glutaredoxin	Homo sapiens	70-75
9115997-1	1997	The apparent pKa for the active site thiol of human thioltransferase (TTase) is about 3.5, but the pH dependence of TTase-catalyzed rates of glutathione (GSH)-dependent reduction of disulfide substrates displays an inflection point near pH 8.5.	Disulfides	182-191	glutaredoxin	Homo sapiens	116-121
9038173-5	1997	Peptides lacking Gly-1 and Val-2 still form a disulfide bond with the protease but do not cause a conformational change in the protease also they are not effective inhibitors of activation as the interaction is readily reversed by full-length pVI-CT.	Disulfides	46-55	threonine aldolase 1, pseudogene	Homo sapiens	17-22
9033398-11	1997	Therefore, despite the large distance between the disulfide bridge and the protein-DNA interface, covalently linking the subunits of MASH-1 increased the specificity of DNA binding significantly.	Disulfides	50-59	achaete-scute family bHLH transcription factor 1	Homo sapiens	133-139
9041640-1	1997	Human glutaredoxin is a member of the glutaredoxin family, which is characterized by a glutathione binding site and a redox-active dithiol/disulfide in the active site.	Disulfides	139-148	glutaredoxin	Homo sapiens	6-18
9041640-1	1997	Human glutaredoxin is a member of the glutaredoxin family, which is characterized by a glutathione binding site and a redox-active dithiol/disulfide in the active site.	Disulfides	139-148	glutaredoxin	Homo sapiens	38-50
9417344-2	1997	It consists of the Lp(a)-specific apo(a) which is bound to the apo-B of an LDL particle by a disulfide bridge.	Disulfides	93-102	lipoprotein(a)	Homo sapiens	19-24
8969236-2	1996	Protein disulfide-isomerase (PDI) catalyzes the formation and isomerization of disulfides during oxidative protein folding in the eukaryotic endoplasmic reticulum.	Disulfides	79-89	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
8969236-2	1996	Protein disulfide-isomerase (PDI) catalyzes the formation and isomerization of disulfides during oxidative protein folding in the eukaryotic endoplasmic reticulum.	Disulfides	79-89	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
9013337-2	1996	It is secreted and deposited in cells and tissues as a disulfide-bonded oligomer identical in size to the previously described recombinant fibulin-2.	Disulfides	55-64	fibulin 2	Homo sapiens	139-148
8931546-3	1996	A consistent relationship between disulfide bond stability and Cys1 thiol pKa value is found here for DsbA, thioredoxin, and the N-terminal thioredoxin-like domain of protein disulfide isomerase (PDI a), which has a very low thiol pKa value of 4.5.	Disulfides	34-43	prolyl 4-hydroxylase subunit beta	Homo sapiens	167-194
8931546-3	1996	A consistent relationship between disulfide bond stability and Cys1 thiol pKa value is found here for DsbA, thioredoxin, and the N-terminal thioredoxin-like domain of protein disulfide isomerase (PDI a), which has a very low thiol pKa value of 4.5.	Disulfides	34-43	prolyl 4-hydroxylase subunit beta	Homo sapiens	196-201
8910492-0	1996	Metabotropic glutamate receptor 5 is a disulfide-linked dimer.	Disulfides	39-48	glutamate metabotropic receptor 5	Homo sapiens	0-33
15299592-0	1996	Crystallization of DsbC, the disulfide bond isomerase of Escherichia coli.	Disulfides	29-38	putative protein DsbC	Escherichia coli	19-23
15299592-1	1996	DsbC is a 2 x 23 kDa soluble dimeric protein molecule involved in protein disulfide bond formation in the E. coli periplasm, primarily catalyzing disulfide bond rearrangements.	Disulfides	74-83	putative protein DsbC	Escherichia coli	0-4
15299592-1	1996	DsbC is a 2 x 23 kDa soluble dimeric protein molecule involved in protein disulfide bond formation in the E. coli periplasm, primarily catalyzing disulfide bond rearrangements.	Disulfides	146-155	putative protein DsbC	Escherichia coli	0-4
8930901-3	1996	The disulfide form of glutathione increases 200-fold and represents 63% of the total glutathione in a glr1 delta mutant compared with only 6% in wild type.	Disulfides	4-13	glutathione-disulfide reductase GLR1	Saccharomyces cerevisiae S288C	102-106
8897385-1	1996	Lipoprotein(a) (Lp(a)) is bound to apolipoprotein B-100 by disulfide linkage and is associated in the upper density range of low density lipoprotein cholesterol.	Disulfides	59-68	lipoprotein(a)	Homo sapiens	0-14
8897385-1	1996	Lipoprotein(a) (Lp(a)) is bound to apolipoprotein B-100 by disulfide linkage and is associated in the upper density range of low density lipoprotein cholesterol.	Disulfides	59-68	lipoprotein(a)	Homo sapiens	16-21
8794751-0	1996	The disulfide folding pathway of tick anticoagulant peptide (TAP), a Kunitz-type inhibitor structurally homologous to BPTI.	Disulfides	4-13	tracheal antimicrobial peptide	Bos taurus	61-64
8794751-3	1996	The picture of TAP folding differs significantly from the well-documented case of bovine pancreatic trypsin inhibitor (BPTI), despite the fact that both proteins share close structural homology in term of 3-D conformation and disulfide pattern.	Disulfides	226-235	tracheal antimicrobial peptide	Bos taurus	15-18
8784194-1	1996	Similar to other proteins of the periplasm of Escherichia coli, TEM 1 beta-lactamase contains only a single disulfide bond.	Disulfides	108-117	TEM-1 beta-lactamase	Escherichia coli	64-84
8799123-0	1996	Agrobacterium tumefaciens VirB7 and VirB9 form a disulfide-linked protein complex.	Disulfides	49-58	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	26-31
8799123-0	1996	Agrobacterium tumefaciens VirB7 and VirB9 form a disulfide-linked protein complex.	Disulfides	49-58	type IV secretion system protein VirB9	Agrobacterium tumefaciens	36-41
8799123-6	1996	Using strains that contain a deletion in a defined virB gene and strains that express specific VirB proteins, we demonstrate that the 36-kDa band is composed of VirB9 and VirB7 that are linked to each other by a disulfide bond.	Disulfides	212-221	type IV secretion system protein VirB9	Agrobacterium tumefaciens	161-166
8799123-6	1996	Using strains that contain a deletion in a defined virB gene and strains that express specific VirB proteins, we demonstrate that the 36-kDa band is composed of VirB9 and VirB7 that are linked to each other by a disulfide bond.	Disulfides	212-221	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	171-176
8756708-7	1996	It still catalyzes only a subset of the thiol/disulfide exchange reactions of intact PDI and has a reduced ability to catalyze protein disulfide rearrangements.	Disulfides	46-55	prolyl 4-hydroxylase subunit beta	Homo sapiens	85-88
8756121-2	1996	Surfactant protein D (SP-D) is preferentially secreted as dodecamers consisting of four collagenous trimers cross-linked by disulfide bonds.	Disulfides	124-133	surfactant protein D	Rattus norvegicus	0-20
8756121-2	1996	Surfactant protein D (SP-D) is preferentially secreted as dodecamers consisting of four collagenous trimers cross-linked by disulfide bonds.	Disulfides	124-133	surfactant protein D	Rattus norvegicus	22-26
8756121-8	1996	These studies strongly suggest that the most important and rate-limiting step for the secretion of SP-D involves the association of cross-linked trimeric subunits to form dodecamers stabilized by specific inter-subunit disulfide cross-links.	Disulfides	219-228	surfactant protein D	Rattus norvegicus	99-103
8654563-4	1996	Analysis by SDS-PAGE and rotary shadowing electron microscopy indicated that TSP1 and TSP2 are disulfide bonded trimers whereas TSP3 is a disulfide-bonded pentamer.	Disulfides	95-104	tumor suppressor region 2	Mus musculus	86-90
8654563-4	1996	Analysis by SDS-PAGE and rotary shadowing electron microscopy indicated that TSP1 and TSP2 are disulfide bonded trimers whereas TSP3 is a disulfide-bonded pentamer.	Disulfides	138-147	tumor suppressor region 3	Mus musculus	128-132
8634257-3	1996	Previous studies have suggested that disulfide-linked homodimers of peripherin/rds and rom-1 can associate noncovalently to form higher order structures.	Disulfides	37-46	peripherin 2	Bos taurus	79-82
8621589-4	1996	Immunoblot analysis of cell lysates showed that all infected cells produced a disulfide-linked homodimer of identical molecular weight as natural granzyme A.	Disulfides	78-87	granzyme A	Homo sapiens	146-156
8621668-9	1996	These studies suggest that the disulfide-rich domain acts to form dimers of the polypeptide chain of mucin.	Disulfides	31-40	LOC100508689	Homo sapiens	101-106
8645293-1	1996	Protein disulfide isomerase (PDI) catalyzes the correct protein disulfide formation and is a key regulator for protein folding.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
8830035-1	1996	The positions of the reactive site and the disulfide bridges in fungal protease inhibitor F (FPI-F) from silkworm (Bombyx mori), which has a unique amino acid sequence and inhibitory specificity, were investigated.	Disulfides	43-52	fungal protease inhibitor F	Bombyx mori	64-91
8830035-1	1996	The positions of the reactive site and the disulfide bridges in fungal protease inhibitor F (FPI-F) from silkworm (Bombyx mori), which has a unique amino acid sequence and inhibitory specificity, were investigated.	Disulfides	43-52	fungal protease inhibitor F	Bombyx mori	93-98
8830035-6	1996	Based on the positions of the reactive site and the disulfide bridges, FPI-F is considered to be a member of a new family of serine protease inhibitors.	Disulfides	52-61	fungal protease inhibitor F	Bombyx mori	71-76
8636437-5	1996	Based on crystallographic structure of chorionic gonadotropin, a disulfide bond between C19 and C105 in the TSH-beta subunit is predicted to form the "buckle" of a "seat belt" that surrounds the common alpha subunit and maintains the conformation and bioactivity of the hormone.	Disulfides	65-74	thyroid stimulating hormone subunit beta	Homo sapiens	108-116
8627662-0	1996	Bovine herpesvirus 1 UL49.5 homolog gene encodes a novel viral envelope protein that forms a disulfide-linked complex with a second virion structural protein.	Disulfides	93-102	tegument protein VP22	Bovine alphaherpesvirus 1	21-25
8576238-5	1996	Strikingly, the ATPase reaction is stimulated in the presence of denatured polypeptides, while the disulfide oxidization activity of PDI is not affected by ATP.	Disulfides	99-108	prolyl 4-hydroxylase subunit beta	Homo sapiens	133-136
8567620-1	1996	Wild type human (h) interleukin 5 (wt IL5) is composed of two identical peptide chains linked by disulfide bonds.	Disulfides	97-106	interleukin 5	Homo sapiens	20-33
8567620-1	1996	Wild type human (h) interleukin 5 (wt IL5) is composed of two identical peptide chains linked by disulfide bonds.	Disulfides	97-106	interleukin 5	Homo sapiens	38-41
8547341-4	1996	Detailed chemical characterization of the recombinant molecule by peptide mapping in conjunction with Edman sequencing and mass spectrometry reveals that the bacterially produced recombinant neu differentiation factor preparation is properly folded and contains the correct disulfide structure.	Disulfides	274-283	neuregulin 1	Homo sapiens	191-217
12232629-3	1996	The expressed rBMP2 was processed into 16 kD C-terminal fragments and formed 30 kD dimmers with disulfide bonds in vivo.	Disulfides	96-105	bone morphogenetic protein 2	Rattus norvegicus	14-19
7498553-4	1995	By disulfide-bond pattern analysis and modeling of the PTTH structure based on the known three-dimensional (3D) structures of growth factor family with cystine-knot motif, we propose that the PTTH protomer adopts the fold unique to the structural superfamily of the growth factors, beta-nerve growth factor (beta-NGF), transforming growth factor-beta 2 (TGF-beta 2), and platelet-derived growth factor-BB (PDGF-BB).	Disulfides	3-12	prothoracicotropic hormone	Bombyx mori	192-196
8747434-0	1995	The superreactive disulfide bonds in alpha-lactalbumin and lysozyme.	Disulfides	18-27	lysozyme	Equus caballus	59-67
7589496-1	1995	The disulfide bridge closed cyclic peptide corresponding to the whole Consensus V3 loop of the envelope protein gp120 of HIV-1 was examined by proton 2D-NMR spectroscopy in water and in a 20% trifluoroethanol/water solution.	Disulfides	4-13	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	112-117
7662965-1	1995	Protein disulfide isomerase (PDI) is an enzyme that catalyzes the formation as well as the isomerization of disulfide bonds.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
7642568-1	1995	Surfactant protein D (SP-D) is a member of the C-type lectin superfamily with four distinct structural domains: an amino terminus involved in forming intermolecular disulfides, a collagen-like domain, a neck region, and a carbohydrate recognition domain.	Disulfides	165-175	surfactant protein D	Rattus norvegicus	0-20
7642568-1	1995	Surfactant protein D (SP-D) is a member of the C-type lectin superfamily with four distinct structural domains: an amino terminus involved in forming intermolecular disulfides, a collagen-like domain, a neck region, and a carbohydrate recognition domain.	Disulfides	165-175	surfactant protein D	Rattus norvegicus	22-26
7541844-4	1995	Second, monomers form dimers by an intermolecular disulfide linkage in the stalk, with a t1/2 of 2.5 min.	Disulfides	50-59	interleukin 1 receptor like 1	Homo sapiens	89-98
7541532-3	1995	Evidence was obtained for cotranslational disulfide formation, generation of conformational epitopes, N-linked glycosylation, and oligosaccharide-dependent binding of calnexin, a membrane-bound chaperone that binds to incompletely folded glycoproteins via partially glucose-trimmed oligosaccharides.	Disulfides	42-51	calnexin	Homo sapiens	167-175
7541042-1	1995	A disulfide-linked homodimer binds two CD86 molecules.	Disulfides	2-11	CD86 molecule	Homo sapiens	39-43
7643855-2	1995	This protein (designated C3b), when purified from plasma, consisted of three disulfide-linked polypeptide chains (77, 72 and 30 kDa).	Disulfides	77-86	endogenous retrovirus group K member 3	Homo sapiens	25-28
7643855-4	1995	However, immunochemical analysis revealed that C3b, after the first step in its purification, consisted of two disulfide-linked polypeptide chains (105 and 72 kDa).	Disulfides	111-120	endogenous retrovirus group K member 3	Homo sapiens	47-50
7567962-4	1995	The sequence alignments identified two cysteine residues in INSR that could be responsible for the additional disulfide bonds known to be involved in dimer formation.	Disulfides	110-119	insulin receptor	Homo sapiens	60-64
7567962-5	1995	The published data on the alignments for the fibronectin type III repeat region of the INSR together with previous cysteine mutagenesis studies indicated that there were two disulfide bonds linking the alpha and beta chains of the INSR, but only one alpha-beta linkage in the insulin-like growth factor 1 receptor (IG1R).	Disulfides	174-183	insulin receptor	Homo sapiens	87-91
7536035-0	1995	Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.	Disulfides	74-83	putative protein DsbC	Escherichia coli	46-50
7536035-1	1995	DsbC is a soluble protein of the bacterial periplasm that was identified genetically as being involved in protein disulfide formation.	Disulfides	114-123	putative protein DsbC	Escherichia coli	0-4
7536035-5	1995	The other two cysteine residues of DsbC form a buried, structural disulfide bond.	Disulfides	66-75	putative protein DsbC	Escherichia coli	35-39
7536035-6	1995	The reactivities and stabilities of the active site disulfide bond of DsbC have been characterized and compared to that of DsbA.	Disulfides	52-61	putative protein DsbC	Escherichia coli	70-74
7536035-9	1995	DsbC is much more active than DsbA in catalyzing protein disulfide rearrangements, and this may be its main function in vivo.	Disulfides	57-66	putative protein DsbC	Escherichia coli	0-4
7711038-1	1995	Multiple sequence alignments including the enterococcal NADH peroxidase and NADH oxidase indicate that residues Ser38 and Cys42 align with the two cysteines of the redox-active disulfides found in glutathione reductase (GR), lipoamide dehydrogenase, mercuric reductase, and trypanothione reductase.	Disulfides	177-187	glutathione-disulfide reductase	Homo sapiens	197-218
7711038-1	1995	Multiple sequence alignments including the enterococcal NADH peroxidase and NADH oxidase indicate that residues Ser38 and Cys42 align with the two cysteines of the redox-active disulfides found in glutathione reductase (GR), lipoamide dehydrogenase, mercuric reductase, and trypanothione reductase.	Disulfides	177-187	glutathione-disulfide reductase	Homo sapiens	220-222
7711038-1	1995	Multiple sequence alignments including the enterococcal NADH peroxidase and NADH oxidase indicate that residues Ser38 and Cys42 align with the two cysteines of the redox-active disulfides found in glutathione reductase (GR), lipoamide dehydrogenase, mercuric reductase, and trypanothione reductase.	Disulfides	177-187	dihydrolipoamide dehydrogenase	Homo sapiens	225-248
7742091-5	1995	Thus, the produced antibody could recognize the disulfide-linked dimeric structure of bioactive BMP-4, regardless of the species.	Disulfides	48-57	bone morphogenetic protein 4	Homo sapiens	96-101
11148053-1	2001	Three of the five disulfide bonds in the glycoprotein hormone alpha-subunit (GPH-alpha) form a cystine knot motif that stabilizes a three-loop antiparallel structure.	Disulfides	18-27	glycoprotein hormones, alpha polypeptide	Homo sapiens	77-86
11460483-2	2001	The mechanism by which Lp(a) may favour this pathological state may be related to its particular structure, a plasminogen-like glycoprotein, apo(a), that is disulfide linked to the apo B100 of an atherogenic LDL-like particle.	Disulfides	157-166	lipoprotein(a)	Homo sapiens	23-28
10942760-5	2000	This motif comprises the active site in enzymes involved in disulfide exchange reactions, including protein-disulfide isomerase (EC ) and thioredoxin.	Disulfides	60-69	prolyl 4-hydroxylase subunit beta	Homo sapiens	100-127
11086197-2	2000	Human pregnancy zone protein (PZP) is a macromolecule of 360 kDa, organized as a disulfide-linked homodimer of two 180 kDa subunits, with an amino acid sequence and structure remarkably similar to that of human alpha2-Macroglobulin.	Disulfides	81-90	PZP alpha-2-macroglobulin like	Homo sapiens	30-33
11041874-3	2000	In C8 from serum, these are arranged as a disulfide-linked C8alpha-gamma dimer that is noncovalently associated with C8beta.	Disulfides	42-51	complement C8 beta chain	Homo sapiens	117-123
11058761-3	2000	These subunits are arranged asymmetrically to form a disulfide-linked C8 alpha-gamma dimer that is noncovalently associated with C8 beta.	Disulfides	53-62	complement C8 beta chain	Homo sapiens	129-136
10837476-1	2000	The assembly of lipoprotein(a) (Lp(a)) involves an initial noncovalent interaction between apolipoprotein (apo) B100 and apo(a), followed by the formation of a disulfide bond between apoB100 cysteine 4326 and apo(a) cysteine 4057.	Disulfides	160-169	lipoprotein(a)	Homo sapiens	32-37
10837476-8	2000	The mutant apoB100 bound to apo(a) and formed bona fide disulfide-linked Lp(a), but Lp(a) assembly was less efficient than with wild-type human apoB100.	Disulfides	56-65	lipoprotein(a)	Homo sapiens	73-78
7814337-0	1995	A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coli.	Disulfides	80-89	cfiA	Bacteroides fragilis	204-208
7814337-3	1995	Data indicated that DsbA interacted with CcrA, creating aberrant disulfide bond linkages that render CcrA proteolytically unstable.	Disulfides	65-74	cfiA	Bacteroides fragilis	41-45
7814337-3	1995	Data indicated that DsbA interacted with CcrA, creating aberrant disulfide bond linkages that render CcrA proteolytically unstable.	Disulfides	65-74	cfiA	Bacteroides fragilis	101-105
19216714-5	2008	However, in contrast to thioredoxin, glutaredoxin reduces GSH-mixed disulfides and catalyzes the reaction not only via a dithiol mechanism but also via monothiol reduction.	Disulfides	68-78	glutaredoxin	Homo sapiens	37-49
10951287-8	2000	Naturally expressed S100A2 dimers in normal human keratinocytes readily underwent intermolecular disulfide cross-linking unless a strong denaturant was present during cell lysis.	Disulfides	97-106	S100 calcium binding protein A2	Homo sapiens	20-26
10951287-10	2000	These results demonstrate that native S100A2 is a homodimer that does not depend on disulfide cross-linking for stability, but undergoes intermolecular cross-linking at cysteine residues in response to oxidative stress.	Disulfides	84-93	S100 calcium binding protein A2	Homo sapiens	38-44
19956338-4	2008	RNase A and B each contain four disulfide bonds, and the addition of a reducing reagent, such as dithiothreitol, was found to be required to achieve efficient acidic proteolysis.	Disulfides	32-41	ribonuclease A family member 1, pancreatic	Homo sapiens	0-7
10982384-4	2000	Substitution of Cys100 with alanine impedes the capture of Ero1p-Pdi1p mixed-disulfide complexes from yeast, and also blocks oxidation of Pdi1p in vivo.	Disulfides	77-86	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	65-70
7814337-4	1995	Mutations in dsbA or dsbB permissive for CcrA expression eliminated or greatly reduced DsbA activity, allowing CcrA to assume a disulfide bond-free and proteolytically stable conformation.	Disulfides	128-137	cfiA	Bacteroides fragilis	41-45
7814337-4	1995	Mutations in dsbA or dsbB permissive for CcrA expression eliminated or greatly reduced DsbA activity, allowing CcrA to assume a disulfide bond-free and proteolytically stable conformation.	Disulfides	128-137	cfiA	Bacteroides fragilis	111-115
18544680-5	2008	Thiol-disulfide exchange appears to contribute to the process based on the effects of thiol-reactive reagents and differences in thiol labeling of TGF-beta1 before and after stirring or shear.	Disulfides	6-15	transforming growth factor, beta 1	Mus musculus	147-156
7822419-1	1995	Before secretion, newly synthesized thyroglobulin (Tg) folds via a series of intermediates: disulfide-linked aggregates and unfolded monomers--&gt;folded monomers--&gt;dimers.	Disulfides	92-101	thyroglobulin	Homo sapiens	36-49
7822419-3	1995	Calnexin might bind selectively to carbohydrates within glycoproteins, or to hydrophobic surfaces of secretory proteins while they form proper disulfide bonds (Wada, I., W.-J.	Disulfides	143-152	calnexin	Homo sapiens	0-8
11853625-5	2000	In the early period of culture (lenses were transparent), NP-SH and P-SH were decreased, while disulfide and MDA were increased, the activity of GSH-PX rose obviously, that of GSH-S also had a tendency of rise, however, the activity of GSSG-R had no obvious changes.	Disulfides	95-104	glutathione synthetase	Rattus norvegicus	176-181
7773173-2	1995	A hinge region connects the two non-disulfide-linked domains of hemopexin, a 35-kDa N-terminal domain (domain I) that binds heme, and a 25-kDa C-terminal domain (domain II).	Disulfides	36-45	hemopexin	Homo sapiens	64-73
18816065-1	2008	Glutaredoxin (Grx)-catalyzed deglutathionylation of protein-glutathione mixed disulfides (protein-SSG) serves important roles in redox homeostasis and signal transduction, regulating diverse physiological and pathophysiological events.	Disulfides	78-88	glutaredoxin	Homo sapiens	0-12
7982938-7	1994	The same but reduced effect was induced by the disulfide C39-C92 containing tryptic angiogenin fragment L-H-G-G-S-P-W-P-P-C92-Q-Y-R-G-L-T-S-P-C39-K, indicating a new, so far unknown biologically active site of angiogenin which is different from the sites responsible for angiogenic or ribonucleolytic activity.	Disulfides	47-56	angiogenin	Homo sapiens	84-94
10931179-11	2000	This work resolves details of the structure of ecto-5"-nucleotidase, with particular regard to the localization and composition of the glycidic moiety, number and localization of the disulfide bridges and characterization of the glycosyl-phosphatidylinositol anchor.	Disulfides	183-192	5'-nucleotidase ecto	Homo sapiens	47-67
7982938-7	1994	The same but reduced effect was induced by the disulfide C39-C92 containing tryptic angiogenin fragment L-H-G-G-S-P-W-P-P-C92-Q-Y-R-G-L-T-S-P-C39-K, indicating a new, so far unknown biologically active site of angiogenin which is different from the sites responsible for angiogenic or ribonucleolytic activity.	Disulfides	47-56	angiogenin	Homo sapiens	210-220
7525589-1	1994	Pulmonary surfactant protein A (SP-A) contains 4 domains: a disulfide forming amino terminus, a collagen-like region, a neck region, and a carbohydrate recognition region.	Disulfides	60-69	surfactant protein A1	Homo sapiens	0-30
7525589-1	1994	Pulmonary surfactant protein A (SP-A) contains 4 domains: a disulfide forming amino terminus, a collagen-like region, a neck region, and a carbohydrate recognition region.	Disulfides	60-69	surfactant protein A1	Homo sapiens	32-36
10920260-0	2000	Stabilization of human RNase 1 by introduction of a disulfide bond between residues 4 and 118.	Disulfides	52-61	ribonuclease A family member 1, pancreatic	Homo sapiens	23-30
10920260-2	2000	The 4-118CL RNase 1 that refolded under redox conditions was a monomer without free SH groups and retained 11% of the activity of the wild-type recombinant RNase 1, indicating that the mutant enzyme was correctly folded with the formation of an additional disulfide bond between Cys4 and Cys118.	Disulfides	256-265	ribonuclease A family member 1, pancreatic	Homo sapiens	12-19
10920260-2	2000	The 4-118CL RNase 1 that refolded under redox conditions was a monomer without free SH groups and retained 11% of the activity of the wild-type recombinant RNase 1, indicating that the mutant enzyme was correctly folded with the formation of an additional disulfide bond between Cys4 and Cys118.	Disulfides	256-265	ribonuclease A family member 1, pancreatic	Homo sapiens	156-163
7961823-1	1994	Lipoprotein(a) (Lp(a)) consists of a low density lipoprotein particle in which apolipoprotein(a) (apo(a)), is disulfide linked to apoB.	Disulfides	110-119	apolipoprotein B-100	Papio anubis	130-134
10891284-3	2000	Under the same regeneration conditions, with oxidized and reduced DTT, used previously for kinetic oxidative-folding studies of this protein, the addition of 4 microM protein disulfide isomerase (PDI) was found to lead to catalysis of each disulfide-formation step, including the rate-limiting rearrangement steps in which the native-like intermediates des-[65-72] and des-[40-95] are formed.	Disulfides	175-184	prolyl 4-hydroxylase subunit beta	Bos taurus	196-199
18816065-1	2008	Glutaredoxin (Grx)-catalyzed deglutathionylation of protein-glutathione mixed disulfides (protein-SSG) serves important roles in redox homeostasis and signal transduction, regulating diverse physiological and pathophysiological events.	Disulfides	78-88	glutaredoxin	Homo sapiens	14-17
18638483-5	2008	The new structures extend earlier observations to reveal that the redox-active disulfide loop in GR is an extreme case of sequential peptide bonds systematically deviating from planarity--a net deviation of 53 degrees across five residues.	Disulfides	79-88	glutathione-disulfide reductase	Homo sapiens	97-99
10912786-7	2000	Chicken and normal human PDI proteins showed tissue- and developmental-specific enhancement of cell aggregation identical to R-cognin, and this activity was blocked by inactivation of the -WCGHC- motifs which function in disulfide exchange.	Disulfides	221-230	prolyl 4-hydroxylase subunit beta	Homo sapiens	25-28
10912786-8	2000	Dependence of retina cell aggregation on disulfide exchange activity was shown by blocking that activity with the inhibitor, DTNB, or with a recombinant human PDI with the -WCGHC- motif cysteines mutated.	Disulfides	41-50	prolyl 4-hydroxylase subunit beta	Homo sapiens	159-162
7534492-1	1994	Interleukin 5 (IL-5) is a homodimeric cytokine arranged in a head-to-tail configuration covalently linked by two disulfide bonds.	Disulfides	113-122	interleukin 5	Homo sapiens	0-13
7534492-1	1994	Interleukin 5 (IL-5) is a homodimeric cytokine arranged in a head-to-tail configuration covalently linked by two disulfide bonds.	Disulfides	113-122	interleukin 5	Homo sapiens	15-19
18664402-1	2008	A family of cell surface and growth-related proteins, designated ECTO-NOX proteins, carry out both copper-dependent NADH and hydroquinone oxidation and protein disulfide-thiol interchange.	Disulfides	160-169	tripartite motif containing 33	Homo sapiens	65-69
7918467-0	1994	Structure of human apolipoprotein D: locations of the intermolecular and intramolecular disulfide links.	Disulfides	88-97	apolipoprotein D	Homo sapiens	19-35
7918467-10	1994	Because apoD contains two intramolecular disulfide linkages and has a high content of proline to disrupt alpha-helical structures, formation of the amphipathic helical regions that characterize the other soluble apolipoproteins is unlikely.	Disulfides	41-50	apolipoprotein D	Homo sapiens	8-12
7918467-11	1994	We conclude that apoD binds to lipoprotein surfaces through structures other than alpha-helices, such as disulfide links.	Disulfides	105-114	apolipoprotein D	Homo sapiens	17-21
11068075-2	2000	This effect of Lp(a) may be related to its composite structure, a plasminogen-like inactive serine-proteinase, apoprotein (a) [apo(a)], which is disulfide-linked to the apoprotein B100 of an atherogenic low-density lipoprotein (LDL) particle.	Disulfides	145-154	lipoprotein(a)	Homo sapiens	15-20
18647175-6	2008	Our findings suggest that increased BBB permeability (i.e., leak) associated with lambda-carrageenan-induced peripheral inflammatory pain is promoted by the disruption of disulfide-bonded occludin oligomeric assemblies, which renders them incapable of forming an impermeant physical barrier to paracellular transport.	Disulfides	171-180	occludin	Rattus norvegicus	188-196
10880278-9	2000	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of extracts of various ocular tissues revealed bands of 43 and 29 kD after disulfide bond reduction that were reactive with anti-SPARC IgG.	Disulfides	133-142	secreted acidic cysteine rich glycoprotein	Mus musculus	187-192
8089145-1	1994	Acyloxyacyl hydrolase, a leukocyte enzyme that acts on bacterial lipopolysaccharides (LPSs) and many glycerolipids, is synthesized as a precursor polypeptide that undergoes internal disulfide linkage before being proteolytically processed into two subunits.	Disulfides	182-191	acyloxyacyl hydrolase	Homo sapiens	0-21
18577522-6	2008	When transgenically expressed in yeast, ETR1 and ERS2 can form disulfide-linked heterodimers.	Disulfides	63-72	ethylene response sensor 2	Arabidopsis thaliana	49-53
7913469-0	1994	The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase.	Disulfides	22-31	prolyl 4-hydroxylase subunit beta	Homo sapiens	115-142
7913469-3	1994	Protein disulfide isomerase (PDI), a resident foldase of the endoplasmic reticulum, catalyzes the in vitro oxidative refolding of reduced, disulfide-containing proteins, including denatured lysozyme.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
10828986-4	2000	We performed equilibrium redox titrations to investigate the thermodynamics of the thiol/disulfide exchange between thioredoxin f and the regulatory sulfhydryl groups of fructose-1,6-bisphosphatase, sedoheptulose-1,7-bisphosphatase, phosphoribulokinase, NADP-glyceraldehyde phosphate dehydrogenase, and the chloroplast ATPsynthase.	Disulfides	89-98	thioredoxin-like protein CITRX, chloroplastic	Solanum lycopersicum	116-127
7913469-7	1994	Its anti-chaperone activity diverts substrate away from productive folding and facilitates disulfide cross-linking of lysozyme into large, inactive aggregates that specifically incorporate PDI.	Disulfides	91-100	prolyl 4-hydroxylase subunit beta	Homo sapiens	189-192
18637987-3	2008	We previously reported the design, mechanistic evaluation, and structure-activity relationships of a disulfide-containing cyclic peptide inhibitor of RGS4, YJ34 (Ac-Val-Lys-c[Cys-Thr-Gly-Ile-Cys]-Glu-NH(2), S-S) (Roof et al., Chem Biol Drug Des, 67, 2006, 266).	Disulfides	101-110	regulator of G protein signaling 4	Homo sapiens	150-154
7913469-9	1994	The dithiol/disulfide sites of PDI are essential for the chaperone activity observed at high PDI concentrations, but they are not required for the anti-chaperone activity found at low PDI concentrations.	Disulfides	12-21	prolyl 4-hydroxylase subunit beta	Homo sapiens	31-34
7913469-9	1994	The dithiol/disulfide sites of PDI are essential for the chaperone activity observed at high PDI concentrations, but they are not required for the anti-chaperone activity found at low PDI concentrations.	Disulfides	12-21	prolyl 4-hydroxylase subunit beta	Homo sapiens	93-96
7913469-9	1994	The dithiol/disulfide sites of PDI are essential for the chaperone activity observed at high PDI concentrations, but they are not required for the anti-chaperone activity found at low PDI concentrations.	Disulfides	12-21	prolyl 4-hydroxylase subunit beta	Homo sapiens	93-96
7913469-14	1994	In a glutathione redox buffer, lysozyme-PDI aggregates are disulfide cross-linked; however, disulfide cross-linking is not required for aggregate formation or for the incorporation of PDI into the aggregates.	Disulfides	59-68	prolyl 4-hydroxylase subunit beta	Homo sapiens	40-43
8034704-2	1994	Like TGF-beta s, activins have 9 conserved cysteine residues and are disulfide-bonded dimers.	Disulfides	69-78	transforming growth factor, beta 1	Mus musculus	5-13
8014011-9	1994	The therapeutic potential of the disulfide-stabilized immunotoxin was evaluated using an animal model of immunodeficient mice bearing subcutaneous tumor xenografts of human IL2R-bearing cells.	Disulfides	33-42	interleukin 2 receptor subunit alpha	Homo sapiens	173-177
10841552-10	2000	The active site is returned to the reduced state for another round of catalysis by a series of thiol-disulfide exchange reactions via Cys-227, DTT, or thioredoxin.	Disulfides	101-110	thioredoxin	Bos taurus	151-162
10982233-4	2000	We discuss the synthesis of MB-1-Cys dimer, a protein with an intermolecular disulfide bridge.	Disulfides	77-86	CD79a molecule	Bos taurus	28-32
10729615-5	2000	Conserved regions for the FAD-binding site, NAD(P)H-binding site, and disulfide active site were identified among the deduced amino acid sequences of cowpea FLbR, soybean FLbR, pea DLDH and other enzymes in the family of the pyridine nucleotide-disulfide oxido-reductases.	Disulfides	70-79	leghemoglobin reductase	Glycine max	157-161
10729615-5	2000	Conserved regions for the FAD-binding site, NAD(P)H-binding site, and disulfide active site were identified among the deduced amino acid sequences of cowpea FLbR, soybean FLbR, pea DLDH and other enzymes in the family of the pyridine nucleotide-disulfide oxido-reductases.	Disulfides	70-79	leghemoglobin reductase	Glycine max	171-175
18650385-1	2008	ERp57 is an oxidoreductase that, in conjunction with calnexin and calreticulin, assists disulfide bond formation in folding glycoproteins.	Disulfides	88-97	calnexin	Homo sapiens	53-61
10847613-11	2000	These data suggest that the relative participation of the thioltransferase (glutaredoxin) and thioredoxin systems in overall cellular disulfide reduction is cell line specific.	Disulfides	134-143	glutaredoxin	Homo sapiens	58-74
7516406-7	1994	These B-subunit-like sequences on CD19 are in close proximity following the organization of intervening amino acids into disulfide-linked domains.	Disulfides	121-130	CD19 molecule	Homo sapiens	34-38
10847613-11	2000	These data suggest that the relative participation of the thioltransferase (glutaredoxin) and thioredoxin systems in overall cellular disulfide reduction is cell line specific.	Disulfides	134-143	glutaredoxin	Homo sapiens	76-88
18441012-1	2008	Coagulation factor XI (FXI) is a covalent homodimer consisting of two identical subunits of 80 kDa linked by a disulfide bond formed by Cys-321 within the Apple 4 domain of each subunit.	Disulfides	111-120	coagulation factor XI	Homo sapiens	23-26
10821658-6	2000	Forming a mixed disulfide between the side chain of Cys41 of K41C RNase A and cysteamine replaces the amino group and increases k(cat)/K(m) by 10(3)-fold.	Disulfides	16-25	ribonuclease A family member 1, pancreatic	Homo sapiens	66-73
8006040-8	1994	Digestion of rSP-D with bacterial collagenase generated a COOH-terminal carbohydrate binding fragment and a smaller peptide (approximately 12 kDa, unreduced) that contains interchain disulfide bonds.	Disulfides	183-192	surfactant protein D	Rattus norvegicus	13-18
8006040-10	1994	These studies demonstrate that SP-D is assembled as homopolymers of four identical trimeric subunits, that interactions between the amino-terminal domains of the trimers are stabilized by interchain disulfide bonds, and that SP-D molecules can associate to form complex multimolecular assemblies.	Disulfides	199-208	surfactant protein D	Rattus norvegicus	31-35
10734121-2	2000	The encoded protein, designated as Asc-1 (asc-type amino acid transporter 1), was found to be structurally related to recently identified mammalian amino acid transporters for the transport systems L, y(+)L, x(C)(-), and b(0,+), which are linked, via a disulfide bond, to the type II membrane glycoproteins, 4F2 heavy chain (4F2hc), or rBAT (related to b(0,+) amino acid transporter).	Disulfides	253-262	solute carrier family 7 member 10	Homo sapiens	35-40
18035847-1	2008	Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is similar in structure and mechanism to glutathione reductase except for a C-terminal 16-amino acid extension containing a rare vicinal selenylsulfide bond.	Disulfides	81-90	glutathione-disulfide reductase	Homo sapiens	162-183
10734121-2	2000	The encoded protein, designated as Asc-1 (asc-type amino acid transporter 1), was found to be structurally related to recently identified mammalian amino acid transporters for the transport systems L, y(+)L, x(C)(-), and b(0,+), which are linked, via a disulfide bond, to the type II membrane glycoproteins, 4F2 heavy chain (4F2hc), or rBAT (related to b(0,+) amino acid transporter).	Disulfides	253-262	solute carrier family 7 member 10	Homo sapiens	42-75
10734121-5	2000	The band shifted to 33 kDa in the reducing condition, confirming that Asc-1 and 4F2hc are linked via a disulfide bond.	Disulfides	103-112	anterior suture cataract 1	Mus musculus	70-75
10753451-4	2000	Protein refolding and renaturation were estimated by the change in the number of disulfide bonds of RNase A and the recovery of the enzymatic activity, respectively.	Disulfides	81-90	ribonuclease A family member 1, pancreatic	Homo sapiens	100-107
10753451-6	2000	However, the formation of disulfide bonds of reduced RNase A was accelerated by adding the modified microspheres, and the rate of renaturation was increased depending on the amount of charged DTT and the reaction time of the immobilization.	Disulfides	26-35	ribonuclease A family member 1, pancreatic	Homo sapiens	53-60
8018729-1	1994	Glutaredoxin (thioltransferase) is a small, heat-stable protein, which is involved in thiol/disulfide exchange reactions.	Disulfides	92-101	glutaredoxin	Homo sapiens	0-12
8018729-1	1994	Glutaredoxin (thioltransferase) is a small, heat-stable protein, which is involved in thiol/disulfide exchange reactions.	Disulfides	92-101	glutaredoxin	Homo sapiens	14-30
7515934-1	1994	Apo(a) is linked to Lp(a) through non-covalent interactions and disulfide bond with apo B.	Disulfides	64-73	lipoprotein(a)	Homo sapiens	0-6
17926344-0	2008	Disulfide linkage patterns of pig zona pellucida glycoproteins ZP3 and ZP4.	Disulfides	0-9	zona pellucida sperm-binding protein 3	Sus scrofa	63-66
10753451-8	2000	The protein adsorption data demonstrated that the disulfide moieties of the modified microspheres react with the thiol moieties of the reduced RNase A to form a mixed disulfide.	Disulfides	50-59	ribonuclease A family member 1, pancreatic	Homo sapiens	143-150
10753451-8	2000	The protein adsorption data demonstrated that the disulfide moieties of the modified microspheres react with the thiol moieties of the reduced RNase A to form a mixed disulfide.	Disulfides	167-176	ribonuclease A family member 1, pancreatic	Homo sapiens	143-150
17926344-3	2008	In this study, we analyzed the disulfide linkages of pig ZP3 and ZP4 purified from ovaries.	Disulfides	31-40	zona pellucida sperm-binding protein 3	Sus scrofa	57-60
10725125-3	2000	Myosin polymers were cross-linked mainly through disulfide bonds.	Disulfides	49-58	myosin, heavy chain 15	Gallus gallus	0-6
10725125-4	2000	Hydroxyl radicals destabilized myosin, lowering its denaturation temperature by up to 4 degrees C. Oxidized myosin also produced a new thermal transition in the 60-80 degrees C temperature range, which could be attributed to the formation of disulfide-stabilized polymers.	Disulfides	242-251	myosin, heavy chain 15	Gallus gallus	31-37
8180220-0	1994	Assignment of disulfide bond location in prothoracicotropic hormone of the silkworm, Bombyx mori: a homodimeric peptide.	Disulfides	14-23	prothoracicotropic hormone	Bombyx mori	41-67
8180220-1	1994	The disulfide bond location of a homodimeric peptide, prothoracicotropic hormone (PTTH) of the silkworm, Bombyx mori, was determined by a combination of partial reduction and sequence analysis of peptide fragments generated through a partial reduction of PTTH followed by alkylation and enzyme digestion.	Disulfides	4-13	prothoracicotropic hormone	Bombyx mori	54-80
8180220-1	1994	The disulfide bond location of a homodimeric peptide, prothoracicotropic hormone (PTTH) of the silkworm, Bombyx mori, was determined by a combination of partial reduction and sequence analysis of peptide fragments generated through a partial reduction of PTTH followed by alkylation and enzyme digestion.	Disulfides	4-13	prothoracicotropic hormone	Bombyx mori	82-86
18076384-1	2008	All small Tim proteins of the mitochondrial intermembrane space contain two conserved CX(3)C motifs, which form two intramolecular disulfide bonds essential for function, but only the cysteine-reduced, but not oxidized, proteins can be imported into mitochondria.	Disulfides	131-140	Rho guanine nucleotide exchange factor 5	Homo sapiens	10-13
8188714-1	1994	The role of eucaryotic protein disulfide isomerase (PDI) in the folding and reoxidation of proteins in vitro was investigated using an antibody Fab fragment as a model substrate, since PDI is known to participate in the disulfide bond formation of immunoglobulins in vivo.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Homo sapiens	52-55
8188714-3	1994	Instead, the role of PDI is limited to disulfide bond formation as demonstrated for the folding of the denatured and reduced Fab fragment.	Disulfides	39-48	prolyl 4-hydroxylase subunit beta	Homo sapiens	21-24
8188714-6	1994	In the presence of PDI, formation of the correct disulfide bonds is possible at higher oxidizing conditions compared to the spontaneous reaction.	Disulfides	49-58	prolyl 4-hydroxylase subunit beta	Homo sapiens	19-22
7513654-6	1994	The 3 Cys residues of bovine alpha 2AP are present as an unpaired residue (Cys131) and as a pair in a disulfide bridge (Cys49-Cys122).	Disulfides	102-111	serpin family F member 2	Bos taurus	29-38
10688888-9	2000	We have expressed recombinant wild-type human gammaD crystallin (HGD) and its Arg-14 to Cys mutant (R14C) in Escherichia coli and show that R14C forms disulfide-linked oligomers, which markedly raise the phase separation temperature of the protein solution.	Disulfides	151-160	crystallin gamma D	Homo sapiens	46-63
11996097-3	2000	MG1 monomers are linked by disulfide bonds located at sparsely glycosylated N- and C-end.	Disulfides	27-36	mucin 5B, oligomeric mucus/gel-forming	Homo sapiens	0-3
18074210-3	2008	Results reveal that PDI has a greater relative impact on thiol-disulfide reshuffling (isomerization) reactions and consequently the structure-forming step in oxidative folding at pH 7, as opposed to pH"s 8 and 9.	Disulfides	63-72	prolyl 4-hydroxylase subunit beta	Homo sapiens	20-23
8065468-1	1994	The disulfide-reducing agent dithiothreitol (DTT) has been shown to reduce angiotensin II (Ang II) subtype 1 receptor (AT1) binding sites in various tissues.	Disulfides	4-13	angiotensin II receptor, type 1a	Rattus norvegicus	75-122
18669274-6	2008	The J-chain is inserted into the sIgA and sIgM molecules to form disulfide bonds with C-terminal sites of alpha- or mu-chains.	Disulfides	65-74	joining chain of multimeric IgA and IgM	Homo sapiens	4-11
8179819-5	1994	We have shown, in addition, that Cys-117 is involved in the formation of a disulfide-bonded homodimer of GRP94.	Disulfides	75-84	heat shock protein 90, beta (Grp94), member 1	Mus musculus	105-110
10968370-2	2000	FRP-1 is a complex composed of a glycosylated heavy chain and a nonglycosylated light chain that are disulfide linked.	Disulfides	101-110	secreted frizzled related protein 1	Homo sapiens	0-5
10623724-0	2000	A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure.	Disulfides	112-121	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	139-144
17981509-1	2008	Protein disulfide isomerase (PDI) enzymes are eukaryotic oxidoreductases that catalyze the correct formation of disulfide bonds during protein folding.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
10820757-0	2000	Mucin domains to explore disulfide-dependent dimer formation.	Disulfides	25-34	LOC100508689	Homo sapiens	0-5
8003969-3	1994	P44 should be stabilized by intrahelical hydrogen bonds, interhelical disulfide and salt bridges, and interior hydrophobic interactions.	Disulfides	70-79	interferon induced protein 44	Homo sapiens	0-3
8187208-3	1994	However, Lp[a-], formed by reduction of the disulfide bond between apo[a] and apoB, behaves much like homologous LDL, whether or not apo[a] is removed from the mixture, and in spite of the fact that one or more apoB disulfides may also have been cleaved.	Disulfides	44-53	lipoprotein(a)	Homo sapiens	9-13
18206967-3	2008	Moreover, AhpC* and several point mutants tested in vitro exhibit an enhanced reductase activity toward mixed disulfides between glutathione and glutaredoxin (Grx-S-SG), consistent with the in vivo requirements for these components.	Disulfides	110-120	glutaredoxin	Homo sapiens	145-157
8187208-3	1994	However, Lp[a-], formed by reduction of the disulfide bond between apo[a] and apoB, behaves much like homologous LDL, whether or not apo[a] is removed from the mixture, and in spite of the fact that one or more apoB disulfides may also have been cleaved.	Disulfides	216-226	lipoprotein(a)	Homo sapiens	9-13
8286122-8	1993	In contrast treatments such as chemical deglycosylation, pronase digestion, or disruption of disulfide bonds abolished the ligand activity of ZP3.	Disulfides	93-102	zona pellucida glycoprotein 3	Homo sapiens	142-145
10684964-8	1999	The unique sequence of 15 amino acids with an internal disulfide bond was inserted in the g3p of the M23 phage clone (M23-g3p).	Disulfides	55-64	BAG cochaperone 6	Homo sapiens	90-93
10684964-8	1999	The unique sequence of 15 amino acids with an internal disulfide bond was inserted in the g3p of the M23 phage clone (M23-g3p).	Disulfides	55-64	BAG cochaperone 6	Homo sapiens	122-125
18206967-3	2008	Moreover, AhpC* and several point mutants tested in vitro exhibit an enhanced reductase activity toward mixed disulfides between glutathione and glutaredoxin (Grx-S-SG), consistent with the in vivo requirements for these components.	Disulfides	110-120	glutaredoxin	Homo sapiens	159-162
18386550-2	2008	It is composed of apolipoprotein B (Apo B)-100 and apolipoprotein(a) which are linked by a disulfide bond.	Disulfides	91-100	lipoprotein(a)	Homo sapiens	51-68
10514510-3	1999	We show here that angiopoietin-1 and -2 form distinct arrays of disulfide-linked homo-oligomeric complexes.	Disulfides	64-73	angiopoietin 1	Homo sapiens	18-39
7688570-12	1993	These results suggest that EGF can react with the reactive thiol ester of proteinase-activated alpha 2M by nucleophilic attack of the alpha-amino group and to a lesser extent by sulfide-disulfide exchange with the free SH of the cleaved thiol ester.	Disulfides	186-195	endogenous retrovirus group K member 18	Homo sapiens	74-84
8344931-5	1993	Protein disulfide isomerase (PDI) increased the in vitro rate of this event (t1/2 = 25 min) without changing the order of disulfide bond formation.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
8344931-8	1993	In vitro, assembly was increased after reduction of two of the carboxyl-terminal disulfide bonds of hCG-beta by PDI.	Disulfides	81-90	prolyl 4-hydroxylase subunit beta	Homo sapiens	112-115
8344931-10	1993	The comparison of in vitro and intracellular hCG-beta folding and hCG subunit assembly which is shown in this report indicates that the assisted folding and assembly pathway that occurs in cells, where proteins such as PDI play a role, differs only in rate but not in the order of disulfide bond formation or in the precursor-product relationships among the folding intermediates.	Disulfides	281-290	chorionic gonadotropin subunit beta 5	Homo sapiens	45-69
8344931-10	1993	The comparison of in vitro and intracellular hCG-beta folding and hCG subunit assembly which is shown in this report indicates that the assisted folding and assembly pathway that occurs in cells, where proteins such as PDI play a role, differs only in rate but not in the order of disulfide bond formation or in the precursor-product relationships among the folding intermediates.	Disulfides	281-290	prolyl 4-hydroxylase subunit beta	Homo sapiens	219-222
10549279-1	1999	Native protein disulfide bond formation in the endoplasmic reticulum (ER) requires protein disulfide isomerase (PDI) and Ero1p.	Disulfides	15-24	prolyl 4-hydroxylase subunit beta	Homo sapiens	83-110
10549279-1	1999	Native protein disulfide bond formation in the endoplasmic reticulum (ER) requires protein disulfide isomerase (PDI) and Ero1p.	Disulfides	15-24	prolyl 4-hydroxylase subunit beta	Homo sapiens	112-115
10549279-4	1999	Direct dithiol-disulfide exchange between PDI and Ero1p is indicated by the capture of PDI-Ero1p mixed disulfides.	Disulfides	15-24	prolyl 4-hydroxylase subunit beta	Homo sapiens	42-45
10549279-4	1999	Direct dithiol-disulfide exchange between PDI and Ero1p is indicated by the capture of PDI-Ero1p mixed disulfides.	Disulfides	15-24	prolyl 4-hydroxylase subunit beta	Homo sapiens	87-90
8251066-0	1993	The disulfide bridges of the immunoglobulin-like domains of Fc gamma RIIIB are essential for efficient expression and biological activity.	Disulfides	4-13	Fc gamma receptor IIIb	Homo sapiens	60-74
10549279-4	1999	Direct dithiol-disulfide exchange between PDI and Ero1p is indicated by the capture of PDI-Ero1p mixed disulfides.	Disulfides	103-113	prolyl 4-hydroxylase subunit beta	Homo sapiens	42-45
18423212-4	2008	Disulfides in microtubule proteins are substrates for both the thioredoxin reductase system and the glutaredoxin/glutathione reductase system.	Disulfides	0-10	glutaredoxin	Homo sapiens	100-112
10549279-4	1999	Direct dithiol-disulfide exchange between PDI and Ero1p is indicated by the capture of PDI-Ero1p mixed disulfides.	Disulfides	103-113	prolyl 4-hydroxylase subunit beta	Homo sapiens	87-90
10549279-5	1999	Mixed disulfides can also be detected between PDI and the ER precursor of carboxypeptidase Y (CPY).	Disulfides	6-16	prolyl 4-hydroxylase subunit beta	Homo sapiens	46-49
10549279-6	1999	Further, PDI1 is required for the net formation of disulfide bonds in newly synthesized CPY, indicating that PDI functions as an oxidase in vivo.	Disulfides	51-60	prolyl 4-hydroxylase subunit beta	Homo sapiens	9-12
7691098-4	1993	Likewise all the IGFBPs have a complex disulfide bond structure that is required for maintenance of normal IGF binding.	Disulfides	39-48	insulin like growth factor binding protein 2	Homo sapiens	17-23
18423212-4	2008	Disulfides in microtubule proteins are substrates for both the thioredoxin reductase system and the glutaredoxin/glutathione reductase system.	Disulfides	0-10	glutathione-disulfide reductase	Homo sapiens	113-134
8338831-1	1993	Human type-alpha transforming growth factor (hTGF alpha) is a small mitogenic protein containing 50 amino acids and 3 disulfide bonds.	Disulfides	118-127	transforming growth factor alpha	Homo sapiens	45-55
17936012-4	2008	Here, we present a high yield expression system for recombinant production and efficient purification of LEKTI domain 15 as a highly soluble protein with a uniform disulfide pattern that is identical to that of other known Kazal-type inhibitors.	Disulfides	164-173	serine peptidase inhibitor Kazal type 5	Homo sapiens	105-110
8123251-0	1993	Proteolytic processing of the pro beta chain of beta-hexosaminidase occurs at basic residues contained within an exposed disulfide loop structure.	Disulfides	121-130	O-GlcNAcase	Homo sapiens	48-67
10597631-1	1999	Protein disulfide isomerase (PDI) is a protein-thiol oxidoreductase that catalyzes the oxidation, reduction and isomerization of protein disulfides.	Disulfides	137-147	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
10597631-1	1999	Protein disulfide isomerase (PDI) is a protein-thiol oxidoreductase that catalyzes the oxidation, reduction and isomerization of protein disulfides.	Disulfides	137-147	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
10597631-2	1999	In the endoplasmic reticulum PDI catalyzes both the oxidation and isomerization of disulfides on nascent polypeptides.	Disulfides	83-93	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
10597631-4	1999	PDI catalyzes the reduction of protein disulfides.	Disulfides	39-49	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
17825428-8	2007	One remarkable feature is that the number and position of cysteine residues were conserved in the mature protein among species examined, suggesting that although the primary amino acid sequences are divergent, the three-dimensional structure of CD59 via disulfide linkages may be conserved through the evolutionary process.	Disulfides	254-263	CD59 glycoprotein	Ictalurus punctatus	245-249
10560010-4	1999	This signal is represented by the N-terminal disulfide-bonded loop of CgB encoded by exon 3 and is necessary to direct CgB to SGs.	Disulfides	45-54	chromogranin B	Homo sapiens	70-73
10560010-4	1999	This signal is represented by the N-terminal disulfide-bonded loop of CgB encoded by exon 3 and is necessary to direct CgB to SGs.	Disulfides	45-54	chromogranin B	Homo sapiens	119-122
8444159-2	1993	Formation of mixed disulfides of the penultimate C-terminal cysteine residue 374 with various low-molecular-mass thiols resulted in filament destabilization, as reflected by an increase in critical concentration and steady-state ATPase activity.	Disulfides	19-29	dynein axonemal heavy chain 8	Homo sapiens	229-235
1472500-7	1992	A revised, albeit putative, model of J chain folding is presented which takes into account the correct disulfide pairing and the predictive secondary structure assignment.	Disulfides	103-112	joining chain of multimeric IgA and IgM	Homo sapiens	37-44
17920002-1	2007	We examined the aggregation of insulin as a result of reduction of disulfide bonds catalyzed by protein disulfide isomerase (PDI) using various techniques.	Disulfides	67-76	prolyl 4-hydroxylase subunit beta	Homo sapiens	96-123
1452336-2	1992	Although its cysteine motif distinguished eNAP-2 from all other currently known endogenous antibiotic peptides, including defensins and granulins, it showed substantial sequence similarity to WDNM1, a putative member of the four-disulfide-core protein family that also includes animal and human antiproteases, snake venom neurotoxins, and rat and mouse whey proteins.	Disulfides	229-238	WAP four-disulfide core domain 18	Rattus norvegicus	192-197
10455175-1	1999	Mammalian secretory phospholipase A(2)s (sPLA(2)s) are classified into several groups according to molecular structure and the localization of intramolecular disulfide bridges.	Disulfides	158-167	phospholipase A2 group IID	Homo sapiens	10-39
10455175-1	1999	Mammalian secretory phospholipase A(2)s (sPLA(2)s) are classified into several groups according to molecular structure and the localization of intramolecular disulfide bridges.	Disulfides	158-167	phospholipase A2 group IID	Homo sapiens	41-49
10438793-4	1999	These results suggest that YscC contains at least one disulfide bond that is essential for the function of this protein in Yop secretion.	Disulfides	54-63	type III secretion protein	Yersinia pestis	27-31
1337116-2	1992	Insulin receptor is a heterotetrameric glycoprotein, consisting of two alpha-subunits and two beta-subunits linked by disulfide bonds.	Disulfides	118-127	insulin receptor	Homo sapiens	0-16
1328193-1	1992	Hepatocyte growth factor (HGF) is a heterodimeric protein consisting of a heavy chain and a light chain held by a disulfide bond.	Disulfides	114-123	hepatocyte growth factor	Homo sapiens	0-24
1328193-1	1992	Hepatocyte growth factor (HGF) is a heterodimeric protein consisting of a heavy chain and a light chain held by a disulfide bond.	Disulfides	114-123	hepatocyte growth factor	Homo sapiens	26-29
17920002-1	2007	We examined the aggregation of insulin as a result of reduction of disulfide bonds catalyzed by protein disulfide isomerase (PDI) using various techniques.	Disulfides	67-76	prolyl 4-hydroxylase subunit beta	Homo sapiens	125-128
1491011-0	1992	Identification of the disulfide bonds in human plasma protein SP-40,40 (apolipoprotein-J).	Disulfides	22-31	clusterin	Homo sapiens	72-88
10439027-10	1999	These results suggested that in the inhibition of papain by cystatin SN, the first disulfide loop is more important than the second.	Disulfides	83-92	cystatin SN	Homo sapiens	60-71
17726162-2	2007	Recent studies have suggested that cryptic TF contains unpaired cysteine thiols and that activation involves the formation of the disulfide bond Cys186-Cys 209 and that protein disulfide isomerase (PDI) regulates TF coagulant and signaling activities by targeting this disulfide bond.	Disulfides	177-186	prolyl 4-hydroxylase subunit beta	Homo sapiens	198-201
10431664-7	1999	Lp(a) assembly is a complex two-step process of multiple non-covalent interactions between apolipoprotein(a) and apolipoprotein B-100 of LDL followed by covalent disulfide linkage of two free cysteine residues on both proteins.	Disulfides	162-171	lipoprotein(a)	Homo sapiens	0-5
1530626-0	1992	Functional implication of disulfide bond, Cys250 -Cys283, in bovine chymosin.	Disulfides	26-35	chymosin	Bos taurus	68-76
1530626-1	1992	The reduction, carboxymethylation and mercuration of disulfide bond, Cys250-Cys283, located on the surface of bovine chymosin molecule resulted in the loss of about 25% of enzyme activity, suggesting that Cys250-Cys283 is not intimately involved in catalytic mechanism.	Disulfides	53-62	chymosin	Bos taurus	117-125
17726162-9	2007	Overall, the present data undermine the recently proposed hypothesis that PDI-mediated disulfide exchange plays a role in regulating TF procoagulant and cell signaling functions.	Disulfides	87-96	prolyl 4-hydroxylase subunit beta	Homo sapiens	74-77
17823115-5	2007	We show here that PAPC forms oligomers that are stabilized by disulfide bonds formed between conserved Cys residues in the extracellular domain.	Disulfides	62-71	protocadherin 8 S homeolog	Xenopus laevis	18-22
10318835-3	1999	Comparison of primary sequence to that of lipoprotein and hepatic lipase reveals conservation of the serine, aspartic acid, and histidine catalytic residues as well as the 10 cysteine residues involved in disulfide bond formation.	Disulfides	205-214	lipase C, hepatic type	Homo sapiens	58-72
17823115-6	2007	Disruption of these disulfide bonds by dithiothreitol or mutation of the conserved cysteines results in defects in oligomerization, post-translational modification, trafficking to the cell surface and cell sorting function of PAPC.	Disulfides	20-29	protocadherin 8 S homeolog	Xenopus laevis	226-230
1321713-3	1992	In contrast, thioredoxin reductase from Escherichia coli showed no direct reaction with selenite, but addition of 3 microM E. coli thioredoxin also resulted in non-stoichiometric oxidation of NADPH, consistent with oxidation of the two active-site thiol groups in thioredoxin to a disulfide.	Disulfides	281-290	thioredoxin	Bos taurus	13-24
17673459-7	2007	Based on the PHE2 structure, we introduced a disulfide bond between the plexin-semaphorin-integrin domain and I-EGF2 domains in the beta2 subunit.	Disulfides	45-54	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	132-137
1321713-3	1992	In contrast, thioredoxin reductase from Escherichia coli showed no direct reaction with selenite, but addition of 3 microM E. coli thioredoxin also resulted in non-stoichiometric oxidation of NADPH, consistent with oxidation of the two active-site thiol groups in thioredoxin to a disulfide.	Disulfides	281-290	thioredoxin	Bos taurus	131-142
1321713-3	1992	In contrast, thioredoxin reductase from Escherichia coli showed no direct reaction with selenite, but addition of 3 microM E. coli thioredoxin also resulted in non-stoichiometric oxidation of NADPH, consistent with oxidation of the two active-site thiol groups in thioredoxin to a disulfide.	Disulfides	281-290	thioredoxin	Bos taurus	131-142
1316152-5	1992	Here we report several of its biochemical characteristics: A structural model for the native protein is proposed in which two disulfide-linked pairs of similar 18-kDa subunits (p18) associate to form a 72-kDa tetramer (p72).	Disulfides	126-135	NME/NM23 nucleoside diphosphate kinase 2	Rattus norvegicus	177-180
10224102-2	1999	Antibodies inhibiting LSR functions showed that the receptor is a heterotrimer or tetramer consisting of 68-kDa (alpha) and 56-kDa (beta) subunits associated through disulfide bridges.	Disulfides	166-175	LOW QUALITY PROTEIN: lipolysis-stimulated lipoprotein receptor	Cricetulus griseus	22-25
17921316-8	2007	Recombinant CYO1 accelerates disulfide bond reduction in the model substrate insulin and renatures RNase A, indicating that CYO1 has protein disulfide isomerase activity.	Disulfides	29-38	protein disulfide isomerase	Arabidopsis thaliana	12-16
10234837-4	1999	Mutations in genes involved primarily in disulfide formation (dsbA and dsbB) generally enhanced the sensitivity to Hg2+ and Cd2+ while a mutation of the dsbC gene (primarily an isomerase of disulfide bonds) had no effect.	Disulfides	190-199	putative protein DsbC	Escherichia coli	153-157
1577725-2	1992	Using the formation of disulfide bonds as an index of conformational changes during protein folding, we have developed a unique system to determine the intracellular folding pathway of the beta subunit of human chorionic gonadotropin (hCG).	Disulfides	23-32	chorionic gonadotropin subunit beta 5	Homo sapiens	235-238
1577725-7	1992	Of the six disulfide bonds in hCG-beta, bonds 34-88 and 38-57 form first.	Disulfides	11-20	chorionic gonadotropin subunit beta 5	Homo sapiens	30-33
17522051-8	2007	A detailed investigation of folding intermediates suggested that disulfide isomerization is an important role of the new plant PDI and is an essential step in the production of insecticidal cyclotides.	Disulfides	65-74	prolyl 4-hydroxylase subunit beta	Homo sapiens	127-130
1577725-9	1992	Disulfide bond 93-100, the formation of which appears to be necessary for assembly with the alpha subunit of the hCG heterodimer, forms next.	Disulfides	0-9	chorionic gonadotropin subunit beta 5	Homo sapiens	113-116
1315360-1	1992	CD69 is a signal transducing disulfide-linked homodimer functionally expressed on platelets, CD3bright thymocytes, and activated lymphocytes.	Disulfides	29-38	CD69 molecule	Homo sapiens	0-4
10383197-1	1999	Protein disulfide isomerase (PDI) is a multifunctional protein of the endoplasmic reticulum, which catalyzes the formation, breakage and rearrangement of disulfide bonds during protein folding.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
10383197-12	1999	Structural comparison of the PDI b domain with thioredoxin and PDI a reveals several features important for thiol-disulfide exchange activity.	Disulfides	114-123	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
10383197-12	1999	Structural comparison of the PDI b domain with thioredoxin and PDI a reveals several features important for thiol-disulfide exchange activity.	Disulfides	114-123	prolyl 4-hydroxylase subunit beta	Homo sapiens	63-66
10024450-1	1999	Yeast proteinase B inhibitor 2 (YIB2), which is composed of 74 amino acid residues, is an unusual serine protease inhibitor, since it lacks disulfide bonds.	Disulfides	140-149	proteinase B	Saccharomyces cerevisiae S288C	6-18
1568474-6	1992	The remaining Cys48 is concluded to link the protein chains into homodimers via an interchain disulfide to its counterpart in a second SP-B polypeptide.	Disulfides	94-103	surfactant protein B	Homo sapiens	135-139
1568474-7	1992	These SS bridges are identical to those in the porcine form and confirm a consestant and unique disulfide pattern for SP-B polypeptides in general.	Disulfides	96-105	surfactant protein B	Homo sapiens	118-122
17504764-3	2007	We demonstrated that CD40 engagement induces the formation of disulfide-linked (dl) CD40 homodimers that predominantly associate with detergent-resistant membrane microdomains.	Disulfides	62-71	CD40 molecule	Homo sapiens	21-25
1556136-8	1992	Thus, a disulfide bond between Cys128 and Cys142 of the AChR alpha or beta subunits is not needed for acetylcholine-binding.	Disulfides	8-17	cholinergic receptor, nicotinic alpha 1 S homeolog	Xenopus laevis	56-66
9933620-3	1999	Neuropsin possesses an N-glycosylated "kallikrein loop" but forms six disulfide bonds corresponding to those of trypsin.	Disulfides	70-79	opsin 5	Mus musculus	0-9
17504764-3	2007	We demonstrated that CD40 engagement induces the formation of disulfide-linked (dl) CD40 homodimers that predominantly associate with detergent-resistant membrane microdomains.	Disulfides	62-71	CD40 molecule	Homo sapiens	84-88
9873049-3	1999	We have purified two proteins that are capable of regulating the formation of this disulfide bond and found them to be members of the protein disulfide isomerase (PDI) family.	Disulfides	83-92	prolyl 4-hydroxylase subunit beta	Homo sapiens	134-161
17504764-4	2007	Mutagenesis and biochemical analyses revealed that (a) the integrity of the detergent-resistant membranes is necessary for dl-CD40 homodimer formation, (b) the cytoplasmic Cys(238) of CD40 is the target for the de novo disulfide oxidation induced by receptor oligomerization, and (c) dl-CD40 homodimer formation is required for CD40-induced interleukin-8 secretion.	Disulfides	219-228	CD40 molecule	Homo sapiens	184-188
9873049-3	1999	We have purified two proteins that are capable of regulating the formation of this disulfide bond and found them to be members of the protein disulfide isomerase (PDI) family.	Disulfides	83-92	prolyl 4-hydroxylase subunit beta	Homo sapiens	163-166
1312472-9	1992	Both disulfide- and non-disulfide-linked TIL T cell lines and clones expressed the delta TCS1 determinant.	Disulfides	5-14	treacle ribosome biogenesis factor 1	Homo sapiens	89-93
17504764-4	2007	Mutagenesis and biochemical analyses revealed that (a) the integrity of the detergent-resistant membranes is necessary for dl-CD40 homodimer formation, (b) the cytoplasmic Cys(238) of CD40 is the target for the de novo disulfide oxidation induced by receptor oligomerization, and (c) dl-CD40 homodimer formation is required for CD40-induced interleukin-8 secretion.	Disulfides	219-228	CD40 molecule	Homo sapiens	184-188
1312472-9	1992	Both disulfide- and non-disulfide-linked TIL T cell lines and clones expressed the delta TCS1 determinant.	Disulfides	24-33	treacle ribosome biogenesis factor 1	Homo sapiens	89-93
17504764-4	2007	Mutagenesis and biochemical analyses revealed that (a) the integrity of the detergent-resistant membranes is necessary for dl-CD40 homodimer formation, (b) the cytoplasmic Cys(238) of CD40 is the target for the de novo disulfide oxidation induced by receptor oligomerization, and (c) dl-CD40 homodimer formation is required for CD40-induced interleukin-8 secretion.	Disulfides	219-228	CD40 molecule	Homo sapiens	184-188
17470433-6	2007	Moreover, the present work demonstrates that three-dimensional domain swapping is involved in the formation of the oligomers, because variants of monomeric cystatin C, stabilized against three-dimensional domain swapping by engineered disulfide bonds, do not produce oligomers upon incubation under non-reducing conditions.	Disulfides	235-244	cystatin C	Homo sapiens	156-166
1535463-0	1992	Aggregation of washed platelets by plasminogen and plasminogen activators is mediated by plasmin and is inhibited by a synthetic peptide disulfide.	Disulfides	137-146	plasminogen	Homo sapiens	35-42
10824861-4	1999	The results of our experiments suggest that the released proteins can be a part of mucin molecule, cleaved by proteolysis and reduction of disulfide bridges.	Disulfides	139-148	LOC100508689	Homo sapiens	83-88
17331072-1	2007	The discovery that the flavoprotein oxidase, Erv2p, provides oxidizing potential for disulfide bond formation in yeast, has led to investigations into the roles of the mammalian homologues of this protein.	Disulfides	85-94	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	45-50
10647820-1	1999	Glutaredoxins are small proteins (12 kDa) with a conserved active sequence Cys-Pro-Tyr(-Phe)-Cys that catalyse GSH-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase.	Disulfides	115-124	2,4-dienoyl CoA reductase 1, mitochondrial	Mus musculus	169-174
10647820-1	1999	Glutaredoxins are small proteins (12 kDa) with a conserved active sequence Cys-Pro-Tyr(-Phe)-Cys that catalyse GSH-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase.	Disulfides	115-124	glutathione reductase	Mus musculus	179-200
9843414-0	1998	The longer isoform and Cys-1 disulfide bridge of rat surfactant protein A are not essential for phospholipid and type II cell interactions.	Disulfides	29-38	cystin 1	Rattus norvegicus	23-28
1377413-6	1992	Studies to determine the antigenic determinant against which 10B2 is directed, show that this is an assembled epitope which involves disulfide bonds of the PF4.	Disulfides	133-142	platelet factor 4	Homo sapiens	156-159
1730598-9	1992	The rate of reduction of the disulfide bonds by dithiothreitol was also faster for TGF-alpha.	Disulfides	29-38	transforming growth factor alpha	Homo sapiens	83-92
1730602-2	1992	Platelet GPIb, a disulfide-linked alpha beta heterodimer (Mr 160,000) that forms a noncovalent complex with GPIX (Mr 22,000), functions as the platelet adhesion receptor for surface-bound von Willebrand factor.	Disulfides	17-26	glycoprotein IX platelet	Homo sapiens	108-112
9843414-3	1998	To examine the role of the Cys-1-dependent multimerization in SP-A function, we disrupted the Cys-1 disulfide bond by deletion of the IKC sequence (SP-Ahyp, DeltaIKC) or the substitution Cys-1 to Ser (SP-Ahyp,C-1S) in mutant recombinant proteins produced in insect cells.	Disulfides	100-109	cystin 1	Rattus norvegicus	94-99
17355958-9	2007	Oxidation of Grx1 induced a complex pattern of disulfide-bonded dimers and oligomers formed between Cys-8 and either Cys-79 or Cys-83.	Disulfides	47-56	glutaredoxin	Homo sapiens	13-17
1738091-0	1992	Contribution of disulfide bonds in the carboxyl terminus of the human immunodeficiency virus type I gp120 glycoprotein to CD4 binding.	Disulfides	16-25	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	100-105
1738091-1	1992	The carboxyl half of the HIV-1 gp120 glycoprotein, which has been implicated in binding to the CD4 receptor, contains two disulfide bonds linking cysteine residues 378-445 and 385-418.	Disulfides	122-131	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	31-36
9799641-2	1998	Recombinant ADA2h is an 81-residue globular domain with no disulfide bridges or cis-prolyl bonds, which follows a two-state folding transition.	Disulfides	59-68	transcriptional adaptor 2A	Homo sapiens	12-16
9765263-7	1998	NMR solution structural calculations on this molecule demonstrate correct formation of the three disulfide bonds of TGF-alpha 8-50 and have established the presence of native secondary structure in the B and C loops of the protein.	Disulfides	97-106	transforming growth factor alpha	Homo sapiens	116-125
1727607-7	1992	Thus a disulfide loop at the V3 portion of gp160 is required for cleavage into gp120 and gp41, presumably because the loop is required for proper tertiary structure.	Disulfides	7-16	glutamyl aminopeptidase	Homo sapiens	43-48
17349612-1	2007	Raman spectroscopy was used to determine the conformation of the disulfide linkage between cysteine residues in the homodimeric construct of the N-terminal alpha helical domain of surfactant protein B (dSP-B(1-25)).	Disulfides	65-74	surfactant protein B	Homo sapiens	180-200
1836482-5	1991	Because zeta, eta, and gamma have the potential to join together to form disulfide linked homo- and heterodimers, it has been postulated that alternative dimeric forms composed of these zeta-related subunits might subserve unique signal transducing functions in hematopoietic cells.	Disulfides	73-82	endothelin receptor type A	Homo sapiens	9-12
9696864-2	1998	By introducing cysteine residues into specific locations along these alpha helices, the normally labile HIV-1 gp160 envelope glycoprotein was converted into a stable disulfide-linked oligomer.	Disulfides	166-175	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	110-137
9703976-1	1998	Protein disulfide isomerase (PDI), the product of the essential PDI1 gene of Saccharomyces cerevisiae catalyzes oxidization of thiols, reduction of disulfide bonds, and isomerization of disulfides.	Disulfides	8-17	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	64-68
9703976-1	1998	Protein disulfide isomerase (PDI), the product of the essential PDI1 gene of Saccharomyces cerevisiae catalyzes oxidization of thiols, reduction of disulfide bonds, and isomerization of disulfides.	Disulfides	186-196	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	64-68
1666014-1	1991	192 IgG, a monoclonal antibody to the rat nerve growth factor (NGF) receptor, was disulfide-coupled to saporin, a ribosome-inactivating protein.	Disulfides	82-91	nerve growth factor receptor	Rattus norvegicus	42-76
17452033-2	2007	It contains three subunits (C8alpha, C8beta, C8gamma) arranged as a disulfide-linked C8alpha-gamma heterodimer that is noncovalently associated with C8beta.	Disulfides	68-77	complement C8 beta chain	Homo sapiens	149-155
1917990-6	1991	Calgizzarin can exist as a dimer by forming a disulfide bridge.	Disulfides	46-55	protein S100-A11	Oryctolagus cuniculus	0-11
9651330-0	1998	Matrilin-3 forms disulfide-linked oligomers with matrilin-1 in bovine epiphyseal cartilage.	Disulfides	17-26	matrilin 3	Bos taurus	0-10
9653033-0	1998	Disulfide analysis reveals a role for macrophage migration inhibitory factor (MIF) as thiol-protein oxidoreductase.	Disulfides	0-9	macrophage migration inhibitory factor	Homo sapiens	38-76
9653033-0	1998	Disulfide analysis reveals a role for macrophage migration inhibitory factor (MIF) as thiol-protein oxidoreductase.	Disulfides	0-9	macrophage migration inhibitory factor	Homo sapiens	78-81
17385906-6	2007	An ability of recoverin to form a disulfide dimer and thiol-oxidized monomer under mild oxidizing conditions was found using SDS-PAGE in reducing and nonreducing conditions and Ellman"s test.	Disulfides	34-43	recoverin	Homo sapiens	14-23
9688536-0	1998	Specific reduction of insulin disulfides by macrophage migration inhibitory factor (MIF) with glutathione and dihydrolipoamide: potential role in cellular redox processes.	Disulfides	30-40	macrophage migration inhibitory factor	Homo sapiens	44-82
9688536-0	1998	Specific reduction of insulin disulfides by macrophage migration inhibitory factor (MIF) with glutathione and dihydrolipoamide: potential role in cellular redox processes.	Disulfides	30-40	macrophage migration inhibitory factor	Homo sapiens	84-87
9688536-3	1998	Here we further investigated this function by examining the reduction of insulin disulfides by wild-type human MIF (wtMIF) using various substrates, namely glutathione (GSH), dihydrolipoamide, L-cysteine, beta-mercaptoethanol and dithiothreitol.	Disulfides	81-91	macrophage migration inhibitory factor	Homo sapiens	111-114
9688536-6	1998	Reduction of insulin disulfides by MIF was closely dependent on the presence of the Cys57-Ala-Leu-Cys60 (CALC) motif-forming cysteines C57 and C60, whereas C81 was not involved (activities: 51+/-13%, 14+/-5%, and 70+/-12% of wtMIF, respectively, and 20+/-3% for the double mutant C57S/C60S).	Disulfides	21-31	macrophage migration inhibitory factor	Homo sapiens	35-38
21239297-1	1991	Lipoprotein(a) [Lp(a)] is a class of lipoprotein particles having the lipid composition of plasma low-density lipoprotein (LDL), but with a distinct protein moiety comprised of two proteins linked together by a disulfide bridge.	Disulfides	211-220	lipoprotein(a)	Homo sapiens	0-14
21239297-1	1991	Lipoprotein(a) [Lp(a)] is a class of lipoprotein particles having the lipid composition of plasma low-density lipoprotein (LDL), but with a distinct protein moiety comprised of two proteins linked together by a disulfide bridge.	Disulfides	211-220	lipoprotein(a)	Homo sapiens	16-21
9675066-2	1998	Lp(a) particles are generated through the formation of a disulfide bond between Cys4057 of kringle IV type 9, (KIVt9), of the multikringle apolipoprotein(a) [apo(a)] and a cysteine in apoB-100 low-density lipoprotein (LDL).	Disulfides	57-66	lipoprotein(a)	Homo sapiens	0-5
17322339-0	2007	The structure of eukaryotic translation initiation factor-4E from wheat reveals a novel disulfide bond.	Disulfides	88-97	eukaryotic translation initiation factor 4E-1	Triticum aestivum	17-60
9675066-2	1998	Lp(a) particles are generated through the formation of a disulfide bond between Cys4057 of kringle IV type 9, (KIVt9), of the multikringle apolipoprotein(a) [apo(a)] and a cysteine in apoB-100 low-density lipoprotein (LDL).	Disulfides	57-66	lipoprotein(a)	Homo sapiens	139-156
9675066-2	1998	Lp(a) particles are generated through the formation of a disulfide bond between Cys4057 of kringle IV type 9, (KIVt9), of the multikringle apolipoprotein(a) [apo(a)] and a cysteine in apoB-100 low-density lipoprotein (LDL).	Disulfides	57-66	lipoprotein(a)	Homo sapiens	158-164
9649309-1	1998	Lipoprotein(a) [Lp(a)] consists of low-density lipoprotein (LDL) and apolipoprotein(a) [apo(a)] linked with a disulfide bond.	Disulfides	110-119	lipoprotein(a)	Homo sapiens	0-14
1800955-1	1991	Amylin, a 37-residue polypeptide with a single disulfide bond originally isolated from the pancreas of type-II diabetic patients, has been shown to cause peripheral insulin resistance and to attenuate the inhibition of hepatic glucose output by insulin.	Disulfides	47-56	islet amyloid polypeptide	Homo sapiens	0-6
2044199-2	1991	wt polypeptide with anti-carcinogenic activity, was coupled to poly(D-lysine) (BBI-SS-PDL) and poly(L-glutamate) (BBI-SS-PLG) with a disulfide-cross-linking agent, N-succinimidyl 3-(2-pyridyldithio)propionate (SPDP).	Disulfides	133-142	plasminogen	Mus musculus	121-124
9649309-1	1998	Lipoprotein(a) [Lp(a)] consists of low-density lipoprotein (LDL) and apolipoprotein(a) [apo(a)] linked with a disulfide bond.	Disulfides	110-119	lipoprotein(a)	Homo sapiens	16-21
17322339-7	2007	A Cys-to-serine mutant of wheat eIF4E, which lacked the ability to form the disulfide, crystallized with m(7)GDP in its binding pocket, with a structure similar to that of the eIF4E-cap complex of other species.	Disulfides	76-85	eukaryotic translation initiation factor 4E-1	Triticum aestivum	32-37
17196395-7	2007	This approach allowed slow LOX-1 refolding and assembly of correct intrachain disulfide bonds.	Disulfides	78-87	oxidized low density lipoprotein receptor 1	Homo sapiens	27-32
9649343-9	1998	The global solvent exposure and the hydrodynamic volume of the denatured protein are much less than for maximally unfolded disulfide-intact RNase A.	Disulfides	123-132	ribonuclease A family member 1, pancreatic	Homo sapiens	140-147
9603915-3	1998	These studies demonstrate that CD3delta proteins exist as both monomeric and oligomeric (disulfide-linked) species that differentially assemble with CD3epsilon subunits in CD4(+)CD8(+) thymocytes and splenic T cells.	Disulfides	89-98	CD3 antigen, epsilon polypeptide	Mus musculus	149-159
9601051-1	1998	Lipoprotein(a) [Lp(a)] particle formation is a two-step process in which initial noncovalent interactions between apolipoprotein(a) [apo(a)] and the apolipoprotein B-100 (apoB-100) component of low-density lipoprotein (LDL) precede disulfide bond formation.	Disulfides	232-241	lipoprotein(a)	Homo sapiens	0-14
9601051-1	1998	Lipoprotein(a) [Lp(a)] particle formation is a two-step process in which initial noncovalent interactions between apolipoprotein(a) [apo(a)] and the apolipoprotein B-100 (apoB-100) component of low-density lipoprotein (LDL) precede disulfide bond formation.	Disulfides	232-241	lipoprotein(a)	Homo sapiens	16-21
9601051-1	1998	Lipoprotein(a) [Lp(a)] particle formation is a two-step process in which initial noncovalent interactions between apolipoprotein(a) [apo(a)] and the apolipoprotein B-100 (apoB-100) component of low-density lipoprotein (LDL) precede disulfide bond formation.	Disulfides	232-241	lipoprotein(a)	Homo sapiens	114-131
1658176-1	1991	Circulating apolipoprotein J (apoJ) is a 70 kDa glycoprotein comprised of disulfide-linked alpha and beta subunits derived from a single precursor.	Disulfides	74-83	clusterin	Homo sapiens	12-28
1658176-1	1991	Circulating apolipoprotein J (apoJ) is a 70 kDa glycoprotein comprised of disulfide-linked alpha and beta subunits derived from a single precursor.	Disulfides	74-83	clusterin	Homo sapiens	30-34
2026606-2	1991	Here we have determined the disulfide bonding pattern of recombinant oncostatin M and have used site-directed mutagenesis to identify regions of this molecule necessary for receptor binding and growth inhibitory activities.	Disulfides	28-37	oncostatin M	Homo sapiens	69-81
2026606-3	1991	Two intramolecular disulfide bonds, C6-C127 and C49-C167, were identified in recombinant oncostatin M.	Disulfides	19-28	oncostatin M	Homo sapiens	89-101
2026606-10	1991	Taken together, these results indicate that biological activity of oncostatin M requires discontinuous regions of the molecule, including residues near the essential disulfide bond, C49-C167, and within a putative amphiphilic helix at the carboxyl terminus.	Disulfides	166-175	oncostatin M	Homo sapiens	67-79
9575164-5	1998	A soluble disulfide-bonded dimer of the TfR is released into the medium in contrast to the cleavage at Arg-100 where a dimer lacking intersubunit disulfide bonds is released.	Disulfides	10-19	transferrin receptor	Homo sapiens	40-43
1988051-3	1991	With catalytic concentrations of PDI and near stoichiometric concentrations of glutathione disulfide, approximately 4 equiv (2 equiv of ribonuclease disulfide) of GSH are formed very rapidly followed by a slower formation of GSH, which corresponds to an additional 2 disulfide bond equiv.	Disulfides	149-158	prolyl 4-hydroxylase subunit beta	Homo sapiens	33-36
17209042-10	2007	We examined the recombinant TLR3 ECD for disulfide bond formation, poly(I:C) binding, and protein-protein interaction.	Disulfides	41-50	toll like receptor 3	Homo sapiens	28-32
1988051-4	1991	The rapid formation of RNase disulfide bonds and the subsequent rearrangement of incorrect disulfide isomers to active RNase are both catalyzed by PDI.	Disulfides	29-38	prolyl 4-hydroxylase subunit beta	Homo sapiens	147-150
1988051-4	1991	The rapid formation of RNase disulfide bonds and the subsequent rearrangement of incorrect disulfide isomers to active RNase are both catalyzed by PDI.	Disulfides	91-100	prolyl 4-hydroxylase subunit beta	Homo sapiens	147-150
1988051-5	1991	In the absence of GSSG or other oxidants, disulfide bond equivalents of PDI can be used to form disulfide bonds in RNase in a stoichiometric reaction.	Disulfides	42-51	prolyl 4-hydroxylase subunit beta	Homo sapiens	72-75
1988051-5	1991	In the absence of GSSG or other oxidants, disulfide bond equivalents of PDI can be used to form disulfide bonds in RNase in a stoichiometric reaction.	Disulfides	96-105	prolyl 4-hydroxylase subunit beta	Homo sapiens	72-75
1805558-0	1991	Structure and function in recombinant HIV-1 gp120 and speculation about the disulfide bonding in the gp120 homologs of HIV-2 and SIV.	Disulfides	76-85	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	101-106
1660393-1	1991	SP-40,40 is a serum glycoprotein consisting of two different subunits (alpha and beta) assembled into a dimer by disulfide bonds.	Disulfides	113-122	clusterin	Homo sapiens	0-5
1985197-7	1991	Mutation of the putative disulfide bridge-forming Cys at residue 336 blocked gp160 cleavage and CD4 binding.	Disulfides	25-34	glutamyl aminopeptidase	Homo sapiens	77-82
2253341-1	1990	Lipoprotein (a) [Lp(a)] represents a class of lipoprotein particles defined by the presence of apolipoprotein(a), a unique glycoprotein linked by a disulfide bond to apolipoprotein B-100 to form a single macromolecule.	Disulfides	148-157	lipoprotein(a)	Homo sapiens	17-22
2175907-2	1990	Immunoblot analysis of reduced and unreduced extracts revealed that p65 exists as a 65-kDa monomer during interphase but forms a 130-kDa disulfide-linked homodimer during mitosis.	Disulfides	137-146	RELA proto-oncogene, NF-kB subunit	Homo sapiens	68-71
9548923-1	1998	Lipoprotein(a) [Lp(a)] consists of LDL and the glycoprotein apolipoprotein(a) [apo(a)], which are covalently linked via a single disulfide bridge.	Disulfides	129-138	lipoprotein(a)	Homo sapiens	0-14
9548923-1	1998	Lipoprotein(a) [Lp(a)] consists of LDL and the glycoprotein apolipoprotein(a) [apo(a)], which are covalently linked via a single disulfide bridge.	Disulfides	129-138	lipoprotein(a)	Homo sapiens	16-21
9548923-1	1998	Lipoprotein(a) [Lp(a)] consists of LDL and the glycoprotein apolipoprotein(a) [apo(a)], which are covalently linked via a single disulfide bridge.	Disulfides	129-138	lipoprotein(a)	Homo sapiens	60-77
9548923-1	1998	Lipoprotein(a) [Lp(a)] consists of LDL and the glycoprotein apolipoprotein(a) [apo(a)], which are covalently linked via a single disulfide bridge.	Disulfides	129-138	lipoprotein(a)	Homo sapiens	79-85
9545296-1	1998	Protein-disulfide isomerase (PDI) has been shown to be a multifunctional enzyme catalyzing the formation of disulfide bonds, as well as being a component of the enzymes prolyl 4-hydroxylase (P4-H) and microsomal triglyceride transfer protein.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
9545296-8	1998	This demonstrates that PDI has multiple functions in the folding of the same protein, that is, as a catalyst for disulfide bond formation, as a subunit of P4-H during proline hydroxylation, and independently as a molecular chaperone during chain assembly.	Disulfides	113-122	prolyl 4-hydroxylase subunit beta	Homo sapiens	23-26
9602168-3	1998	Previous studies have shown that LTBP-1 binds the small latent TGF-beta 1 complex through a disulfide bond between an 8-cysteine structural motif of LTBP-1 (TGF-bp repeat) and the propeptide dimer of latent TGF-beta 1 (TGF-beta 1 latency associated peptide).	Disulfides	92-101	transforming growth factor, beta 1	Mus musculus	63-73
9602168-3	1998	Previous studies have shown that LTBP-1 binds the small latent TGF-beta 1 complex through a disulfide bond between an 8-cysteine structural motif of LTBP-1 (TGF-bp repeat) and the propeptide dimer of latent TGF-beta 1 (TGF-beta 1 latency associated peptide).	Disulfides	92-101	transforming growth factor, beta 1	Mus musculus	207-217
9602168-3	1998	Previous studies have shown that LTBP-1 binds the small latent TGF-beta 1 complex through a disulfide bond between an 8-cysteine structural motif of LTBP-1 (TGF-bp repeat) and the propeptide dimer of latent TGF-beta 1 (TGF-beta 1 latency associated peptide).	Disulfides	92-101	transforming growth factor, beta 1	Mus musculus	207-217
9508767-0	1998	Essential role of the disulfide-bonded loop of chromogranin B for sorting to secretory granules is revealed by expression of a deletion mutant in the absence of endogenous granin synthesis.	Disulfides	22-31	chromogranin B	Homo sapiens	47-61
9507005-10	1998	Two of these half-cystines, Cys13244 and Cys13246, are in the highly conserved sequence C13244LC13246C in the disulfide-rich domain of several other human mucins and in prepro-von Willebrand factor and norrin, a protein that in mutant forms gives rise to Norrie disease.	Disulfides	110-119	norrin cystine knot growth factor NDP	Homo sapiens	202-208
9507005-11	1998	Support for the involvement of these half-cystines in formation of disulfide-bonded dimers of these molecules is also provided by known mutations in prepro-von Willebrand factor and norrin.	Disulfides	67-76	norrin cystine knot growth factor NDP	Homo sapiens	182-188
9521669-8	1998	We also examined the effects of ATP, calcium, and disulfide reduction on the lectin properties of calnexin and calreticulin.	Disulfides	50-59	calnexin	Homo sapiens	98-106
9478964-2	1998	OCIF is present both as a approximately 60-kDa monomer and a disulfide-linked homodimer.	Disulfides	61-70	TNF receptor superfamily member 11b	Homo sapiens	0-4
2238472-2	1990	When expressed from a recombinant vaccinia virus and analyzed by velocity gradient sedimentation and polyacrylamide gel electrophoresis, a significant proportion of gp160 molecules formed oligomers that were stabilized by intermolecular disulfide bonds.	Disulfides	237-246	glutamyl aminopeptidase	Homo sapiens	165-170
2238472-5	1990	These results indicate that there are two populations of gp160 precursors, one that is folded and processed correctly into gp120 and gp41 and another that is intermolecularly disulfide bonded and remains uncleaved.	Disulfides	175-184	glutamyl aminopeptidase	Homo sapiens	57-62
2238472-6	1990	We propose that the formation of intermolecular disulfide bonds is not an intermediate step in the maturation of the envelope glycoprotein, but rather a result of misfolding of the gp160 precursor which prevents it from being properly processed.	Disulfides	48-57	glutamyl aminopeptidase	Homo sapiens	181-186
2144550-5	1990	In the absence of the CD3-gamma, delta, epsilon, and zeta polypeptide chains the disulfide bridged TCR-alpha/beta heterodimer was not formed and the Ag receptor did not appear at the cell surface.	Disulfides	81-90	T cell receptor alpha constant	Homo sapiens	99-108
2085387-3	1990	Plasma desorption mass spectrometry and amino acid sequence analysis now confirm that bovine PTP contains two disulfide-bonded polypeptides, an A chain of 101 amino acid residues with a molecular weight of 11,073 and a B chain of 35 residues with a molecular weight of 3970.	Disulfides	110-119	regenerating islet-derived protein 3-gamma	Bos taurus	93-96
1698288-7	1990	Metabolic labeling and immunoprecipitation of oocyte microinjected with a mixture of CD3 zeta plus Fc epsilon RI alpha and Fc epsilon RI beta RNAs reveals a noncovalent association between the CD3 zeta-zeta disulfide-linked homodimer and Fc epsilon RI alpha-beta.	Disulfides	207-216	CD247 molecule L homeolog	Xenopus laevis	85-93
17005419-6	2007	Co-expression of the E. coli disulfide bond isomerase dsbC increased scFv yields by delaying lysis of the host bacterial cells though this effect was not synergistic with molecular chaperone co-production.	Disulfides	29-38	putative protein DsbC	Escherichia coli	54-58
1698288-7	1990	Metabolic labeling and immunoprecipitation of oocyte microinjected with a mixture of CD3 zeta plus Fc epsilon RI alpha and Fc epsilon RI beta RNAs reveals a noncovalent association between the CD3 zeta-zeta disulfide-linked homodimer and Fc epsilon RI alpha-beta.	Disulfides	207-216	CD247 molecule L homeolog	Xenopus laevis	193-201
2387851-1	1990	Apolipoprotein J (apoJ), a unique 70-kDa component of high density lipoproteins in human plasma, consists of two disulfide-linked subunits designated apoJ alpha (34-36 kDa), and apoJ beta (36-39 kDa) which share pI values of 4.9-5.4 and which are recognized by a monoclonal antibody (mAb) 11.	Disulfides	113-122	clusterin	Homo sapiens	0-16
2387851-1	1990	Apolipoprotein J (apoJ), a unique 70-kDa component of high density lipoproteins in human plasma, consists of two disulfide-linked subunits designated apoJ alpha (34-36 kDa), and apoJ beta (36-39 kDa) which share pI values of 4.9-5.4 and which are recognized by a monoclonal antibody (mAb) 11.	Disulfides	113-122	clusterin	Homo sapiens	18-22
2387851-1	1990	Apolipoprotein J (apoJ), a unique 70-kDa component of high density lipoproteins in human plasma, consists of two disulfide-linked subunits designated apoJ alpha (34-36 kDa), and apoJ beta (36-39 kDa) which share pI values of 4.9-5.4 and which are recognized by a monoclonal antibody (mAb) 11.	Disulfides	113-122	clusterin	Homo sapiens	150-154
2387851-1	1990	Apolipoprotein J (apoJ), a unique 70-kDa component of high density lipoproteins in human plasma, consists of two disulfide-linked subunits designated apoJ alpha (34-36 kDa), and apoJ beta (36-39 kDa) which share pI values of 4.9-5.4 and which are recognized by a monoclonal antibody (mAb) 11.	Disulfides	113-122	clusterin	Homo sapiens	150-154
9468508-3	1998	However, the human MARCO polypeptide chain lacked the intracellular cysteine present in mouse, as well as two extracellular cysteines that form interchain disulfide bonds in the murine protein.	Disulfides	155-164	macrophage receptor with collagenous structure	Homo sapiens	19-24
9468508-6	1998	The bacteria-binding region of MARCO was determined in binding studies with full-length and truncated variants of MARCO, and localized to a region proximal to the cysteine-rich part of the COOH-terminal domain V. The intrachain disulfide bond pattern of domain V was established showing that these bonds are between cysteine pairs C1-C5, C2-C6, and C3-C4.	Disulfides	228-237	macrophage receptor with collagenous structure	Homo sapiens	31-36
9463371-1	1998	Protein disulfide isomerase (PDI) is a very efficient catalyst of folding of many disulfide-bonded proteins.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
17249696-0	2007	Modification of protein by disulfide S-monoxide and disulfide S-dioxide: distinctive effects on PKC.	Disulfides	27-36	protein kinase C, beta	Mus musculus	96-99
9491903-2	1998	It is similar to low-density lipoprotein with an additional molecule of apo A covalently linked to apo B-100 by one disulfide bridge.	Disulfides	116-125	lipoprotein(a)	Homo sapiens	72-77
17116644-7	2007	Human RNase 8 represents one of the first examples in which the presumable evolutionary change of a disulfide bond involves 1 loss and 1 gain of cysteine, instead of 2 losses or 2 gains.	Disulfides	100-109	ribonuclease A family member 8	Homo sapiens	6-13
9806942-1	1998	BACKGROUND: Cellular retinoic acid binding protein I (CRABPI) is a small, predominantly beta-sheet protein with a simple architecture and no disulfides or cofactors.	Disulfides	141-151	cellular retinoic acid binding protein 1	Homo sapiens	12-52
9806942-1	1998	BACKGROUND: Cellular retinoic acid binding protein I (CRABPI) is a small, predominantly beta-sheet protein with a simple architecture and no disulfides or cofactors.	Disulfides	141-151	cellular retinoic acid binding protein 1	Homo sapiens	54-60
2188973-3	1990	Protein disulfide-isomerase contains two redox-active disulfides/molecule which were reduced by NADPH and calf thioredoxin reductase (Km approximately 35 microM).	Disulfides	54-64	prolyl 4-hydroxylase subunit beta	Bos taurus	0-27
2188973-6	1990	Fluorescence measurements demonstrated that thioredoxin--(SH)2 reduced the disulfides of the isomerase and allowed the kinetics of the reaction to be followed; the reaction was also catalyzed by calf thioredoxin reductase.	Disulfides	75-85	thioredoxin	Bos taurus	44-55
2318861-0	1990	High level bacterial expression of uteroglobin, a dimeric eukaryotic protein with two interchain disulfide bridges, in its natural quaternary structure.	Disulfides	97-106	uteroglobin	Oryctolagus cuniculus	35-46
2318861-5	1990	We have constructed three plasmids which are able to direct expression of recombinant rabbit uteroglobin, a homodimeric protein with two interchain disulfide bridges, in Escherichia coli.	Disulfides	148-157	uteroglobin	Oryctolagus cuniculus	93-104
2310758-5	1990	The antibody R377 bound to the non-reduced rat platelet phospholipase A2 bearing intact intramolecular disulfide bonds, but not to the reduced enzyme.	Disulfides	103-112	phospholipase A2 group IIA	Rattus norvegicus	47-72
9451015-6	1998	Each of the precursors of MUC2, MUC5AC, MUC5B, and MUC6 formed a single species of disulfide-linked homo-oligomer within 1 h after pulse labeling.	Disulfides	83-92	mucin 5B, oligomeric mucus/gel-forming	Homo sapiens	40-45
9451015-6	1998	Each of the precursors of MUC2, MUC5AC, MUC5B, and MUC6 formed a single species of disulfide-linked homo-oligomer within 1 h after pulse labeling.	Disulfides	83-92	mucin 6, oligomeric mucus/gel-forming	Homo sapiens	51-55
9407136-0	1997	Norrie disease protein (norrin) forms disulfide-linked oligomers associated with the extracellular matrix.	Disulfides	38-47	norrin cystine knot growth factor NDP	Homo sapiens	0-22
9407136-0	1997	Norrie disease protein (norrin) forms disulfide-linked oligomers associated with the extracellular matrix.	Disulfides	38-47	norrin cystine knot growth factor NDP	Homo sapiens	24-30
17116644-8	2007	Our results provide the foundation for detailed analysis toward understanding the impact of disulfide-bond reshuffling on the structure, function, and evolution of proteins in general and human RNase 8 in particular.	Disulfides	92-101	ribonuclease A family member 8	Homo sapiens	194-201
17098255-7	2007	Furthermore, LC-MS/MS analysis of oxidized DmGPx exposed to a reduced Trx C35S mutant yielded a dead-end intermediate containing a disulfide between Trx C32 and DmGPx C91.	Disulfides	131-140	PHGPx	Drosophila melanogaster	43-48
9527497-1	1997	The atherogenic plasma lipoprotein complex Lp(a) consists of low density lipoprotein (LDL) and the highly polymorphic glycoprotein apolipoprotein(a) covalently linked by a disulfide bridge.	Disulfides	172-181	lipoprotein(a)	Homo sapiens	43-48
2361960-1	1990	The complete peptide map of purified recombinant human interleukin 5 (rhIL-5) was determined to verify its primary structure, glycosylation sites, and disulfide bonding structure.	Disulfides	151-160	interleukin 5	Homo sapiens	55-68
17098255-7	2007	Furthermore, LC-MS/MS analysis of oxidized DmGPx exposed to a reduced Trx C35S mutant yielded a dead-end intermediate containing a disulfide between Trx C32 and DmGPx C91.	Disulfides	131-140	PHGPx	Drosophila melanogaster	161-166
17098255-8	2007	Thus, the catalytic mechanism of DmGPx, unlike that of selenocysteine (Sec)GPxs, involves formation of an internal disulfide that is pivotal to the interaction with Trx.	Disulfides	115-124	PHGPx	Drosophila melanogaster	33-38
17145752-0	2007	Cell surface detachment of pregnancy-associated plasma protein-A requires the formation of intermolecular proteinase-inhibitor disulfide bonds and glycosaminoglycan covalently bound to the inhibitor.	Disulfides	127-136	pappalysin 1	Homo sapiens	27-64
1688430-0	1990	Role of disulfide bond formation in the folding of human chorionic gonadotropin beta subunit into an alpha beta dimer assembly-competent form.	Disulfides	8-17	chorionic gonadotropin subunit beta 5	Homo sapiens	57-92
1688430-5	1990	The earliest biosynthetic precursor of the human chorionic gonadotropin beta subunit detectable in JAR cells pulse labeled for 2 min is p beta 1, a form that lacks half of the six intrachain disulfide bonds observed in the fully processed dimer form of beta and that does not combine with the alpha subunit.	Disulfides	191-200	chorionic gonadotropin subunit beta 5	Homo sapiens	49-84
1688430-6	1990	p beta 1 is rapidly (t1/2 approximately 4 min) converted into p beta 2, which has a full complement of intrachain disulfide bonds and does combine with the alpha subunit.	Disulfides	114-123	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	64-70
1688430-7	1990	In this study, we have identified the three late forming disulfide bonds involved in the transition of p beta 1 into the assembly-compete form, p beta 2.	Disulfides	57-66	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	146-152
9368005-0	1997	The disulfide bonds in the C-terminal domains of the human insulin receptor ectodomain.	Disulfides	4-13	insulin receptor	Homo sapiens	59-75
9368005-1	1997	The human insulin receptor is a homodimer consisting of two monomers linked by disulfide bonds.	Disulfides	79-88	insulin receptor	Homo sapiens	10-26
9368005-4	1997	There are two classes of disulfide bonds in the insulin receptor, those that can be reduced under mild reducing conditions to give alpha-beta monomers (class I) and those that require stronger reducing conditions (class II).	Disulfides	25-34	insulin receptor	Homo sapiens	48-64
9348303-4	1997	In this report, we demonstrate for the first time that pT alpha-containing pre-TCR complexes are expressed at low levels on the surface of primary thymocytes and that these pre-TCR complexes comprise a disulfide-linked pT alpha-TCR-beta heterodimer associated not only with CD3-gamma and -epsilon, as previously reported, but also with zeta and delta.	Disulfides	202-211	pre T cell antigen receptor alpha	Mus musculus	55-63
9348303-4	1997	In this report, we demonstrate for the first time that pT alpha-containing pre-TCR complexes are expressed at low levels on the surface of primary thymocytes and that these pre-TCR complexes comprise a disulfide-linked pT alpha-TCR-beta heterodimer associated not only with CD3-gamma and -epsilon, as previously reported, but also with zeta and delta.	Disulfides	202-211	pre T cell antigen receptor alpha	Mus musculus	219-231
32796317-6	2021	A sex-dependent temporal profile in expression of inflammatory factors in the ankle joint was observed in response to intra-articular injection of disulfide HMGB1, with male mice showing a delayed, yet longer lasting increase in mRNA levels for several of the investigated factors.	Disulfides	147-156	high mobility group box 1	Mus musculus	157-162
9348303-4	1997	In this report, we demonstrate for the first time that pT alpha-containing pre-TCR complexes are expressed at low levels on the surface of primary thymocytes and that these pre-TCR complexes comprise a disulfide-linked pT alpha-TCR-beta heterodimer associated not only with CD3-gamma and -epsilon, as previously reported, but also with zeta and delta.	Disulfides	202-211	CD3 antigen, epsilon polypeptide	Mus musculus	274-296
17145752-3	2007	In human pregnancy, the majority of PAPP-A circulates as a disulfide-bonded complex with its inhibitor, the proform of eosinophil major basic protein (proMBP).	Disulfides	59-68	pappalysin 1	Homo sapiens	36-42
17145752-3	2007	In human pregnancy, the majority of PAPP-A circulates as a disulfide-bonded complex with its inhibitor, the proform of eosinophil major basic protein (proMBP).	Disulfides	59-68	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	119-149
9404661-0	1997	Generation and characterization of an anti-CD19 single-chain Fv immunotoxin composed of C-terminal disulfide-linked dgRTA.	Disulfides	99-108	CD19 molecule	Homo sapiens	43-47
17145752-3	2007	In human pregnancy, the majority of PAPP-A circulates as a disulfide-bonded complex with its inhibitor, the proform of eosinophil major basic protein (proMBP).	Disulfides	59-68	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	151-157
9404661-8	1997	Our study with anti-CD19 scFv immunotoxin indicates that the formation of a disulfide-linked scFv immunotoxin is an alternative to the recombinant method of producing scFv immunotoxin.	Disulfides	76-85	CD19 molecule	Homo sapiens	20-24
9520123-4	1997	Apo(a) exhibited a prolonged and complex folding pathway in the ER, which included incorporation of apo(a) into high molecular weight, disulfide-linked aggregates.	Disulfides	135-144	lipoprotein(a)	Homo sapiens	0-6
9520123-4	1997	Apo(a) exhibited a prolonged and complex folding pathway in the ER, which included incorporation of apo(a) into high molecular weight, disulfide-linked aggregates.	Disulfides	135-144	lipoprotein(a)	Homo sapiens	100-106
9520125-3	1997	Specific kringle-4 domains in apo(a), mainly T-6 and T-7, bind in a first step to circulating LDL, followed by the stabilization of the newly formed Lp(a) complex by a disulfide bridge.	Disulfides	168-177	lipoprotein(a)	Homo sapiens	149-154
31590051-3	2019	Human serum albumin (HSA) was attached to the pore openings of MCN via disulfide bonds to serve as a gatekeeper due to its biocompatibility and appropriate molecular size.	Disulfides	71-80	albumin	Mus musculus	6-19
34780781-0	2022	Disulfide bonds play a critical role in the structure and function of the receptor-binding domain of the SARS-CoV-2 Spike antigen.	Disulfides	0-9	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	116-121
34780781-2	2022	The Spike proteins of coronaviruses, responsible for cell receptor binding and viral internalization, possess multiple and frequently conserved disulfide bonds raising the question about their role in these proteins.	Disulfides	144-153	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	4-9
34780781-3	2022	Here, we present a detailed structural and functional investigation of the disulfide bonds of the SARS-CoV-2 Spike receptor-binding domain (RBD).	Disulfides	75-84	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	109-114
34780781-5	2022	This flexibility is particularly prominent for the disulfide bond-containing surface loop (residues 456-490) that participates in the formation of the interaction surface with the Spike cell receptor ACE2.	Disulfides	51-60	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	180-185
34780781-5	2022	This flexibility is particularly prominent for the disulfide bond-containing surface loop (residues 456-490) that participates in the formation of the interaction surface with the Spike cell receptor ACE2.	Disulfides	51-60	angiotensin converting enzyme 2	Homo sapiens	200-204
17145752-5	2007	We show here that proMBP detaches surface-bound PAPP-A in a process that depends on the proMBP GAG and also on the formation of intermolecular disulfide bonds between PAPP-A and proMBP.	Disulfides	143-152	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	18-24
34780781-6	2022	In vitro, disulfide bond reducing agents affect the RBD secondary structure, lower its melting temperature from 52 C to 36-39 C and decrease its binding affinity to ACE2 by two orders of magnitude at 37 C. Consistent with these in vitro findings, the reducing agents tris(2-carboxyethyl)phosphine (TCEP) and dithiothreitol (DTT) were able to inhibit viral replication at low millimolar levels in cell-based assays.	Disulfides	10-19	angiotensin converting enzyme 2	Homo sapiens	165-169
34780781-7	2022	Our research demonstrates the mechanism by which the disulfide bonds contribute to the molecular structure of the RBD of the Spike protein, allowing the RBD to execute its viral function.	Disulfides	53-62	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	125-130
9352906-0	1997	Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.	Disulfides	29-38	putative protein DsbC	Escherichia coli	55-59
17145752-5	2007	We show here that proMBP detaches surface-bound PAPP-A in a process that depends on the proMBP GAG and also on the formation of intermolecular disulfide bonds between PAPP-A and proMBP.	Disulfides	143-152	pappalysin 1	Homo sapiens	48-54
9352906-2	1997	For DsbC to attack incorrectly formed disulfide bonds in substrate proteins, its two active-site cysteines should be in the reduced form.	Disulfides	38-47	putative protein DsbC	Escherichia coli	4-8
17145752-5	2007	We show here that proMBP detaches surface-bound PAPP-A in a process that depends on the proMBP GAG and also on the formation of intermolecular disulfide bonds between PAPP-A and proMBP.	Disulfides	143-152	pappalysin 1	Homo sapiens	167-173
9352906-7	1997	The redox state of the active-site cysteines of DsbC correlates quite closely with its ability to assist in the folding of proteins with multiple disulfide bonds.	Disulfides	146-155	putative protein DsbC	Escherichia coli	48-52
17041908-8	2007	We postulate that presentation of charged, hydrogen bonding and hydrophobic structural elements within the disulfide-constrained peptide drives IL5Ralpha recruitment by AF17121.	Disulfides	107-116	interleukin 5 receptor subunit alpha	Homo sapiens	144-153
9315864-9	1997	The structural analysis of the intermediates formed during the refolding of RNase A showed for the first time that Grx is actually able to catalyze both formation and reduction of mixed disulfides involving glutatione.	Disulfides	186-196	ribonuclease A family member 1, pancreatic	Homo sapiens	76-83
34975921-6	2021	Combined with mutagenesis assays, the residue Cys20 of ORF8 is responsible for forming the covalent disulfide-linked dimer in crystal packing and in vitro biochemical conditions.	Disulfides	100-109	ORF8 protein	Severe acute respiratory syndrome coronavirus 2	55-59
17376729-2	2007	The most common mutation, C282Y, disrupts the disulfide bond necessary for the association of HFE with beta-2-microglobulin and abrogates cell surface HFE expression.	Disulfides	46-55	beta-2 microglobulin	Mus musculus	103-123
34910441-1	2021	BACKGROUND: The aim of this study is to investigate the correlation between serum meteorin-like protein levels and thiol/disulfide balance in patients with COVID-19.	Disulfides	121-130	meteorin like, glial cell differentiation regulator	Homo sapiens	82-103
9315864-9	1997	The structural analysis of the intermediates formed during the refolding of RNase A showed for the first time that Grx is actually able to catalyze both formation and reduction of mixed disulfides involving glutatione.	Disulfides	186-196	glutaredoxin	Homo sapiens	115-118
9315864-16	1997	Present data suggest that the synergistic effect can be explained assuming that Grx actually facilitates PDI action by catalyzing formation or reduction of mixed disulfides.	Disulfides	162-172	glutaredoxin	Homo sapiens	80-83
9315864-16	1997	Present data suggest that the synergistic effect can be explained assuming that Grx actually facilitates PDI action by catalyzing formation or reduction of mixed disulfides.	Disulfides	162-172	prolyl 4-hydroxylase subunit beta	Homo sapiens	105-108
9315864-17	1997	The mixed disulfides are then rapidly converted into intramolecular disulfides in the presence of PDI.	Disulfides	10-20	prolyl 4-hydroxylase subunit beta	Homo sapiens	98-101
9315864-17	1997	The mixed disulfides are then rapidly converted into intramolecular disulfides in the presence of PDI.	Disulfides	68-78	prolyl 4-hydroxylase subunit beta	Homo sapiens	98-101
17365173-0	2007	The Sep15 protein family: roles in disulfide bond formation and quality control in the endoplasmic reticulum.	Disulfides	35-44	selenoprotein F	Homo sapiens	4-9
9399568-1	1997	TGF-alpha, a 50 amino acid growth factor containing 3 disulfide bonds, was fused to the N-terminal domain of the pIII protein of fusN, a derivative of phagemid fd-tet, to form a TGF-alpha phage.	Disulfides	54-63	transforming growth factor alpha	Homo sapiens	0-9
34538222-8	2021	Importantly, vaccination with peptide 446-480 or with a cyclic version of peptide 446-488 containing a disulfide bridge between cysteines 480 and 488, protected humanized K18-hACE2 mice from a lethal dose of SARS-CoV-2 (62.5 and 75% of protection; P<0.01 and P<0.001, respectively).	Disulfides	103-112	angiotensin converting enzyme 2	Homo sapiens	175-180
34830487-0	2021	Disulfide Dimerization of Neuronal Calcium Sensor-1: Implications for Zinc and Redox Signaling.	Disulfides	0-9	neuronal calcium sensor 1	Homo sapiens	26-51
34830487-3	2021	Here, with the use of cellular models and various biophysical and computational techniques, we demonstrate that NCS-1 is a redox-sensitive protein, which responds to oxidizing conditions by the formation of disulfide dimer (dNCS-1), involving its single, highly conservative cysteine C38.	Disulfides	207-216	neuronal calcium sensor 1	Homo sapiens	112-117
34791819-4	2021	Our explanation for this behavior is that, when BST2 gets in contact with Zn bound to the orf7a Cys15 ligand, it has the ability of displacing the metal owing to the creation of a new disulfide bridge across the two proteins.	Disulfides	184-193	ORF7a protein	Severe acute respiratory syndrome coronavirus 2	90-95
9325143-2	1997	Human interleukin-5 is a disulfide-linked homodimeric cytokine implicated in asthmatic response.	Disulfides	25-34	interleukin 5	Homo sapiens	6-19
9315698-4	1997	Mutation of the last three residues of the hBNP disulfide ring, G23F/L24W/G25R, resulted in about 9-fold improved selectivity.	Disulfides	48-57	natriuretic peptide B	Homo sapiens	43-47
17365173-4	2007	Recently, a selenocysteine-containing oxidoreductase, Sep15, has been implicated in disulfide bond assisted protein folding, and a role in quality control for this selenoprotein has been proposed.	Disulfides	84-93	selenoprotein F	Homo sapiens	54-59
9288781-3	1997	ANI-E peptide was derived from the phage clone, which binds to angiogenin via the disulfide-constrained octapeptide epitope that is displayed on its surface, and is displaced by actin.	Disulfides	82-91	angiogenin	Homo sapiens	63-73
9288781-4	1997	Disulfide-constrained ANI-E peptide inhibits the interaction of angiogenin with actin, which is regarded as the angiogenin-binding protein on the surface of endothelial cells, without any visible effect on the ribonucleolytic activity of angiogenin.	Disulfides	0-9	angiogenin	Homo sapiens	64-74
17518268-1	2007	Phenoxodiol, a synthetic isoflavene with clinical efficacy in the management of ovarian and other forms of human cancer, blocked the activity of a cancer-specific and growth-related cell surface ECTO-NOX protein with both oxidative (hydroquinone) and protein disulfide-thiol interchange activity designated tNOX.	Disulfides	259-268	tripartite motif-containing 33	Mus musculus	195-199
9288781-4	1997	Disulfide-constrained ANI-E peptide inhibits the interaction of angiogenin with actin, which is regarded as the angiogenin-binding protein on the surface of endothelial cells, without any visible effect on the ribonucleolytic activity of angiogenin.	Disulfides	0-9	angiogenin	Homo sapiens	112-122
9288781-4	1997	Disulfide-constrained ANI-E peptide inhibits the interaction of angiogenin with actin, which is regarded as the angiogenin-binding protein on the surface of endothelial cells, without any visible effect on the ribonucleolytic activity of angiogenin.	Disulfides	0-9	angiogenin	Homo sapiens	112-122
34771233-10	2021	Moreover, the terminal thiol end-functionality in the (PNVCL-SH)6 star polymers was linked via disulfide bond formation to l-cysteine to further demonstrate its reactivity.	Disulfides	95-104	steroidogenic acute regulatory protein	Homo sapiens	66-70
34664930-3	2021	Cytotoxic ribonuclease A (RNase A) was effectively caged in the matrix of disulfide-hybridized silica NPs (encapsulation efficiency of ~64%), which were further functionalized with cancer targeting capability via surface imprinting with SA as imprinting template.	Disulfides	74-83	ribonuclease A family member 1, pancreatic	Homo sapiens	26-33
17518268-5	2007	Both the oxidative and protein disulfide-thiol interchange activities that alternate to generate the complex set of oscillations with a period length of 22 min (24 min for the constitutive counterpart CNOX) that characterize ECTO-NOX proteins respond to phenoxodiol.	Disulfides	31-40	ecto-NOX disulfide-thiol exchanger 1	Mus musculus	201-205
9256258-6	1997	Tetranectin has three intramolecular disulfide bridges.	Disulfides	37-46	C-type lectin domain family 3 member B	Homo sapiens	0-11
17518268-5	2007	Both the oxidative and protein disulfide-thiol interchange activities that alternate to generate the complex set of oscillations with a period length of 22 min (24 min for the constitutive counterpart CNOX) that characterize ECTO-NOX proteins respond to phenoxodiol.	Disulfides	31-40	tripartite motif-containing 33	Mus musculus	225-229
9256258-9	1997	In tetranectin, the third disulfide bridge tethers the CRD to the long helix in the coiled coil.	Disulfides	26-35	C-type lectin domain family 3 member B	Homo sapiens	3-14
17136616-5	2007	The disulfide bond locations are conserved among human MBP1, MBP2 and C-type lectins.	Disulfides	4-13	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	55-59
34619770-2	2022	To date, only 6 variants causing PT-VWD have been described, 5 in the C-terminal disulfide loop of the VWF-binding domain of GPIbalpha and 1 in the macroglycopeptide.	Disulfides	81-90	von Willebrand factor	Cricetulus griseus	103-106
16935843-9	2006	Additional investigations of the structure of Insl6 protein provided evidence for posttranslational modifications of Insl6, including the presence of disulfide bonds, glycosylation, and ubiquitination.	Disulfides	150-159	insulin-like peptide INSL6	Cricetulus griseus	46-51
34619770-9	2022	Our data demonstrate for the first time that GoF variants outside the GPIbalpha C-terminal disulfide loop may be pathogenic and that aminoacidic changes in the LRR may cause allosterically conformational changes in the C-terminal disulfide loop of GPIbalpha inducing a conformation with high affinity for VWF.	Disulfides	91-100	von Willebrand factor	Cricetulus griseus	305-308
34619770-9	2022	Our data demonstrate for the first time that GoF variants outside the GPIbalpha C-terminal disulfide loop may be pathogenic and that aminoacidic changes in the LRR may cause allosterically conformational changes in the C-terminal disulfide loop of GPIbalpha inducing a conformation with high affinity for VWF.	Disulfides	230-239	von Willebrand factor	Cricetulus griseus	305-308
9211880-9	1997	The formation and disruption of disulfide bonds involving these cysteine residues may be a mechanism by which EP24.15 activity is regulated through changes in intra- and extracellular redox potential.	Disulfides	32-41	thimet oligopeptidase 1	Homo sapiens	110-117
17055437-3	2006	Here, we identify protein disulfide isomerase (PDI), an enzyme critical to the formation of correct disulfide bonds in proteins, as a component of the peptide-loading complex.	Disulfides	26-35	prolyl 4-hydroxylase subunit beta	Homo sapiens	47-50
9202220-0	1997	An intramolecular disulfide bond between conserved extracellular cysteines in the gonadotropin-releasing hormone receptor is essential for binding and activation.	Disulfides	18-27	gonadotropin releasing hormone receptor	Homo sapiens	82-121
34760179-3	2021	The grand principles of supramolecular chemistry, that is the pH dependence of dynamic covalent disulfide exchange with known thiols on the transferrin receptor, are proposed to account for transcytosis into deep tissue, while the known but elusive exchange cascades along the same or other partners assure cytosolic delivery in kinetic competition.	Disulfides	96-105	transferrin receptor	Homo sapiens	140-160
17055437-4	2006	We show that PDI stabilizes a peptide-receptive site by regulating the oxidation state of the disulfide bond in the MHC peptide-binding groove, a function that is essential for selecting optimal peptides.	Disulfides	94-103	prolyl 4-hydroxylase subunit beta	Homo sapiens	13-16
34600560-4	2021	METHODS: We prepared atovaquone-loaded human serum albumin (HSA) nanoparticles stabilized by intramolecular disulfide bonds, termed HSA-ATO NPs.	Disulfides	108-117	albumin	Mus musculus	45-58
9192627-4	1997	Both IL-5 isomers folded into stable monomers in solution as shown by sedimentation equilibrium and CD and formed an intrachain disulfide bond predicted from the structure of wild type IL-5.	Disulfides	128-137	interleukin 5	Homo sapiens	5-9
9192627-4	1997	Both IL-5 isomers folded into stable monomers in solution as shown by sedimentation equilibrium and CD and formed an intrachain disulfide bond predicted from the structure of wild type IL-5.	Disulfides	128-137	interleukin 5	Homo sapiens	185-189
9220401-3	1997	Using recombinant Tat in which cysteine residues were blocked by sulfitolysis to prevent disulfide aggregation (S-Tat) we were unable to observe this phenomenon, possibly because of improper protein folding.	Disulfides	89-98	tyrosine aminotransferase	Homo sapiens	18-21
34667943-1	2021	A flavin-dependent enzyme quiescin Q6 sulfhydryl oxidase 1 (QSOX1) catalyzes the oxidation of thiol groups into disulfide bonds.	Disulfides	112-121	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	26-58
34667943-1	2021	A flavin-dependent enzyme quiescin Q6 sulfhydryl oxidase 1 (QSOX1) catalyzes the oxidation of thiol groups into disulfide bonds.	Disulfides	112-121	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	60-65
16930550-3	2006	Four of the proteins were found to belong to the Kazal protease inhibitor family and were named SPINK8, SPINK10, SPINK11, and SPINK12, whereas one of the proteins, WFDC10, contained the WAP four-disulfide core domain structure.	Disulfides	195-204	serine peptidase inhibitor, Kazal type 11	Mus musculus	113-120
34174476-5	2021	The mature CG42782, Met75C and Acp54A1 peptides each have a cyclic structure formed by a disulfide bond, which will reduce conformational freedom and enhance metabolic stability.	Disulfides	89-98	uncharacterized protein	Drosophila melanogaster	11-18
9144160-6	1997	A probable explanation is that MAO-generated H2O2 oxidizes glutathione to glutathione disulfide (GSSG), which undergoes thiol-disulfide interchange to form protein mixed disulfides, thereby interfering reversibly with thiol-dependent enzymatic function.	Disulfides	86-95	monoamine oxidase A	Rattus norvegicus	31-34
9223229-1	1997	The B cell antigen receptor, (BCR) comprises surface immunoglobulin and disulfide-bonded heterodimer of Ig-alpha and Ig-beta chains, which are the products of the mb-1 and B29 genes, respectively.	Disulfides	72-81	BCR activator of RhoGEF and GTPase	Bos taurus	4-34
16737954-6	2006	They recruit calnexin to monitor their productive folding pathway characterized by the post-translational formation of buried disulfides.	Disulfides	126-136	calnexin	Homo sapiens	13-21
9223229-1	1997	The B cell antigen receptor, (BCR) comprises surface immunoglobulin and disulfide-bonded heterodimer of Ig-alpha and Ig-beta chains, which are the products of the mb-1 and B29 genes, respectively.	Disulfides	72-81	CD79a molecule	Bos taurus	104-112
9223229-1	1997	The B cell antigen receptor, (BCR) comprises surface immunoglobulin and disulfide-bonded heterodimer of Ig-alpha and Ig-beta chains, which are the products of the mb-1 and B29 genes, respectively.	Disulfides	72-81	CD79a molecule	Bos taurus	163-167
9111002-5	1997	The elastase-induced fragmentation of apo(a) was the same whether free or as a member of Lp(a), indicating that the disulfide bond between apo(a) and the apoB100 component of Lp(a) did not hinder the elastase action.	Disulfides	116-125	lipoprotein(a)	Homo sapiens	175-180
9111002-6	1997	Lp(a) fragments containing kringle IV-9 retained the linkage to apoB100 via the disulfide bond, forming mini-Lp(a) particles in which the size of apo(a) varied according to the size of the fragments produced by the elastase digestion.	Disulfides	80-89	lipoprotein(a)	Homo sapiens	0-5
34062155-8	2021	Using a yeast torsinA expression system, we demonstrate that a specific protein disulfide isomerase, Pdi1, affects the folding and N-linked glycosylation of torsinA and torsinA E in a redox-dependent manner, suggesting that the acquisition of early torsinA folding intermediates is sensitive to perturbed interactions between Cys residues and the quality control machinery.	Disulfides	80-89	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	101-105
34098868-3	2021	HMGB1 contains three conserved redox-sensitive cysteine residues: cysteines in position 23 and 45 (C23 and C45) can form an intramolecular disulfide bond, whereas C106 is unpaired and is essential for the interaction with Toll-Like Receptor (TLR) 4.	Disulfides	139-148	high mobility group box 1	Mus musculus	0-5
34098868-8	2021	Mild oxidation forming a C23-C45 disulfide bond, while leaving C106 with a thiol group, was required for HMGB1 to induce phosphorylated NF-KB p65 subunit and TNF-alpha production.	Disulfides	33-42	high mobility group box 1	Mus musculus	105-110
34098868-9	2021	The importance of a C23-C45 disulfide bond was confirmed by mutation of C45 to C45A HMGB1, which abolished the ability for cytokine induction.	Disulfides	28-37	high mobility group box 1	Mus musculus	84-89
16846241-5	2006	Inactivation of glutaredoxin required the reduced (dithiol) form of the enzyme, the oxidized (intramolecular disulfide) form of sporidesmin, and molecular oxygen.	Disulfides	109-118	glutaredoxin	Homo sapiens	16-28
34098868-10	2021	Further oxidation of the disulfide isoform also inactivated HMGB1.	Disulfides	25-34	high mobility group box 1	Mus musculus	60-65
9125178-1	1997	Apolipoprotein A-IMilano is a molecular variant of apoA-I, containing the Arg173--&gt;Cys substitution that forms a disulfide linked homodimer (A-IM/A-IM).	Disulfides	116-125	lipoprotein(a)	Homo sapiens	0-16
16846241-6	2006	The inactivated glutaredoxin could be reactivated by dithiothreitol only in the presence of urea, followed by removal of the denaturant, indicating that inactivation of the enzyme involves a conformationally inaccessible disulfide bond(s).	Disulfides	221-230	glutaredoxin	Homo sapiens	16-28
16846241-9	2006	Mass spectrometry of the modified protein is consistent with formation of intermolecular disulfides, containing one adducted toxin per glutaredoxin but with elimination of two sulfur atoms from the detected product.	Disulfides	89-99	glutaredoxin	Homo sapiens	135-147
9056493-4	1997	These studies suggest that the soluble truncated form of human CA IV expressed in E. coli, which is disulfide-bonded zinc metalloenzyme, can provide a useful model enzyme for studies of protein folding and enzyme activation in vitro.	Disulfides	100-109	carbonic anhydrase 4	Homo sapiens	63-68
9056493-5	1997	Furthermore, the procedure described for recovery of CA IV following expression in E. coli may be useful for in vitro activation and subsequent purification of other disulfide-containing proteins.	Disulfides	166-175	carbonic anhydrase 4	Homo sapiens	53-58
34004056-0	2021	Disruption of disulfides within RBD of SARS-CoV-2 spike protein prevents fusion and represents a target for viral entry inhibition by registered drugs.	Disulfides	14-24	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	50-55
16507315-1	2006	Cell-surface protein disulfide isomerase (PDI) has been proposed to promote disulfide bond rearrangements in HIV-1 envelope protein (Env) that accompany Env-mediated fusion.	Disulfides	21-30	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	133-136
16507315-1	2006	Cell-surface protein disulfide isomerase (PDI) has been proposed to promote disulfide bond rearrangements in HIV-1 envelope protein (Env) that accompany Env-mediated fusion.	Disulfides	21-30	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	153-156
16507315-6	2006	We found that the ability of thioredoxin to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 Env gp120 and that thioredoxin also reduces disulfide bonds in gp120 directly in the absence of CD4.	Disulfides	55-64	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	114-117
16507315-6	2006	We found that the ability of thioredoxin to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 Env gp120 and that thioredoxin also reduces disulfide bonds in gp120 directly in the absence of CD4.	Disulfides	55-64	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	118-123
34071205-0	2021	Therapeutic Targeting of Protein Disulfide Isomerase PDIA1 in Multiple Myeloma.	Disulfides	33-42	prolyl 4-hydroxylase subunit beta	Homo sapiens	53-58
34071205-2	2021	The endoplasmic reticulum (ER) resident protein disulfide isomerase, PDIA1 is indispensable for maintaining structural integrity of cysteine-rich antibodies and cytokines that require accurate intramolecular disulfide bond arrangement.	Disulfides	48-57	prolyl 4-hydroxylase subunit beta	Homo sapiens	69-74
34071205-2	2021	The endoplasmic reticulum (ER) resident protein disulfide isomerase, PDIA1 is indispensable for maintaining structural integrity of cysteine-rich antibodies and cytokines that require accurate intramolecular disulfide bond arrangement.	Disulfides	208-217	prolyl 4-hydroxylase subunit beta	Homo sapiens	69-74
34142531-2	2021	Based on the structure of the complex of the protein S receptor-binding domain (RBD) and ACE2, the design of chimeric molecules consisting of two 22-23-mer peptides linked to each other by disulfide bonds was carried out.	Disulfides	189-198	angiotensin converting enzyme 2	Homo sapiens	89-93
9063871-1	1997	This paper reports a detailed conformational analysis by 1H NMR (DMSO-d6, 300 K) and molecular modeling of the octapeptide D-Phe1-Cys2-Phe3-D-Trp4-Lys5-Thr6-Cys7+ ++-Thr8-ol (disulfide bridged) known as sandostatin (or SMS 201-995 or octreotide) with both somatostatin-like and opioid-like bioactivities.	Disulfides	175-184	dihydrolipoamide dehydrogenase	Homo sapiens	135-139
9119370-5	1997	Since the bacterially expressed protein of nucleoredoxin showed oxidoreductase activity of the insulin disulfide bonds with kinetics similar to that of thioredoxin, it may be a redox regulator of the nuclear proteins, such as transcription factors.	Disulfides	103-112	nucleoredoxin	Homo sapiens	43-56
9023204-4	1997	Two-dimensional gel electrophoresis identified one complex as a heterodimer of VirB9 and VirB7 covalently linked by a disulfide bond, as well as VirB7 homodimers and monomers.	Disulfides	118-127	type IV secretion system protein VirB9	Agrobacterium tumefaciens	79-84
9023204-4	1997	Two-dimensional gel electrophoresis identified one complex as a heterodimer of VirB9 and VirB7 covalently linked by a disulfide bond, as well as VirB7 homodimers and monomers.	Disulfides	118-127	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	89-94
16828895-6	2006	CCS also oxidizes an intrasubunit disulfide in SOD1.	Disulfides	34-43	copper chaperone for superoxide dismutase	Homo sapiens	0-3
16777100-4	2006	Two cysteine residues (Cys67 and Cys73) within the characteristic 12 amino acids loop form a disulfide bond, contributing to the structural stability of cytochrome c(6A).	Disulfides	93-102	Cytochrome c	Arabidopsis thaliana	153-165
9013867-8	1997	Various mixed disulfide intermediates (CTX-A1-S-S-CTX-A1; PDI-S-S-A2; PDI-S-S-A1) appear during CTX-A reduction.	Disulfides	14-23	prolyl 4-hydroxylase subunit beta	Homo sapiens	58-61
9013867-8	1997	Various mixed disulfide intermediates (CTX-A1-S-S-CTX-A1; PDI-S-S-A2; PDI-S-S-A1) appear during CTX-A reduction.	Disulfides	14-23	prolyl 4-hydroxylase subunit beta	Homo sapiens	70-73
35636191-4	2022	In addition, phosphorylation pretreatment enhanced hydrophobic interactions and disulfide bond formation between TGase-induced WG gels, thus leading to a more homogeneous and dense three-dimensional network structure of gel, which was confirmed by SEM micrographs.	Disulfides	80-89	transglutaminase 1	Homo sapiens	113-118
23045137-1	2006	Proteins contain free, exposed thiols that can be glutathionylated in the native state as a result of thiol-disulfide exchange reactions with glutathione disulfide, catalyzed by glutaredoxin.	Disulfides	108-117	glutaredoxin	Homo sapiens	178-190
35367810-6	2022	Monte Carlo simulations illustrate how disulfides and S-thiolations on these cysteines increase the dynamics of the protein at physiological forces, while enabling load- and isoform-dependent regulation of titin stiffness.	Disulfides	39-49	titin	Homo sapiens	206-211
9143695-1	1997	The pre-T cell receptor (pre-TCR) that minimally consists of the TCR beta chain and the disulfide-linked pre-T cell receptor alpha (pT alpha) chain in association with signal-transducing CD3 molecules rescues from programmed cell death cells with productive TCR beta rearrangements.	Disulfides	88-97	pre T cell antigen receptor alpha	Mus musculus	132-140
9143695-1	1997	The pre-T cell receptor (pre-TCR) that minimally consists of the TCR beta chain and the disulfide-linked pre-T cell receptor alpha (pT alpha) chain in association with signal-transducing CD3 molecules rescues from programmed cell death cells with productive TCR beta rearrangements.	Disulfides	88-97	CD3 antigen, epsilon polypeptide	Mus musculus	187-190
16633351-2	2006	We show that native disulfides in human interferon alpha-2b and in a fragment of an antibody to CD4(+) can be modified by site-specific bisalkylation of the two cysteine sulfur atoms to form a three-carbon PEGylated bridge.	Disulfides	20-30	interferon alpha 2	Homo sapiens	40-59
8977443-10	1996	This mutation occurs within a disulfide loop of protein S that is believed to be responsible for binding to C4b binding protein and may result in greater affinity between protein S and C4b, consequently leading to thrombotic disease.	Disulfides	30-39	complement C4B (Chido blood group)	Homo sapiens	108-111
8977462-9	1996	In summary, the results of our study indicate that apo(a) kringle IV types 7 and 8 are required for maximal efficiency of Lp(a) formation, likely by virtue of their ability to mediate lysine-dependent non-covalent interactions with apoB-100 that precede disulfide bond formation.	Disulfides	254-263	lipoprotein(a)	Homo sapiens	122-127
35549281-4	2022	Here, we use single-molecule spectroscopy AFM and molecular dynamics simulations to capture both intra- and intermolecular disulfide bonds in gammaD-crystallin, a cysteine-rich, structural human lens protein involved in age-related eye cataracts.	Disulfides	123-132	crystallin gamma D	Homo sapiens	142-159
16675266-1	2006	NKG2D is a type II transmembrane-anchored glycoprotein expressed as a disulfide-linked homodimer on the surface of all mouse and human natural killer cells (NK cells).	Disulfides	70-79	killer cell lectin like receptor K1	Homo sapiens	0-5
35628668-4	2022	NKG2C+ subsets were preferentially expanded by a feeder cell line engineered to express an artificial disulfide-stabilized trimeric HLA-E ligand (HLA-E*spG).	Disulfides	102-111	major histocompatibility complex, class I, E	Homo sapiens	132-137
35628668-4	2022	NKG2C+ subsets were preferentially expanded by a feeder cell line engineered to express an artificial disulfide-stabilized trimeric HLA-E ligand (HLA-E*spG).	Disulfides	102-111	major histocompatibility complex, class I, E	Homo sapiens	146-151
35606080-3	2022	The major structural difference between Lp(a) and LDL is that Lp(a) has a second large protein, apolipoprotein (a) (apo(a)), bound to the apolipoprotein B100 moiety of an LDL sized particle by a single disulfide bond.	Disulfides	202-211	lipoprotein(a)	Homo sapiens	40-45
35606080-3	2022	The major structural difference between Lp(a) and LDL is that Lp(a) has a second large protein, apolipoprotein (a) (apo(a)), bound to the apolipoprotein B100 moiety of an LDL sized particle by a single disulfide bond.	Disulfides	202-211	lipoprotein(a)	Homo sapiens	62-67
35606080-3	2022	The major structural difference between Lp(a) and LDL is that Lp(a) has a second large protein, apolipoprotein (a) (apo(a)), bound to the apolipoprotein B100 moiety of an LDL sized particle by a single disulfide bond.	Disulfides	202-211	lipoprotein(a)	Homo sapiens	96-114
8931546-4	1996	This thiolate anion is stabilized by 5.7 kcal/mol in the dithiol form, giving rise to the corresponding instability of the disulfide bond and the oxidizing properties of PDI a.	Disulfides	123-132	prolyl 4-hydroxylase subunit beta	Homo sapiens	170-175
8950484-1	1996	Ricin toxin, the heterodimeric 65 kDa glycoprotein synthesized in castor bean seeds, contains a cell binding lectin subunit (RTB) disulfide linked to an RNA N-glycosidase protein synthesis-inactivating subunit (RTA).	Disulfides	130-139	RNA binding fox-1 homolog 2	Homo sapiens	211-214
8885843-0	1996	Glutathione-dependent pathways of refolding of RNase T1 by oxidation and disulfide isomerization: catalysis by protein disulfide isomerase.	Disulfides	73-82	prolyl 4-hydroxylase subunit beta	Homo sapiens	111-138
35606080-3	2022	The major structural difference between Lp(a) and LDL is that Lp(a) has a second large protein, apolipoprotein (a) (apo(a)), bound to the apolipoprotein B100 moiety of an LDL sized particle by a single disulfide bond.	Disulfides	202-211	lipoprotein(a)	Homo sapiens	116-122
35078862-2	2022	STC2 is a disulfide-linked homodimeric secreted glycoprotein that plays role in various physiological processes including cell metabolism, inflammation, endoplasmic reticulum and oxidative stress, calcium regulation, cell proliferation and apoptosis.	Disulfides	10-19	stanniocalcin 2	Mus musculus	0-4
16626818-1	2006	An insertion of residues in the third extracellular loop and a disulfide bond linking this loop to the N-terminal domain were identified in a structural model of a G-protein coupled receptor specific to angiotensin II (AT1 receptor), built in homology to the seven-transmembrane-helix bundle of rhodopsin.	Disulfides	63-72	angiotensin II receptor type 1	Homo sapiens	219-222
35192131-5	2022	We found that interaction between rP2 and RNA molecules interfered with the dynamics of rP2 dimers formation, involved in disulfide bonds and/or postranslational alterations in distinct stage of SDS-stable dimers formation.	Disulfides	122-131	macrophage expressed 1	Rattus norvegicus	34-37
8905463-6	1996	Quantification experiments with disulfide-reducing agent, mixtures of CSF and urine as well as frozen and stored CSF samples indicated parallelism between the precipitate-forming immunologic reactions of apo D in different sample matrices when performed with ZIA.	Disulfides	32-41	apolipoprotein D	Homo sapiens	204-209
16626818-3	2006	It was postulated that the insertion and the disulfide bond, also found in other receptors such as those for bradykinin, endothelin, purine and other ligands, might play a role in regulating the function of the AT1 receptor.	Disulfides	45-54	angiotensin II receptor type 1	Homo sapiens	211-214
35192131-5	2022	We found that interaction between rP2 and RNA molecules interfered with the dynamics of rP2 dimers formation, involved in disulfide bonds and/or postranslational alterations in distinct stage of SDS-stable dimers formation.	Disulfides	122-131	macrophage expressed 1	Rattus norvegicus	88-91
16771671-2	2006	In the major pathway, the membrane-associated flavoprotein Ero1 generates disulfide bonds for transfer to protein disulfide isomerase (PDI), which is responsible for directly introducing disulfide bonds into secretory proteins.	Disulfides	74-83	prolyl 4-hydroxylase subunit beta	Homo sapiens	135-138
8809084-0	1996	Carbonic anhydrase IV: purification of a secretory form of the recombinant human enzyme and identification of the positions and importance of its disulfide bonds.	Disulfides	146-155	carbonic anhydrase 4	Homo sapiens	0-21
16771671-2	2006	In the major pathway, the membrane-associated flavoprotein Ero1 generates disulfide bonds for transfer to protein disulfide isomerase (PDI), which is responsible for directly introducing disulfide bonds into secretory proteins.	Disulfides	114-123	prolyl 4-hydroxylase subunit beta	Homo sapiens	135-138
16771671-3	2006	In a minor fungal-specific protein oxidation pathway, the membrane-associated flavoprotein Erv2 can catalyze disulfide bond formation via the transfer of oxidizing equivalents to PDI.	Disulfides	109-118	prolyl 4-hydroxylase subunit beta	Homo sapiens	179-182
8809084-4	1996	Occasional CA IV preparations contained proteolytic fragments of 18 and 15 kDa held together by disulfide bonds.	Disulfides	96-105	carbonic anhydrase 4	Homo sapiens	11-16
16618117-2	2006	It contains three subunits (C8alpha, C8beta, C8gamma) arranged as a disulfide-linked C8alpha-gamma dimer that is noncovalently associated with C8beta.	Disulfides	68-77	complement C8 beta chain	Homo sapiens	37-43
8798403-8	1996	Oxidation of Ng by the various oxidants apparently resulted in the formation of intramolecular disulfide bond(s) as judged by a reduction of apparent Mr on SDS-polyacrylamide gel electrophoresis; this oxidized form, unlike the reduced form, did not bind to CaM-affinity column.	Disulfides	95-104	calmodulin 1	Rattus norvegicus	257-260
35163624-0	2022	A Multi-Disulfide Receptor-Binding Domain (RBD) of the SARS-CoV-2 Spike Protein Expressed in E. coli Using a SEP-Tag Produces Antisera Interacting with the Mammalian Cell Expressed Spike (S1) Protein.	Disulfides	8-17	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	66-71
35163624-0	2022	A Multi-Disulfide Receptor-Binding Domain (RBD) of the SARS-CoV-2 Spike Protein Expressed in E. coli Using a SEP-Tag Produces Antisera Interacting with the Mammalian Cell Expressed Spike (S1) Protein.	Disulfides	8-17	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	181-186
35123263-0	2022	The function of SARS-CoV-2 spike protein is impaired by disulfide-bond disruption with mutation at cysteine-488 and by thiol-reactive N-acetyl-cysteine and glutathione.	Disulfides	56-65	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	27-32
35123263-3	2022	The cysteine residue at position 488, consisting of a disulfide bridge with cysteine 480 is located in an important structural loop at ACE2-binding surface of RBD, and is highly conserved among SARS-related coronaviruses.	Disulfides	54-63	angiotensin converting enzyme 2	Homo sapiens	135-139
16618117-2	2006	It contains three subunits (C8alpha, C8beta, C8gamma) arranged as a disulfide-linked C8alpha-gamma dimer that is noncovalently associated with C8beta.	Disulfides	68-77	complement C8 beta chain	Homo sapiens	143-149
34609517-6	2022	PDI-L members AtPDI2/5/6 mainly serve as an isomerase, while PDI-M/S members AtPDI9/10/11 are more efficient in accepting oxidizing equivalents from AtERO1 and catalyzing disulfide bond formation.	Disulfides	171-180	protein disulfide isomerase	Arabidopsis thaliana	61-64
8930128-1	1996	Modification of protein thiol by mixed disulfide formation with low molecular weight cellular thiols has been proposed as one of the post-translational modifications of amino acid side chains and is known to be catalyzed by thioltransferase.	Disulfides	39-48	glutaredoxin	Homo sapiens	224-240
16686937-0	2006	The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase.	Disulfides	25-34	Acetylcholine esterase	Drosophila melanogaster	85-105
34609517-6	2022	PDI-L members AtPDI2/5/6 mainly serve as an isomerase, while PDI-M/S members AtPDI9/10/11 are more efficient in accepting oxidizing equivalents from AtERO1 and catalyzing disulfide bond formation.	Disulfides	171-180	PDI-like 2-3	Arabidopsis thaliana	77-89
34609517-7	2022	Accordingly, the pdi9/10/11 triple mutant exhibited much stronger inhibition than pdi1/2/5/6 quadruple mutant under dithiothreitol treatment, which caused disruption of disulfide bonds in plant proteins.	Disulfides	169-178	PDI-like 2-3	Arabidopsis thaliana	17-21
34609517-8	2022	Furthermore, AtPDI2/5 work synergistically with PDI-M/S members in relaying disulfide bonds from AtERO1 to substrates.	Disulfides	76-85	protein disulfide isomerase	Arabidopsis thaliana	48-51
16686937-4	2006	RESULTS: To create a disulfide bond that could increase the stability of the Drosophila melanogaster acetylcholinesterase, we selected seven positions taking into account first the distance between Cbeta of two residues, in which newly introduced cysteines will form the new disulfide bond and second the conservation of the residues in the cholinesterase family.	Disulfides	21-30	Acetylcholine esterase	Drosophila melanogaster	101-121
8902616-5	1996	A mutant PDI (hPDIM), which has no thiol-disulfide exchange activity, suppressed the reductive cleavage of the mixed disulfide of C77A-a with hPDI, suggesting that hPDI non-covalently interacted with the substrates.	Disulfides	117-126	prolyl 4-hydroxylase subunit beta	Homo sapiens	9-12
8902616-5	1996	A mutant PDI (hPDIM), which has no thiol-disulfide exchange activity, suppressed the reductive cleavage of the mixed disulfide of C77A-a with hPDI, suggesting that hPDI non-covalently interacted with the substrates.	Disulfides	117-126	prolyl 4-hydroxylase subunit beta	Homo sapiens	14-18
8902616-5	1996	A mutant PDI (hPDIM), which has no thiol-disulfide exchange activity, suppressed the reductive cleavage of the mixed disulfide of C77A-a with hPDI, suggesting that hPDI non-covalently interacted with the substrates.	Disulfides	117-126	prolyl 4-hydroxylase subunit beta	Homo sapiens	142-146
8902616-6	1996	Taking account of the results of the structural analysis, we conclude that one of the functions of PDI in vivo lies in relaxing the structure around the disulfide bond, as well as in exchanging the thiol-disulfide bonds.	Disulfides	153-162	prolyl 4-hydroxylase subunit beta	Homo sapiens	99-102
8902616-6	1996	Taking account of the results of the structural analysis, we conclude that one of the functions of PDI in vivo lies in relaxing the structure around the disulfide bond, as well as in exchanging the thiol-disulfide bonds.	Disulfides	204-213	prolyl 4-hydroxylase subunit beta	Homo sapiens	99-102
16686937-4	2006	RESULTS: To create a disulfide bond that could increase the stability of the Drosophila melanogaster acetylcholinesterase, we selected seven positions taking into account first the distance between Cbeta of two residues, in which newly introduced cysteines will form the new disulfide bond and second the conservation of the residues in the cholinesterase family.	Disulfides	21-30	Acetylcholine esterase	Drosophila melanogaster	107-121
8755505-8	1996	Taken together, these results support a model in which the formation of disulfide cross-linked VirB7 dimers represent critical early steps in the biogenesis of the T-complex transport apparatus.	Disulfides	72-81	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	95-100
16446016-1	2006	The two major membrane-associated proteins of porcine reproductive and respiratory syndrome virus (PRRSV), GP5 and M (encoded by ORF5 and ORF6 genes, respectively), are associated as disulfide-linked heterodimers (GP5/M) in the virus particle.	Disulfides	183-192	zinc finger, HIT domain containing 2	Mus musculus	138-142
8895095-10	1996	The proteins were expressed in Escherichia coli, purified from inclusion bodies, and were able to refold with the disulfide homodimeric topology typical of interleukin-5.	Disulfides	114-123	interleukin 5	Homo sapiens	156-169
16483732-6	2006	Due to this frameshift mutation, the putative proteins encoded by these sequences do not harbor the features of a usual WAP protein with two four-disulfide core domains.	Disulfides	146-155	whey acidic protein	Sus scrofa	120-123
8662837-3	1996	M-T2 secreted from virus-infected cells is detected as both a monomer and a disulfide-linked dimer, both of which were shown by Scatchard analysis to bind rabbit TNFalpha (Kd values of 170 pM and 195 pM, respectively), values that are comparable with the affinities of mammalian TNFs with their receptors.	Disulfides	76-85	M-T2	Myxoma virus	0-4
16387780-4	2006	NMR spectroscopy showed that the trans-azo and cis-azo isomer of the cyclic PDI peptide exhibit different, but well-defined structures when the two cystine residues form a disulfide bridge.	Disulfides	172-181	prolyl 4-hydroxylase subunit beta	Homo sapiens	76-79
16517741-6	2006	In multiple expression systems, 5-30% of MOPICE, SPICE, and VCP consisted of function-enhancing disulfide-linked homodimers.	Disulfides	96-105	valosin containing protein	Homo sapiens	60-63
16467570-3	2006	In addition, calnexin and calreticulin possess binding sites for ATP, Ca2+, non-native polypeptides and ERp57, an enzyme that catalyzes disulfide bond formation, reduction and isomerization.	Disulfides	136-145	calnexin	Homo sapiens	13-21
17379941-9	2006	A model has been developed whereby the plasma membrane AAA-ATPase is linked via disulfide bonds, formed and broken by the ECTO-NOX protein, to membrane structural proteins.	Disulfides	80-89	dynein axonemal heavy chain 8	Homo sapiens	59-65
8649415-7	1996	IL-3-induced receptor dimers were disulfide and nondisulfide linked and were dependent on IL-3 interacting with both IL-3R alpha and beta c.	Disulfides	34-43	interleukin 3 receptor subunit alpha	Homo sapiens	117-128
8649415-10	1996	Two-dimensional gel electrophoresis and Western blotting (immunoblotting) demonstrated the presence of both IL-3R alpha and beta c in the disulfide-linked complexes.	Disulfides	138-147	interleukin 3 receptor subunit alpha	Homo sapiens	108-119
8639587-0	1996	Nonrandom distribution of the one-disulfide intermediates in the regeneration of ribonuclease A.	Disulfides	34-43	ribonuclease A family member 1, pancreatic	Homo sapiens	81-95
8639587-1	1996	The one-disulfide intermediates formed during the oxidative refolding of ribonuclease A (RNase A) have been characterized.	Disulfides	8-17	ribonuclease A family member 1, pancreatic	Homo sapiens	73-87
8639587-1	1996	The one-disulfide intermediates formed during the oxidative refolding of ribonuclease A (RNase A) have been characterized.	Disulfides	8-17	ribonuclease A family member 1, pancreatic	Homo sapiens	89-96
16403016-6	2006	It is shown that chemical cleavage at aspartate residues in the protease resistant RNase A, followed by tryptic digestion can be optimized so that the rigid protein breaks up into MALDI-MS detectable fragments, leaving the disulfide bonds intact.	Disulfides	223-232	ribonuclease A family member 1, pancreatic	Homo sapiens	83-90
8626682-3	1996	Both I-1 and I-2 contain a native-like disulfide bond, Cys4-Cys89 and Cys43-Cys138, respectively, and I-3 forms a mispaired disulfide, Cys43-Cys89.	Disulfides	124-133	brain protein I3	Homo sapiens	102-105
8626682-6	1996	I-3 may serve as an intermediate for disulfide rearrangment between I-1 and I-2.	Disulfides	37-46	brain protein I3	Homo sapiens	0-3
17003517-3	2006	These include the molecular chaperones calnexin and calreticulin, which enhance the proper folding and subunit assembly of class I molecules and also retain assembly intermediates within the ER; ERp57, a thiol oxidoreductase that promotes heavy chain disulfide formation and proper assembly of the peptide loading complex; tapasin, which recruits class I molecules to the TAP peptide transporter and enhances the loading of high affinity peptide ligands; and Bap31, which is involved in clustering assembled class I molecules at ER exit sites for export along the secretory pathway.	Disulfides	251-260	calnexin	Homo sapiens	39-47
8626858-9	1996	The results show that part of extracellular human TG undergoes multimerization, primarily by the formation of intermolecular disulfide bonds, thus allowing the storage of TG at excessively high, previously unknown, concentrations.	Disulfides	125-134	thyroglobulin	Homo sapiens	50-52
16215261-7	2005	OPG is also a member of the TNF receptor superfamily and contains four disulfide-rich ligand-binding domains, yet lacks a transmembrane region separating the ligand-binding region from the two death domains, as observed for other receptor family members.	Disulfides	71-80	TNF receptor superfamily member 11b	Homo sapiens	0-3
8626858-9	1996	The results show that part of extracellular human TG undergoes multimerization, primarily by the formation of intermolecular disulfide bonds, thus allowing the storage of TG at excessively high, previously unknown, concentrations.	Disulfides	125-134	thyroglobulin	Homo sapiens	171-173
16331989-12	2005	However, the pH-dependent effects are larger for full-length IAPP than for the disulfide-truncated, acetylated analogue.	Disulfides	79-88	islet amyloid polypeptide	Homo sapiens	61-65
8611544-10	1996	Refolding of rPrP by oxidation to form a disulfide bond between the two Cys residues of this polypeptide produced a soluble protein with a high alpha-helical content similar to PrPC.	Disulfides	41-50	prion protein	Rattus norvegicus	13-17
8925908-5	1996	Distortion of the conformation of NGFRe by inhibition of disulfide formation did not promote O-glycosylation, whereas N-glycosylation was enhanced.	Disulfides	57-66	nerve growth factor receptor	Rattus norvegicus	34-39
16367905-1	2005	Breast cancer resistance protein (BCRP/ABCG2) is a half-molecule ATP-binding cassette transporter that we have previously suggested might function as a homodimer, bridged by disulfide bonds.	Disulfides	174-183	ATP binding cassette subfamily G member 2 (Junior blood group)	Mus musculus	34-38
8845753-2	1996	The structure presents: (1) an 8-residue insertion near the first disulfide (Cys 45-Cys 50, pepsin numbering) that results in a broad flap extending toward the active site; (2) a 7-residue deletion replacing helix hN2 (Ser 110-Tyr 114), which enlarges the S3 pocket; (3) a short polar connection between the two rigid body domains that alters their relative orientation and provides certain specificity; and (4) an ordered 11-residue addition at the carboxy terminus.	Disulfides	66-75	MT-RNR2 like 2 (pseudogene)	Homo sapiens	214-217
16367905-1	2005	Breast cancer resistance protein (BCRP/ABCG2) is a half-molecule ATP-binding cassette transporter that we have previously suggested might function as a homodimer, bridged by disulfide bonds.	Disulfides	174-183	ATP binding cassette subfamily G member 2 (Junior blood group)	Mus musculus	39-44
16262253-6	2005	We also found that the C-terminal penultimate selenocysteine was required for transfer of reducing equivalents from the thiol/disulfide active site of TGR to the glutaredoxin domain.	Disulfides	126-135	glutaredoxin	Homo sapiens	162-174
8838810-1	1996	Glutaredoxin is a small protein (12 kDa) catalyzing glutathione-dependent disulfide oxidoreduction reactions in a coupled system with NADPH, GSH, and glutathione reductase.	Disulfides	74-83	glutaredoxin	Homo sapiens	0-12
8838810-1	1996	Glutaredoxin is a small protein (12 kDa) catalyzing glutathione-dependent disulfide oxidoreduction reactions in a coupled system with NADPH, GSH, and glutathione reductase.	Disulfides	74-83	glutathione-disulfide reductase	Homo sapiens	150-171
16106046-9	2005	We propose that one disulfide bond between C65 and C89 and free cysteine residues at C330 and C371 and the triad, serine-198, aspartic acid-360, and histidine-392, are required for the full expression of mLPLA2 activity.	Disulfides	20-29	phospholipase A2, group XV	Mus musculus	204-210
8617749-15	1996	However, cellular thiol-disulfide redox status and formation of disulfide linked aggregates of cellular proteins are linked to HSF1 activation and hsp70 transcriptional activation.	Disulfides	24-33	heat shock transcription factor 1	Homo sapiens	127-131
8617749-15	1996	However, cellular thiol-disulfide redox status and formation of disulfide linked aggregates of cellular proteins are linked to HSF1 activation and hsp70 transcriptional activation.	Disulfides	64-73	heat shock transcription factor 1	Homo sapiens	127-131
16236729-6	2005	Reduction assays show that the cysteine thiols in the RCXXC motif of AtCCMH can form a disulfide bond that can be reduced by enzymatic thiol reductants.	Disulfides	87-96	cytochrome c biogenesis protein family	Arabidopsis thaliana	69-75
8597574-1	1996	Isolated oxoglutarate carrier (OGC) can be cross-linked to dimers by disulfide-forming reagents such as Cu2+-phenanthroline and diamide.	Disulfides	69-78	solute carrier family 25 member 11	Homo sapiens	31-34
8597574-7	1996	Cross-linking of OGC is prevented by SH reagents and reversed by SH-reducing reagents, which shows that it is mediated by disulfide bridge(s).	Disulfides	122-131	solute carrier family 25 member 11	Homo sapiens	17-20
8597574-10	1996	The number and localization of disulfide bridge(s) in the cross-linked OGC were examined by peptide fragmentation and subsequent cleavage of disulfide bond(s) by beta-mercaptoethanol.	Disulfides	31-40	solute carrier family 25 member 11	Homo sapiens	71-74
8597574-10	1996	The number and localization of disulfide bridge(s) in the cross-linked OGC were examined by peptide fragmentation and subsequent cleavage of disulfide bond(s) by beta-mercaptoethanol.	Disulfides	141-150	solute carrier family 25 member 11	Homo sapiens	71-74
8597574-11	1996	Our experimental results show that cross-linking of OGC is accomplished by a single disulfide bond between the cysteines 184 of the two subunits and suggest that these residues in the putative transmembrane helix four are fairly close to the twofold axis of the native dimer structure.	Disulfides	84-93	solute carrier family 25 member 11	Homo sapiens	52-55
16236729-7	2005	A reduced form of AtCCMH can reduce the intra-disulfide bridge of a model peptide of apocytochrome c. When expressed in Escherichia coli, AtCCMH coimmunoprecipitates with the bacterial CcmF, a proposed component of the heme lyase.	Disulfides	46-55	cytochrome c biogenesis protein family	Arabidopsis thaliana	18-24
8639681-1	1996	Protein disulfide isomerase (PDI), a very abundant protein in the endoplasmic reticulum, facilitates the formation and rearrangement of disulfide bonds using two nonequivalent redox active-sites, located in two different thioredoxin homology domains [Lyles, M. M., &amp; Gilbert, H. F. (1994) J. Biol.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Bos taurus	29-32
16236729-7	2005	A reduced form of AtCCMH can reduce the intra-disulfide bridge of a model peptide of apocytochrome c. When expressed in Escherichia coli, AtCCMH coimmunoprecipitates with the bacterial CcmF, a proposed component of the heme lyase.	Disulfides	46-55	cytochrome c biogenesis protein family	Arabidopsis thaliana	138-144
8639681-1	1996	Protein disulfide isomerase (PDI), a very abundant protein in the endoplasmic reticulum, facilitates the formation and rearrangement of disulfide bonds using two nonequivalent redox active-sites, located in two different thioredoxin homology domains [Lyles, M. M., &amp; Gilbert, H. F. (1994) J. Biol.	Disulfides	8-17	thioredoxin	Bos taurus	221-232
8639681-4	1996	Each dithiol/disulfide active-site contains the thioredoxin consensus sequence CXXC.	Disulfides	13-22	thioredoxin	Bos taurus	48-59
16115028-4	2005	The catalytic thiol-protein oxidoreductase (TPOR) activity of MIF is mediated by a Cys-Ala-Leu-Cys active site between residues 57 and 60 that can undergo reversible intramolecular disulfide formation.	Disulfides	181-190	macrophage migration inhibitory factor	Homo sapiens	62-65
8639681-11	1996	Since both active-site cysteines are essential for catalysis of disulfide formation, the dominant mechanism for RNase oxidation may involve direct oxidation by the active-site PDI disulfide.	Disulfides	64-73	prolyl 4-hydroxylase subunit beta	Bos taurus	176-179
8639681-11	1996	Since both active-site cysteines are essential for catalysis of disulfide formation, the dominant mechanism for RNase oxidation may involve direct oxidation by the active-site PDI disulfide.	Disulfides	180-189	prolyl 4-hydroxylase subunit beta	Bos taurus	176-179
15814132-4	2005	A synthetic peptide, RGDSGGC containing RGDS moiety that is known as one of the most important cell adhesive peptides, was readily coupled by disulfide bonds formation with sulfhydryl groups of SH-chitosan in the presence of dimethyl sulfoxide.	Disulfides	142-151	ral guanine nucleotide dissociation stimulator	Homo sapiens	21-25
8575862-7	1996	A molecular form of some 400 kDa was identified to represent a disulfide-bound oligomer of the p150/160apc molecules.	Disulfides	63-72	chromatin assembly factor 1 subunit A	Homo sapiens	95-103
16117831-4	2005	However, a novel class of Kazal domains with two disulfide bridges resulting from the absence of the third and sixth cysteines have been found in biologically important molecules, such as human LEKTI, a 15-domain inhibitor associated with the severe congenital disease Netherton syndrome.	Disulfides	49-58	serine peptidase inhibitor Kazal type 5	Homo sapiens	194-199
8549805-9	1996	Fluorescence spectra demonstrated only tyrosine fluorescence in human Grx with a peak at 310 nm which increased 20% upon reduction and decreased by addition of GSSG demonstrating that glutathione-containing disulfides are excellent substrates.	Disulfides	207-217	glutaredoxin	Homo sapiens	70-73
8989507-1	1996	Lipoprotein(a) [Lp(a)] represents an LDL-like particle to which the Lp(a)-specific apolipoprotein(a) is linked via a disulfide bridge.	Disulfides	117-126	lipoprotein(a)	Homo sapiens	0-14
8989507-1	1996	Lipoprotein(a) [Lp(a)] represents an LDL-like particle to which the Lp(a)-specific apolipoprotein(a) is linked via a disulfide bridge.	Disulfides	117-126	lipoprotein(a)	Homo sapiens	16-21
8989507-1	1996	Lipoprotein(a) [Lp(a)] represents an LDL-like particle to which the Lp(a)-specific apolipoprotein(a) is linked via a disulfide bridge.	Disulfides	117-126	lipoprotein(a)	Homo sapiens	68-73
16042419-3	2005	We have expressed a mutant FXI/G326C in which the Gly326 residue of factor XI has been mutated to Cys326, reasoning that Cys321 would form an intrachain disulfide bond with Cys326 as in prekallikrein, a plasma protein that exists as a monomer even with 58% amino acid sequence identity and a domain structure very similar to factor XI.	Disulfides	153-162	coagulation factor XI	Homo sapiens	27-30
8856971-4	1996	A wide range of studies has established that in presence of a redox pair, PDI acts catalytically to both form and reduce disulfide bonds, therefore acting as a disulfide isomerase.	Disulfides	121-130	prolyl 4-hydroxylase subunit beta	Homo sapiens	74-77
15831706-1	2005	Semaphorin 3A (Sema3A) is a secreted disulfide-bound homodimeric molecule that induces growth cone collapse and repulsion of axon growth in the nervous system.	Disulfides	37-46	semaphorin 3A	Homo sapiens	0-13
8628734-3	1996	Of particular importance for inhibitor binding are four amino acid residues in the disulfide substrate-binding site of TR that are not conserved in human GR, namely, Glu-18 (Ala-34 in GR), Trp-21 (Arg-37), Ser-109 (Ile-113), and Met-113 (Asn-117).	Disulfides	83-92	glutathione-disulfide reductase	Homo sapiens	184-186
8618853-2	1995	At this stage TCR beta chain can form disulfide-linked heterodimers with the pre-T-cell receptor alpha chain (pTalpha).	Disulfides	38-47	pre T cell antigen receptor alpha	Homo sapiens	77-108
15831706-1	2005	Semaphorin 3A (Sema3A) is a secreted disulfide-bound homodimeric molecule that induces growth cone collapse and repulsion of axon growth in the nervous system.	Disulfides	37-46	semaphorin 3A	Homo sapiens	15-21
16013863-4	2005	For RNAse A, quantitative reduction of the disulfide bonds lead to the exposure of an additional arginine residue and two different conformations of the reduced protein were observed by ESI-MS that could be distinguished according to their charge-state distribution.	Disulfides	43-52	ribonuclease A family member 1, pancreatic	Homo sapiens	4-11
7500359-1	1995	Recombinant mouse and human fibulin-2 were obtained as disulfide-bonded trimers from transfected kidney cell clones and used in solid phase, biosensor and radioligand binding assays.	Disulfides	55-64	fibulin 2	Homo sapiens	28-37
15998240-5	2005	We have established that PKC isozymes are regulated by S-thiolation, a posttranslational modification entailing disulfide linkage of low-molecular-weight species to select protein sulfhydryls.	Disulfides	112-121	protein kinase C delta	Homo sapiens	25-28
15998240-6	2005	Our recent studies demonstrate that physiologically occurring disulfides with cysteinyl constituents, e.g., cystine, regulate cellular PKC isozymes by S-thiolation-triggered mechanisms.	Disulfides	62-72	protein kinase C delta	Homo sapiens	135-138
24178881-0	1995	Synthesis of symmetric disulfides as potential alternative substrates for trypanothione reductase and glutathione reductase: Part 1.	Disulfides	23-33	glutathione-disulfide reductase	Homo sapiens	102-123
24178881-1	1995	The synthesis of a series of symmetrical disulfides as potential substrates of trypanothione reductase and glutathione reductase was described.	Disulfides	41-51	glutathione-disulfide reductase	Homo sapiens	107-128
15998240-7	2005	This report shows that PKC isozymes are also molecular targets of a chemically distinct class of disulfides.	Disulfides	97-107	protein kinase C delta	Homo sapiens	23-26
24178882-0	1995	Synthesis of asymmetric disulfides as potential alternative substrates for trypanothione reductase and glutathione reductase: Part 2.	Disulfides	24-34	glutathione-disulfide reductase	Homo sapiens	103-124
16284729-0	2005	Disulfide linkages and a three-dimensional structure model of the extracellular ligand-binding domain of guanylyl cyclase C.	Disulfides	0-9	guanylate cyclase 2C	Homo sapiens	105-123
7479743-1	1995	Lipoprotein(a) [Lp(a)] is a lipoprotein formed by the disulfide linkage of apolipoprotein (apo) B100 of a low density lipoprotein particle to apolipoprotein(a).	Disulfides	54-63	lipoprotein(a)	Homo sapiens	0-14
7479743-1	1995	Lipoprotein(a) [Lp(a)] is a lipoprotein formed by the disulfide linkage of apolipoprotein (apo) B100 of a low density lipoprotein particle to apolipoprotein(a).	Disulfides	54-63	lipoprotein(a)	Homo sapiens	16-21
7479743-1	1995	Lipoprotein(a) [Lp(a)] is a lipoprotein formed by the disulfide linkage of apolipoprotein (apo) B100 of a low density lipoprotein particle to apolipoprotein(a).	Disulfides	54-63	lipoprotein(a)	Homo sapiens	142-159
16284729-2	2005	Using combined HPLC separation and MS analysis techniques the positions of the disulfide linkages in the extracellular ligand-binding domain (ECD) of GC-C were determined to be between Cys7-Cys94, Cys72-Cys77, Cys101-Cys128 and Cys179-Cys226.	Disulfides	79-88	guanylate cyclase 2C	Homo sapiens	150-154
15939022-2	2005	We have determined the crystal structure of the ligand binding domain of LOX-1, with a short stalk region connecting the domain to the membrane-spanning region, as a homodimer linked by an interchain disulfide bond.	Disulfides	200-209	oxidized low density lipoprotein receptor 1	Homo sapiens	73-78
7592666-4	1995	Furthermore, all four disulfide bonds found in mammalian cathepsin D sequences are present in Sjpasp, although the beta-hairpin (loop 3), which is cleaved during maturation of vertebrate cathepsin Ds to yield light and heavy chain subunits, is absent from Sjpasp.	Disulfides	22-31	cathepsin D	Homo sapiens	57-68
15713716-7	2005	These results demonstrate that the absence of the disulfide bridge Cys-53 to Cys-165 affects the binding affinity of GH for the GHR and subsequently the potency of GH to activate the Jak2/Stat5 signaling pathway.	Disulfides	50-59	Janus kinase 2	Homo sapiens	183-187
7556671-5	1995	These results suggested that PDIR has oxidoreductase activity of disulfide bonds against polypeptides and that it acts as a catalyst of protein folding in the lumen of the ER.	Disulfides	65-74	protein disulfide isomerase family A member 5	Homo sapiens	29-33
15642731-0	2005	The nonconsecutive disulfide bond of Escherichia coli phytase (AppA) renders it dependent on the protein-disulfide isomerase, DsbC.	Disulfides	19-28	putative protein DsbC	Escherichia coli	126-130
7629495-1	1995	Immunoprecipitation experiments reveal that the LGL-1 protein exists as a disulfide-linked 40-kD homodimer.	Disulfides	74-83	killer cell lectin-like receptor, subfamily A, member 7	Mus musculus	48-53
7629496-3	1995	5E6 is nearly identical to Ly-49C; the deduced amino acid sequence reveals a polypeptide of 266 amino acids with a molecular weight of 31,284 that contains multiple cysteine residues to explain its disulfide-linked homodimer structure and five potential N-linked glycosylation sites.	Disulfides	198-207	killer cell lectin-like receptor, subfamily A, member 3	Mus musculus	0-3
15642731-2	2005	Many eukaryotic proteins with nonconsecutive disulfide bonds expressed in E. coli require an additional protein for proper folding, the disulfide bond isomerase DsbC.	Disulfides	45-54	putative protein DsbC	Escherichia coli	161-165
7608548-9	1995	Our results suggest that conformational differences between human and rabbit pIgR may account for differences in disulfide bonding to pIgA, and show that efficient transcytosis of pIgA is correlated better with noncovalent than covalent binding to pIgR.	Disulfides	113-122	polymeric immunoglobulin receptor	Oryctolagus cuniculus	77-81
7635143-5	1995	Since rhodanese contains no disulfide bonds, the chaperone-like activity of PDI acting on rhodanese is independent of its disulfide-isomerase activity.	Disulfides	28-37	prolyl 4-hydroxylase subunit beta	Homo sapiens	76-79
15642731-5	2005	However, the activity of an AppA mutant lacking its nonconsecutive disulfide bond is DsbC-independent.	Disulfides	67-76	putative protein DsbC	Escherichia coli	85-89
15623537-10	2005	The MUC1/ZD protein is expressed in tissues as an oligomeric complex composed of monomers linked by disulfide bonds contributed by MUC1/ZD cysteine residues.	Disulfides	100-109	mucin 1, cell surface associated	Homo sapiens	4-11
7779780-8	1995	The Cter domain of apo(a), which remained in disulfide linkage with apo B100 of Lp(a), was isolated as a lipoprotein particle by a combination of chromatographic steps on heparin-Sepharose and Q-Sepharose columns.	Disulfides	45-54	lipoprotein(a)	Homo sapiens	19-25
15623537-10	2005	The MUC1/ZD protein is expressed in tissues as an oligomeric complex composed of monomers linked by disulfide bonds contributed by MUC1/ZD cysteine residues.	Disulfides	100-109	mucin 1, cell surface associated	Homo sapiens	4-8
7738018-4	1995	The disulfide loop contains the sequence (Arg-X-X-Arg), which is a consensus motif for cleavage by the membrane-anchored protease furin.	Disulfides	4-13	furin, paired basic amino acid cleaving enzyme	Homo sapiens	130-135
15647258-6	2005	In the PAPP-A.pro-MBP complex, two of these form the basis of both two interchain disulfide bonds between the PAPP-A and the pro-MBP subunits and two disulfide bonds responsible for pro-MBP dimerization, respectively.	Disulfides	82-91	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	14-21
15647258-6	2005	In the PAPP-A.pro-MBP complex, two of these form the basis of both two interchain disulfide bonds between the PAPP-A and the pro-MBP subunits and two disulfide bonds responsible for pro-MBP dimerization, respectively.	Disulfides	82-91	myelin basic protein	Homo sapiens	129-132
7664466-2	1995	Lp(a) is a low-density lipoprotein (LDL)-like particle which contains a glycoprotein (apoprotein(a)) disulfide linked to apo B-100.	Disulfides	101-110	lipoprotein(a)	Homo sapiens	0-5
15647258-6	2005	In the PAPP-A.pro-MBP complex, two of these form the basis of both two interchain disulfide bonds between the PAPP-A and the pro-MBP subunits and two disulfide bonds responsible for pro-MBP dimerization, respectively.	Disulfides	150-159	pappalysin 1	Homo sapiens	7-13
15647258-6	2005	In the PAPP-A.pro-MBP complex, two of these form the basis of both two interchain disulfide bonds between the PAPP-A and the pro-MBP subunits and two disulfide bonds responsible for pro-MBP dimerization, respectively.	Disulfides	150-159	myelin basic protein	Homo sapiens	18-21
15647258-6	2005	In the PAPP-A.pro-MBP complex, two of these form the basis of both two interchain disulfide bonds between the PAPP-A and the pro-MBP subunits and two disulfide bonds responsible for pro-MBP dimerization, respectively.	Disulfides	150-159	pappalysin 1	Homo sapiens	110-116
15647258-6	2005	In the PAPP-A.pro-MBP complex, two of these form the basis of both two interchain disulfide bonds between the PAPP-A and the pro-MBP subunits and two disulfide bonds responsible for pro-MBP dimerization, respectively.	Disulfides	150-159	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	14-21
7873520-1	1995	Human type-alpha transforming growth factor (hTGF alpha) is a small mitogenic protein containing 50 amino acids and three disulfide bonds.	Disulfides	122-131	transforming growth factor alpha	Homo sapiens	45-55
7873520-17	1995	The distribution of these sites on the three-dimensional protein structure suggests that these dynamic fluctuations are due to (i) partial unfolding of the core beta-sheet, (ii) hinge-bending motions between the N- and C-terminal subdomains, and/or (iii) disulfide bond isomerization in the solution structure of hTGF alpha at neutral pH.	Disulfides	255-264	transforming growth factor alpha	Homo sapiens	313-323
15647258-6	2005	In the PAPP-A.pro-MBP complex, two of these form the basis of both two interchain disulfide bonds between the PAPP-A and the pro-MBP subunits and two disulfide bonds responsible for pro-MBP dimerization, respectively.	Disulfides	150-159	myelin basic protein	Homo sapiens	129-132
15669088-5	2005	The E. coli periplasmic disulfide isomerase, DsbC, was also added to rearrange incorrectly formed disulfide linkages.	Disulfides	24-33	putative protein DsbC	Escherichia coli	45-49
7721952-2	1995	Recently it has been shown that SPARC inhibits the progression of the endothelial cell cycle in mid-G1, and that a synthetic peptide (amino acids 54-73 of secreted murine SPARC, peptide 2.1) from a cationic, disulfide-bonded region was in part responsible for the growth-suppressing activity [Funk and Sage (1991): Proc Natl Acad Sci USA 88:2648-2652].	Disulfides	208-217	secreted acidic cysteine rich glycoprotein	Mus musculus	171-176
15623505-1	2005	The endoplasmic reticulum (ER) contains a number of thiol-disulfide oxidoreductases of the protein-disulfide isomerase (PDI) family that catalyze the formation of disulfide bonds in newly synthesized proteins.	Disulfides	58-67	prolyl 4-hydroxylase subunit beta	Homo sapiens	91-118
7798222-1	1994	A baculovirus system was used to express full-length recombinant mouse thrombospondin 2 (rTSP2) as a disulfide-bonded homotrimer with an NH2 terminus beginning with Asp20.rTSP2, like TSP1, was more sensitive to trypsin digestion if depleted of calcium ion.	Disulfides	101-110	thrombospondin 2	Mus musculus	71-87
15623505-1	2005	The endoplasmic reticulum (ER) contains a number of thiol-disulfide oxidoreductases of the protein-disulfide isomerase (PDI) family that catalyze the formation of disulfide bonds in newly synthesized proteins.	Disulfides	58-67	prolyl 4-hydroxylase subunit beta	Homo sapiens	120-123
15735342-7	2005	The overall secondary and tertiary structures of hCyPJ are similar to those of hCyPA, but hCyPJ contains an additional disulfide bridge and four segments with conformations that are strikingly different from those of hCyPA.	Disulfides	119-128	peptidylprolyl isomerase like 3	Homo sapiens	90-95
7964477-2	1994	CD69 was found expressed on all peripheral blood monocytes, as a 28- and 32-kD disulfide-linked dimer.	Disulfides	79-88	CD69 molecule	Homo sapiens	0-4
15709754-1	2005	The conformational changes at the cytoplasmic ends of transmembrane helices 5 and 6 (TMH5 and TMH6) of thyrotropin-releasing hormone (TRH) receptor type I (TRH-R1) during activation were analyzed by cysteine-scanning mutagenesis followed by disulfide cross-linking and molecular modeling.	Disulfides	241-250	thyrotropin releasing hormone	Homo sapiens	134-137
7526035-4	1994	Recent analyses of sera from pregnant women have revealed that pregnancy-associated plasma protein-A (PAPP-A), previously thought to be a homotetramer of PAPP-A subunits, is actually composed of PAPP-A subunits bound by disulfide bonds to equimolar amounts of proMBP molecules to form a complex, PAPP-A/proMBP.	Disulfides	220-229	pappalysin 1	Homo sapiens	63-100
7526035-4	1994	Recent analyses of sera from pregnant women have revealed that pregnancy-associated plasma protein-A (PAPP-A), previously thought to be a homotetramer of PAPP-A subunits, is actually composed of PAPP-A subunits bound by disulfide bonds to equimolar amounts of proMBP molecules to form a complex, PAPP-A/proMBP.	Disulfides	220-229	pappalysin 1	Homo sapiens	102-108
15709754-1	2005	The conformational changes at the cytoplasmic ends of transmembrane helices 5 and 6 (TMH5 and TMH6) of thyrotropin-releasing hormone (TRH) receptor type I (TRH-R1) during activation were analyzed by cysteine-scanning mutagenesis followed by disulfide cross-linking and molecular modeling.	Disulfides	241-250	thyrotropin releasing hormone	Homo sapiens	156-159
7983787-2	1994	The basic structure of the insulin receptor is a disulfide-linked tetramer, composed of the alpha subunit (135 kDa), which is extracellular and provides the binding site for insulin, and the beta subunit (95 kDa), contains the transmembrane domain, tyrosine kinase domain and C-terminal domain.	Disulfides	49-58	insulin receptor	Homo sapiens	27-43
8089137-1	1994	The major alpha-amylase inhibitor (AAI) present in the seeds of Amaranthus hypocondriacus, a variety of the Mexican crop plant amaranth, is a 32-residue-long polypeptide with three disulfide bridges.	Disulfides	181-190	alpha-amylase	Tribolium castaneum	10-23
15709754-3	2005	The cross-linking experiments indicate that four mutants, Q263C/G212C, Q263C/Y211C, T265C/G212C, and T265C/Y211C, exhibited disulfide bond formation that was sensitive to TRH occupancy.	Disulfides	124-133	thyrotropin releasing hormone	Homo sapiens	171-174
8071354-0	1994	Ab initio association with beta 2-microglobulin during biosynthesis of the H-2Ld class I major histocompatibility complex heavy chain promotes proper disulfide bond formation and stable peptide binding.	Disulfides	150-159	beta-2 microglobulin	Mus musculus	27-47
8071354-1	1994	In vitro translation studies indicate that the beta 2-microglobulin (beta 2-m) light chain influences the formation of intrachain disulfide bonds in class I major histocompatibility complex (MHC) molecules during their biosynthesis.	Disulfides	130-139	beta-2 microglobulin	Mus musculus	47-67
15725757-1	2005	The third variable region, V3, of the gp120 surface envelope glycoprotein is an approximately 35-residue-long, frequently glycosylated, highly variable, disulfide-bonded structure that has a major influence on HIV-1 tropism.	Disulfides	153-162	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	38-43
8071354-1	1994	In vitro translation studies indicate that the beta 2-microglobulin (beta 2-m) light chain influences the formation of intrachain disulfide bonds in class I major histocompatibility complex (MHC) molecules during their biosynthesis.	Disulfides	130-139	beta-2 microglobulin	Mus musculus	47-55
8071354-2	1994	We now have examined the influence of beta 2-m on class I MHC intrachain disulfide bond formation in vivo.	Disulfides	73-82	beta-2 microglobulin	Mus musculus	38-46
8071354-5	1994	Only those H-2Ld molecules from beta 2-m- cells, which have both intrachain disulfide bonds, undergo a peptide- and beta 2-m-induced conformational change in vitro.	Disulfides	76-85	beta-2 microglobulin	Mus musculus	32-40
8071354-5	1994	Only those H-2Ld molecules from beta 2-m- cells, which have both intrachain disulfide bonds, undergo a peptide- and beta 2-m-induced conformational change in vitro.	Disulfides	76-85	beta-2 microglobulin	Mus musculus	116-124
8071354-7	1994	From these results emerges a greater understanding of the role of beta 2-m at the time of class I MHC molecule synthesis: beta 2-m promotes intrachain disulfide bond formation in the class I MHC molecule and additionally affects class I MHC structure to render it competent to form stable trimolecular complexes with peptide and beta 2-m.	Disulfides	151-160	beta-2 microglobulin	Mus musculus	66-74
8071354-7	1994	From these results emerges a greater understanding of the role of beta 2-m at the time of class I MHC molecule synthesis: beta 2-m promotes intrachain disulfide bond formation in the class I MHC molecule and additionally affects class I MHC structure to render it competent to form stable trimolecular complexes with peptide and beta 2-m.	Disulfides	151-160	beta-2 microglobulin	Mus musculus	122-130
8071354-7	1994	From these results emerges a greater understanding of the role of beta 2-m at the time of class I MHC molecule synthesis: beta 2-m promotes intrachain disulfide bond formation in the class I MHC molecule and additionally affects class I MHC structure to render it competent to form stable trimolecular complexes with peptide and beta 2-m.	Disulfides	151-160	beta-2 microglobulin	Mus musculus	122-130
15862094-3	2005	A related disulfide protein, protein disulfide isomerase (PDI) acts in protein assembly.	Disulfides	10-19	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-56
7831284-10	1994	However, the frequent occurrence of additional Cys residues in both the CDR1 and CDR3 might lead to the formation of a second internal disulfide bridge, thereby stabilizing the CDR structure as in the DAW antibody.	Disulfides	135-144	LOW QUALITY PROTEIN: cerebellar degeneration-related antigen 1	Camelus dromedarius	72-76
15862094-3	2005	A related disulfide protein, protein disulfide isomerase (PDI) acts in protein assembly.	Disulfides	10-19	prolyl 4-hydroxylase subunit beta	Homo sapiens	58-61
15607655-2	2005	In the mutant, a disulfide linkage between the heavy (H) and light (L) chains, which is essential for the intracellular transport and secretion of fibroin, is not formed because of a partial deletion of the L-chain gene.	Disulfides	17-26	fibroin light chain	Bombyx mori	147-154
7516709-1	1994	As a model for understanding how protein disulfide isomerase (PDI) catalyzes disulfide bond formation in proteins, its action on a 28-residue disordered peptide containing only two cysteine residues has been examined.	Disulfides	41-50	prolyl 4-hydroxylase subunit beta	Homo sapiens	62-65
15576552-5	2005	IAPP possesses an intramolecular disulfide bond between residues 2 and 7.	Disulfides	33-42	islet amyloid polypeptide	Homo sapiens	0-4
8033966-1	1994	An immunotoxin composed of a monoclonal antibody that recognizes the p75 nerve growth factor (NGF) receptor disulfide-linked to the ribosome-inactivating protein saporin selectively eliminates p75-expressing cholinergic neurons in the basal forebrain, while sparing other neurons in the forebrain, both cholinergic and noncholinergic.	Disulfides	108-117	nerve growth factor receptor	Rattus norvegicus	69-72
8033966-1	1994	An immunotoxin composed of a monoclonal antibody that recognizes the p75 nerve growth factor (NGF) receptor disulfide-linked to the ribosome-inactivating protein saporin selectively eliminates p75-expressing cholinergic neurons in the basal forebrain, while sparing other neurons in the forebrain, both cholinergic and noncholinergic.	Disulfides	108-117	nerve growth factor receptor	Rattus norvegicus	193-196
15545364-5	2004	The antagonistic effect and the stabilization effect observed above a threshold pressure value of 600 MPa were thought to be related to the disruption of disulfide bonds in plasmin and plasminogen.	Disulfides	154-163	plasminogen	Homo sapiens	173-180
8175752-0	1994	Inhibition of vacuolar H(+)-ATPase by disulfide bond formation between cysteine 254 and cysteine 532 in subunit A.	Disulfides	38-47	ATPase H+ transporting V1 subunit B2	Bos taurus	14-34
8175752-1	1994	We have previously demonstrated that the coated vesicle vacuolar H(+)-ATPase (V-ATPase) can be inactivated by formation of intramolecular disulfide bonds (Feng, Y., and Forgac, M. (1992) J. Biol.	Disulfides	138-147	ATPase H+ transporting V1 subunit B2	Bos taurus	56-76
8175752-1	1994	We have previously demonstrated that the coated vesicle vacuolar H(+)-ATPase (V-ATPase) can be inactivated by formation of intramolecular disulfide bonds (Feng, Y., and Forgac, M. (1992) J. Biol.	Disulfides	138-147	ATPase H+ transporting V1 subunit B2	Bos taurus	78-86
8175752-6	1994	After analyzing the proteolytic fragments that contain the labeled cysteine residues, we found that cysteine 254 and cysteine 532 in subunit A of the bovine V-ATPase are the residues that form the disulfide bond resulting in inactivation of the enzyme.	Disulfides	197-206	ATPase H+ transporting V1 subunit B2	Bos taurus	157-165
15375179-1	2004	Lipoprotein(a) [Lp(a)] is assembled via an initial noncovalent interaction between apolipoprotein B100 (apoB) and apolipoprotein(a) [apo(a)] that facilitates the formation of a disulfide bond between the two proteins.	Disulfides	177-186	lipoprotein(a)	Homo sapiens	0-14
8070970-3	1994	AP-A is a 49 residue peptide crosslinked by three disulfide bonds; its tertiary structure has been determined by NMR.	Disulfides	50-59	glutamyl aminopeptidase	Homo sapiens	0-4
8158137-2	1994	We showed that this 116/130 kDa protein is a disulfide dimer of peripherin, because it gave rise to a single protein band comigrating with peripherin under reducing conditions and yielded the same proteolytic pattern as peripherin upon N-chlorosuccinimide digestion.	Disulfides	45-54	peripherin	Rattus norvegicus	64-74
15375179-1	2004	Lipoprotein(a) [Lp(a)] is assembled via an initial noncovalent interaction between apolipoprotein B100 (apoB) and apolipoprotein(a) [apo(a)] that facilitates the formation of a disulfide bond between the two proteins.	Disulfides	177-186	lipoprotein(a)	Homo sapiens	16-21
8158137-2	1994	We showed that this 116/130 kDa protein is a disulfide dimer of peripherin, because it gave rise to a single protein band comigrating with peripherin under reducing conditions and yielded the same proteolytic pattern as peripherin upon N-chlorosuccinimide digestion.	Disulfides	45-54	peripherin	Rattus norvegicus	139-149
8158137-2	1994	We showed that this 116/130 kDa protein is a disulfide dimer of peripherin, because it gave rise to a single protein band comigrating with peripherin under reducing conditions and yielded the same proteolytic pattern as peripherin upon N-chlorosuccinimide digestion.	Disulfides	45-54	peripherin	Rattus norvegicus	139-149
15375179-1	2004	Lipoprotein(a) [Lp(a)] is assembled via an initial noncovalent interaction between apolipoprotein B100 (apoB) and apolipoprotein(a) [apo(a)] that facilitates the formation of a disulfide bond between the two proteins.	Disulfides	177-186	lipoprotein(a)	Homo sapiens	114-131
15377672-1	2004	In vitro, protein disulfide isomerase (Pdi1p) introduces disulfides into proteins (oxidase activity) and provides quality control by catalyzing the rearrangement of incorrect disulfides (isomerase activity).	Disulfides	57-67	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	39-44
7512537-6	1994	Treatment of the mucin antigen by heating, reduction of disulfide bonds, or protease digestion abolished immunoreactivity with PAM4.	Disulfides	56-65	LOC100508689	Homo sapiens	17-22
15377672-1	2004	In vitro, protein disulfide isomerase (Pdi1p) introduces disulfides into proteins (oxidase activity) and provides quality control by catalyzing the rearrangement of incorrect disulfides (isomerase activity).	Disulfides	175-185	protein disulfide isomerase PDI1	Saccharomyces cerevisiae S288C	39-44
15364921-4	2004	AAT-1 and AAT-3 contain a cysteine residue in the second putative extracellular loop through which a disulfide bridge can form with a heavy chain.	Disulfides	101-110	Amino Acid Transporter	Caenorhabditis elegans	0-5
8168497-6	1994	The in vivo function of DsbC seems to be the formation of disulfide bonds in proteins.	Disulfides	58-67	putative protein DsbC	Escherichia coli	24-28
15511233-3	2004	Using a disulfide cross-linking strategy, we demonstrate that at least three different sites (positions 52, 54 and 68) within the N terminus may be tethered in a reformable manner to position 195 in the loop region between helix D and strand s2A of the HCII molecule, suggesting that the N-terminal domain may interact with the inhibitor scaffold in a permissive manner.	Disulfides	8-17	serpin family D member 1	Homo sapiens	253-257
8196177-1	1994	PDI catalyzes the formation of disulfide bonds and plays a central role in the correct folding of nascent polypeptides.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
15294898-4	2004	Here we report a decrease in motility of RPTPalpha from cells treated with H2O2 on non-reducing SDS-polyacrylamide gels to a position that corresponds to RPTPalpha dimers, indicating intermolecular disulfide bond formation.	Disulfides	198-207	protein tyrosine phosphatase receptor type A	Homo sapiens	41-50
15294898-5	2004	Using mutants of all individual cysteines in RPTPalpha and constructs encoding the individual protein-tyrosine phosphatase domains, we located the intermolecular disulfide bond to the catalytic Cys-723 in D2.	Disulfides	162-171	protein tyrosine phosphatase receptor type A	Homo sapiens	45-54
8054846-1	1994	Protein disulfide isomerase (PDI) catalyzes the formation and rearrangement of disulfide bonds during protein folding.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
15294898-8	2004	Intermolecular disulfide bond formation and rotational coupling were also found using a chimera of the extracellular domain of RPTPalpha fused to the transmembrane and intracellular domain of the leukocyte common antigen-related protein (LAR).	Disulfides	15-24	protein tyrosine phosphatase receptor type A	Homo sapiens	127-136
8054846-2	1994	PDI coupled to cyanogen bromide-activated agarose retains its catalytic activity, and a column of this material increases both the rate and the yield for folding disulfide-containing proteins.	Disulfides	162-171	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
15351709-2	2004	We report that peroxynitrite and H2O2-induced disulfides in the porcine brain microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH.	Disulfides	46-56	glutathione-disulfide reductase	Homo sapiens	216-237
15388920-0	2004	Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli.	Disulfides	25-34	putative protein DsbC	Escherichia coli	50-54
8132560-8	1994	These results suggest that the cysteine residues of Tat are involved in the formation of intramolecular disulfide bonds.	Disulfides	104-113	tyrosine aminotransferase	Homo sapiens	52-55
15388920-4	2004	The other pair of Cys residues (141 and 163) in DsbC form a disulfide bond.	Disulfides	60-69	putative protein DsbC	Escherichia coli	48-52
15295109-0	2004	Hexa-histidin tag position influences disulfide structure but not binding behavior of in vitro folded N-terminal domain of rat corticotropin-releasing factor receptor type 2a.	Disulfides	38-47	hexosaminidase subunit alpha	Rattus norvegicus	0-4
7764724-4	1994	It was as active as natural PDI derived from human placenta as determined by its ability to reactivate scrambled ribonuclease that was a fully oxidized mixture containing randomly formed disulfide bonds.	Disulfides	187-196	prolyl 4-hydroxylase subunit beta	Homo sapiens	28-31
7764724-6	1994	These indicate that the characteristics of rhPDI are similar to those reported for mammalian PDI and that it can be used for refolding inactive proteins having incorrect disulfide bonds.	Disulfides	170-179	prolyl 4-hydroxylase subunit beta	Homo sapiens	45-48
15341729-3	2004	Interestingly, these proteins contain active sites in the same area, where the disulfide bond of oxidized CI-B8 is located.	Disulfides	79-88	NADH:ubiquinone oxidoreductase subunit A2	Homo sapiens	106-111
7907332-6	1994	PDI"s anti-chaperone activity results in extensive intermolecular disulfide crosslinking of lysozyme into large, inactive aggregates.	Disulfides	66-75	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
7907332-9	1994	The schizophrenic chaperone/anti-chaperone nature of PDI activity accounts for a number of observations on in vivo protein folding, including the necessity for maintaining a high concentration of PDI in the endoplasmic reticulum and the formation of disulfide cross-linked aggregates in the endoplasmic reticulum during the expression of disulfide-containing proteins (deSilva, A., Braakman, I., and Helenius, A.	Disulfides	250-259	prolyl 4-hydroxylase subunit beta	Homo sapiens	53-56
7907332-9	1994	The schizophrenic chaperone/anti-chaperone nature of PDI activity accounts for a number of observations on in vivo protein folding, including the necessity for maintaining a high concentration of PDI in the endoplasmic reticulum and the formation of disulfide cross-linked aggregates in the endoplasmic reticulum during the expression of disulfide-containing proteins (deSilva, A., Braakman, I., and Helenius, A.	Disulfides	338-347	prolyl 4-hydroxylase subunit beta	Homo sapiens	53-56
8307992-1	1994	Protein disulfide isomerase (PDI) and the DsbA/PpfA protein catalyze the oxidation of mutant human lysozyme, L79CC81A, which has two native disulfide bonds, Cys6-Cys128 and Cys30-Cys116, a non-native Cys79-Cys95, and 2 free cysteine residues at positions 65 and 77.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
8307992-8	1994	The dependence on GSSG of the B-form formation with PDI can be explained by the formation of two transient intermolecular disulfide bonds between PDI and the R-form and the attack of GSSG by the resultant thiolate anion of Cys79 or Cys95.	Disulfides	122-131	prolyl 4-hydroxylase subunit beta	Homo sapiens	52-55
8307992-8	1994	The dependence on GSSG of the B-form formation with PDI can be explained by the formation of two transient intermolecular disulfide bonds between PDI and the R-form and the attack of GSSG by the resultant thiolate anion of Cys79 or Cys95.	Disulfides	122-131	prolyl 4-hydroxylase subunit beta	Homo sapiens	146-149
8307992-10	1994	The possible formation of the two transient intermolecular disulfide bonds involving two sulfur atoms of PDI and 2 cysteine or half-cystine residues of the substrate could explain the high isomerase activity of PDI.	Disulfides	59-68	prolyl 4-hydroxylase subunit beta	Homo sapiens	105-108
8307992-10	1994	The possible formation of the two transient intermolecular disulfide bonds involving two sulfur atoms of PDI and 2 cysteine or half-cystine residues of the substrate could explain the high isomerase activity of PDI.	Disulfides	59-68	prolyl 4-hydroxylase subunit beta	Homo sapiens	211-214
15242783-1	2004	Human adamalysin 19 (a disintegrin and metalloproteinase 19, hADAM19) is activated by furin-mediated cleavage of the prodomain followed by an autolytic processing within the cysteine-rich domain at Glu586-Ser587, which occurs intramolecularly, producing an NH2 terminal fragment (N-fragment) associated with its COOH-terminal fragment (C-fragment), most likely through disulfide bonds.	Disulfides	369-378	furin, paired basic amino acid cleaving enzyme	Homo sapiens	86-91
15260832-7	2004	Next, the MT1-MMP activity converted the cell surface-associated pro-alphav into the mature alphav integrin, represented by the disulfide-bonded heavy and light chains, and promoted the formation of the functional integrin alphavbeta3 heterodimer.	Disulfides	128-137	matrix metallopeptidase 14	Homo sapiens	10-17
15161913-3	2004	However, oxidation must be limited, as some reduced PDI is necessary for disulfide isomerization and ER-associated degradation.	Disulfides	73-82	prolyl 4-hydroxylase subunit beta	Homo sapiens	52-55
15161913-4	2004	Here we show that in semipermeable cells, PDI is more oxidized, disulfide bonds are formed faster, and high molecular mass covalent protein aggregates accumulate in the absence of cytosol.	Disulfides	64-73	prolyl 4-hydroxylase subunit beta	Homo sapiens	42-45
15084579-5	2004	The presence of two disulfide bridges in the MAM molecule was evidenced and their integrity was found to be essential for MAM homophilic interaction.	Disulfides	20-29	sarcoglycan gamma	Homo sapiens	45-48
15084579-5	2004	The presence of two disulfide bridges in the MAM molecule was evidenced and their integrity was found to be essential for MAM homophilic interaction.	Disulfides	20-29	sarcoglycan gamma	Homo sapiens	122-125
15147964-4	2004	We have used intracellularly acting peptides, conjugated to Tat by a disulfide bond, to modulate protein kinase C (PKC) signaling; these PKC-modulating peptides are released from Tat upon intracellular delivery.	Disulfides	69-78	tyrosine aminotransferase	Homo sapiens	60-63
15147964-4	2004	We have used intracellularly acting peptides, conjugated to Tat by a disulfide bond, to modulate protein kinase C (PKC) signaling; these PKC-modulating peptides are released from Tat upon intracellular delivery.	Disulfides	69-78	tyrosine aminotransferase	Homo sapiens	179-182
15075343-1	2004	The insulin receptor is a transmembrane protein dimer composed of two alphabeta monomers held together by inter-alpha-chain disulfide bonds.	Disulfides	124-133	insulin receptor	Homo sapiens	4-20
15554160-1	2004	Lipoprotein(a) [Lp(a)] represents a class of lipoprotein particles having as a protein moiety apoB-100 linked by a single disulfide bond to apolipoprotein(a) [apo(a)], a multikringle structure with a high degree of homology with plasminogen.	Disulfides	122-131	lipoprotein(a)	Homo sapiens	0-14
15554160-1	2004	Lipoprotein(a) [Lp(a)] represents a class of lipoprotein particles having as a protein moiety apoB-100 linked by a single disulfide bond to apolipoprotein(a) [apo(a)], a multikringle structure with a high degree of homology with plasminogen.	Disulfides	122-131	lipoprotein(a)	Homo sapiens	16-21
15134458-6	2004	The spin label MTSSL, attached to Cys11 on PLB by a disulfide bond, was stable at position 11 in the absence of SERCA.	Disulfides	52-61	phospholamban	Homo sapiens	43-46
15060279-2	2004	However, production of Ang1 is hindered by aggregation and insolubility resulting from disulfide-linked higher-order structures.	Disulfides	87-96	angiopoietin 1	Homo sapiens	23-27
14749330-11	2004	These data indicate that this oligomeric mucin follows a similar assembly to the von Willebrand factor glycoprotein to yield long linear disulfide-linked chains.	Disulfides	137-146	LOC100508689	Homo sapiens	41-46
15063614-4	2004	Oxalate oxidase from barley is a secreted multimeric glycosylated manganese-containing enzyme with several disulfide bridges, which have been found to be essential for the catalytic activity.	Disulfides	107-116	LOC548260	Hordeum vulgare	0-15
15047843-3	2004	We show that protein p54 behaves in vitro and in infected cells as a type I membrane-anchored protein that forms disulfide-linked homodimers through its unique luminal cysteine.	Disulfides	113-122	interferon induced protein with tetratricopeptide repeats 2	Homo sapiens	21-24
15044724-9	2004	Owing to the structure-based sequence alignment revealing homology between the "nonessential" disulfide of bpDNase and the active-site motif of thioredoxin, we measured 39% of the thioredoxin-like activity for bpDNase based on the rate of insulin precipitation (DeltaA650nm/min).	Disulfides	94-103	thioredoxin	Bos taurus	180-191
14966801-1	2004	The human gene encoding the mature form of bone morphogenetic protein-2 (hBMP-2), a dimeric disulfide-bonded protein of the cystine knot growth factor family, was expressed in recombinant Escherichia coli using a temperature-inducible expression system.	Disulfides	92-101	bone morphogenetic protein 2	Homo sapiens	43-71
14966801-1	2004	The human gene encoding the mature form of bone morphogenetic protein-2 (hBMP-2), a dimeric disulfide-bonded protein of the cystine knot growth factor family, was expressed in recombinant Escherichia coli using a temperature-inducible expression system.	Disulfides	92-101	bone morphogenetic protein 2	Homo sapiens	73-79
15049843-2	2004	It was shown previously that 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB identical with Ellman"s reagent), when attached to polyethylene glycol-polystyrene (PEG-PS), controlled-pore glass (CPG), or modified Sephadex supports, was an effective oxidizing agent that promoted disulfide formation under mild conditions.	Disulfides	271-280	dystrobrevin beta	Homo sapiens	66-70
15112912-5	2004	We describe a compound heterozygous patient with TSHbeta mutations at codons 57 and 105 that interfered with a critical disulfide bond in the TSH molecule and caused CH.	Disulfides	120-129	glycoprotein hormones, alpha polypeptide	Homo sapiens	49-56
14711516-4	2004	The disulfide linkage pattern and glycoform distribution on each N-glycosylation site of recombinant chicken Thy-1 from both cell lines were determined by a combination of amino-terminal sequencing and mass spectrometry.	Disulfides	4-13	Thy-1 cell surface antigen	Gallus gallus	109-114
14645556-0	2003	Intra- and intermolecular disulfide bonds of the GP2b glycoprotein of equine arteritis virus: relevance for virus assembly and infectivity.	Disulfides	26-35	glycoprotein 2b (GP2b)	Equine arteritis virus	49-53
2624683-1	1989	The quaternary structure of bovine seminal ribonuclease, the only dimeric protein in the superfamily of ribonucleases, is maintained both by noncovalent forces and by two intersubunit disulfides.	Disulfides	184-194	seminal ribonuclease	Bos taurus	35-55
12923196-3	2003	In this study, the function of conserved gp120 contact residues, Leu593, Trp596, Gly597, Lys601, and Trp610 within the disulfide-bonded region of gp41, was examined in envelope glycoproteins derived from diverse HIV-1 isolates.	Disulfides	119-128	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	41-46
2605244-8	1989	Ca2+ or Mg2+ was able to prevent this disulfide formation in the RLC of myosin by 50% at a free ion concentration of 1.1 X 10(-8) and 4.0 X 10(-7) M, respectively, at 25 degrees C and pH 7.6.	Disulfides	38-47	myosin heavy chain 14	Homo sapiens	72-78
2530243-3	1989	An analogous pattern of specific EGF or TGF-alpha growth inhibitory activity was obtained using a synthetic peptide analog encompassing the third disulfide loop region of TGF-alpha, but containing additional modifications designed for increased membrane affinity [( Ac-D-hArg(Et)2(31),Gly32,33]HuTGF-alpha(31-43)NH2).	Disulfides	146-155	epidermal growth factor	Homo sapiens	33-36
14529290-2	2003	To create a more efficient redox buffer for the in vitro folding of disulfide containing proteins, aromatic thiols were investigated for their ability to increase the folding rate of scrambled RNase A.	Disulfides	68-77	ribonuclease A family member 1, pancreatic	Homo sapiens	193-200
2677399-5	1989	In r-p22 capsids, further disulfide bonds, conceivably involving the carboxy-terminal cysteines of r-p22 polypeptides, joined the dimers together, converting the structure into a covalently closed lattice.	Disulfides	26-35	calcineurin like EF-hand protein 1	Homo sapiens	5-8
14529290-3	2003	Scrambled RNase A is fully oxidized RNase A with a relatively random distribution of disulfide bonds.	Disulfides	85-94	ribonuclease A family member 1, pancreatic	Homo sapiens	10-17
2677399-5	1989	In r-p22 capsids, further disulfide bonds, conceivably involving the carboxy-terminal cysteines of r-p22 polypeptides, joined the dimers together, converting the structure into a covalently closed lattice.	Disulfides	26-35	calcineurin like EF-hand protein 1	Homo sapiens	101-104
14516194-4	2003	These dimers are stabilized by disulfide bonds formed between cysteines present in the NC2 domain and cysteines present in the triple-helical domain.	Disulfides	31-40	down-regulator of transcription 1	Mus musculus	87-90
12796500-5	2003	Following disulfide-mediated cyclization, MIF-(50-65) adapted a beta-turn conformation comparable with that of beta-turn-containing cyclo-57,60-[Asp57,Dap60]MIF-(50-65).	Disulfides	10-19	macrophage migration inhibitory factor	Homo sapiens	42-45
2752977-11	1989	These similarities and the ability of hamster PL-II to form a disulfide-bonded complex with alpha 2-macroglobulin in vitro suggest that the major circulating form of PL-II in the hamster may be a disulfide-bonded complex of one or more PL monomers with alpha 2-macroglobulin or a related plasma protein.	Disulfides	62-71	alpha-2-macroglobulin	Homo sapiens	92-113
2663861-10	1989	This early step would lead to the formation of hormone-depleted Tg molecules that are cleaved at discrete sites, the resulting polypeptides remaining bound through disulfide bonds to yield Tg molecules with an apparently normal size and a slightly altered structure.	Disulfides	164-173	thyroglobulin	Sus scrofa	64-66
12796500-12	2003	Cyclo-57,60-[Asp57,Dap60]MIF-(50-65) activated ERK1/2, indicating that CXXC-dependent disulfide and beta-turn formation is associated with an activity-inducing conformation.	Disulfides	86-95	macrophage migration inhibitory factor	Homo sapiens	25-28
14577379-7	2003	The fifth amino acid residue of MCDP in A. cerana cerana and P. hebraeus is arginine, replacing the cysteine, an important disulfide bridges element, in the position as in A. mellifera ligustica.	Disulfides	123-132	mast cell degranulating peptide	Apis mellifera	32-36
2473918-0	1989	Identification of thiol groups and a disulfide crosslink site in bovine myelin proteolipid protein.	Disulfides	37-46	proteolipid protein 1	Bos taurus	72-98
2785559-2	1989	A 40-kDa TCR gamma-chain is disulfide-linked to the TCR delta-chain in form 1, whereas 40-kDa or 55-kDa TCR-gamma polypeptides are noncovalently associated with the TCR delta-chain in forms 2bc and 2abc, respectively.	Disulfides	28-37	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	9-12
13678529-1	2003	Protein disulfide isomerase (PDI) catalyzes the formation of native disulfide pairings in secretory proteins.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
2785559-2	1989	A 40-kDa TCR gamma-chain is disulfide-linked to the TCR delta-chain in form 1, whereas 40-kDa or 55-kDa TCR-gamma polypeptides are noncovalently associated with the TCR delta-chain in forms 2bc and 2abc, respectively.	Disulfides	28-37	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	52-55
2785559-2	1989	A 40-kDa TCR gamma-chain is disulfide-linked to the TCR delta-chain in form 1, whereas 40-kDa or 55-kDa TCR-gamma polypeptides are noncovalently associated with the TCR delta-chain in forms 2bc and 2abc, respectively.	Disulfides	28-37	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	52-55
2785559-2	1989	A 40-kDa TCR gamma-chain is disulfide-linked to the TCR delta-chain in form 1, whereas 40-kDa or 55-kDa TCR-gamma polypeptides are noncovalently associated with the TCR delta-chain in forms 2bc and 2abc, respectively.	Disulfides	28-37	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	52-55
13678529-6	2003	Studies of PDI and its homologues have led to the development of small-molecule folding catalysts that are able to accelerate disulfide isomerization in vitro and in vivo.	Disulfides	126-135	prolyl 4-hydroxylase subunit beta	Homo sapiens	11-14
13678530-5	2003	Oxidative stress-induced disulfide bond formation appears to be the main strategy to adjust the protein activity of the oxidative stress transcription factors Yap1 and OxyR, the molecular chaperone Hsp33, and the anti-sigma factor RsrA.	Disulfides	25-34	Yes1 associated transcriptional regulator	Homo sapiens	159-163
12879493-1	2003	The hemoglobin from Biomphalaria glabrata is an extracellular respiratory protein of high molecular mass composed by subunits of 360 kDa, each one containing two 180 kDa chains linked by disulfide bridges.	Disulfides	187-196	uncharacterized protein LOC106051763	Biomphalaria glabrata	4-14
2930195-0	1989	Regulation of rat liver microsomal glutathione S-transferase activity by thiol/disulfide exchange.	Disulfides	79-88	hematopoietic prostaglandin D synthase	Rattus norvegicus	35-60
2930195-6	1989	These results indicate that microsomal glutathione S-transferase activity may be regulated by reversible thiol/disulfide exchange and that mixed disulfide formation of the microsomal glutathione S-transferase with glutathione disulfide may be catalyzed enzymatically in vivo.	Disulfides	111-120	hematopoietic prostaglandin D synthase	Rattus norvegicus	39-64
2930195-6	1989	These results indicate that microsomal glutathione S-transferase activity may be regulated by reversible thiol/disulfide exchange and that mixed disulfide formation of the microsomal glutathione S-transferase with glutathione disulfide may be catalyzed enzymatically in vivo.	Disulfides	145-154	hematopoietic prostaglandin D synthase	Rattus norvegicus	39-64
2930195-6	1989	These results indicate that microsomal glutathione S-transferase activity may be regulated by reversible thiol/disulfide exchange and that mixed disulfide formation of the microsomal glutathione S-transferase with glutathione disulfide may be catalyzed enzymatically in vivo.	Disulfides	145-154	hematopoietic prostaglandin D synthase	Rattus norvegicus	183-208
2466666-10	1989	The epitope for monoclonal antibody A5 is located within residues 1-393, and its recognition of antithrombin III or antithrombin-III-thrombin is strongly dependent on the integrity of the disulfide bonds.	Disulfides	188-197	serpin family C member 1	Homo sapiens	96-112
2466666-10	1989	The epitope for monoclonal antibody A5 is located within residues 1-393, and its recognition of antithrombin III or antithrombin-III-thrombin is strongly dependent on the integrity of the disulfide bonds.	Disulfides	188-197	serpin family C member 1	Homo sapiens	116-132
2928113-1	1989	The murine 4F2 molecule is a 125 kilodalton disulfide-linked heterodimeric cell-surface glycoprotein which has been shown to be involved in the processes of cellular activation and proliferation (1).	Disulfides	44-53	solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2	Mus musculus	11-14
12748182-4	2003	Moreover, a conserved disulfide in SOD1 that is essential for activity must be reduced to facilitate mitochondrial uptake of SOD1.	Disulfides	22-31	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	35-39
12748182-4	2003	Moreover, a conserved disulfide in SOD1 that is essential for activity must be reduced to facilitate mitochondrial uptake of SOD1.	Disulfides	22-31	superoxide dismutase SOD1	Saccharomyces cerevisiae S288C	125-129
2916840-0	1989	Raman spectroscopic evidence for a disulfide bridge in calf gamma II crystallin.	Disulfides	35-44	G protein subunit gamma 7	Bos taurus	60-68
2916840-4	1989	The magnitude of this increase corresponds to the presence of 1 mol of disulfide/mol of gamma II as determined both by the Raman data and the previous biochemical analysis from this laboratory.	Disulfides	71-80	G protein subunit gamma 7	Bos taurus	88-96
12660150-0	2003	Function and stability of human transcobalamin II: role of intramolecular disulfide bonds C98-C291 and C147-C187.	Disulfides	74-83	transcobalamin 2	Homo sapiens	32-49
2703017-13	1989	The results are consistent with the view that mitogenic lectins interact with certain disulfide-linked molecules on human lymphocytes, including the TcR alpha/beta and perhaps TcR gamma; while some nonmitogenic lectins also recognize these receptors, the interaction is of low affinity.	Disulfides	86-95	T cell receptor alpha joining 60 (pseudogene)	Homo sapiens	149-158
12660150-1	2003	The current studies have investigated the role of three disulfide bonds of human transcobalamin II (TC II), a plasma transporter of cobalamin (Cbl; vitamin B12), in its function and stability.	Disulfides	56-65	transcobalamin 2	Homo sapiens	81-98
2703017-13	1989	The results are consistent with the view that mitogenic lectins interact with certain disulfide-linked molecules on human lymphocytes, including the TcR alpha/beta and perhaps TcR gamma; while some nonmitogenic lectins also recognize these receptors, the interaction is of low affinity.	Disulfides	86-95	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	149-152
12660150-1	2003	The current studies have investigated the role of three disulfide bonds of human transcobalamin II (TC II), a plasma transporter of cobalamin (Cbl; vitamin B12), in its function and stability.	Disulfides	56-65	transcobalamin 2	Homo sapiens	100-105
12660150-8	2003	These studies suggest that optimal binding of Cbl by human TC II is supported by disulfide bonds C98-C291 and C147-C187 and that their disruption results in loss of Cbl binding and their rapid degradation by the proteasomal machinery.	Disulfides	81-90	transcobalamin 2	Homo sapiens	59-64
12827456-6	2003	The disulfide-bridged dimers formed from Ni(CGH-CONH(2)) in the presence of air were characterized and found to have the typical coordination found in the amino-terminal binding motif of the serum albumins.	Disulfides	4-13	hypertrichosis 2 (generalised, congenital)	Homo sapiens	44-47
2562841-1	1989	Using an antiserum raised against the purified atrial natriuretic peptide (ANP) receptor that has a disulfide-linked homodimeric structure and represents one subtype of the multiple ANP receptors, we showed that the receptor is coupled to the guanylate cyclase activation; formerly, this type of ANP receptor is not considered to be coupled to the cyclase.	Disulfides	100-109	natriuretic peptide A	Bos taurus	47-73
2562841-1	1989	Using an antiserum raised against the purified atrial natriuretic peptide (ANP) receptor that has a disulfide-linked homodimeric structure and represents one subtype of the multiple ANP receptors, we showed that the receptor is coupled to the guanylate cyclase activation; formerly, this type of ANP receptor is not considered to be coupled to the cyclase.	Disulfides	100-109	natriuretic peptide A	Bos taurus	75-78
2849548-3	1988	Out of the 26 clones studied, only 3 TcR gamma/delta+ Ti gamma A- cells were found to express a disulfide-linked C1-encoded gamma chain.	Disulfides	96-105	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	37-40
12686538-6	2003	Furthermore, the subunits of the GR3 dimers are covalently connected via a disulfide bond between the Cys-736 residues in the two molecules.	Disulfides	75-84	semaphorin 4D	Homo sapiens	33-36
3170604-4	1988	RF inactivation in GSSG-induced inhibition appears to be due to two separate but additive effects: (i) the formation of the phosphorylated 15 S RF complex, RF.eIF-2(alpha P), and (ii) the formation of disulfide complexes which inhibit RF activity.	Disulfides	201-210	eukaryotic translation initiation factor 2 subunit beta	Homo sapiens	159-164
12781781-4	2003	In this study, a peptide with the sequence of the third extracellular loop (eLP3, residues 271-289) of the TP receptor was synthesized, and its termini were constrained by the formation of a disulfide bond between the additional homocysteines located at both ends.	Disulfides	191-200	thromboxane A2 receptor	Homo sapiens	107-118
3170604-4	1988	RF inactivation in GSSG-induced inhibition appears to be due to two separate but additive effects: (i) the formation of the phosphorylated 15 S RF complex, RF.eIF-2(alpha P), and (ii) the formation of disulfide complexes which inhibit RF activity.	Disulfides	201-210	eukaryotic translation initiation factor 2 subunit beta	Homo sapiens	165-172
2458152-9	1988	Both non-disulfide-bonded and disulfide-bonded vitronectin bound to antibody-Sepharose from a mixture of vitronectin and thrombin-antithrombin III.	Disulfides	30-39	serpin family C member 1	Homo sapiens	130-146
12773488-4	2003	We found that gp160 has an intricate folding process: disulfide bonds start to form during synthesis but undergo extensive isomerization until the correct native conformation is reached.	Disulfides	54-63	glutamyl aminopeptidase	Homo sapiens	14-19
3180835-0	1988	The occurrence of glutathione-insulin transhydrogenase (protein-disulfide interchange enzyme) in the lens.	Disulfides	64-73	insulin	Bos taurus	30-37
12773488-8	2003	We show here that newly synthesized HIV-1 Envelope glycoprotein apparently follows a slow but high-yield folding path in which co- and post-translational formation of disulfide bonds in gp120, disulfide isomerization and conformation dependent removal of the leader sequence are determining and intertwined events.	Disulfides	167-176	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	186-191
12606683-0	2003	Streptozotocin-induced diabetes increases disulfide bond formation on cardiac ryanodine receptor (RyR2).	Disulfides	42-51	ryanodine receptor 2	Rattus norvegicus	98-102
12606683-13	2003	These data suggest that the dysfunction of RyR2 induced by diabetes may be due in part to formation of disulfide bonds between adjacent sulfhydryl groups and that these changes were attenuated with insulin treatment.	Disulfides	103-112	ryanodine receptor 2	Rattus norvegicus	43-47
3166978-2	1988	The results indicate that the four half-cystines in the extracellular domain of TF form two disulfide bonds and the half-cystine in the cytoplasmic region is acylated by palmitic acid and stearic acid.	Disulfides	92-101	coagulation factor III, tissue factor	Homo sapiens	80-82
3166978-7	1988	Deacylation of TF with hydroxylamine resulted in the spontaneous generation of disulfide-linked TF dimers.	Disulfides	79-88	coagulation factor III, tissue factor	Homo sapiens	15-17
3408716-2	1988	These forms have two chains disulfide linked and are of the same molecular weight as native antithrombin III.	Disulfides	28-37	serpin family C member 1	Homo sapiens	92-108
7504740-3	1994	The system was used to express two disulfide-bonded domains from gp120, the surface protein of human immunodeficiency virus type 1 (HIV-1), that include potent neutralization epitopes.	Disulfides	35-44	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	65-70
7505444-2	1993	It has been hypothesized that a disulfide bond might exist between Cys4057 of apolipoprotein(a) and Cys3734 in apolipoprotein B-100.	Disulfides	32-41	lipoprotein(a)	Homo sapiens	78-95
7505444-8	1993	Our results strongly suggest the existence of a disulfide bridge between Cys4057 of apolipoprotein(a) and apolipoprotein B-100 within recombinant lipoprotein(a) particles.	Disulfides	48-57	lipoprotein(a)	Homo sapiens	84-101
12743278-0	2003	Formation of disulfide-linked complexes between the three minor envelope glycoproteins (GP2b, GP3, and GP4) of equine arteritis virus.	Disulfides	13-22	glycoprotein 2b (GP2b)	Equine arteritis virus	88-92
8405431-1	1993	Lipase from Pseudomonas aeruginosa is a M(r) 29 kDa protein with a single functional disulfide bond as shown by a shift in electrophoretic mobility after treatment with dithiothreitol and iodoacetamide.	Disulfides	85-94	lipase	Staphylococcus aureus	0-6
3364984-8	1988	The data are consistent with approximately 1 mol of intramolecular disulfide per mole of protein being present in gamma II.	Disulfides	67-76	G protein subunit gamma 7	Bos taurus	114-122
3364984-9	1988	X-ray crystallography of gamma II has shown that the spatial location of Cys18 and Cys22 in the tertiary structure permits disulfide bond formation.	Disulfides	123-132	G protein subunit gamma 7	Bos taurus	25-33
12743278-0	2003	Formation of disulfide-linked complexes between the three minor envelope glycoproteins (GP2b, GP3, and GP4) of equine arteritis virus.	Disulfides	13-22	glycoprotein 3 (GP3)	Equine arteritis virus	94-97
12758148-14	2003	Since seven of the mutations were totally inactive, it is likely that these seven Cys residues play a role in maintaining an active conformation of soluble C2GnT1 by forming disulfide bonds.	Disulfides	174-183	glucosaminyl (N-acetyl) transferase 1	Homo sapiens	156-162
2832473-8	1988	In contrast, modification of any of the other 10 Cys residues, either singly or in combinations corresponding to the predicted disulfide bonds, greatly reduced the ability of the corresponding protein to bind IL-2 or either of two mAb (anti-Tac and 7G7/B6) which recognize the Tac protein.	Disulfides	127-136	interleukin 2	Mus musculus	209-213
8282724-10	1993	Disulfide bonds in brushin seemed to be necessary for the complex formation, since reductive cleavage of the bonds resulted in failure of the protein to associate with HBP-44 in a ligand blotting experiment.	Disulfides	0-9	low density lipoprotein receptor-related protein associated protein 1	Mus musculus	168-174
8344427-2	1993	Protein disulfide isomerase (PDI), which is believed to catalyze disulfide bond formation and associated protein folding in the endoplasmic reticulum, attacked the glutathionylated h-lysozyme C77A-a to dissociate the glutathione molecule.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
8344427-5	1993	These results strongly suggest that PDI can catalyze the disulfide formation in intermediates with compact structure like the native states in the later step of in vivo protein folding.	Disulfides	57-66	prolyl 4-hydroxylase subunit beta	Homo sapiens	36-39
12725245-4	2003	Thermolytic digestion demonstrated three disulfide bond pairings of the EGF-like domain in HB-EGF is consistent with that of human-EGF and human-TGF-alpha.	Disulfides	41-50	transforming growth factor alpha	Homo sapiens	145-154
7686555-1	1993	Thrombospondin-1 (TSP1) is a large modular matrix protein containing three identical disulfide-linked 180-kD chains that inhibits neovascularization in vivo (Good et al., 1990).	Disulfides	85-94	thrombospondin 1	Rattus norvegicus	0-16
7686555-1	1993	Thrombospondin-1 (TSP1) is a large modular matrix protein containing three identical disulfide-linked 180-kD chains that inhibits neovascularization in vivo (Good et al., 1990).	Disulfides	85-94	thrombospondin 1	Rattus norvegicus	18-22
2826432-1	1988	Phosphoribulokinase is light-regulated via thioredoxin by reversible oxidation/reduction of sulfhydryl/disulfide groups.	Disulfides	103-112	thioredoxin	Homo sapiens	43-54
2447879-4	1987	These results, taken with the fact that monomeric units of alpha 2M cannot bind these proteinases, strongly suggest that each active site of alpha 2M consists in a specific arrangement of two monomeric units linked by disulfide bridges.	Disulfides	218-227	alpha-2-macroglobulin	Homo sapiens	141-149
12591954-4	2003	NPC2 has an Ig-like fold stabilized by three disulfide bonds.	Disulfides	45-54	NPC intracellular cholesterol transporter 2	Homo sapiens	0-4
2822039-2	1987	These three ANF receptor subtypes include; (1) a disulfide-linked 140 kDa protein found in RTASM cells which was reduced by sulfhydryl reagent dithiothreitol (DTT) to a 70 kDa band, (2) a disulfide-unlinked 120 kDa protein, specific to MDCK cells whose Mr was not reduced by DTT and (3) a 68-70 kDa protein prevalent in both RTASM and MDCK cells whose Mr was not reduced by DTT.	Disulfides	49-58	natriuretic peptide A	Canis lupus familiaris	12-15
2822039-2	1987	These three ANF receptor subtypes include; (1) a disulfide-linked 140 kDa protein found in RTASM cells which was reduced by sulfhydryl reagent dithiothreitol (DTT) to a 70 kDa band, (2) a disulfide-unlinked 120 kDa protein, specific to MDCK cells whose Mr was not reduced by DTT and (3) a 68-70 kDa protein prevalent in both RTASM and MDCK cells whose Mr was not reduced by DTT.	Disulfides	188-197	natriuretic peptide A	Canis lupus familiaris	12-15
8518281-6	1993	A series of disulfide-bridged dimeric peptides containing the complete sequences of the G- and H-helices of myoglobin were synthesized and their conformational preferences examined.	Disulfides	12-21	myoglobin	Physeter catodon	108-117
12527141-6	2003	We here examine the agonistic efficacy of N-terminal rat alpha-CGRP peptides containing the disulfide bridge (Cys(2)-Cys(7)) with amidated C-terminal in prevention of HPH.	Disulfides	92-101	calcitonin-related polypeptide alpha	Rattus norvegicus	63-67
7685339-0	1993	Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein.	Disulfides	59-68	pappalysin 1	Homo sapiens	18-55
7685339-2	1993	PAPP-A isolated from pooled pregnancy serum is shown to be a disulfide-bridged complex with proMBP (PAPP-A/proMBP) in which the subunits of the constituents are present in a 1:1 molar ratio.	Disulfides	61-70	pappalysin 1	Homo sapiens	0-6
7685339-2	1993	PAPP-A isolated from pooled pregnancy serum is shown to be a disulfide-bridged complex with proMBP (PAPP-A/proMBP) in which the subunits of the constituents are present in a 1:1 molar ratio.	Disulfides	61-70	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	92-98
3115179-1	1987	Recombinant human interleukin-2 (rIL-2) produced in Escherichia coli possesses a free thiol group at Cys-125 and a disulfide linkage between Cys-58 and Cys-105, as in the case for natural human interleukin-2.	Disulfides	115-124	interleukin 2	Rattus norvegicus	33-38
3115179-2	1987	Treatment of rIL-2 with 200 mM dithiothreitol resulted in the cleavage of the Cys-58-Cys-105 disulfide bond.	Disulfides	93-102	interleukin 2	Rattus norvegicus	13-18
3597437-16	1987	Human bone osteonectin contains a large number of cysteines, more than 90% of which appear to be in disulfide bonds.	Disulfides	100-109	secreted protein acidic and cysteine rich	Bos taurus	11-22
2443487-11	1987	By analogy with human alpha 2M, the 35 kDa subunit would be located at the C-terminal end of murine alpha 2M, disulfide-bonded to the major 165 kDa subunit.	Disulfides	110-119	alpha-2-macroglobulin	Homo sapiens	22-30
7685339-2	1993	PAPP-A isolated from pooled pregnancy serum is shown to be a disulfide-bridged complex with proMBP (PAPP-A/proMBP) in which the subunits of the constituents are present in a 1:1 molar ratio.	Disulfides	61-70	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	100-113
8461300-1	1993	To study the substrate specificity and mechanism of thioltransferase (TTase) catalysis, we have used 14C- and 35S-radiolabeled mixed disulfides of cysteine and glutathione (GSH) with various cysteine-containing proteins.	Disulfides	133-143	glutaredoxin	Homo sapiens	52-68
8461300-1	1993	To study the substrate specificity and mechanism of thioltransferase (TTase) catalysis, we have used 14C- and 35S-radiolabeled mixed disulfides of cysteine and glutathione (GSH) with various cysteine-containing proteins.	Disulfides	133-143	glutaredoxin	Homo sapiens	70-75
8461300-4	1993	GSH-dependent dethiolation of [35S]glutathione-papain mixed disulfide (papain-SSG) and the corresponding bovine serum albumin mixed disulfide (BSA-SSG) were catalyzed by thioltransferase (from human red blood cells) as shown by the radiolabel assay, and equivalent rates were measured by the spectrophotometric assay.	Disulfides	60-69	glutaredoxin	Homo sapiens	170-186
8461300-4	1993	GSH-dependent dethiolation of [35S]glutathione-papain mixed disulfide (papain-SSG) and the corresponding bovine serum albumin mixed disulfide (BSA-SSG) were catalyzed by thioltransferase (from human red blood cells) as shown by the radiolabel assay, and equivalent rates were measured by the spectrophotometric assay.	Disulfides	132-141	glutaredoxin	Homo sapiens	170-186
3593416-6	1987	The amount of mixed disulfides produced and the kinetics of their formation were dependent on both the intracellular GSH/GSSG ratio and the activity of glutathione reductase.	Disulfides	20-30	glutathione-disulfide reductase	Rattus norvegicus	152-173
14695918-1	2003	Our laboratories have described a novel class of ectoproteins at the cell surface with both NADH or hydroquinone oxidase (NOX) and protein disulfide-thiol interchange activities (ECTO-NOX proteins).	Disulfides	139-148	tripartite motif containing 33	Homo sapiens	179-183
8461300-5	1993	Dethiolation of [35S]hemoglobin-glutathione mixed disulfide (Hb-SSG) was also catalyzed by TTase.	Disulfides	50-59	glutaredoxin	Homo sapiens	91-96
15969027-11	2003	Studies on the refolding of prochymosin unequivocally demonstrated that the formation of native disulfides is the prerequisite to the recovery of the native conformation.	Disulfides	96-106	chymosin	Bos taurus	28-39
8457543-7	1993	The disulfide bridge pairings were chemically determined for sP05-NH2 and thereby deduced for P05 and leiurotoxin I: linkages were between Cys3 and Cys21, Cys8 and Cys26, and Cys12 and Cys28.	Disulfides	4-13	cystathionase (cystathionine gamma-lyase)	Mus musculus	139-143
8386013-6	1993	The result strongly implicates Cys3734 of apo B-100 as the residue forming the disulfide linkage with Cys4057 of apo[a].	Disulfides	79-88	lipoprotein(a)	Homo sapiens	113-118
8386013-13	1993	These results support and extend previously suggested mechanisms for a complex interaction between apo[a] and apo B-100 that involve more than a simple covalent disulfide bond.	Disulfides	161-170	lipoprotein(a)	Homo sapiens	99-104
2430963-2	1986	The disulfide bridge pattern of human alpha 2-macroglobulin (alpha 2M) given earlier (Sottrup-Jensen, L., Stepanik, T. M., Kristensen, T., Wierzbicki, D. M., Jones, C. M., Lonblad, P. B., Magnusson, S., and Petersen, T. E. (1984) J. Biol.	Disulfides	4-13	alpha-2-macroglobulin	Homo sapiens	38-59
2430963-2	1986	The disulfide bridge pattern of human alpha 2-macroglobulin (alpha 2M) given earlier (Sottrup-Jensen, L., Stepanik, T. M., Kristensen, T., Wierzbicki, D. M., Jones, C. M., Lonblad, P. B., Magnusson, S., and Petersen, T. E. (1984) J. Biol.	Disulfides	4-13	alpha-2-macroglobulin	Homo sapiens	61-69
2430963-5	1986	Thus, the alpha 2M-dimer contains two interchain disulfide bridges, and the individual subunits are arranged in an antiparallel fashion.	Disulfides	49-58	alpha-2-macroglobulin	Homo sapiens	10-18
2430963-8	1986	The disulfide bridge pattern of alpha 2M has been completed by showing that the alpha 2M subunit contains 11 intrachain bridges, including a bridge connecting Cys447 with Cys540.	Disulfides	4-13	alpha-2-macroglobulin	Homo sapiens	32-40
2430963-8	1986	The disulfide bridge pattern of alpha 2M has been completed by showing that the alpha 2M subunit contains 11 intrachain bridges, including a bridge connecting Cys447 with Cys540.	Disulfides	4-13	alpha-2-macroglobulin	Homo sapiens	80-88
12370176-11	2002	Interestingly, the proteolytically inactive, disulfide-bound complex of PAPP-A and the proform of eosinophil major basic protein (proMBP), PAPP-A.proMBP, shows only weak surface binding, probably because the adhesion site of PAPP-A is occupied by heparan sulfate, known to be covalently bound to proMBP.	Disulfides	45-54	pappalysin 1	Homo sapiens	72-78
3490668-3	1986	This report describes solution NMR data that provide evidence that the solution conformation of murine EGF includes an anti-parallel beta-sheet structure involving residues S2-P4, V19-I23, and S28-N32; a small anti-parallel beta-sheet involving residues Y37-S38 and T44-R45; and a multiple-bend (or short irregular helix) structure for residues C6-C14 that is disulfide bonded to the V19-I23/S28-N32 beta-sheet.	Disulfides	360-369	epidermal growth factor	Mus musculus	103-106
3531211-5	1986	The disulfide arrangement of the active TGF alpha was determined after digestion with thermolysin, and found to be analogous to the disulfide arrangement previously determined for EGF (Savage, C. R., Hash, J. H., and Cohen, S. (1973) J. Biol.	Disulfides	132-141	epidermal growth factor	Homo sapiens	180-183
8438588-6	1993	Gp160t, gp160t/sec, and gp120 formed oligomers which were stabilized by intermolecular disulfide bonds and/or noncovalent interactions and were also found to bind to soluble CD4.	Disulfides	87-96	glutamyl aminopeptidase	Homo sapiens	8-13
8374001-7	1993	Second, single cysteine substitutions in PRPs (Pa from PRH1 and G1 8 from PRB3) may lead to disulfide bonded homodimers as well as heterodimers with salivary peroxidase.	Disulfides	92-101	G protein signaling modulator 3	Homo sapiens	64-68
12370176-11	2002	Interestingly, the proteolytically inactive, disulfide-bound complex of PAPP-A and the proform of eosinophil major basic protein (proMBP), PAPP-A.proMBP, shows only weak surface binding, probably because the adhesion site of PAPP-A is occupied by heparan sulfate, known to be covalently bound to proMBP.	Disulfides	45-54	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	98-128
1472500-0	1992	Disulfide bond assignment in human J chain and its covalent pairing with immunoglobulin M. The assignment of disulfide bonds in human J chain and its covalent pairing with immunoglobulin M was determined under conditions which minimize disulfide bond interchange.	Disulfides	0-9	joining chain of multimeric IgA and IgM	Homo sapiens	35-42
12370176-11	2002	Interestingly, the proteolytically inactive, disulfide-bound complex of PAPP-A and the proform of eosinophil major basic protein (proMBP), PAPP-A.proMBP, shows only weak surface binding, probably because the adhesion site of PAPP-A is occupied by heparan sulfate, known to be covalently bound to proMBP.	Disulfides	45-54	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	130-136
1472500-0	1992	Disulfide bond assignment in human J chain and its covalent pairing with immunoglobulin M. The assignment of disulfide bonds in human J chain and its covalent pairing with immunoglobulin M was determined under conditions which minimize disulfide bond interchange.	Disulfides	0-9	joining chain of multimeric IgA and IgM	Homo sapiens	134-141
1472500-0	1992	Disulfide bond assignment in human J chain and its covalent pairing with immunoglobulin M. The assignment of disulfide bonds in human J chain and its covalent pairing with immunoglobulin M was determined under conditions which minimize disulfide bond interchange.	Disulfides	109-118	joining chain of multimeric IgA and IgM	Homo sapiens	35-42
1472500-0	1992	Disulfide bond assignment in human J chain and its covalent pairing with immunoglobulin M. The assignment of disulfide bonds in human J chain and its covalent pairing with immunoglobulin M was determined under conditions which minimize disulfide bond interchange.	Disulfides	109-118	joining chain of multimeric IgA and IgM	Homo sapiens	134-141
1472036-0	1992	Identification of a disulfide bridge connecting the alpha-subunits of the extracellular domain of the insulin receptor.	Disulfides	20-29	insulin receptor	Homo sapiens	102-118
3818560-2	1986	On SDS-polyacrylamide gel electrophoresis in either the presence or absence of dithiothreitol, GPIV gave a single band with an apparent molecular weight of 97,000, suggesting that GPIV is composed of a single polypeptide chain without interchain disulfide bonds.	Disulfides	246-255	CD36 molecule	Homo sapiens	95-99
3818560-2	1986	On SDS-polyacrylamide gel electrophoresis in either the presence or absence of dithiothreitol, GPIV gave a single band with an apparent molecular weight of 97,000, suggesting that GPIV is composed of a single polypeptide chain without interchain disulfide bonds.	Disulfides	246-255	CD36 molecule	Homo sapiens	180-184
2419904-8	1986	Conservation of disulfide bridges and of amino acids thought to compose the iron binding pockets suggests that p97 is also related to transferrin in tertiary structure and function.	Disulfides	16-25	melanotransferrin	Homo sapiens	111-114
1472036-1	1992	The alpha 2 beta 2 structure of the insulin receptor has previously been shown to involve one disulfide bridge between the alpha-subunits in the region containing Cys435, Cys468 and Cys524.	Disulfides	94-103	insulin receptor	Homo sapiens	36-52
12370176-11	2002	Interestingly, the proteolytically inactive, disulfide-bound complex of PAPP-A and the proform of eosinophil major basic protein (proMBP), PAPP-A.proMBP, shows only weak surface binding, probably because the adhesion site of PAPP-A is occupied by heparan sulfate, known to be covalently bound to proMBP.	Disulfides	45-54	pappalysin 1	Homo sapiens	139-145
1472036-4	1992	Since it has been shown that the extracellular domain of the insulin receptor has no free thiols and since no other sequences containing cysteine were found in these fractions, we conclude that Cys524 forms a disulfide bond to the Cys524 in the other alpha-subunit.	Disulfides	209-218	insulin receptor	Homo sapiens	61-77
12370176-11	2002	Interestingly, the proteolytically inactive, disulfide-bound complex of PAPP-A and the proform of eosinophil major basic protein (proMBP), PAPP-A.proMBP, shows only weak surface binding, probably because the adhesion site of PAPP-A is occupied by heparan sulfate, known to be covalently bound to proMBP.	Disulfides	45-54	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	146-152
2420357-1	1986	An alpha-macroglobulin (alpha 2M), which is a dimer consisting of two non-disulfide-bonded subunits, was identified and purified from frog plasma by Ni2+ chelate affinity chromatography.	Disulfides	74-83	alpha-2-macroglobulin	Homo sapiens	24-32
12370176-11	2002	Interestingly, the proteolytically inactive, disulfide-bound complex of PAPP-A and the proform of eosinophil major basic protein (proMBP), PAPP-A.proMBP, shows only weak surface binding, probably because the adhesion site of PAPP-A is occupied by heparan sulfate, known to be covalently bound to proMBP.	Disulfides	45-54	pappalysin 1	Homo sapiens	139-145
12370176-11	2002	Interestingly, the proteolytically inactive, disulfide-bound complex of PAPP-A and the proform of eosinophil major basic protein (proMBP), PAPP-A.proMBP, shows only weak surface binding, probably because the adhesion site of PAPP-A is occupied by heparan sulfate, known to be covalently bound to proMBP.	Disulfides	45-54	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	146-152
12491104-7	2002	The glycoprotein gp150 formed oligomers held by disulfide bonding.	Disulfides	48-57	alanyl aminopeptidase, membrane	Homo sapiens	17-22
3484639-0	1986	Complete amino acid sequence and location of the five disulfide bridges in porcine pancreatic alpha-amylase.	Disulfides	54-63	amylase alpha 2A	Homo sapiens	83-107
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	Disulfides	190-199	xanthine dehydrogenase	Homo sapiens	166-169
1400510-1	1992	Angiogenin is a 14.4-kDa human plasma protein with 65% homology to RNase A that retains the key active site residues and three of the four RNase A disulfide bonds.	Disulfides	147-156	angiogenin	Homo sapiens	0-10
1400510-1	1992	Angiogenin is a 14.4-kDa human plasma protein with 65% homology to RNase A that retains the key active site residues and three of the four RNase A disulfide bonds.	Disulfides	147-156	ribonuclease A family member 1, pancreatic	Homo sapiens	67-74
12324460-0	2002	Dual effects of an extra disulfide bond on the activity and stability of a cold-adapted alpha-amylase.	Disulfides	25-34	LOW QUALITY PROTEIN: pancreatic alpha-amylase	Sus scrofa	88-101
1505516-6	1992	Indeed, replacing the transmembrane domain of the Tac antigen (alpha chain of the interleukin-2 receptor) by that of the zeta chain resulted in the formation of disulfide-linked dimers of Tac.	Disulfides	161-170	interleukin 2 receptor subunit alpha	Homo sapiens	50-61
3002789-5	1986	Chemical and model-building studies suggest that the pair Cys-43/Cys-93 forms a disulfide in native AK2.	Disulfides	80-89	adenylate kinase 2	Bos taurus	100-103
3492399-3	1986	Reduction-carboxymethylation and reduction-mercuration resulted in complete loss of Meg-CSF and Epo activities, suggesting that one of the essential chemical groups of Meg-CSF and Epo is a disulfide bond.	Disulfides	189-198	colony stimulating factor 2	Homo sapiens	88-91
12239218-0	2002	Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain.	Disulfides	47-56	calnexin	Homo sapiens	0-8
4084533-3	1985	Comparisons of the NMR results obtained for the hinge fragment with those for the intact IgG1 and its fragments led us to conclude that a significant change in conformation of the segment preceding the disulfide-linked Cys-Pro-Pro-Cys core is induced when the Fab portion is cleaved off and the presence or absence of the Fc portion affects very little, if any, of the conformation of this part of the hinge.	Disulfides	202-211	FA complementation group B	Homo sapiens	260-263
12547227-3	2002	Hephaestin is homologous to the plasma copper-containing protein ceruloplasmin, and all residues involved in copper binding and disulfide bond formation in ceruloplasmin are conserved in hephaestin.	Disulfides	128-137	hephaestin	Mus musculus	187-197
2935182-3	1985	The F(ab")2 fragment of one monoclonal (B5) that is specific for the Fab region of IgER was labeled with donor probes and bound to IgER, and the quenching of the fluorescence of these donors due to simultaneous binding of the Fab" fragment of an anti-Fc monoclonal (A2) that was labeled with an acceptor probe at its interchain disulfide bond was measured.	Disulfides	328-337	FA complementation group B	Homo sapiens	69-72
2410908-6	1985	The results suggest that disulfide linkage of the alpha and beta 2 subunits, insertion into the cell surface membrane, and attainment of a functional conformation are closely related late events in the biogenesis of the Na channel.	Disulfides	25-34	sodium voltage-gated channel alpha subunit 8	Rattus norvegicus	220-230
3986191-9	1985	Analyses of bovine antithrombin in 6 M GdmCl indicated that the second transition reflects the total unfolding of the protein to a disulfide-cross-linked random coil.	Disulfides	131-140	serpin family C member 1	Homo sapiens	19-31
1501280-1	1992	In the spherical capsid of hepatitis B virus (HBV), intermolecular disulfide bonds cross-link the approximately 180 p21.5 capsid protein subunits into a stable lattice.	Disulfides	67-76	cyclin-dependent kinase inhibitor 1A L homeolog	Xenopus laevis	116-119
1321713-1	1992	The thioredoxin system, comprising NADPH, thioredoxin reductase and thioredoxin reduces protein disulfides via redox-active dithiols.	Disulfides	96-106	thioredoxin	Bos taurus	4-15
1321713-1	1992	The thioredoxin system, comprising NADPH, thioredoxin reductase and thioredoxin reduces protein disulfides via redox-active dithiols.	Disulfides	96-106	thioredoxin	Bos taurus	42-53
1624802-4	1992	Immunologic analyses indicated that the secreted baculovirus p42 (BVp42) expressed native, disulfide-dependent conformational epitopes, whereas these epitopes were poorly represented in the intracellular yeast p42.	Disulfides	91-100	cyclin-dependent kinase 20	Mus musculus	61-64
1624802-4	1992	Immunologic analyses indicated that the secreted baculovirus p42 (BVp42) expressed native, disulfide-dependent conformational epitopes, whereas these epitopes were poorly represented in the intracellular yeast p42.	Disulfides	91-100	cyclin-dependent kinase 20	Mus musculus	68-71
12183464-6	2002	The final products of human and bovine ALR2 oxidation contained the intramolecular disulfide bond Cys(298)-Cys(303).	Disulfides	83-92	lens aldose reductase pseudogene	Bos taurus	39-43
2986311-5	1985	The purified thrombomodulin was inactivated by disulfide bond reduction, but was stable to heat, pH extremes and protein denaturants.	Disulfides	47-56	thrombomodulin	Homo sapiens	13-27
12403808-4	2002	We show that upon oxidation of the COOH-terminal disulfide bond in PDI by the enzyme Ero1, the A1 chain is released.	Disulfides	49-58	prolyl 4-hydroxylase subunit beta	Homo sapiens	67-70
2578194-8	1985	We suggest that (i) gC1 and gC2 arise by proteolytic cleavage from the same precursor molecule and stay joined via disulfide bridges and (ii) gC0 is an uncleaved precursor.	Disulfides	115-124	solute carrier family 25 member 22	Homo sapiens	20-23
1413252-3	1992	This indicates that the arms of the molecules are relatively free to move and the binding to the mica substrate is located near the disulfide bridge between the two subunits of the molecule.	Disulfides	132-141	MHC class I polypeptide-related sequence A	Homo sapiens	97-101
12389098-5	2002	Here we further analyzed the two IgNAR types, "type 1" having one cysteine in CDR3 and "type 2" with an even number (two or four) of CDR3 cysteines, and discovered that placement of the disulfide bridges in the IgNAR V domain differentially influences the selection of mutations in CDR1 and CDR2.	Disulfides	186-195	cerebellar degeneration related protein 2	Homo sapiens	291-295
1627147-3	1992	The disulfide structures of fully active synthetic elafin and the inactive product were determined by amino acid analysis, gas-phase sequencing and mass spectrometry of their proteolytic fragments.	Disulfides	4-13	peptidase inhibitor 3	Homo sapiens	51-57
1534287-1	1992	BACKGROUND: Lipoprotein(a) [Lp(a)] is a low density lipoprotein-like particle whose apolipoprotein B (apo B) moiety is disulfide-linked to apo(a), a plasminogen-like inhibitor of fibrinolysis in vitro.	Disulfides	119-128	lipoprotein(a)	Homo sapiens	12-26
3918304-4	1985	These findings imply that intramolecular disulfide bonds affect native p21 conformation.	Disulfides	41-50	H3 histone pseudogene 16	Homo sapiens	71-74
12354420-1	2002	Skin sulfhydryl oxidase (SOx) is an enzyme that catalyzes disulfide (S-S) cross-linking through the oxidation of sulfhydryl compounds in the skin.	Disulfides	58-67	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	0-23
6438823-0	1984	Structure-function relationships of human factor VIII complex studied by thioredoxin dependent disulfide reduction.	Disulfides	95-104	thioredoxin	Homo sapiens	73-84
1534287-1	1992	BACKGROUND: Lipoprotein(a) [Lp(a)] is a low density lipoprotein-like particle whose apolipoprotein B (apo B) moiety is disulfide-linked to apo(a), a plasminogen-like inhibitor of fibrinolysis in vitro.	Disulfides	119-128	lipoprotein(a)	Homo sapiens	28-33
12354420-1	2002	Skin sulfhydryl oxidase (SOx) is an enzyme that catalyzes disulfide (S-S) cross-linking through the oxidation of sulfhydryl compounds in the skin.	Disulfides	58-67	quiescin Q6 sulfhydryl oxidase 1	Mus musculus	25-28
6484310-2	1984	As based on polyacrylamide disc electrophoresis, inactivation of the testicular isozyme, LDH-X, was almost complete with penicillamine and its disulfide, somewhat less with GSH and GSSG, least with thioglycolate and its disulfide and inconsistent with cysteine, 2-mercaptoethanol and 2-mercaptoethylamine.	Disulfides	143-152	lactate dehydrogenase C	Homo sapiens	89-94
6484310-2	1984	As based on polyacrylamide disc electrophoresis, inactivation of the testicular isozyme, LDH-X, was almost complete with penicillamine and its disulfide, somewhat less with GSH and GSSG, least with thioglycolate and its disulfide and inconsistent with cysteine, 2-mercaptoethanol and 2-mercaptoethylamine.	Disulfides	220-229	lactate dehydrogenase C	Homo sapiens	89-94
1612175-6	1992	The results provide evidence that the 150 kDa glycopeptide so-called salivary mucin "link" component is neither an integral part of the mucin molecule, nor linked to mucin subunits by disulfide bonds, but is a fibronectin fragment which associates with <protein-id="4585">mucin.	Disulfides	184-193	LOC100508689	Homo sapiens	78-83
12234918-0	2002	The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.	Disulfides	4-13	putative protein DsbC	Escherichia coli	29-33
1409556-2	1992	Like mature uteroglobin from rabbit endometrium (UG), the E.coli produced uteroglobin (UG1) dimerizes in vitro, forms an antiparallel dimer with Cys3-Cys69" and Cys69-Cys3" disulfide bonds and binds progesterone under reducing conditions.	Disulfides	173-182	uteroglobin	Oryctolagus cuniculus	74-85
6203906-2	1984	Primary structure of three large disulfide-bridged CNBr fragments, located in the COOH-terminal part of alpha 2-macroglobulin and accounting for 301 residues.	Disulfides	33-42	alpha-2-macroglobulin	Homo sapiens	104-125
6203906-3	1984	The amino acid sequences have been determined for three CNBr fragments of human alpha 2-macroglobulin which form a disulfide-bridged Mr = 40,000 fragment set.	Disulfides	115-124	alpha-2-macroglobulin	Homo sapiens	80-101
12234918-0	2002	The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDalpha complex.	Disulfides	4-13	putative protein DsbC	Escherichia coli	120-124
1567868-0	1992	Conserved residues flanking the thiol/disulfide centers of protein disulfide isomerase are not essential for catalysis of thiol/disulfide exchange.	Disulfides	38-47	prolyl 4-hydroxylase subunit beta	Homo sapiens	59-86
12234918-1	2002	The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding.	Disulfides	21-30	putative protein DsbC	Escherichia coli	46-50
1567868-1	1992	Protein disulfide isomerase (PDI) catalyzes the oxidative folding of proteins containing disulfide bonds by increasing the rate of disulfide bond rearrangements which normally occur during the folding process.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
1567868-1	1992	Protein disulfide isomerase (PDI) catalyzes the oxidative folding of proteins containing disulfide bonds by increasing the rate of disulfide bond rearrangements which normally occur during the folding process.	Disulfides	89-98	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
1567868-1	1992	Protein disulfide isomerase (PDI) catalyzes the oxidative folding of proteins containing disulfide bonds by increasing the rate of disulfide bond rearrangements which normally occur during the folding process.	Disulfides	89-98	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
1387094-1	1992	Lipoprotein(a), or Lp(a), is a lipoprotein having lipid composition similar to that of LDL, but a protein moiety consisting of ApoB 100 linked by disulfide bridge to apo(a), a glycoprotein with structural similarity to plasminogen.	Disulfides	146-155	lipoprotein(a)	Homo sapiens	19-24
12234918-1	2002	The Escherichia coli disulfide bond isomerase DsbC rearranges incorrect disulfide bonds during oxidative protein folding.	Disulfides	72-81	putative protein DsbC	Escherichia coli	46-50
12119363-3	2002	Dissection of the degradation process revealed that upon release from calnexin, extensively oxidized BACE457 transiently entered in disulfide-bonded complexes associated with the lumenal chaperones BiP and protein disulfide isomerase (PDI) before unfolding and dislocation into the cytosol for degradation.	Disulfides	132-141	calnexin	Homo sapiens	70-78
1314748-4	1992	The remaining 50% reacted with the BB3 monoclonal antibody, which recognizes products of the V gamma 9/V delta 2 rearrangement and the disulfide-linked form of receptor.	Disulfides	135-144	bombesin receptor subtype 3	Homo sapiens	35-38
12022871-11	2002	A model of human TGH structure suggested a lipase alpha/beta hydrolase fold with a buried active site and two disulfide bridges (C87-C116 and C274-C285).	Disulfides	110-119	carboxylesterase 1	Homo sapiens	17-20
1569180-9	1992	These data suggest that when isolated from patient plasma, FVIII-EH cysteine-1689 is present in a disulfide bond.	Disulfides	98-107	coagulation factor VIII	Homo sapiens	59-64
12009896-0	2002	Identification of human vesicle monoamine transporter (VMAT2) lumenal cysteines that form an intramolecular disulfide bond.	Disulfides	108-117	solute carrier family 18 member A2	Homo sapiens	55-60
1371696-7	1992	However, instead of the two most C-terminal cysteines in alpha 2-macroglobulin, which forms a disulfide bridge in the receptor binding domain, alpha 1-macroglobulin contains phenylalanine.	Disulfides	94-103	alpha-2-macroglobulin	Rattus norvegicus	57-78
12009896-10	2002	We conclude that human VMAT2 Cys 126 in loop 1/2 and Cys 333 in loop 7/8 form a disulfide bond which contributes to efficient monoamine transport.	Disulfides	80-89	solute carrier family 18 member A2	Homo sapiens	23-28
11875066-2	2002	The fragments contained one or both cysteine residues (amino acids 524 and 682) that form disulfides between alpha-subunits in native IR.	Disulfides	90-100	insulin receptor	Homo sapiens	134-136
1371577-10	1992	Several leucine zippers are located on the hydrophobic face of the alpha-helix in paramyosin which, together with disulfide bonds between cysteines, are probably involved in the stabilization of the dimer.	Disulfides	114-123	Paramyosin	Drosophila melanogaster	82-92
6378631-6	1984	Evidence is presented that the acrosin light chain is connected via two disulfide bridges to the heavy chain which contains about 320 amino acids including the active-site residues of the proteinase.	Disulfides	72-81	acrosin	Homo sapiens	31-38
6209020-1	1984	Epidermal growth factor (EGF) was derivatized at the amino terminus with N-succinimidyl 3-(2-pyridyldithio)propionate and then cross-linked to the cysteinyl residues of alpha 2-macroglobulin (alpha 2M) via disulfide bonds.	Disulfides	206-215	epidermal growth factor	Mus musculus	0-23
6209020-1	1984	Epidermal growth factor (EGF) was derivatized at the amino terminus with N-succinimidyl 3-(2-pyridyldithio)propionate and then cross-linked to the cysteinyl residues of alpha 2-macroglobulin (alpha 2M) via disulfide bonds.	Disulfides	206-215	epidermal growth factor	Mus musculus	25-28
1319549-6	1992	The loss of thioredoxin reductase activity promoted by NADPH was much faster and complete in the presence of NAD+ glycohydrolase, thus suggesting that inactivation was related to full reduction of the redox-active disulfide.	Disulfides	214-223	thioredoxin	Bos taurus	12-23
11982363-0	2002	Development of a novel method to populate native disulfide-bonded intermediates for structural characterization of proteins: implications for the mechanism of oxidative folding of RNase A.	Disulfides	49-58	ribonuclease A family member 1, pancreatic	Homo sapiens	180-187
12192853-1	2002	The formation of disulfide bonds in secreted proteins of E. coli is a synergetic process depending on a series of Dsb proteins containing DsbA, DsbB, DsbC, DsbD, DsbE and DsbG.	Disulfides	17-26	putative protein DsbC	Escherichia coli	150-154
1530858-6	1992	Furthermore, functional studies showed that triggering this disulfide-linked dimer through BB18 epitope in the presence of submitogenic concentrations of PMA induced strong lymphocyte proliferation.	Disulfides	60-69	semaphorin 4D	Homo sapiens	91-95
6202699-6	1984	This form of myotendinous antigen is a large glycoprotein complex consisting of several disulfide linked subunits (Mr approximately 150,000-240,000).	Disulfides	88-97	tenascin C	Gallus gallus	13-33
12192853-3	2002	Both DsbC and DsbG, two periplasmic proteins with isomerase activity, can correct mis-paired disulfide bonds introduced by DsbA although they recognize different substrates.	Disulfides	93-102	putative protein DsbC	Escherichia coli	5-9
6201733-9	1984	Therefore, the results suggest that reduction of most or all the inter-chain disulfide bonds, in rat as in human IgE, induces changes in quaternary structure, more especially in the relationship between the Fab and Fc parts of the molecule, leading to steric blockade, by Fab, of the binding sites for mast cells present on Fc.	Disulfides	77-86	FA complementation group B	Homo sapiens	207-210
6201733-9	1984	Therefore, the results suggest that reduction of most or all the inter-chain disulfide bonds, in rat as in human IgE, induces changes in quaternary structure, more especially in the relationship between the Fab and Fc parts of the molecule, leading to steric blockade, by Fab, of the binding sites for mast cells present on Fc.	Disulfides	77-86	FA complementation group B	Homo sapiens	272-275
1294187-11	1992	Covalent polymerization products, mainly formed during storage of amorphously suspended insulin at higher temperature, were shown to be due to disulfide interactions.	Disulfides	143-152	insulin	Oryctolagus cuniculus	88-95
12192853-6	2002	All DsbA, DsbC and DsbG have chaperone activity besides involving in the formation of disulfide bonds.	Disulfides	86-95	putative protein DsbC	Escherichia coli	10-14
12192853-8	2002	There are a few reports dealing with soluble expression of heterologous proteins containing disulfide bonds assisted by DsbA and DsbC in E. coli.	Disulfides	92-101	putative protein DsbC	Escherichia coli	129-133
1738091-4	1992	Mutant gp120 molecules lacking both disulfide bonds were not stably expressed or exported.	Disulfides	36-45	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	7-12
6693405-8	1984	The site of labeling corresponds to Trp 49, which is located within the disulfide-stabilized loops near the NH2-terminal end of the antithrombin III molecule.	Disulfides	72-81	serpin family C member 1	Homo sapiens	132-148
11782484-1	2002	Phosphoglycerate kinase (PGK) is secreted by tumor cells and facilitates reduction of disulfide bond(s) in plasmin (Lay, A. J., Jiang, X.-M., Kisker, O., Flynn, E., Underwood, A., Condron, R., and Hogg, P. J.	Disulfides	86-95	plasminogen	Homo sapiens	107-114
6358356-6	1983	The primary cleavage for the IgG2a heavy chain appears to be on the COOH terminal side of the interheavy chain disulfides, and secondary cleavage is on the NH2-terminal side.	Disulfides	111-121	immunoglobulin heavy variable V1-9	Mus musculus	29-34
6860677-1	1983	A synthetic model peptide, (formula; see text) which mimics the active-site disulfide loop of thioredoxin has been prepared.	Disulfides	76-85	thioredoxin	Homo sapiens	94-105
6860677-7	1983	Large structural differences have been established between the thioredoxin active-site model disulfide and its acyclic precursor.	Disulfides	93-102	thioredoxin	Homo sapiens	63-74
6304440-1	1983	The enkephalin analogs, [D-Pen2,L-Cys5]- and [D-Pen2,D-Cys5]-enkephalin are cyclic compounds, conformationally constrained by virtue of their 14-membered, disulfide containing rings and by the rigidizing effect of the beta, beta dimethyl substituents of the penicillamine side chain.	Disulfides	155-164	proenkephalin	Rattus norvegicus	4-14
6304440-1	1983	The enkephalin analogs, [D-Pen2,L-Cys5]- and [D-Pen2,D-Cys5]-enkephalin are cyclic compounds, conformationally constrained by virtue of their 14-membered, disulfide containing rings and by the rigidizing effect of the beta, beta dimethyl substituents of the penicillamine side chain.	Disulfides	155-164	proenkephalin	Rattus norvegicus	61-71
1794612-2	1991	The pro-region of POMC is 49 amino acid long with two disulfide bonds between cysteine residues 2 and 24 and 8 and 20.	Disulfides	54-63	pro-opiomelanocortin-alpha	Mus musculus	18-22
1944272-2	1991	p190MET is a heterodimer composed of two disulfide-linked chains of 50 kDa (p50 alpha) and 145 kDa (p145 beta).	Disulfides	41-50	contactin associated protein 1	Homo sapiens	0-4
1724753-2	1991	Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis of HABP under reducing as well as nonreducing conditions revealed a single protein band of 34 kDa, thus indicating that kidney HABP is a homodimer and lacks interchain disulfide bond.	Disulfides	246-255	hyaluronan binding protein 2	Rattus norvegicus	205-209
12096896-1	2002	A 480-kDa disulfide-linked heterodimer single-pass transmembrane protein, the insulin receptor, is autophosphorylated upon insulin binding to its extracellular domain.	Disulfides	10-19	insulin receptor	Homo sapiens	78-94
1915897-0	1991	Formation of enzyme-substrate disulfide linkage during catalysis by protein disulfide isomerase.	Disulfides	30-39	prolyl 4-hydroxylase subunit beta	Homo sapiens	68-95
1915897-1	1991	During the regeneration of native ribonuclease A (RNase) from the disulfide scrambled molecule by protein disulfide isomerase (PDI), the substrate forms a covalent intermediate with the enzyme through disulfide linkage(s).	Disulfides	66-75	prolyl 4-hydroxylase subunit beta	Homo sapiens	98-125
1915897-1	1991	During the regeneration of native ribonuclease A (RNase) from the disulfide scrambled molecule by protein disulfide isomerase (PDI), the substrate forms a covalent intermediate with the enzyme through disulfide linkage(s).	Disulfides	66-75	prolyl 4-hydroxylase subunit beta	Homo sapiens	127-130
1915897-1	1991	During the regeneration of native ribonuclease A (RNase) from the disulfide scrambled molecule by protein disulfide isomerase (PDI), the substrate forms a covalent intermediate with the enzyme through disulfide linkage(s).	Disulfides	106-115	prolyl 4-hydroxylase subunit beta	Homo sapiens	127-130
6871261-9	1983	It is concluded that in Ca2+-saturated alpha-lactalbumin some tryptophane residues are located near the quenching groups (dynamic quenching), most likely the disulfide bridges.	Disulfides	158-167	lactalbumin alpha	Bos taurus	39-56
6602098-4	1983	Prior to erythrocyte sensitization, the agglutinator site on Fab fragments can be blocked by thiol-disulfide exchange.	Disulfides	99-108	FA complementation group B	Homo sapiens	61-64
11807788-7	2002	These results clearly indicate that BCRP forms a homodimer bridged by disulfide bonds.	Disulfides	70-79	ATP binding cassette subfamily G member 2 (Junior blood group)	Mus musculus	36-40
7096325-4	1982	About one-third of C9 in this C5b-9 complex was found to be in a disulfide-linked dimeric form.	Disulfides	65-74	complement C5	Homo sapiens	30-33
1892325-5	1991	Reduction not only cleaves the mucin molecule but opens, presumably by breaking intramolecular disulfide bonds, cryptic "naked" protein regions.	Disulfides	95-104	LOC100508689	Homo sapiens	31-36
11795890-11	2002	Molecular models of oxidized TXNPx show C52 disulfide-bridged with C173" that can be attacked by C41 of TXN2.	Disulfides	44-53	tryparedoxin peroxidase	Leishmania donovani	29-34
1837065-1	1991	Lipoprotein(a) [Lp(a)] is a low density lipoprotein which has apo(a) disulfide-linked to apoB100.	Disulfides	69-78	lipoprotein(a)	Homo sapiens	0-14
1837065-1	1991	Lipoprotein(a) [Lp(a)] is a low density lipoprotein which has apo(a) disulfide-linked to apoB100.	Disulfides	69-78	lipoprotein(a)	Homo sapiens	16-21
6180768-1	1982	Localization by synthesis of antigenic site 4 of bovine serum albumin to the region around the disulfide bond 166-175.	Disulfides	95-104	albumin	Oryctolagus cuniculus	56-69
11698394-10	2002	In accordance with this, DmGCLC and DmGCLM have the ability to form reversible intermolecular disulfide bridges.	Disulfides	94-103	Glutamate-cysteine ligase modifier subunit	Drosophila melanogaster	36-42
6461713-9	1982	Analysis by sodium dodecyl sulfate- polyacrylamide get electrophoresis of the [(3)H]leucine intrinsically labeled B cell proteins reactive with the purified aaH revealed proteins of 100,000 M(r) and 50,000 M(r) without reduction, and after complete reduction of disulfide bonds, a single protein band of 50,000 M(r).	Disulfides	262-271	aspartate beta-hydroxylase	Homo sapiens	157-160
6178839-2	1982	These monoclonal antibodies recognized a new type of viral antigenic determinant which appeared to be a conformational determinant associated with the env precursor polyprotein (pr80env) or its disulfide-linked gp70-p15(E) complex (gp80) but not with free gp70 or p15(E) or any other virion or virus-induced protein.	Disulfides	194-203	embigin	Mus musculus	211-215
6178839-2	1982	These monoclonal antibodies recognized a new type of viral antigenic determinant which appeared to be a conformational determinant associated with the env precursor polyprotein (pr80env) or its disulfide-linked gp70-p15(E) complex (gp80) but not with free gp70 or p15(E) or any other virion or virus-induced protein.	Disulfides	194-203	embigin	Mus musculus	256-260
1898065-7	1991	These results indicate that inactivation of guanidinoacetate methyltransferase by GSSG is the consequence of the formation of a mixed disulfide between a protein thiol and glutathione.	Disulfides	134-143	guanidinoacetate N-methyltransferase	Rattus norvegicus	44-78
11784324-0	2002	Disulfide bond formation through Cys186 facilitates functionally relevant dimerization of trimeric hyaluronan-binding protein 1 (HABP1)/p32/gC1qR.	Disulfides	0-9	complement C1q binding protein	Homo sapiens	99-127
2040276-5	1991	The binding was reduced or abolished by metal-ion-chelating or chaotropic agents, high salt and reduction of disulfide bonds in BM-40.	Disulfides	109-118	secreted acidic cysteine rich glycoprotein	Mus musculus	128-133
7306531-10	1981	It is proposed that inactivation of pyruvate kinase by 5"-FSBG proceeds by formation of thiol sulfonate followed by a rapid displacement of the sulfinic acid moiety by a second cysteine to yield a disulfide.	Disulfides	197-206	pyruvate kinase PKLR	Oryctolagus cuniculus	36-51
11784324-0	2002	Disulfide bond formation through Cys186 facilitates functionally relevant dimerization of trimeric hyaluronan-binding protein 1 (HABP1)/p32/gC1qR.	Disulfides	0-9	complement C1q binding protein	Homo sapiens	129-134
2037074-0	1991	Human interleukin-5 expressed in Escherichia coli: assignment of the disulfide bridges of the purified unglycosylated protein.	Disulfides	69-78	interleukin 5	Homo sapiens	6-19
2037074-1	1991	Human interleukin-5 is a homodimer; each subunit contains two cysteine residues that form two inter-subunit disulfide bonds.	Disulfides	108-117	interleukin 5	Homo sapiens	6-19
2037074-2	1991	The topology of the disulfides in recombinant human interleukin-5 produced in Escherichia coli was studied by proteolytic digestion and peptide mapping.	Disulfides	20-30	interleukin 5	Homo sapiens	52-65
6166674-11	1981	SDS-PAGE under nonreducing conditions indicated that p97 is monomeric, probably with intrachain disulfide bonds.	Disulfides	96-105	melanotransferrin	Homo sapiens	53-56
7016180-3	1981	The peptide alpha 1(III)-CB9 represents the COOH terminus of the helical (pepsin-resistant) portion of type III collagen and terminates in a Cys-Cys sequence responsible for the intramolecular disulfide cross-linkages with other chains.	Disulfides	193-202	adrenoceptor alpha 1D	Homo sapiens	12-28
1709384-0	1991	The delta TCS1 determinant is expressed on both disulfide- and non-disulfide-linked gamma delta T-cell antigen receptors.	Disulfides	48-57	treacle ribosome biogenesis factor 1	Homo sapiens	10-14
11784324-0	2002	Disulfide bond formation through Cys186 facilitates functionally relevant dimerization of trimeric hyaluronan-binding protein 1 (HABP1)/p32/gC1qR.	Disulfides	0-9	complement C1q binding protein	Homo sapiens	136-139
1709384-0	1991	The delta TCS1 determinant is expressed on both disulfide- and non-disulfide-linked gamma delta T-cell antigen receptors.	Disulfides	67-76	treacle ribosome biogenesis factor 1	Homo sapiens	10-14
6970769-1	1981	Murine Interleukin 2 (IL2) was denatured with sodium dodecyl sulfate (SDS) with or without concomitant reduction of disulfide bonds.	Disulfides	116-125	interleukin 2	Mus musculus	7-20
11784324-0	2002	Disulfide bond formation through Cys186 facilitates functionally relevant dimerization of trimeric hyaluronan-binding protein 1 (HABP1)/p32/gC1qR.	Disulfides	0-9	complement C1q binding protein	Homo sapiens	140-145
6970769-1	1981	Murine Interleukin 2 (IL2) was denatured with sodium dodecyl sulfate (SDS) with or without concomitant reduction of disulfide bonds.	Disulfides	116-125	interleukin 2	Mus musculus	22-25
11784324-5	2002	The gradual structural transition caused by cysteine-mediated disulfide linkage is evident as the fluorescence intensity increases with increasing Hg(2+) concentration until all the HABP1 trimer is converted into hexamer.	Disulfides	62-71	complement C1q binding protein	Homo sapiens	182-187
11752136-0	2002	Vaccinia virus G4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assembly.	Disulfides	78-87	glutaredoxin	Homo sapiens	19-31
2039503-0	1991	Quantitation of the class I disulfides of the insulin receptor.	Disulfides	28-38	insulin receptor	Homo sapiens	46-62
2039503-1	1991	The disulfide structure of the insulin receptor was probed using dithiothreitol and [3H]-N-ethylmaleimide to reduce purified human placental receptor and label the cysteine residues.	Disulfides	4-13	insulin receptor	Homo sapiens	31-47
11752136-2	2002	Repression of E10R prevented the formation of intramolecular disulfide bonds of the G4L glutaredoxin, the L1R membrane protein, and the structurally related F9L protein.	Disulfides	61-70	glutaredoxin	Vaccinia virus	88-100
6450201-2	1981	Plasmin-cleaved hPL and hGH each consist of an NH2-terminal fragment (1-134) connected to a COOH-terminal fragment (141-191) through a Cys53-Cys165 disulfide bond.	Disulfides	148-157	galectin 1	Homo sapiens	16-19
11740506-0	2002	A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.	Disulfides	40-49	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	79-84
7212634-5	1980	B2m (-), HLA (-) Daudi human male Burkitt lymphoma cells excreted a group of several proteins that shared the three distinctive characteristics in common; their extreme hydrophobicity, their tendency beyond saturation to form irreversibly water insoluble aggregates by extensive interchain disulfide bridges, and their conspicuously slower turn over rates compared to other Daudi excreted proteins.	Disulfides	290-299	beta-2-microglobulin	Homo sapiens	0-3
2021630-3	1991	The mutant repressor, Tyr88----Cys, forms an intersubunit disulfide linkage and exhibits enhancement of both structural stability and operator affinity.	Disulfides	58-67	LexA family transcriptional regulator	Escherichia virus Lambda	11-20
2037039-4	1991	Antibodies directed against the N-terminal sequence of SP-B react with the native protein only in the reduced state suggesting that this domain has a conformation dependent on disulfide bond formation.	Disulfides	176-185	surfactant protein B	Homo sapiens	55-59
6102993-4	1980	Nonenzymatic transhydrogenation reactions of these disulfides with glutathione yield glutathione disulfide and thus account for the apparent glutathione oxidase activity of gamma-glutamyl transpeptidase.	Disulfides	51-61	gamma-glutamyltransferase 1	Rattus norvegicus	173-202
11740506-1	2002	Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide bond formation during protein biosynthesis in the yeast endoplasmic reticulum.	Disulfides	62-71	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	0-5
2016314-2	1991	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that renin consists of two polypeptide chains linked by a disulfide bond, one of Mr = 36,000 (heavy chain) and the other of Mr = 3,000 (light chain).	Disulfides	123-132	renin	Rattus norvegicus	70-75
12189052-3	2002	This review discusses disulfide bond cleavage in the secreted soluble protein, plasmin.	Disulfides	22-31	plasminogen	Homo sapiens	79-86
1678010-1	1991	Certain disulfide analogues of cystamine were prepared and evaluated for the ability to inhibit gamma-glutamylcysteine synthetase (GCS), the rate-limiting enzyme in glutathione synthesis.	Disulfides	8-17	glutamate-cysteine ligase catalytic subunit	Homo sapiens	131-134
39074-0	1979	Reduction of disulfides by thioredoxin.	Disulfides	13-23	thioredoxin	Homo sapiens	27-38
12189052-4	2002	Cleavage of plasmin disulfide bond(s) triggers peptide bond cleavage and formation of the tumour angiogenesis inhibitor, angiostatin.	Disulfides	20-29	plasminogen	Homo sapiens	12-19
12189052-5	2002	Tumour cells secrete phosphoglycerate kinase which facilitates cleavage of the plasmin disulfide bond(s).	Disulfides	87-96	plasminogen	Homo sapiens	79-86
12189052-7	2002	We propose that phosphoglycerate kinase facilitates cleavage of a particular plasmin disulfide bond by hydroxide ion, which results in formation of a sulfenic acid and a free thiol.	Disulfides	85-94	plasminogen	Homo sapiens	77-84
479159-7	1979	The data indicate that there are regions of the hydrophobic disulfide knot, Ho1-DSK, which are surface-oriented.	Disulfides	60-69	heme oxygenase 1	Homo sapiens	76-79
11754956-7	2001	The peptide was determined to be AM (11-26) which has one intramolecular disulfide bond.	Disulfides	73-82	adrenomedullin	Bos taurus	33-35
468826-0	1979	Interchain disulfide bonds and subunit organization in human serum cholinesterase.	Disulfides	11-20	butyrylcholinesterase	Homo sapiens	67-81
1821789-1	1991	Rat liver protein disulfide isomerase (PDI) catalyzes the oxidative folding of proteins containing disulfide bonds.	Disulfides	18-27	prolyl 4-hydroxylase subunit beta	Bos taurus	39-42
1821789-7	1991	After complete reduction and denaturation in 6 M guanidinium hydrochloride, PDI regains complete activity within 3 min after removal of the denaturant, implying that disulfide bonds are not essential for the maintenance of PDI tertiary structure.	Disulfides	166-175	prolyl 4-hydroxylase subunit beta	Bos taurus	76-79
11910764-10	2001	The first Cys of hBMP-2 mature peptide might be necessary for integrity of three pairs of disulfide bond, and also essential for bone-inducing activity of hBMP-2.	Disulfides	90-99	bone morphogenetic protein 2	Homo sapiens	17-23
1898658-3	1991	The omega chain is disulfide linked to mu and was predicted to be the product of the lambda 5 gene.	Disulfides	19-28	immunoglobulin lambda-like polypeptide 1	Mus musculus	85-93
1702723-6	1990	In one case only 40% of this population reacted with delta TCS1 mAb, that recognizes the non-disulfide-linked form of TcR1, and co-expressed the CD8 antigen.	Disulfides	93-102	treacle ribosome biogenesis factor 1	Homo sapiens	59-63
712836-0	1978	Three-dimensional structure and disulfide bond connections in bovine pancreatic phospholipase A2.	Disulfides	32-41	LOC104974671	Bos taurus	80-96
681081-1	1978	An insulin fragment containing residues A 18-21 and B 19-26 linked by the disulfide bond between residues A 20 and B 19 was synthesized.	Disulfides	74-83	insulin	Bos taurus	3-10
566268-0	1978	Ionization and reactivities of the thiol groups which participate in the formation of interchain disulfide bonds of Bence Jones proteins and an Fab(t) fragment.	Disulfides	97-106	FA complementation group B	Homo sapiens	144-147
911764-0	1977	Optical activity of disulfide bonds in proteins: studies on human choriomammotropin and bovine pituitary somatotropin.	Disulfides	20-29	somatotropin	Bos taurus	105-117
11489900-4	2001	In vitro transfection studies in HEK-293 cells established the specificity and disulfide-linked nature of the CaR:mGluR1alpha (CaR:mGluR5) interactions.	Disulfides	79-88	glutamate receptor, ionotropic, kainate 1	Mus musculus	131-137
2265202-0	1990	Polymeric structure of human respiratory mucin: studies on two protein components released upon reduction of disulfide bonds.	Disulfides	109-118	LOC100508689	Homo sapiens	41-46
2265202-13	1990	These observations suggest that the availability of high-affinity probe binding sites upon reduction of mucin disulfide bonds may be either due to binding of the probe to the released component(s) and/or due to noncovalent interaction of the released component(s) with the mucin causing a conformational change in the mucin structure.	Disulfides	110-119	LOC100508689	Homo sapiens	104-109
2265202-13	1990	These observations suggest that the availability of high-affinity probe binding sites upon reduction of mucin disulfide bonds may be either due to binding of the probe to the released component(s) and/or due to noncovalent interaction of the released component(s) with the mucin causing a conformational change in the mucin structure.	Disulfides	110-119	LOC100508689	Homo sapiens	273-278
11438534-0	2001	Chloroplast glyceraldehyde-3-phosphate dehydrogenase contains a single disulfide bond located in the C-terminal extension to the B subunit.	Disulfides	71-80	SULA_RS08180	Saccharolobus solfataricus	12-52
2265202-13	1990	These observations suggest that the availability of high-affinity probe binding sites upon reduction of mucin disulfide bonds may be either due to binding of the probe to the released component(s) and/or due to noncovalent interaction of the released component(s) with the mucin causing a conformational change in the mucin structure.	Disulfides	110-119	LOC100508689	Homo sapiens	273-278
873911-14	1977	Cross-linking studies showed that the non-disulfide-bonded form of HLA antigens contains one subunit each of the Mr = 44,000 heavy chain and the Mr = 12,000 light chain (beta2-microglobulin).	Disulfides	42-51	beta-2-microglobulin	Homo sapiens	170-189
993201-2	1976	Detached tomato leaves, supplied with the proteinase inhibitor inducing factor (PIIF) and incubated with water under constant light, exhibited a specificity of intracellular protein turnover directed toward the selective accumulation of heat-stable proteins having disulfide corss-linkages.	Disulfides	265-274	wound-induced proteinase inhibitor 1	Solanum lycopersicum	42-78
11438534-1	2001	Mass mapping analysis based on cyanylation and CN-induced cleavage indicates that the two cysteine residues in the C-terminal extension of the B subunit of the light-activated pea leaf chloroplast glyceraldehyde-3-phosphate dehydrogenase form a disulfide bond.	Disulfides	245-254	SULA_RS08180	Saccharolobus solfataricus	197-237
993201-2	1976	Detached tomato leaves, supplied with the proteinase inhibitor inducing factor (PIIF) and incubated with water under constant light, exhibited a specificity of intracellular protein turnover directed toward the selective accumulation of heat-stable proteins having disulfide corss-linkages.	Disulfides	265-274	wound-induced proteinase inhibitor 1	Solanum lycopersicum	80-84
2171674-7	1990	The results of additional experiments using erythrocyte lysate and of kinetic experiments on solutions containing PSSG and/or GSH, NADPH and glutathione reductase suggest that the predominant mechanism for reduction of PSSG is by a thiol-disulfide exchange reaction with GSH to form PSH and GSSG, which in turn undergoes enzyme-catalyzed reduction by NADPH.	Disulfides	238-247	glutathione-disulfide reductase	Homo sapiens	141-162
11481439-8	2001	The C-terminal extension typical of mammalian TrxRs has two functions: (i) it extends the electron transport chain from the catalytic disulfide to the enzyme surface, where it can react with Trx, and (ii) it prevents the enzyme from acting as a GR by blocking the redox-active disulfide.	Disulfides	134-143	glutathione-disulfide reductase	Homo sapiens	245-247
2211816-2	1990	Early during biosynthesis the Tfr monomer is converted to a disulfide-linked Tfr dimer.	Disulfides	60-69	transferrin receptor	Homo sapiens	30-33
938633-1	1976	Mouse submaxillary epidermal growth factor (EGF) is a 53-residue single chain peptide hormone of known amino acid sequence which contains three disulfides, five tyrosines, and two tryptophans.	Disulfides	144-154	epidermal growth factor	Mus musculus	19-42
938633-1	1976	Mouse submaxillary epidermal growth factor (EGF) is a 53-residue single chain peptide hormone of known amino acid sequence which contains three disulfides, five tyrosines, and two tryptophans.	Disulfides	144-154	epidermal growth factor	Mus musculus	44-47
2211816-2	1990	Early during biosynthesis the Tfr monomer is converted to a disulfide-linked Tfr dimer.	Disulfides	60-69	transferrin receptor	Homo sapiens	77-80
11481439-8	2001	The C-terminal extension typical of mammalian TrxRs has two functions: (i) it extends the electron transport chain from the catalytic disulfide to the enzyme surface, where it can react with Trx, and (ii) it prevents the enzyme from acting as a GR by blocking the redox-active disulfide.	Disulfides	277-286	glutathione-disulfide reductase	Homo sapiens	245-247
11470753-2	2001	In this report we demonstrate that, in addition to cPKCalpha, six other PKC isozymes that are representative of the three subfamilies within the PKC family (cPKCbeta1, cPKCbeta2 and cPKCgamma, nPKCdelta and nPKCepsilon and aPKC-zeta) are subject to inactivation by S-glutathiolation induced by the thiol-specific oxidant diamide, which induces disulfide bridge formation.	Disulfides	344-353	protein kinase C delta	Homo sapiens	72-75
2222458-5	1990	The critical catalytic residues of human angiogenin are conserved in the mouse protein, as are the six cysteines necessary for disulfide bond formation.	Disulfides	127-136	angiogenin	Homo sapiens	41-51
1168065-0	1975	Dissociation of bovine seminal ribonuclease into catalytically active monomers by selective reduction and alkylation of the intersubunit disulfide bridges.	Disulfides	137-146	seminal ribonuclease	Bos taurus	23-43
1168065-1	1975	The hypothesis previously advanced that interchain disulfide bridges link the two identical subunits of bovine seminal ribonuclease BS-1 has been confirmed.	Disulfides	51-60	seminal ribonuclease	Bos taurus	111-131
1168065-5	1975	This indicates that the dimeric structure of seminal ribonuclease is maintained not only by disulfide bridges, but also by noncovalent forces.	Disulfides	92-101	seminal ribonuclease	Bos taurus	45-65
11470753-2	2001	In this report we demonstrate that, in addition to cPKCalpha, six other PKC isozymes that are representative of the three subfamilies within the PKC family (cPKCbeta1, cPKCbeta2 and cPKCgamma, nPKCdelta and nPKCepsilon and aPKC-zeta) are subject to inactivation by S-glutathiolation induced by the thiol-specific oxidant diamide, which induces disulfide bridge formation.	Disulfides	344-353	protein kinase C delta	Homo sapiens	157-218
1152307-2	1975	This is a newly developed compound, in which the disulfide bond and [Pro-7] of deamino-oxytocin are substituted by an ethylene linkage and glycine respectively.	Disulfides	49-58	oxytocin	Oryctolagus cuniculus	87-95
4846413-2	1974	This protein, termed the major basic protein (MBP), readily aggregates and becomes insoluble, and the formation of aggregates is dependent on the establishment of disulfide bonds.	Disulfides	163-172	myelin basic protein	Cavia porcellus	25-44
4846413-2	1974	This protein, termed the major basic protein (MBP), readily aggregates and becomes insoluble, and the formation of aggregates is dependent on the establishment of disulfide bonds.	Disulfides	163-172	myelin basic protein	Cavia porcellus	46-49
2393862-7	1990	Since the Mr 70,000 molecule appears to be associated with the breast mucin by disulfide bonds, its study could help elucidate the structure of this latter complex and how it is organized in the cell membrane, and prove useful in diagnosis and therapy of breast cancer.	Disulfides	79-88	LOC100508689	Homo sapiens	70-75
2144007-2	1990	The TCR for Ag, on the majority of human T cells, is a disulfide-linked heterodimer composed of TCR-alpha and -beta chains noncovalently associated with the monomorphic CD3 complex composed of the CD3-gamma, -delta, -epsilon, and -zeta chains.	Disulfides	55-64	T cell receptor alpha constant	Homo sapiens	96-105
2144290-5	1990	When TCRs from both human and murine T lymphocytes were immunoprecipitated with monoclonal antibodies against either CD3 epsilon or Ti, a 40-kDa disulfide-linked dimer was coprecipitated with the other TCR subunits from digitonin lysates.	Disulfides	145-154	CD3 antigen, epsilon polypeptide	Mus musculus	117-128
11470753-6	2001	The results provide evidence that at least some pro-oxidant environments may support the potent inactivation of nPKCepsilon and other PKC isozymes implicated in tumor promotion/progression by the mechanisms of S-glutathiolation and, in some cases, disulfide bridge formation among the isozyme thiols, without inducing substantial nPKCdelta inactivation.	Disulfides	248-257	protein kinase C delta	Homo sapiens	113-116
11375984-7	2001	In contrast, the presence of five additional C-terminal triplets in COL1 allows the formation of triple-helical disulfide-bonded trimers, suggesting that the presence of a triple-helix is essential for the assembly of collagen XII.	Disulfides	112-121	collagen type XII alpha 1 chain	Gallus gallus	218-230
2394726-6	1990	These results suggest that thioltransferase and PDI contribute to the regeneration of oxidized ascorbic acid in mammalian cells, and based on their cellular location, thioltransferase is proposed to be the major cytoplasmic activity, whereas interaction of DHA with microsomal membrane PDI may catalyze regeneration of ascorbic acid and initiate oxidation of intralumenal protein thiols to disulfides.	Disulfides	390-400	glutaredoxin	Homo sapiens	27-43
2394726-6	1990	These results suggest that thioltransferase and PDI contribute to the regeneration of oxidized ascorbic acid in mammalian cells, and based on their cellular location, thioltransferase is proposed to be the major cytoplasmic activity, whereas interaction of DHA with microsomal membrane PDI may catalyze regeneration of ascorbic acid and initiate oxidation of intralumenal protein thiols to disulfides.	Disulfides	390-400	prolyl 4-hydroxylase subunit beta	Homo sapiens	48-51
2394726-6	1990	These results suggest that thioltransferase and PDI contribute to the regeneration of oxidized ascorbic acid in mammalian cells, and based on their cellular location, thioltransferase is proposed to be the major cytoplasmic activity, whereas interaction of DHA with microsomal membrane PDI may catalyze regeneration of ascorbic acid and initiate oxidation of intralumenal protein thiols to disulfides.	Disulfides	390-400	glutaredoxin	Homo sapiens	167-183
4151431-0	1974	Enzymatic reduction of disulfide bonds in fibrin-ogen by the thioredoxin system.	Disulfides	23-32	thioredoxin	Homo sapiens	61-72
5532232-0	1970	The disulfide bonds of bovine alpha-lactalbumin.	Disulfides	4-13	lactalbumin alpha	Bos taurus	30-47
11335709-6	2001	Our results supported the existence of MT1-MMP oligomers and demonstrated that a disulfide bridge involving the Cys(574) of the enzyme"s cytoplasmic tail covalently links MT1-MMP monomers on the MCF7 cell surface.	Disulfides	81-90	matrix metallopeptidase 14	Homo sapiens	171-178
1980817-5	1990	The finding that the carbon analogue 11 (two methylenes for the disulfide bridge) was devoid of activity is consistent with the hypothesis that histamine H2-receptor inhibition is the result of a covalent bond formation by a way of a disulfide-thiol interchange reaction between the disulfide moiety of tetraamine disulfides and a receptor thiol group.	Disulfides	234-243	histamine receptor H2	Homo sapiens	144-165
11309389-8	2001	The GH concentration dependence for inhibition of PMA-induced GHR proteolysis paralleled that for its promotion of receptor dimerization (as monitored by formation of GHR disulfide linkage).	Disulfides	171-180	growth hormone receptor	Oryctolagus cuniculus	167-170
1980817-5	1990	The finding that the carbon analogue 11 (two methylenes for the disulfide bridge) was devoid of activity is consistent with the hypothesis that histamine H2-receptor inhibition is the result of a covalent bond formation by a way of a disulfide-thiol interchange reaction between the disulfide moiety of tetraamine disulfides and a receptor thiol group.	Disulfides	234-243	histamine receptor H2	Homo sapiens	144-165
2388032-2	1990	Biochemical analysis revealed that platelet CD69 appears on sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a broad 55-65-kD band, in which three 55-, 60-, and 65-kD components were detectable when nonreduced, and as two 28- and 32-kD bands when reduced, corresponding to the two disulfide-linked chains of the dimer.	Disulfides	293-302	CD69 molecule	Homo sapiens	44-48
5260926-1	1969	p-(trimethyl ammonium) benzene diazonium difluoroborate (TDF), an affinity-labeling reagent of the acetylcholine receptor site(s), which in the normal cell acts as an irreversible inhibitor becomes a reversible activator after in vivo exposure of the electroplax to dithiothreitol (DTT), a disulfide bond reducing agent.	Disulfides	290-299	sex determining region Y	Homo sapiens	57-60
11320084-2	2001	We showed that diamide, a reagent that promotes disulfide bond formation, caused a loss of immunorecognition of the monomeric hHSF1 protein in a standard Western blot detection procedure.	Disulfides	48-57	heat shock transcription factor 1	Homo sapiens	126-131
14285236-0	1965	ENZYMATIC MODIFICATION OF MYOSIN BY DISULFIDE EXCHANGE.	Disulfides	36-45	myosin heavy chain 14	Homo sapiens	26-32
2144901-7	1990	Since CD3-epsilon was shown to form disulfide-linked homodimers both in human and murine T cells, the two CD3-epsilon subunits present in the TCR-CD3 complex were in direct contact with one another.	Disulfides	36-45	CD3 antigen, epsilon polypeptide	Mus musculus	106-117
11320084-3	2001	Modification of the Western blot procedure to include dithiothreitol in the equilibration and transfer buffers after gel electrophoresis allowed for the detection of a compact, intramolecularly disulfide cross-linked oxidized hHSF1 (ox-hHSF1) in the diamide-treated sample.	Disulfides	194-203	heat shock transcription factor 1	Homo sapiens	226-231
11320084-3	2001	Modification of the Western blot procedure to include dithiothreitol in the equilibration and transfer buffers after gel electrophoresis allowed for the detection of a compact, intramolecularly disulfide cross-linked oxidized hHSF1 (ox-hHSF1) in the diamide-treated sample.	Disulfides	194-203	heat shock transcription factor 1	Homo sapiens	236-241
2392685-1	1990	The principal neutralizing determinant (PND) of human immunodeficiency virus HIV-1 is part of a disulfide bridged loop in the third variable region of the external envelope protein, gp120.	Disulfides	96-105	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	182-187
2389142-2	1990	A peptide model for the basic region of the yeast transcriptional activator GCN4 has been developed in which the leucine zipper has been replaced by a disulfide bond.	Disulfides	151-160	amino acid starvation-responsive transcription factor GCN4	Saccharomyces cerevisiae S288C	76-80
34020817-6	2021	The clade A trimer, which we named "BG505 DS-SOSIP.664", contained an engineered disulfide (201C-433C; DS) within gp120, which further stabilized this trimer in a prefusion-closed conformation resistant to CD4-induced triggering.	Disulfides	81-90	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	114-119
11388807-0	2001	Accurate disulfide formation in Escherichia coli: overexpression and characterization of the first domain (HF6478) of the multiple Kazal-type inhibitor LEKTI.	Disulfides	9-18	serine peptidase inhibitor Kazal type 5	Homo sapiens	152-157
33985344-6	2021	Four of the six H1 and H3 HA bonds are cleaved by the vascular thiol isomerases, thioredoxin and protein disulphide isomerase, in recombinant proteins, which correlated with surface exposure of the disulfides in crystal structures.	Disulfides	198-208	thioredoxin	Homo sapiens	81-92
2355006-0	1990	Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells.	Disulfides	25-34	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	150-171
11279007-0	2001	Localization of disulfide bonds in the frizzled module of Ror1 receptor tyrosine kinase.	Disulfides	16-25	receptor tyrosine kinase-like orphan receptor 1	Rattus norvegicus	58-62
2315701-5	1990	Two PTTH subunits are linked together by disulfide bonds, before or after cleavage from prepro-PTTH, to form a homodimeric PTTH.	Disulfides	41-50	prothoracicotropic hormone	Bombyx mori	4-8
2137383-3	1990	In addition, Lp(a) contains the glycoprotein apolipoprotein(a) [apo(a)], which is disulfide-linked to apo B-100.	Disulfides	82-91	lipoprotein(a)	Homo sapiens	13-18
2137383-3	1990	In addition, Lp(a) contains the glycoprotein apolipoprotein(a) [apo(a)], which is disulfide-linked to apo B-100.	Disulfides	82-91	lipoprotein(a)	Homo sapiens	45-62
33756234-0	2021	Synthesis and biological evaluation of disulfides as anticancer agents with thioredoxin inhibition.	Disulfides	39-49	thioredoxin	Homo sapiens	76-87
33756234-3	2021	Herein, we synthesized 72 disulfides and evaluated theirinhibition for Trx and antitumor activity.	Disulfides	26-36	thioredoxin	Homo sapiens	71-74
33756234-7	2021	Next, we performed kinetic studies of both two disulfides, 68 had faster inhibition of Trx than 69.	Disulfides	47-57	thioredoxin	Homo sapiens	87-90
11342438-1	2001	Human coagulation factor XI (FXI) is a plasma serine protease composed of 2 identical 80-kd polypeptides connected by a disulfide bond.	Disulfides	120-129	coagulation factor XI	Homo sapiens	6-27
33855279-2	2021	Herein, we developed an in vitro system for directly monitoring PDI- or ERp46-catalyzed disulfide bond formation in ribosome-associated nascent chains of human serum albumin.	Disulfides	88-97	thioredoxin domain containing 5	Homo sapiens	72-77
33855279-3	2021	The results indicated that ERp46 more efficiently introduced disulfide bonds into nascent chains with a short segment exposed outside the ribosome exit site than PDI.	Disulfides	61-70	thioredoxin domain containing 5	Homo sapiens	27-32
33855279-5	2021	Thus, ERp46 serves as a more potent disulfide introducer especially during the early stages of translation, whereas PDI can catalyze disulfide formation when longer nascent chains emerge out from ribosome.	Disulfides	36-45	thioredoxin domain containing 5	Homo sapiens	6-11
33855279-5	2021	Thus, ERp46 serves as a more potent disulfide introducer especially during the early stages of translation, whereas PDI can catalyze disulfide formation when longer nascent chains emerge out from ribosome.	Disulfides	133-142	thioredoxin domain containing 5	Homo sapiens	6-11
2153301-0	1990	Labile disulfide bonds in human placental insulin receptor.	Disulfides	7-16	insulin receptor	Homo sapiens	42-58
2153301-1	1990	The disulfide crosslinking pattern of human placental insulin receptor was investigated using selective reduction with tributylphosphine followed by alkylation with N-[3H]ethylmaleimide.	Disulfides	4-13	insulin receptor	Homo sapiens	54-70
33797881-3	2021	Herein, we describe the use of two ligation manifolds, namely, diselenide-selenoester ligation and native chemical ligation, to assemble a 31.5 kDa phosphorylated insulin-like growth factor binding protein (IGFBP-2) that comprises 290 amino acid residues, a phosphoserine post-translational modification, and nine disulfide bonds.	Disulfides	314-323	insulin like growth factor binding protein 2	Homo sapiens	207-214
11278905-0	2001	Discrimination between native and non-native disulfides by protein-disulfide isomerase.	Disulfides	45-55	prolyl 4-hydroxylase subunit beta	Bos taurus	59-86
22239709-1	2012	Mature prion protein (PrP) is a 208-residue polypeptide that contains a single disulfide bond.	Disulfides	79-88	prion protein	Mus musculus	22-25
32235917-7	2021	We found that the V(D)J recombination-generated junctional and somatic hypermutation-induced disulfide bridge (C-C) motif in the CDRH3 is critical for the broad neutralization and binding activity of 8D6.	Disulfides	93-102	CD320 molecule	Homo sapiens	200-203
11278905-1	2001	The folding assistant and chaperone protein-disulfide isomerase (PDI) catalyzes disulfide formation, reduction, and isomerization of misfolded proteins.	Disulfides	44-53	prolyl 4-hydroxylase subunit beta	Bos taurus	65-68
11278905-2	2001	PDI substrates are not restricted to misfolded proteins; PDI catalyzes the dithiothreitol (DTT)-dependent reduction of native ribonuclease A, microbial ribonuclease, and pancreatic trypsin inhibitor, suggesting that an ongoing surveillance by PDI can test even native disulfides for their ability to rearrange.	Disulfides	268-278	prolyl 4-hydroxylase subunit beta	Bos taurus	0-3
11278905-2	2001	PDI substrates are not restricted to misfolded proteins; PDI catalyzes the dithiothreitol (DTT)-dependent reduction of native ribonuclease A, microbial ribonuclease, and pancreatic trypsin inhibitor, suggesting that an ongoing surveillance by PDI can test even native disulfides for their ability to rearrange.	Disulfides	268-278	prolyl 4-hydroxylase subunit beta	Bos taurus	57-60
11278905-2	2001	PDI substrates are not restricted to misfolded proteins; PDI catalyzes the dithiothreitol (DTT)-dependent reduction of native ribonuclease A, microbial ribonuclease, and pancreatic trypsin inhibitor, suggesting that an ongoing surveillance by PDI can test even native disulfides for their ability to rearrange.	Disulfides	268-278	prolyl 4-hydroxylase subunit beta	Bos taurus	57-60
34294886-7	2022	Moreover, we revealed that co-administration of CEP and epirubicin markedly increased the generation of mitochondrial superoxide, resulting in oxidation of the actin-remodeling protein cofilin, which promoted formation of an intramolecular disulfide bridge between Cys39 and Cys80 as well as Ser3 dephosphorylation, leading to mitochondria translocation of cofilin, thus causing mitochondrial fission and apoptosis.	Disulfides	240-249	cofilin 1	Homo sapiens	185-192
33185461-7	2021	Results: In both humans and mice, myocardial PKARIalpha disulfide formation was found to be significantly increased (2-fold in humans, p=0.023; 2.4-fold in mice, p<0.001) in response to I/R in vivo.	Disulfides	56-65	protein kinase, cAMP dependent regulatory, type I, alpha	Mus musculus	45-55
33185461-8	2021	In mouse LV cardiomyocytes, disulfide-containing PKARIalpha was not found to impact catalytic activity, but instead led to enhanced A-kinase-anchoring protein (AKAP) binding with preferential localization of the holoenzyme to the lysosome.	Disulfides	28-37	protein kinase, cAMP dependent regulatory, type I, alpha	Mus musculus	49-59
33185461-8	2021	In mouse LV cardiomyocytes, disulfide-containing PKARIalpha was not found to impact catalytic activity, but instead led to enhanced A-kinase-anchoring protein (AKAP) binding with preferential localization of the holoenzyme to the lysosome.	Disulfides	28-37	A kinase (PRKA) anchor protein 1	Mus musculus	132-158
33185461-8	2021	In mouse LV cardiomyocytes, disulfide-containing PKARIalpha was not found to impact catalytic activity, but instead led to enhanced A-kinase-anchoring protein (AKAP) binding with preferential localization of the holoenzyme to the lysosome.	Disulfides	28-37	A kinase (PRKA) anchor protein 1	Mus musculus	160-164
33185461-11	2021	Conclusions: Disulfide-modification targets PKARIalpha to the lysosome where it acts as a gatekeeper for TPC-mediated triggering of global calcium release.	Disulfides	13-22	protein kinase, cAMP dependent regulatory, type I, alpha	Mus musculus	44-54
34585392-3	2021	In this study, a novel combretastatin A-4 derivative (CA4D) was designed and developed, which was further conjugated with glucose via disulfide-bond-bridged (CA4D-SS-Glu) to enhance the BBB penetration capacity.	Disulfides	134-143	carbonic anhydrase 4	Homo sapiens	23-41
11278905-7	2001	An extensively unfolded polypeptide may be required by PDI to distinguish native from non-native disulfides.	Disulfides	97-107	prolyl 4-hydroxylase subunit beta	Bos taurus	55-58
34698634-2	2021	We previously showed that EDEM2 stably disulfide-bonded to the thioredoxin domain-containing protein TXNDC11 is responsible for the first step (George et al., 2020).	Disulfides	39-48	ER degradation enhancing alpha-mannosidase like protein 2	Homo sapiens	26-31
11285220-2	2001	The DsbA-DsbB pathway introduces disulfide bonds de novo, while the DsbC-DsbD pathway functions to isomerize disulfides.	Disulfides	109-119	putative protein DsbC	Escherichia coli	68-72
34274401-8	2021	The presence of disulfide linkages and thiol groups were shown to favor improved binding of cross-linked nanogels to mucin.	Disulfides	16-25	LOC100508689	Homo sapiens	117-122
34456199-1	2021	AIMS: Lipoprotein(a) (Lp(a)) is a plasma lipoprotein consisting of a low-density lipoprotein (LDL)-like particle with apolipoprotein (Apo)(a), attached via a disulfide bond to Apo B100.	Disulfides	158-167	lipoprotein(a)	Homo sapiens	6-20
34456199-1	2021	AIMS: Lipoprotein(a) (Lp(a)) is a plasma lipoprotein consisting of a low-density lipoprotein (LDL)-like particle with apolipoprotein (Apo)(a), attached via a disulfide bond to Apo B100.	Disulfides	158-167	lipoprotein(a)	Homo sapiens	22-27
11264342-5	2001	The release of E1 from the interaction with calnexin coincides with the beginning of E1 and E2 association into disulfide-linked heterodimers.	Disulfides	112-121	calnexin	Homo sapiens	44-52
11231292-0	2001	Disulfide bond assignment, lipid transfer activity and secondary structure of a 7-kDa plant lipid transfer protein, LTP2.	Disulfides	0-9	non-specific lipid-transfer protein Cw18	Triticum aestivum	116-120
34395389-0	2021	Chemical Synthesis of the Sec-To-Cys Homologue of Human Selenoprotein F and Elucidation of Its Disulfide-pairing Mode.	Disulfides	95-104	selenoprotein F	Homo sapiens	56-71
34395389-4	2021	Moreover, the disulfide pairing mode of the SelF was elucidated through a combination of site-directed mutagenesis and LC-MS study.	Disulfides	14-23	selenoprotein F	Homo sapiens	44-48
11231292-5	2001	Trypsin and chymotrypsin digestions of the native LTP2 afforded the sequence of both isoforms and assignment of disulfide bonds.	Disulfides	112-121	non-specific lipid-transfer protein Cw18	Triticum aestivum	50-54
11231292-8	2001	By analogy with the structure of the LTP1, we discussed what structural changes are required to accommodate the LTP2 disulfide pattern.	Disulfides	117-126	non-specific lipid-transfer protein Cw18	Triticum aestivum	112-116
34126068-0	2021	The IgG Fc-binding protein FCGBP is secreted with all GDPH sequences cleaved, but maintained by inter-fragment disulfide bonds.	Disulfides	111-120	Fc gamma binding protein	Homo sapiens	27-32
11371007-4	2001	Our findings imply that the binding of NADP+ and AADP+ at the NADP(H)-binding site of A. thaliana TR, and/or the binding of TRX in the vicinity of the catalytic disulfide increase the content of fluorescent FR conformer (NADP(H)-binding site adjacent to flavin).	Disulfides	161-170	thioredoxin H-type 1	Arabidopsis thaliana	124-127
34078439-11	2021	GO analysis indicated that BolA family members might regulate the function of metal ion binding and protein disulfide oxidoreductase activity.	Disulfides	108-117	hydroxysteroid 17-beta dehydrogenase 6	Homo sapiens	118-132
11226250-4	2001	Furthermore, alphaLbeta2 containing a locked open I domain was completely resistant to inhibition by mAbs to the beta2 I-like domain, but became fully susceptible to inhibition after disulfide reduction with DTT.	Disulfides	183-192	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	19-24
34071440-4	2021	Our results demonstrate that disulfide HMGB1 (dsHMGB1) induces a unique macrophage phenotype that secretes pro-inflammatory cytokines, rather than inducing metabolic changes leading to nitric oxide production.	Disulfides	29-38	high mobility group box 1	Mus musculus	39-44
34745440-2	2021	Based on the structure of the complex of the protein S receptor-binding domain (RBD) and ACE2, the design of chimeric molecules consisting of two 22-23-mer peptides linked to each other by disulfide bonds was carried out.	Disulfides	189-198	angiotensin converting enzyme 2	Homo sapiens	89-93
35247515-0	2022	Inhibitors of ERp44, PDIA1, and AGR2 induce disulfide-mediated oligomerization of Death Receptors 4 and 5 and cancer cell death.	Disulfides	44-53	prolyl 4-hydroxylase subunit beta	Homo sapiens	21-26
35247515-0	2022	Inhibitors of ERp44, PDIA1, and AGR2 induce disulfide-mediated oligomerization of Death Receptors 4 and 5 and cancer cell death.	Disulfides	44-53	TNF receptor superfamily member 10a	Homo sapiens	82-105
11330840-8	2001	Western-blotting analysis in the presence or absence of the reducing agent suggested that mPR--in its binding state--consists of at least two identical subunits with an apparent molecular mass of 28 kDa which are linked by a disulfide bridge.	Disulfides	225-234	progestin and adipoQ receptor family member VII	Mus musculus	90-93
35398099-6	2022	Furthermore, our structure captured a fortuitous higher-order assembly between IL-18 and IL-18BP coordinated by a disulfide-bond distal to the binding surface connecting IL-18 and IL-18BP molecules from different complexes, resulting in a novel tetramer with 2:2 stoichiometry.	Disulfides	114-123	interleukin 18 binding protein	Homo sapiens	89-96
35398099-6	2022	Furthermore, our structure captured a fortuitous higher-order assembly between IL-18 and IL-18BP coordinated by a disulfide-bond distal to the binding surface connecting IL-18 and IL-18BP molecules from different complexes, resulting in a novel tetramer with 2:2 stoichiometry.	Disulfides	114-123	interleukin 18 binding protein	Homo sapiens	180-187
11330840-10	2001	In addition, it is shown that mPR can form disulfide-linked homodimers.	Disulfides	43-52	progestin and adipoQ receptor family member VII	Mus musculus	30-33
11042167-0	2001	Disulfide-dependent folding and export of Escherichia coli DsbC.	Disulfides	0-9	putative protein DsbC	Escherichia coli	59-63
35453458-2	2022	Upon light irradiation, Trx reduces the disulfide bonds of Trx target proteins (thereby turning on their activities) using reducing equivalents obtained from the photosynthetic electron transport chain.	Disulfides	40-49	thioredoxin H-type 1	Arabidopsis thaliana	24-27
35453458-2	2022	Upon light irradiation, Trx reduces the disulfide bonds of Trx target proteins (thereby turning on their activities) using reducing equivalents obtained from the photosynthetic electron transport chain.	Disulfides	40-49	thioredoxin H-type 1	Arabidopsis thaliana	59-62
35385753-1	2022	Protein disulfide isomerase (PDI) plays a key role in maintaining cellular homeostasis by mediating protein folding via catalyzing disulfide bond formation, breakage, and rearrangement in the endoplasmic reticulum.	Disulfides	131-140	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
35385753-1	2022	Protein disulfide isomerase (PDI) plays a key role in maintaining cellular homeostasis by mediating protein folding via catalyzing disulfide bond formation, breakage, and rearrangement in the endoplasmic reticulum.	Disulfides	131-140	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
11042167-6	2001	DsbC mutated in either Cys residue of nonactive site disulfide shows higher sensitivity to unfolding by guanidine hydrochloride and slower refolding compared with wild-type DsbC and the active site Cys mutants.	Disulfides	53-62	putative protein DsbC	Escherichia coli	0-4
11042167-7	2001	The above results provide experimental evidence for structural role of the nonactive site disulfide in folding and biological activities of DsbC.	Disulfides	90-99	putative protein DsbC	Escherichia coli	140-144
11824504-9	2001	For bioactivation of leptin the importance of disulfide-binding site is suggested.	Disulfides	46-55	leptin	Rattus norvegicus	21-27
35325335-2	2022	Chloroplast-localized classical Trx is a small redox-active protein that regulates many target proteins by reducing their disulfide bonds in a light-dependent manner.	Disulfides	122-131	thioredoxin H-type 1	Arabidopsis thaliana	32-35
11146114-2	2000	One of the major consequences of oxidative stress in brain is formation of protein-glutathione mixed disulfide (through oxidation of protein thiols) which can be reversed by thioltransferase during recovery of brain from oxidative stress.	Disulfides	101-110	glutaredoxin	Homo sapiens	174-190
35112407-4	2022	The redox potential of the CXU motif, together with insulin turbidimetric assay suggested that SELENOF may catalyze the reduction of disulfides in misfolded proteins.	Disulfides	133-143	selenoprotein F	Homo sapiens	95-102
35236515-5	2022	With an increase in the degree of denaturation and disulfide bond formation, the bonding between beta-lactoglobulin and kappa-casein was suppressed to decrease the amount of kappa-casein-WPI complexes.	Disulfides	51-60	casein kappa	Homo sapiens	120-132
35236515-5	2022	With an increase in the degree of denaturation and disulfide bond formation, the bonding between beta-lactoglobulin and kappa-casein was suppressed to decrease the amount of kappa-casein-WPI complexes.	Disulfides	51-60	casein kappa	Homo sapiens	174-186
11146114-8	2000	These discrete neuronal concentrations of thioltransferase would be consistent with an essential role in modulating recovery of protein thiols from mixed disulfides formed during oxidative stress.	Disulfides	154-164	glutaredoxin	Homo sapiens	42-58
11150184-0	2000	Disulfide-strapped porphyrins for monolayer formation on gold Porphyrins with a disulfide-containing strap have been prepared as an alternative to dithiols for self-assembled monolayer formation on gold surfaces.	Disulfides	0-9	serine/threonine kinase receptor associated protein	Homo sapiens	10-15
11150184-0	2000	Disulfide-strapped porphyrins for monolayer formation on gold Porphyrins with a disulfide-containing strap have been prepared as an alternative to dithiols for self-assembled monolayer formation on gold surfaces.	Disulfides	80-89	serine/threonine kinase receptor associated protein	Homo sapiens	10-15
11206080-1	2000	The folding of ribonuclease A (RNase A) has been extensively studied by characterizing the disulfide containing intermediates using different experimental conditions and analytical techniques.	Disulfides	91-100	ribonuclease A family member 1, pancreatic	Homo sapiens	15-29
35259130-4	2022	Retinoschisin is a homo-octamer complex with disulfide links that are released by retinal cells.	Disulfides	45-54	retinoschisin 1	Homo sapiens	0-13
11206080-1	2000	The folding of ribonuclease A (RNase A) has been extensively studied by characterizing the disulfide containing intermediates using different experimental conditions and analytical techniques.	Disulfides	91-100	ribonuclease A family member 1, pancreatic	Homo sapiens	31-38
35204259-8	2022	Some glutaredoxin-deficient bacteria had stronger fast disulfide reducibility.	Disulfides	55-64	glutaredoxin	Homo sapiens	5-17
11206080-3	2000	We have studied the oxidative folding of a RNase A derivative containing at position 67 the substitution Asn --&gt; isoAsp where the local structure of the loop 65-72 has been modified keeping intact the C65-C72 disulfide bond.	Disulfides	212-221	ribonuclease A family member 1, pancreatic	Homo sapiens	43-50
35204259-11	2022	It also indicated that cellular disulfide reduction could be classified into fast and slow reaction, which are predominantly catalyzed by E. coli Trx and Grx system, respectively.	Disulfides	32-41	glutaredoxin	Homo sapiens	154-157
10945991-1	2000	Metabotropic glutamate receptor 1 (mGluR1) expresses at the cell surface as disulfide-linked dimers and can be reduced to monomers with sulfhydryl reagents.	Disulfides	76-85	glutamate metabotropic receptor 1	Homo sapiens	0-33
10945991-1	2000	Metabotropic glutamate receptor 1 (mGluR1) expresses at the cell surface as disulfide-linked dimers and can be reduced to monomers with sulfhydryl reagents.	Disulfides	76-85	glutamate metabotropic receptor 1	Homo sapiens	35-41
10945991-10	2000	Taken together, the results suggest that Cys-140 contributes to intermolecular disulfide-linked dimerization of mGluR1.	Disulfides	79-88	glutamate metabotropic receptor 1	Homo sapiens	112-118
35014648-3	2022	In this study, an injectable disulfide-cross-linked chitosan hydrogel loaded with bFGF was prepared via a thiol-disulfide exchange reaction for MI treatment.	Disulfides	29-38	fibroblast growth factor 2	Rattus norvegicus	82-86
11009618-5	2000	By comparison of the folding kinetics of the mutants with that of wild-type RNase A, the contribution of each disulfide bond to the folding process has been evaluated.	Disulfides	110-119	ribonuclease A family member 1, pancreatic	Homo sapiens	76-83
35014648-3	2022	In this study, an injectable disulfide-cross-linked chitosan hydrogel loaded with bFGF was prepared via a thiol-disulfide exchange reaction for MI treatment.	Disulfides	112-121	fibroblast growth factor 2	Rattus norvegicus	82-86
35111980-0	2022	Sensitive and resistant of the homologous disulfide-bridged proteins alpha-lactalbumin and lysozyme to attack of hydrogen-atoms, dithiothreitol and trifluoroacetic acid, examined by matrix-assisted laser desorption/ionization mass spectrometry.	Disulfides	42-51	lysozyme C, tracheal isozyme	Bos taurus	91-99
11009618-8	2000	The removal of the C58-C110 and C26-C84 disulfide bonds has a dramatic effect on the kinetics of RNase A folding.	Disulfides	40-49	ribonuclease A family member 1, pancreatic	Homo sapiens	97-104
35111980-1	2022	Background: Evolutionarily homologous proteins bovine alpha-lactoalbumin (alphaLA) and hen egg-white lysozyme (HEL) are very similar in primary, secondary and tertiary structures involving the location of disulfide-bridges (S-S), and are resistant to the action of hydrolytic enzymes and reagents.	Disulfides	205-214	lysozyme C, tracheal isozyme	Bos taurus	101-109
10889195-6	2000	After reduction of the disulfide-bonds in the N-terminal domain of the receptor, the reduced LDL receptor was visualized using cryoEM; reduced LDL receptors showed images with a diffuse density region at the distal end of the extracellular domain.	Disulfides	23-32	low density lipoprotein receptor	Bos taurus	93-105
34609517-2	2022	In eukaryotes, protein disulfide isomerase (PDI) is an enzyme catalyzing the disulfide bond formation and isomerization in substrates.	Disulfides	77-86	protein disulfide isomerase	Arabidopsis thaliana	15-42
34609517-2	2022	In eukaryotes, protein disulfide isomerase (PDI) is an enzyme catalyzing the disulfide bond formation and isomerization in substrates.	Disulfides	77-86	protein disulfide isomerase	Arabidopsis thaliana	44-47
10993731-1	2000	The CD3 polypeptides (epsilon, gamma, and delta) are non-covalently associated signaling subunits of the T cell receptor which form non-disulfide linked epsilongamma and epsilondelta heterodimers.	Disulfides	136-145	CD3 antigen, epsilon polypeptide	Mus musculus	4-7
10874032-3	2000	Here, we have identified a cysteine residue responsible for the intermolecular disulfide bond and determined domain organization of the extracellular region of mGluR1.	Disulfides	79-88	glutamate metabotropic receptor 1	Homo sapiens	160-166
10846182-8	2000	By using NMR, we have determined the major conformation of the N terminus of SDF-1 in a 17-mer (residues 1-17 of SDF-1) and a 9-mer dimer (residues 1-9 of SDF-1 linked by a disulfide bond at residue 9).	Disulfides	173-182	C-X-C motif chemokine ligand 12	Homo sapiens	77-82
10906068-8	2000	Even though the ubiquitin cross-reactivity was transiently lost from the sperm mitochondria during epididymal passage, likely as a result of disulfide bond cross-linking, it was restored and amplified after fertilization.	Disulfides	141-150	ubiquitin	Bos taurus	16-25
10931192-5	2000	Titration experiments have shown the presence of six free cysteines and three disulfide bridges in native rat DPPIV.	Disulfides	78-87	dipeptidylpeptidase 4	Rattus norvegicus	110-115
10931199-3	2000	Enzyme-based proteolytic cleavage of the synthetic Pi1 (sPi1) demonstrates half-cystine pairings between Cys4-Cys25, Cys10-Cys30, Cys14-Cys32 and Cys20-Cys35, which is in agreement with the disulfide bridge organization initially reported on the natural toxin.	Disulfides	190-199	Pancreas inflammation QTL 1	Rattus norvegicus	51-54
10891368-6	2000	Furthermore, in vitro synthesized Id2 homodimers became monomers under reducing conditions, indicating that the formation of an intermolecular disulfide bond is critical for Id2 homodimerization.	Disulfides	143-152	inhibitor of DNA binding 2	Mus musculus	34-37
10891368-6	2000	Furthermore, in vitro synthesized Id2 homodimers became monomers under reducing conditions, indicating that the formation of an intermolecular disulfide bond is critical for Id2 homodimerization.	Disulfides	143-152	inhibitor of DNA binding 2	Mus musculus	174-177
10806188-0	2000	Drug-stimulated ATPase activity of human P-glycoprotein is blocked by disulfide cross-linking between the nucleotide-binding sites.	Disulfides	70-79	dynein axonemal heavy chain 8	Homo sapiens	16-22
10858494-7	2000	These data indicate that: (a) ecto-sulfhydryls are necessary for integrin-mediated platelet adhesion; (b) disulfide exchange takes place during this process; (c) surface PDI is involved in integrin-mediated adhesion.	Disulfides	106-115	prolyl 4-hydroxylase subunit beta	Homo sapiens	170-173
10841762-6	2000	After redox shuffling, they showed unspecific disulfide bridge patterns similar to that of the chemically synthesized wild-type PLB transmembrane domain.	Disulfides	46-55	phospholamban	Homo sapiens	128-131
10841762-9	2000	In contrast, a designed recombinant COMPcc mutant, COMP-ARCC, which was engineered to contain the two PLB cysteines that potentially could form an interchain disulfide bridge, formed a specific disulfide bond pattern.	Disulfides	158-167	phospholamban	Homo sapiens	102-105
10841762-9	2000	In contrast, a designed recombinant COMPcc mutant, COMP-ARCC, which was engineered to contain the two PLB cysteines that potentially could form an interchain disulfide bridge, formed a specific disulfide bond pattern.	Disulfides	194-203	phospholamban	Homo sapiens	102-105
10799583-0	2000	Variable-loop-deleted variants of the human immunodeficiency virus type 1 envelope glycoprotein can be stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits.	Disulfides	135-144	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	162-167
10737941-1	2000	Yeast phosphoglycerate kinase is a structurally well-characterized enzyme consisting of 415 amino acids without disulfide bonds.	Disulfides	112-121	phosphoglycerate kinase	Saccharomyces cerevisiae S288C	6-29
10788425-1	2000	Protein-disulfide isomerase (PDI) is a catalyst of folding of disulfide-bonded proteins and also a multifunctional polypeptide that acts as the beta-subunit in the prolyl 4-hydroxylase alpha(2)beta(2)-tetramer (P4H) and the microsomal triglyceride transfer protein alphabeta-dimer.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
10803663-1	2000	Plasma lipoprotein(a) [Lp(a)]-consisting of a disulfide-linked complex of apolipoprotein B and apolipoprotein (a)--levels are considered to be an independent risk factor for coronary heart disease.	Disulfides	46-55	lipoprotein(a)	Homo sapiens	23-28
10722741-5	2000	This protein contains altogether eight cysteine residues, and interchain disulfide bonds could be located in the NC1 domain and possibly at the junction of COL1 and NC2, while the two cysteine residues in NC4 are likely to form intrachain bonds.	Disulfides	73-82	down-regulator of transcription 1	Homo sapiens	165-168
10683254-0	2000	Development of disulfide peptide mapping and determination of disulfide structure of recombinant human osteoprotegerin chimera produced in Escherichia coli.	Disulfides	62-71	TNF receptor superfamily member 11b	Homo sapiens	103-118
10683254-3	2000	A cysteine-rich region in osteoprotegerin contains nine disulfide bridges homologous to the cysteine-rich signature structure of the tumor necrosis factor receptor/nerve growth factor receptor superfamily.	Disulfides	56-65	TNF receptor superfamily member 11b	Homo sapiens	26-41
10752614-4	2000	In the same experimental conditions, protein disulfide isomerase (PDI) was shown to catalyze formation and reduction of mixed disulfides with glutathione as well as formation of intramolecular S-S bonds.	Disulfides	126-136	prolyl 4-hydroxylase subunit beta	Homo sapiens	37-64
10752614-4	2000	In the same experimental conditions, protein disulfide isomerase (PDI) was shown to catalyze formation and reduction of mixed disulfides with glutathione as well as formation of intramolecular S-S bonds.	Disulfides	126-136	prolyl 4-hydroxylase subunit beta	Homo sapiens	66-69
10752614-5	2000	This paper reports the structural characterization of the one-disulfide intermediate population during the oxidative refolding of Ribonuclease A under the presence of PDI and glutathione with the aim of defining the role of the enzyme at the early stages of the reaction.	Disulfides	62-71	prolyl 4-hydroxylase subunit beta	Homo sapiens	167-170
10752614-6	2000	The one-disulfide intermediate population occurring at the early stages of both the uncatalyzed and the PDI-catalyzed refolding was purified and structurally characterized by proteolytic digestion followed by MALDI-MS and LC/ESIMS analyses.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	104-107
10752614-8	2000	Under the presence of PDI, only two additional nonnative disulfides were detected.	Disulfides	57-67	prolyl 4-hydroxylase subunit beta	Homo sapiens	22-25
10752614-13	2000	The presence of PDI does not significantly alter the distribution of S-S bonds, suggesting that the ensemble of single-disulfide species is formed under thermodynamic control.	Disulfides	119-128	prolyl 4-hydroxylase subunit beta	Homo sapiens	16-19
33176263-3	2021	ERdj5, an ER-resident disulfide reductase that promotes ER-associated degradation, reduces nonnative disulfide bonds of misfolded proteins utilizing the dynamics of its N-terminal and C-terminal clusters.	Disulfides	22-31	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	0-5
10684647-0	2000	ATP-dependent dissociation of non-disulfide-linked aggregates of coagulation factor VIII is a rate-limiting step for secretion.	Disulfides	34-43	coagulation factor VIII	Homo sapiens	65-88
33419032-6	2021	Therefore, the conservative thiol of rWT Ocm is prone to disulfide dimerization under physiological redox conditions.	Disulfides	57-66	oncomodulin	Rattus norvegicus	41-44
33212041-3	2021	Here, we demonstrate that GQQ-792, a thiodiketopiperazine derivative from marine nature products, is a non-ATP-competitive inhibitor of PGK1 with the disulfide group within the structure of GQQ-792 as a key pharmacophore.	Disulfides	150-159	phosphoglycerate kinase 1	Homo sapiens	136-140
33212041-4	2021	The disulfide group of GQQ-792 binds to Cys379 and Cys380 of PGK1, resulting in occlusion of ATP from binding to PGK1.	Disulfides	4-13	phosphoglycerate kinase 1	Homo sapiens	61-65
10684647-4	2000	In contrast to the numerous examples of interchain disulfide-linked aggregates, factor VIII is the first protein characterized to form non-disulfide-linked high molecular weight aggregates within the ER.	Disulfides	51-60	cytochrome c oxidase subunit 8A	Homo sapiens	87-91
10684647-4	2000	In contrast to the numerous examples of interchain disulfide-linked aggregates, factor VIII is the first protein characterized to form non-disulfide-linked high molecular weight aggregates within the ER.	Disulfides	139-148	cytochrome c oxidase subunit 8A	Homo sapiens	87-91
32805308-1	2021	The thioredoxin domain containing 5 (TXNDC5) is a recently discovered member of the protein disulfide isomerase family (PDI), which is mainly involved in the proper folding of and the correct formation of disulfide bonds in newly synthesized proteins via its disulfide isomerase and chaperone activities.	Disulfides	92-101	thioredoxin domain containing 5	Homo sapiens	37-43
10653666-7	2000	PDI-facilitated aggregation occurs even when disulfide formation is precluded by the presence of dithiothreitol (10 mM).	Disulfides	45-54	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
32805308-1	2021	The thioredoxin domain containing 5 (TXNDC5) is a recently discovered member of the protein disulfide isomerase family (PDI), which is mainly involved in the proper folding of and the correct formation of disulfide bonds in newly synthesized proteins via its disulfide isomerase and chaperone activities.	Disulfides	205-214	thioredoxin domain containing 5	Homo sapiens	37-43
33210532-6	2020	Subsequently, the modification of a HER2-targeting Fab with a fluorescein-conjugated variant of DiPODS (DiPODS-PEG4-FITC) reinforced the site-specificity of the reagent, illustrated its ability to rebridge disulfide linkages, and produced an immunoconjugate with in vitro properties superior to those of an analogous construct created using traditional stochastic bioconjugation techniques.	Disulfides	206-215	FA complementation group B	Homo sapiens	51-54
11193762-3	2000	A phylogenetic analysis shows that the family can be grouped into five subfamilies, A to E. Subfamily A contains rabbit uteroglobin and its orthologues from various species; most of these have been described to form antiparallel homodimers via two intermolecular disulfide bonds.	Disulfides	263-272	uteroglobin	Oryctolagus cuniculus	120-131
33291690-4	2020	The blood clotting protein, fibrinogen, and the protease inhibitor, alpha2-macroglobulin, exist in multiple disulfide-bonded or covalent states in the circulation.	Disulfides	108-117	alpha-2-macroglobulin	Homo sapiens	68-88
10637488-1	2000	The anti-CD25 immunotoxin RFT5.dgA was constructed by coupling the monoclonal antibody RFT5 via a sterically hindered disulfide linker to deglycosylated ricin A-chain and was administered to patients with relapsed Hodgkin"s lymphoma in four bolus infusions over 7 days (day 1, 3, 5 and 7).	Disulfides	118-127	interleukin 2 receptor subunit alpha	Homo sapiens	9-13
33291690-6	2020	In this study, probabilities for disulfide bond formation are employed to estimate numbers of covalent states of a model polypeptide with reference to alpha2-macroglobulin.	Disulfides	33-42	alpha-2-macroglobulin	Homo sapiens	151-171
33030311-5	2020	Acromelic dysplasia subtypes that share symptoms with Marfan syndrome are associated with FBN1-TB5 disulfide disruptions, which are also commonly found in Marfan syndrome.	Disulfides	99-108	fibrillin 1	Homo sapiens	90-94
11013399-3	2000	Reduced and carboxyamidated ribonuclease A (RCAM) is a member of a class of disulfide-free RNase A molecules believed to be random coils (extensively denatured) in aqueous solution.	Disulfides	76-85	ribonuclease A family member 1, pancreatic	Homo sapiens	91-98
33271741-3	2020	A human anti-gp41 antibody (7B2) was conjugated to two photosensitizers (PSs) with different charges through different linking strategies; "Click" conjugation by using an azide-bearing porphyrin attached via a disulfide bridge linker with a drug-to-antibody ratio (DAR) of exactly 4, and "Lysine" conjugation by using phthalocyanine IRDye 700DX dye with average DARs of 2.1, 3.0 and 4.4.	Disulfides	210-219	secretogranin V	Homo sapiens	28-31
10611525-1	1999	Glial cell line-derived neurotrophic factor (GDNF) is a glycosylated, disulfide-bonded homodimer, and a member of the transforming growth factor-beta superfamily.	Disulfides	70-79	glial cell derived neurotrophic factor	Rattus norvegicus	0-43
33016372-3	2020	System xc - consists of two subunits, the light chain subunit SLC7A11 (xCT) and the heavy chain subunit SLC3A2 (also known as CD98hc or 4F2hc), which are linked by a conserved disulfide bridge.	Disulfides	176-185	solute carrier family 3 member 2	Homo sapiens	104-110
33016372-3	2020	System xc - consists of two subunits, the light chain subunit SLC7A11 (xCT) and the heavy chain subunit SLC3A2 (also known as CD98hc or 4F2hc), which are linked by a conserved disulfide bridge.	Disulfides	176-185	solute carrier family 3 member 2	Homo sapiens	136-141
10611525-1	1999	Glial cell line-derived neurotrophic factor (GDNF) is a glycosylated, disulfide-bonded homodimer, and a member of the transforming growth factor-beta superfamily.	Disulfides	70-79	glial cell derived neurotrophic factor	Rattus norvegicus	45-49
10559209-2	1999	While Cys-14 and Cys-17 have previously been shown to be Hg(2+)-binding residues, MerP is readily isolated in an inactive Cys-14-Cys-17 disulfide form.	Disulfides	136-145	mercuric transport protein periplasmic component MerP	Escherichia coli	82-86
33136379-7	2020	Importantly, we demonstrate the advantages of our newly developed method for the protection and deprotection of native cysteine with a succinimide group in a peptide fragment derived from thioredoxin-1 (Trx-1) obtained via intein based expression to enable ligation/desulfurization and subsequent disulfide bond formation in a one-pot process.	Disulfides	297-306	thioredoxin	Homo sapiens	188-201
33136379-7	2020	Importantly, we demonstrate the advantages of our newly developed method for the protection and deprotection of native cysteine with a succinimide group in a peptide fragment derived from thioredoxin-1 (Trx-1) obtained via intein based expression to enable ligation/desulfurization and subsequent disulfide bond formation in a one-pot process.	Disulfides	297-306	thioredoxin	Homo sapiens	203-208
10753067-6	1999	RESULTS: After transient transfection of COS-7 cells, IFNgammaR/IgG1 and IL-4/IgG1 fusion proteins are secreted in vitro as disulfide-linked homodimers, with the expected biological activity.	Disulfides	124-133	interferon gamma receptor 1	Mus musculus	54-63
32848019-6	2020	The in vitro studies using recombinant proteins from Arabidopsis thaliana showed that a specific PGDH isoform, PGDH1, forms the intramolecular disulfide bond under non-reducing conditions, which lowers PGDH enzyme activity.	Disulfides	143-152	D-3-phosphoglycerate dehydrogenase	Arabidopsis thaliana	97-101
32848019-6	2020	The in vitro studies using recombinant proteins from Arabidopsis thaliana showed that a specific PGDH isoform, PGDH1, forms the intramolecular disulfide bond under non-reducing conditions, which lowers PGDH enzyme activity.	Disulfides	143-152	D-3-phosphoglycerate dehydrogenase	Arabidopsis thaliana	111-115
10521522-4	1999	Our prior work has demonstrated that the CLV1 receptor-like kinase (RLK) is present as a disulfide-linked multimer in vivo.	Disulfides	89-98	Leucine-rich receptor-like protein kinase family protein	Arabidopsis thaliana	41-45
32848019-7	2020	Mass spectrometry and site-directed mutagenesis analyses allowed us to identify the redox-active Cys pair that is mainly involved in disulfide bond formation in PGDH1; this Cys pair is uniquely found in land plant PGDH.	Disulfides	133-142	D-3-phosphoglycerate dehydrogenase	Arabidopsis thaliana	161-165
33103597-6	2022	We show that the Cys33-Cys33 intermolecular disulfide bridge that stabilizes the Hp1:Hp1 complex is replaced by the Phe33, Pro34, and Phe48 hydrophobic core in the Hpr:Hpr dimer.	Disulfides	44-53	chromobox 5	Homo sapiens	81-84
33103597-6	2022	We show that the Cys33-Cys33 intermolecular disulfide bridge that stabilizes the Hp1:Hp1 complex is replaced by the Phe33, Pro34, and Phe48 hydrophobic core in the Hpr:Hpr dimer.	Disulfides	44-53	chromobox 5	Homo sapiens	85-88
33105619-11	2020	This variation induces an altered folate receptor alpha protein and underlines the role of a disulfide bond: Cys66-Cys109, essential to transport 5-MTHF into the central nervous system.	Disulfides	93-102	folate receptor alpha	Homo sapiens	34-55
10521522-4	1999	Our prior work has demonstrated that the CLV1 receptor-like kinase (RLK) is present as a disulfide-linked multimer in vivo.	Disulfides	89-98	receptor lectin kinase	Arabidopsis thaliana	68-71
32505675-3	2020	Each EGF repeat consists of about 40 amino acids with 3 conserved disulfide bonds.	Disulfides	66-75	epidermal growth factor	Mus musculus	5-8
10464289-4	1999	Importantly, co-incubation with PGE(2) protected PGT from this inhibition, suggesting that MTSES gains access to the aqueous pore pathway of PGT to form a mixed disulfide near the substrate-binding site.	Disulfides	161-170	solute carrier organic anion transporter family member 2A1	Homo sapiens	49-52
32505675-10	2020	With the fusion tag, EGF27 was refolded to produce the correct disulfide bond arrangement, which was verified enzymatically with the glycosyltransferases, Protein O-fucosyltransferase 1 (POFUT1) and Lunatic Fringe (LFNG).	Disulfides	63-72	LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase	Mus musculus	199-213
32505675-10	2020	With the fusion tag, EGF27 was refolded to produce the correct disulfide bond arrangement, which was verified enzymatically with the glycosyltransferases, Protein O-fucosyltransferase 1 (POFUT1) and Lunatic Fringe (LFNG).	Disulfides	63-72	LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase	Mus musculus	215-219
33011677-8	2020	A mechanistic explanation that ADAM17cyto favors the monomeric, active state of Trx-1 is the formation of a disulfide bond between Cys824 at the C-terminal of ADAM17cyto with the Cys73 of Trx-1, which is involved in the dimerization site of Trx-1.	Disulfides	108-117	thioredoxin	Homo sapiens	80-85
33011677-8	2020	A mechanistic explanation that ADAM17cyto favors the monomeric, active state of Trx-1 is the formation of a disulfide bond between Cys824 at the C-terminal of ADAM17cyto with the Cys73 of Trx-1, which is involved in the dimerization site of Trx-1.	Disulfides	108-117	thioredoxin	Homo sapiens	188-193
10464289-4	1999	Importantly, co-incubation with PGE(2) protected PGT from this inhibition, suggesting that MTSES gains access to the aqueous pore pathway of PGT to form a mixed disulfide near the substrate-binding site.	Disulfides	161-170	solute carrier organic anion transporter family member 2A1	Homo sapiens	141-144
10439027-3	1999	Human cystatin C and salivary cystatin SN are 120- and 121-amino-acid (a.a.) proteins, respectively, and both contain 2 disulfide bonds.	Disulfides	120-129	cystatin C	Homo sapiens	6-16
33011677-8	2020	A mechanistic explanation that ADAM17cyto favors the monomeric, active state of Trx-1 is the formation of a disulfide bond between Cys824 at the C-terminal of ADAM17cyto with the Cys73 of Trx-1, which is involved in the dimerization site of Trx-1.	Disulfides	108-117	thioredoxin	Homo sapiens	188-193
10439027-3	1999	Human cystatin C and salivary cystatin SN are 120- and 121-amino-acid (a.a.) proteins, respectively, and both contain 2 disulfide bonds.	Disulfides	120-129	cystatin SN	Homo sapiens	30-41
10503268-1	1999	Lipoprotein(a) [Lp(a)] is formed when apolipoprotein(a) is linked to low density lipoprotein (LDL)-cholesterol via a single disulfide bond.	Disulfides	124-133	lipoprotein(a)	Homo sapiens	0-14
33061675-2	2020	A high level of effectiveness of hEGF can be obtained when three disulfide bonds fold perfectly.	Disulfides	65-74	epidermal growth factor	Homo sapiens	33-37
10503268-1	1999	Lipoprotein(a) [Lp(a)] is formed when apolipoprotein(a) is linked to low density lipoprotein (LDL)-cholesterol via a single disulfide bond.	Disulfides	124-133	lipoprotein(a)	Homo sapiens	16-21
10452546-3	1999	In the presence of PDI, major changes were found in the distribution of intermediates in the three-disulfide region at 25 and 15 degrees C and also in the one-disulfide region at 15 degrees C, with the fast accumulation of the two native-like species des-[65-72] and des-[40-95].	Disulfides	99-108	prolyl 4-hydroxylase subunit beta	Bos taurus	19-22
33024804-3	2020	Human cofilin-2 contains two cysteines (Cys39 and Cys80) which can be oxidized in suitable conditions and form a disulfide bridge [1].	Disulfides	113-122	cofilin 2	Homo sapiens	6-15
10452546-3	1999	In the presence of PDI, major changes were found in the distribution of intermediates in the three-disulfide region at 25 and 15 degrees C and also in the one-disulfide region at 15 degrees C, with the fast accumulation of the two native-like species des-[65-72] and des-[40-95].	Disulfides	159-168	prolyl 4-hydroxylase subunit beta	Bos taurus	19-22
32779864-3	2020	Here, we show that the CHCHD4/GFER disulfide relay system in the mitochondrial intermembrane space (IMS) is required for PINK1 stabilization when mitochondrial membrane potential is lost.	Disulfides	35-44	growth factor, augmenter of liver regeneration	Homo sapiens	30-34
10409115-8	1999	Moreover, on transient expression in GH(4)C(1) cells, CgA and a CgA mutant lacking the conserved disulfide bond showed comparable multimeric aggregation properties and targeting to secretory granules, as measured by stimulated secretion assays.	Disulfides	97-106	chromogranin A	Rattus norvegicus	54-57
32848143-3	2020	Here we show that an ER protein disulfide isomerase, thioredoxin domain containing 5 (TXNDC5), is highly upregulated in the lung tissues from both patients with idiopathic pulmonary fibrosis and a mouse model of bleomycin (BLM)-induced PF.	Disulfides	32-41	thioredoxin domain containing 5	Homo sapiens	53-84
32848143-3	2020	Here we show that an ER protein disulfide isomerase, thioredoxin domain containing 5 (TXNDC5), is highly upregulated in the lung tissues from both patients with idiopathic pulmonary fibrosis and a mouse model of bleomycin (BLM)-induced PF.	Disulfides	32-41	thioredoxin domain containing 5	Homo sapiens	86-92
10409115-8	1999	Moreover, on transient expression in GH(4)C(1) cells, CgA and a CgA mutant lacking the conserved disulfide bond showed comparable multimeric aggregation properties and targeting to secretory granules, as measured by stimulated secretion assays.	Disulfides	97-106	chromogranin A	Rattus norvegicus	64-67
32449244-5	2020	Computational docking simulations predict a greater binding affinity to the TrxR active site in comparison to its disulfide analogue.	Disulfides	114-123	peroxiredoxin 5	Homo sapiens	76-80
10387094-4	1999	During biosynthetic processing, C8 alpha and C8 gamma associate to form a disulfide-linked dimer (C8 alpha-gamma) that binds to C8 beta through a site located on C8 alpha.	Disulfides	74-83	complement C8 beta chain	Homo sapiens	128-135
32449244-6	2020	In vitro imaging studies further confirmed the diselenide probe exhibited improved signaling of TrxR activity compared to the disulfide analogue.	Disulfides	126-135	peroxiredoxin 5	Homo sapiens	96-100
32171739-0	2020	Influence of disulfide bonds in human beta defensin-3 on its strain specific activity against Gram-negative bacteria.	Disulfides	13-22	defensin beta 103B	Homo sapiens	38-53
32171739-10	2020	However, the stability of hBD-3 against protease activity decreases with decreasing number of disulfide bonds.	Disulfides	94-103	defensin beta 103B	Homo sapiens	26-31
10336870-0	1999	Heterologous expression of 5"-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus: characterization of the recombinant protein and involvement of disulfide bonds in thermophilicity and thermostability.	Disulfides	170-179	peptide chain release factor aRF-1	Saccharolobus solfataricus	27-63
32376199-5	2020	Their mixture contains a mixed disulfide between insulin B-chain and thioredoxin-Cys73, which limits their activities.	Disulfides	31-40	thioredoxin	Homo sapiens	69-80
32472977-6	2020	The identified PKD1 mutation is inherited and unreported variant, which can alter the formation of intramolecular disulfide bonds essential for polycystin-1 function.	Disulfides	114-123	polycystin 1, transient receptor potential channel interacting	Homo sapiens	15-19
32472977-6	2020	The identified PKD1 mutation is inherited and unreported variant, which can alter the formation of intramolecular disulfide bonds essential for polycystin-1 function.	Disulfides	114-123	polycystin 1, transient receptor potential channel interacting	Homo sapiens	144-156
10336870-4	1999	The heterologously expressed enzyme is identical to the original S. solfataricus 5"-methylthioadenosine phosphorylase regarding molecular weight, substrate specificity, and the presence of intersubunit disulfide bonds.	Disulfides	202-211	peptide chain release factor aRF-1	Saccharolobus solfataricus	81-117
33397549-0	2020	Enhanced Suppression of Disulfide Cross-Linking Micelles Nanocarriers Loaded miR-145 Delivering System via Down-Regulation of MYC and FSCN1 in Colon Cancer Cells.	Disulfides	24-33	microRNA 145	Homo sapiens	77-84
10336870-5	1999	On the other hand, the recombinant 5"-methylthioadenosine phosphorylase is less thermophilic and thermostable than the S. solfataricus enzyme, since an incorrect positioning of disulfide bonds within the molecule generates structures less stable to thermal unfolding.	Disulfides	177-186	peptide chain release factor aRF-1	Saccharolobus solfataricus	35-71
33397549-0	2020	Enhanced Suppression of Disulfide Cross-Linking Micelles Nanocarriers Loaded miR-145 Delivering System via Down-Regulation of MYC and FSCN1 in Colon Cancer Cells.	Disulfides	24-33	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	126-129
10231542-2	1999	Short-term treatment of intact cells expressing large numbers of IR with GSH or NAC led to a rapid and reversible reduction of IR alpha-subunit disulfides, without affecting the receptor beta-subunit thiol reactivity.	Disulfides	144-154	insulin receptor	Homo sapiens	65-67
32518155-4	2020	beta2GPI exists in two almost equally populated redox states: oxidized, in which all the disulfide bonds are formed, and reduced, in which one or more disulfide bonds are broken.	Disulfides	89-98	apolipoprotein H	Homo sapiens	0-8
10231542-2	1999	Short-term treatment of intact cells expressing large numbers of IR with GSH or NAC led to a rapid and reversible reduction of IR alpha-subunit disulfides, without affecting the receptor beta-subunit thiol reactivity.	Disulfides	144-154	insulin receptor	Homo sapiens	127-129
32518155-4	2020	beta2GPI exists in two almost equally populated redox states: oxidized, in which all the disulfide bonds are formed, and reduced, in which one or more disulfide bonds are broken.	Disulfides	151-160	apolipoprotein H	Homo sapiens	0-8
10231542-4	1999	Similar findings were obtained in cells transfected with IR mutants lacking cysteine524, one of the class I disulfides that link the two IR alpha-subunits.	Disulfides	108-118	insulin receptor	Homo sapiens	57-59
32681182-3	2020	Protein disulfide isomerase (PDI) is a member of the thioredoxin (Trx) superfamily, is capable of catalyzing the formation and heterogeneity of protein disulfide bonds and inhibiting the aggregation of misfolded proteins.	Disulfides	8-17	thioredoxin	Homo sapiens	53-64
32681182-3	2020	Protein disulfide isomerase (PDI) is a member of the thioredoxin (Trx) superfamily, is capable of catalyzing the formation and heterogeneity of protein disulfide bonds and inhibiting the aggregation of misfolded proteins.	Disulfides	8-17	thioredoxin	Homo sapiens	66-69
10327168-7	1999	The hydrophobic regions in G1 AChE probably provide conformational stability to disulfide-linked subunits in hydrophilic dimers.	Disulfides	80-89	acetylcholinesterase	Mus musculus	30-34
10066758-4	1999	Several proteins involved in disulfide exchange reactions contain the sequence Cys-X-X-Cys in their active sites, including thioredoxin and protein-disulfide isomerase.	Disulfides	29-38	prolyl 4-hydroxylase subunit beta	Homo sapiens	140-167
10036174-4	1999	When a sample of partially denatured RNase A was placed under mild reducing conditions (0.2-1 mM dithiothreitol for 10 min), the disulfide bonds of the native RNase A remain intact, whereas those of scrambled isomers become fully reduced.	Disulfides	129-138	ribonuclease A family member 1, pancreatic	Homo sapiens	37-44
32434885-0	2020	Per Os Infectivity Factor 5 Identified as a Substrate of P33 in the Baculoviral Disulfide Bond Formation Pathway.	Disulfides	80-89	inhibitor of growth family member 1	Homo sapiens	57-60
32434885-11	2020	Further, the disulfide bonds in PIF5 play an essential role in its function in oral infection.IMPORTANCE Similar to some large DNA viruses that encode their own disulfide bond pathway, baculovirus encodes a viral sulfhydryl oxidase, P33.	Disulfides	13-22	inhibitor of growth family member 1	Homo sapiens	233-236
32434885-11	2020	Further, the disulfide bonds in PIF5 play an essential role in its function in oral infection.IMPORTANCE Similar to some large DNA viruses that encode their own disulfide bond pathway, baculovirus encodes a viral sulfhydryl oxidase, P33.	Disulfides	161-170	inhibitor of growth family member 1	Homo sapiens	233-236
10036174-4	1999	When a sample of partially denatured RNase A was placed under mild reducing conditions (0.2-1 mM dithiothreitol for 10 min), the disulfide bonds of the native RNase A remain intact, whereas those of scrambled isomers become fully reduced.	Disulfides	129-138	ribonuclease A family member 1, pancreatic	Homo sapiens	159-166
10196112-1	1999	The insulin receptor (IR) is a four-chain, transmembrane dimer held together by disulfide bonds.	Disulfides	80-89	insulin receptor	Homo sapiens	4-20
32548971-3	2020	Subsequently, polyethylene glycolated fluorescein isothiocyanate (FITC-PEG) is incorporated into the COFs via the exchange reactions between the disulfide in insulin chains and the thiol in FITC-PEG to afford a robust nano-assembly (FITC-PEG-COF@Ins-GOx).	Disulfides	145-154	hydroxyacid oxidase 1, liver	Mus musculus	250-253
32630599-6	2020	Within recent years, the formation of disulfide-linked heterodimers was documented for TFF1 and TFF3, e.g., with gastrokine-2 and IgG Fc binding protein (FCGBP).	Disulfides	38-47	trefoil factor 1	Mus musculus	87-91
32587593-5	2020	We currently investigated that peroxiredoxins I and II (PrxI/II) induce the intramolecular disulfide bond formation of HMGB1 in the nucleus.	Disulfides	91-100	peroxiredoxin 1	Homo sapiens	31-63
10196112-1	1999	The insulin receptor (IR) is a four-chain, transmembrane dimer held together by disulfide bonds.	Disulfides	80-89	insulin receptor	Homo sapiens	22-24
32587593-6	2020	Disulfide HMGB1 is preferentially transported out of the nucleus by binding to the nuclear exportin chromosome-region maintenance 1 (CRM1).	Disulfides	0-9	exportin 1	Homo sapiens	133-137
10072399-5	1999	In each complex, CLV1 is part of a disulfide-linked multimer of approximately 185 kD.	Disulfides	35-44	Leucine-rich receptor-like protein kinase family protein	Arabidopsis thaliana	17-21
32457455-4	2020	Recently, it was reported that AspH substrates have a non-canonical EGFD disulfide pattern.	Disulfides	73-82	aspartate beta-hydroxylase	Homo sapiens	31-35
32398758-3	2020	Ubiquitin exhibits weak binding to MavC alone, but shows an increase in affinity when tethered to Ube2N in a disulfide-linked substrate that mimics the charged E2~Ub conjugate.	Disulfides	109-118	ubiquitin conjugating enzyme E2 N	Homo sapiens	98-103
10072399-8	1999	We propose that CLV1 is present as an inactive disulfide-linked heterodimer and that CLV3 functions to promote the assembly of the active 450-kD complex, which then relays signal transduction through a Rho GTPase.	Disulfides	47-56	Leucine-rich receptor-like protein kinase family protein	Arabidopsis thaliana	16-20
31891446-3	2020	The HLA-B*38:55Q allele was detected as an HLA-B blank specificity; DNA sequencing identified a single polymorphism at position 373 in exon 3 (TGC > CGC), which results in the replacement of cysteine 101 with an arginine in the HLA-B heavy chain, thus, impairing disulfide bridge formation in the alpha-2 domain, essential for the normal expression of the HLA molecules.	Disulfides	263-272	major histocompatibility complex, class I, B	Homo sapiens	4-9
9988687-5	1999	Similar to yeast Tsa1p, Ahp1p forms a disulfide-linked homodimer upon oxidation and in vivo requires the presence of the thioredoxin system but not of glutathione to perform its antioxidant protective function.	Disulfides	38-47	thioredoxin peroxidase AHP1	Saccharomyces cerevisiae S288C	24-29
31623019-8	2020	Although oxidative stress induces relatively moderate structural changes in thioredoxin, the formation of intramolecular disulfide bridges leads to a considerable conformational rearrangement of the thioredoxin-binding interface on ASK1.	Disulfides	121-130	thioredoxin	Homo sapiens	199-210
31623019-8	2020	Although oxidative stress induces relatively moderate structural changes in thioredoxin, the formation of intramolecular disulfide bridges leads to a considerable conformational rearrangement of the thioredoxin-binding interface on ASK1.	Disulfides	121-130	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	232-236
10022847-0	1999	The disulfide-bonded loop of chromogranin B mediates membrane binding and directs sorting from the trans-Golgi network to secretory granules.	Disulfides	4-13	chromogranin B	Homo sapiens	29-43
32265930-5	2020	Disulfide HMGB1 activates the TLR4 complex by binding to MD-2.	Disulfides	0-9	toll like receptor 4	Homo sapiens	30-34
10022847-1	1999	The disulfide-bonded loop of chromogranin B (CgB), a regulated secretory protein with widespread distribution in neuroendocrine cells, is known to be essential for the sorting of CgB from the trans-Golgi network (TGN) to immature secretory granules.	Disulfides	4-13	chromogranin B	Homo sapiens	29-43
32091905-10	2020	The current work emphasized the structural diversity of hBD-3 interacting with negatively charged lipid membrane aected by the disulfide bonding states.	Disulfides	127-136	defensin beta 103B	Homo sapiens	56-61
10022847-1	1999	The disulfide-bonded loop of chromogranin B (CgB), a regulated secretory protein with widespread distribution in neuroendocrine cells, is known to be essential for the sorting of CgB from the trans-Golgi network (TGN) to immature secretory granules.	Disulfides	4-13	chromogranin B	Homo sapiens	45-48
10022847-1	1999	The disulfide-bonded loop of chromogranin B (CgB), a regulated secretory protein with widespread distribution in neuroendocrine cells, is known to be essential for the sorting of CgB from the trans-Golgi network (TGN) to immature secretory granules.	Disulfides	4-13	chromogranin B	Homo sapiens	179-182
32172212-2	2020	Protein disulfide isomerase (PDI) is an enzyme that catalyzes formation and isomerization of disulfide bonds and also acts as a chaperone that survives the cells against cell death by removal of misfolded proteins.	Disulfides	8-17	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	29-32
10022847-5	1999	Furthermore, the disulfide-bonded loop of CgB mediates membrane binding in the TGN and does so with 5-fold higher efficiency if two loops are present on the reporter protein.	Disulfides	17-26	chromogranin B	Homo sapiens	42-45
10048337-3	1999	The oxidation of these cysteine residues to form disulfide bonds is a rapid, cooperative process that inactivates hRI.	Disulfides	49-58	eukaryotic translation initiation factor 2 alpha kinase 1	Homo sapiens	114-117
32152335-3	2020	We investigated the hypothesis that MSE supplementation increases the adiponectin (APN) multimerization via the up-regulation of disulfide bond A oxidoreductase-like protein (DsbA-L) under either or both physiological and obese conditions.	Disulfides	129-138	glutathione S-transferase kappa 1	Mus musculus	175-181
9882436-12	1999	In summary, these data are consistent with a role for PDI-catalyzed formation of disulfide-linked complexes of TSP with other proteins.	Disulfides	81-90	prolyl 4-hydroxylase subunit beta	Homo sapiens	54-57
9852069-4	1998	We previously characterized KARAP (killer cell activating receptor-associated protein), a novel disulfide-linked tyrosine-phosphorylated dimer that selectively associates with the activating NKR isoforms.	Disulfides	96-105	tachykinin receptor 3	Mus musculus	191-194
31971218-2	2020	Herein, we report the design and synthesis of a tetrazine-based disulfide rebridging reagent, which allows the site-selective installation of a tetrazine group into disulfide-containing peptides and proteins such as the hormone somatostatin (SST) and the antigen binding fragment (Fab) of human immunoglobulin G (IgG).	Disulfides	64-73	FA complementation group B	Homo sapiens	281-284
31971218-2	2020	Herein, we report the design and synthesis of a tetrazine-based disulfide rebridging reagent, which allows the site-selective installation of a tetrazine group into disulfide-containing peptides and proteins such as the hormone somatostatin (SST) and the antigen binding fragment (Fab) of human immunoglobulin G (IgG).	Disulfides	165-174	FA complementation group B	Homo sapiens	281-284
32038043-0	2020	The thrombospondin module 1 domain of the matricellular protein CCN3 shows an atypical disulfide pattern and incomplete CWR layers.	Disulfides	87-96	cellular communication network factor 3	Homo sapiens	64-68
32038043-3	2020	Here, the crystal structure of the thrombospondin module 1 (TSP1) domain of CCN3 (previously known as Nov) is presented, which shares a similar three-stranded fold with the thrombospondin type 1 repeats of thrombospondin-1 and spondin-1, but with variations in the disulfide connectivity.	Disulfides	265-274	cellular communication network factor 3	Homo sapiens	76-80
9928079-1	1998	Protein disulfide isomerase (PDI) is the physiological catalyst of native disulfide bond formation of nascent peptides in the cells.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
31857189-0	2020	Tracing and attribution of V-type nerve agents in human exposure by strategy of assessing the phosphonylated and disulfide adducts on ceruloplasmin.	Disulfides	113-122	ceruloplasmin	Homo sapiens	134-147
9928079-4	1998	Both chaperone and isomerase activities are required for PDI to assist folding of denatured and reduced disulfide-containing proteins.	Disulfides	104-113	prolyl 4-hydroxylase subunit beta	Homo sapiens	57-60
31857189-3	2020	This paper investigates the phosphonylated and disulfide adducts between human ceruloplasmin and O-ethyl S-(2-(diisopropylamino)ethyl) methylphosphonothioate (VX), O-isobutyl S-(2-(diethylamino)ethyl) methylphosphonothioate (VR), and O-butyl S-(2-(diethylamino)ethyl) methylphosphonothioate (Vs).	Disulfides	47-56	ceruloplasmin	Homo sapiens	79-92
31857189-7	2020	Moreover, four disulfide adducts on human ceruloplasmin were also discovered during this research, specifically confirming exposure to the V-type agents.	Disulfides	15-24	ceruloplasmin	Homo sapiens	42-55
9860827-4	1998	To understand the molecular basis of TTase specificity for the glutathione moiety, we engineered a quadruple Cys to Ser mutant of human TTase (C7S, C25S, C78S, and C82S) which retains only the active site cysteine residue (C22), and we solved its high-resolution NMR solution structure in the mixed disulfide intermediate with glutathione (QM-TTase-SSG).	Disulfides	299-308	glutaredoxin	Homo sapiens	136-141
31963721-11	2020	Furthermore, a minor subset of Tff1 forms a disulfide-linked heterodimer with IgG Fc binding protein (Fcgbp).	Disulfides	44-53	trefoil factor 1	Mus musculus	31-35
31940927-2	2020	The peptides are post-translationally modified, containing six cysteines with an unusual disulfide connectivity of Cys1-Cys6, Cys2-Cys5, and Cys3-Cys4 and an amidated C-terminus.	Disulfides	89-98	cystin 1	Homo sapiens	115-119
31782617-5	2020	GPx8 binds covalently to caspase-4/11 via disulfide bonding between cysteine 79 of GPx8 and cysteine 118 of caspase-4 and thus restrains caspase-4/11 activation, while GPx8 deficiency leads to caspase-4/11-induced inflammation during colitis and septic shock.	Disulfides	42-51	glutathione peroxidase 8 (putative)	Mus musculus	0-4
31782617-5	2020	GPx8 binds covalently to caspase-4/11 via disulfide bonding between cysteine 79 of GPx8 and cysteine 118 of caspase-4 and thus restrains caspase-4/11 activation, while GPx8 deficiency leads to caspase-4/11-induced inflammation during colitis and septic shock.	Disulfides	42-51	glutathione peroxidase 8 (putative)	Mus musculus	83-87
31782617-5	2020	GPx8 binds covalently to caspase-4/11 via disulfide bonding between cysteine 79 of GPx8 and cysteine 118 of caspase-4 and thus restrains caspase-4/11 activation, while GPx8 deficiency leads to caspase-4/11-induced inflammation during colitis and septic shock.	Disulfides	42-51	glutathione peroxidase 8 (putative)	Mus musculus	83-87
29848267-6	2020	In contrast to the sulfinic and sulfonic acids, the mixed disulfide and the intramolecular disulfide bond are reversible oxidation products that can be reduced in the presence of GSH or thioredoxin.	Disulfides	58-67	thioredoxin	Homo sapiens	186-197
9860827-4	1998	To understand the molecular basis of TTase specificity for the glutathione moiety, we engineered a quadruple Cys to Ser mutant of human TTase (C7S, C25S, C78S, and C82S) which retains only the active site cysteine residue (C22), and we solved its high-resolution NMR solution structure in the mixed disulfide intermediate with glutathione (QM-TTase-SSG).	Disulfides	299-308	glutaredoxin	Homo sapiens	136-141
29848267-6	2020	In contrast to the sulfinic and sulfonic acids, the mixed disulfide and the intramolecular disulfide bond are reversible oxidation products that can be reduced in the presence of GSH or thioredoxin.	Disulfides	91-100	thioredoxin	Homo sapiens	186-197
9860827-5	1998	This mutant which cannot form a C22-S-S-C25 intramolecular disulfide displays the same catalytic efficiency (Vmax/KM) and specificity for glutathionyl mixed disulfide substrates as wild-type TTase, indicating that the Cys-25-SH moiety is not required for catalysis or glutathionyl specificity.	Disulfides	59-68	glutaredoxin	Homo sapiens	191-196
9860827-5	1998	This mutant which cannot form a C22-S-S-C25 intramolecular disulfide displays the same catalytic efficiency (Vmax/KM) and specificity for glutathionyl mixed disulfide substrates as wild-type TTase, indicating that the Cys-25-SH moiety is not required for catalysis or glutathionyl specificity.	Disulfides	157-166	glutaredoxin	Homo sapiens	191-196
9860827-7	1998	The disulfide-adducted glutathione in the TTase-SSG complex has an extended conformation and is localized in a cleft near the protein surface encompassing the residues from helices-alpha2,alpha3, the active site loop, and the loop connecting helix-alpha3 and strand-beta3.	Disulfides	4-13	glutaredoxin	Homo sapiens	42-47
9834122-4	1998	Recently, it has been reported that enzymes that catalyze disulfide exchanges such as protein disulfide isomerase (PDI) are present on the surface of lymphoid cells, raising the possibility that such enzymes might be involved in the control of lymphocyte adhesion.	Disulfides	58-67	prolyl 4-hydroxylase subunit beta	Homo sapiens	86-113
31619555-2	2019	The prototypic design, designated BG505 SOSIP.664, incorporates an inter-subunit disulfide bond (SOS) to covalently link the gp120 and gp41 ectodomain (gp41ECTO) subunits and a point substitution, I559P (IP) to further stabilize the gp41ECTO components.	Disulfides	81-90	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	125-130
31839995-11	2019	Our results indicate that DDAs are unique in causing DR5 accumulation and oligomerization and inducing downstream caspase activation and cancer cell death through mechanisms involving altered DR5 disulfide bonding.	Disulfides	196-205	TNF receptor superfamily member 10b	Homo sapiens	192-195
30477399-5	2019	To address this, based on the fact that the rectification and association of BK alpha to beta2 subunits are highly sensitive to disruption of the disulfide bonds in the extracellular loop of beta2, we developed a rectification ratio based assay by combining the site-directed mutagenesis, electrophysiology and enzymatic cleavage.	Disulfides	146-155	FCF1 rRNA-processing protein	Homo sapiens	77-85
30477399-6	2019	Three disulfide bonds: C1(C84)-C5(C113), C3(C101)-C7(C148) and C6(C142)-C8C(174) are successfully deduced in beta2 subunit in complex with a BK alpha subunit, which are helpful to predict structural model of beta2 subunits through computational simulation and to understand the interface between the extracellular domain of the beta subunits and the pore-forming alpha subunit.	Disulfides	6-15	FCF1 rRNA-processing protein	Homo sapiens	141-149
9834122-4	1998	Recently, it has been reported that enzymes that catalyze disulfide exchanges such as protein disulfide isomerase (PDI) are present on the surface of lymphoid cells, raising the possibility that such enzymes might be involved in the control of lymphocyte adhesion.	Disulfides	58-67	prolyl 4-hydroxylase subunit beta	Homo sapiens	115-118
9819101-4	1998	A typical Lp(a) represents a low-density lipoprotein (LDL)-like particle having as a protein moiety apo B-100 linked by a single interchain disulfide bond to a unique multikringle glycoprotein, called apolipoprotein(a) (apo[a]).	Disulfides	140-149	lipoprotein(a)	Homo sapiens	10-15
31776724-7	2019	Inference of the domain architecture suggested that the Crim1C140S mutation disturbs an intramolecular disulfide bond in IR1, leading to the protein instability and the functional defects of CRIM1.	Disulfides	103-112	cysteine rich transmembrane BMP regulator 1 (chordin like)	Mus musculus	56-61
31776724-7	2019	Inference of the domain architecture suggested that the Crim1C140S mutation disturbs an intramolecular disulfide bond in IR1, leading to the protein instability and the functional defects of CRIM1.	Disulfides	103-112	cysteine rich transmembrane BMP regulator 1 (chordin like)	Mus musculus	191-196
9735324-3	1998	Immunoblots of human brain tissues with and without reduction show that the DRPLA protein is a disulfide-bond complex and that more of this complex is formed in DRPLA brains than in control brains.	Disulfides	95-104	atrophin 1	Homo sapiens	76-81
31597700-1	2019	Thioredoxin (Trx) is a redox-responsive protein that modulates the activities of its target proteins mostly by reducing their disulfide bonds.	Disulfides	126-135	thioredoxin	Homo sapiens	0-11
31597700-1	2019	Thioredoxin (Trx) is a redox-responsive protein that modulates the activities of its target proteins mostly by reducing their disulfide bonds.	Disulfides	126-135	thioredoxin	Homo sapiens	13-16
9735324-5	1998	Immunohistochemical findings show that DRPLA protein is localized in the cytoplasm of the neuron, evidence that it undergoes rare disulfide bonding there.	Disulfides	130-139	atrophin 1	Homo sapiens	39-44
9722511-3	1998	HGF/NK4 contains the N-terminal hairpin and four kringle domains, while HGF/beta is composed of the C-terminal 16 amino acids of the alpha-chain and the entire beta-chain, linked by a disulfide bridge.	Disulfides	184-193	hepatocyte growth factor	Homo sapiens	72-75
31562139-2	2019	Here, we present evidence that whey acidic protein (WAP) four-disulfide core domain protease inhibitor 2 (Wfdc2), a protease inhibitor previously unrecognized in respiratory disease, may be a causal factor in infant respiratory failure.	Disulfides	62-71	WAP four-disulfide core domain 2	Homo sapiens	106-111
31050145-4	2019	The redox couple thioredoxin reductase-thioredoxin (TrxR-Trx) was identified as the responsible for reduction of this disulfide occurring on the cytosolic surface of synaptic vesicles.	Disulfides	118-127	thioredoxin	Homo sapiens	52-55
9694669-1	1998	Protein disulfide isomerase (PDI) is an enzyme that promotes protein folding by catalyzing disulfide bridge isomerization.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
31548351-4	2019	METHODS: To investigate whether receptor-mediated endocytosis by the megalin/LRP2 pathway of ultrafiltrated, disulfide-rich plasma proteins could be a source of cystine in proximal tubular cells, we used a mouse model of cystinosis in which conditional excision of floxed megalin/LRP2 alleles in proximal tubular cells of cystinotic mice was achieved by a Cre-LoxP strategy using Wnt4-CRE.	Disulfides	109-118	low density lipoprotein receptor-related protein 2	Mus musculus	69-76
31720508-8	2019	The structural flexibility of the disulfide bridge was confirmed by the Raman markers arising from the Cys1-Cys6 disulfide bond-stretch motions.	Disulfides	34-43	cystin 1	Homo sapiens	103-107
9665719-3	1998	The DNaseY gene product had 42% identity to DNaseI, including conserved critical active site residues, the essential disulfide bridge, the calcium binding domain, and a signal peptide, as well as 2 of the 3 signature boxes.	Disulfides	117-126	deoxyribonuclease 1-like 3	Rattus norvegicus	4-10
9651330-11	1998	Although the mechanism of polymeric assembly is unknown, the matrilin-3 chain appears to function in the matrix linked to matrilin-1 in the form of disulfide-bonded heteromeric molecules.	Disulfides	148-157	matrilin 3	Bos taurus	61-71
31557263-10	2019	Activation of the chaperone function of Trx2 appears to be triggered by temperature-mediated structural changes and inhibited by oxidative disulfide bond formation.	Disulfides	139-148	thioredoxin 2	Mus musculus	40-44
9688933-9	1998	Under nonreducing conditions, the mass of the SP-A and A2R binding protein was approximately 210 kDa, indicating that the SP-A receptor is composed of disulfide-linked subunits.	Disulfides	151-160	surfactant protein A1	Homo sapiens	46-50
30238832-5	2019	From our findings, we hypothesize that disulfide A-box fragment binds as an anchor toward the TLR4-MD-2 but does not facilitate the TLR4 dimer formation, thereby competing with the HMGb1-binding site and preventing HMGb1-induced signaling and downstream inflammation, whereas the pro-inflammatory B-box fragment retains the MD-2 active conformation and binds to both TLR4 proteins in the complex to aid TLR4 dimer formation, which activates the intracellular signaling for downstream inflammatory pathways and cytokine release.	Disulfides	39-48	toll like receptor 4	Homo sapiens	94-98
30238846-0	2019	Contribution of allosteric disulfide in the structural regulation of membrane-bound tissue factor-factor VIIa binary complex.	Disulfides	27-36	coagulation factor III, tissue factor	Homo sapiens	84-97
30238846-7	2019	Dynamic study depicts that disulfide bond provides structural rigidity of TF in both free and ligand-bound forms.	Disulfides	27-36	coagulation factor III, tissue factor	Homo sapiens	74-76
30238846-12	2019	We suggest that the redox status of the disulfide bond also governs the lipid-mediated interactions with both TF and FVIIa.	Disulfides	40-49	coagulation factor III, tissue factor	Homo sapiens	110-112
31266802-6	2019	Thioredoxin (Trx) and glutaredoxin (Grx) systems have been implicated as electron donors for the RNR disulfide reduction via the swinging arm.	Disulfides	101-110	thioredoxin	Homo sapiens	0-11
31266802-6	2019	Thioredoxin (Trx) and glutaredoxin (Grx) systems have been implicated as electron donors for the RNR disulfide reduction via the swinging arm.	Disulfides	101-110	thioredoxin	Homo sapiens	13-16
9688933-9	1998	Under nonreducing conditions, the mass of the SP-A and A2R binding protein was approximately 210 kDa, indicating that the SP-A receptor is composed of disulfide-linked subunits.	Disulfides	151-160	surfactant protein A1	Homo sapiens	122-126
9647238-2	1998	In C8 isolated from serum, these are arranged as a disulfide-linked C8 alpha-gamma dimer that is noncovalently associated with C8 beta.	Disulfides	51-60	complement C8 beta chain	Homo sapiens	127-134
31355389-4	2019	Protein tyrosine kinase 7 (PTK7) antibody mediated active targetability can facilitate the cellular uptake of triphenylphosphine-docetaxel (TD) and microRNA-31(miR-31) and the breakage of the disulfide bond can also enhance intracellular drug release.	Disulfides	192-201	microRNA 31	Homo sapiens	160-166
9603957-0	1998	Porcine submaxillary mucin forms disulfide-linked multimers through its amino-terminal D-domains.	Disulfides	33-42	LOC100508689	Homo sapiens	21-26
31272791-5	2019	SN-2, an oxidative type of prodrug of SN-1 with 2-nitrophenylthio groups via disulfide, has the minimum structure for an inhibitor of TRAF6, as seen with cellular experiments.	Disulfides	77-86	TNF receptor associated factor 6	Homo sapiens	134-139
31387209-0	2019	SUSD2 Proteolytic Cleavage Requires the GDPH Sequence and Inter-Fragment Disulfide Bonds for Surface Presentation of Galectin-1 on Breast Cancer Cells.	Disulfides	73-82	galectin 1	Homo sapiens	117-127
9603957-8	1998	Coexpression in the same cells of the amino-terminal region and the disulfide-rich carboxyl-terminal domain of the mucin showed that these structures were not disulfide-linked with one another.	Disulfides	68-77	LOC100508689	Homo sapiens	115-120
9603957-9	1998	Cells expressing a DNA construct encoding a fusion protein between the amino- and carboxyl-terminal regions of the mucin secreted disulfide-linked dimeric and high molecular weight multimeric species of the recombinant mucin.	Disulfides	130-139	LOC100508689	Homo sapiens	115-120
9603957-9	1998	Cells expressing a DNA construct encoding a fusion protein between the amino- and carboxyl-terminal regions of the mucin secreted disulfide-linked dimeric and high molecular weight multimeric species of the recombinant mucin.	Disulfides	130-139	LOC100508689	Homo sapiens	219-224
31260268-4	2019	The only available crystal structure is that of a c-MYC:MAX complex artificially tethered by an engineered disulfide linker and prebound to DNA.	Disulfides	107-116	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	50-55
9603957-11	1998	These studies suggest that disulfide-linked dimers of mucin are subsequently assembled into disulfide-linked multimers by the amino-terminal regions.	Disulfides	27-36	LOC100508689	Homo sapiens	54-59
9603957-11	1998	These studies suggest that disulfide-linked dimers of mucin are subsequently assembled into disulfide-linked multimers by the amino-terminal regions.	Disulfides	92-101	LOC100508689	Homo sapiens	54-59
31324690-2	2019	To overcome this challenge, we demonstrate the use of functionally empty MHC class I molecules stabilized by a disulfide bond to link the alpha1 and alpha2 helices close to the F pocket.	Disulfides	111-120	adrenoceptor alpha 1D	Homo sapiens	138-155
9603957-12	1998	They also suggest that the porcine mucin forms branched disulfide-linked multimers.	Disulfides	56-65	LOC100508689	Homo sapiens	35-40
9603957-13	1998	This ability of the amino-terminal region of mucin to aid in the assembly of multimers is consistent with its amino acid identities to the amino-terminal region of human von Willebrand factor, which also serves to form disulfide-linked multimers of this protein.	Disulfides	219-228	LOC100508689	Homo sapiens	45-50
30919767-1	2019	BACKGROUND: A well-known tissue marker of ovarian cancer, Human Epididymis protein 4 (HE4) is the member of whey acidic four-disulfide core proteins family.	Disulfides	125-134	WAP four-disulfide core domain 2	Homo sapiens	86-89
9562633-9	1998	Interestingly, the 66-kDa Endo H-sensitive form of the TNSALP mutants but not that of the wild-type, was found to form an interchain disulfide-bonded high-molecular-mass aggregate within the cells.	Disulfides	133-142	alkaline phosphatase, biomineralization associated	Homo sapiens	55-61
31269964-3	2019	HA was connected to MoS2 via a disulfide linkage, forming a sheddable HA shell on the surface of MoS2.	Disulfides	31-40	mago homolog, exon junction complex core component	Mus musculus	20-24
31269964-3	2019	HA was connected to MoS2 via a disulfide linkage, forming a sheddable HA shell on the surface of MoS2.	Disulfides	31-40	mago homolog, exon junction complex core component	Mus musculus	97-101
9571241-9	1998	Thus, Grx1 and Grx2 function differently in the cell, and we suggest that glutaredoxins may act as one of the primary defenses against mixed disulfides formed following oxidative damage to proteins.	Disulfides	141-151	dithiol glutaredoxin GRX2	Saccharomyces cerevisiae S288C	15-19
31269696-6	2019	The elimination of one disulfide bond resulted in a significant loss of blocking activity at NaV1.4, highlighting the importance of the 3-disulfide-bonded architecture for micro-PIIIA.	Disulfides	23-32	sodium voltage-gated channel alpha subunit 4	Homo sapiens	93-99
9679553-5	1998	Kox is independent of the total glutathione concentration, indicating that S-thiolation by mixed disulfide formation, rather than interchain or intrachain disulfide bridge formation, is responsible for activation.	Disulfides	97-106	NADPH oxidase 4	Homo sapiens	0-3
31117586-1	2019	Different reactivity of homologous disulfides toward Pd2+ was previously reported: stepwise complexation to Pd2+ for l-cystine and cystamine ligands, while for dl-homocystine and 3,3"-dithiodipropionic acid, disulfide"s disproportionation toward thiolate and sulfinic acid complexes is observed.	Disulfides	35-44	PAF1 homolog, Paf1/RNA polymerase II complex component	Homo sapiens	53-56
31117586-1	2019	Different reactivity of homologous disulfides toward Pd2+ was previously reported: stepwise complexation to Pd2+ for l-cystine and cystamine ligands, while for dl-homocystine and 3,3"-dithiodipropionic acid, disulfide"s disproportionation toward thiolate and sulfinic acid complexes is observed.	Disulfides	35-44	PAF1 homolog, Paf1/RNA polymerase II complex component	Homo sapiens	108-111
31117586-2	2019	The disulfide/thiolate interconversion of four different disulfide ligands in the presence of nonredox metal cation Pd2+ in aqueous solution has been computationally investigated.	Disulfides	4-13	PAF1 homolog, Paf1/RNA polymerase II complex component	Homo sapiens	116-119
31117586-2	2019	The disulfide/thiolate interconversion of four different disulfide ligands in the presence of nonredox metal cation Pd2+ in aqueous solution has been computationally investigated.	Disulfides	57-66	PAF1 homolog, Paf1/RNA polymerase II complex component	Homo sapiens	116-119
31117586-4	2019	We thus devise a theoretical model that rationalizes experimentally observed phenomenon of disulfides different reactivity toward nonredox transition metal cation Pd2+.	Disulfides	91-101	PAF1 homolog, Paf1/RNA polymerase II complex component	Homo sapiens	163-166
9556523-1	1998	Protein disulfide isomerase (PDI) is not only an isomerase catalyzing the formation of native disulfide bond(s) of nascent peptide, but also a molecular chaperone assisting chain folding.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
30959459-6	2019	Structure comparisons revealed similar disulfide bonds also in ST3Gal-I, suggesting that this O-glycan and glycolipid modifying sialyltransferase is also sensitive to hypoxia and thereby contribute to attenuated sialylation of O-linked glycans in hypoxic cells.	Disulfides	39-48	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	63-71
9556523-2	1998	The intrinsic chaperone activity of PDI is independent of its isomerase activity as shown by its ability of promoting in vitro reactivation and suppressing aggregation during refolding of denatured proteins containing no disulfide.	Disulfides	221-230	prolyl 4-hydroxylase subunit beta	Homo sapiens	36-39
9593640-6	1998	In other tissues, an enzyme, thioltransferase (TTase), has been shown to be responsible for thiol/disulfide regulation.	Disulfides	98-107	glutaredoxin	Homo sapiens	47-52
31293664-6	2019	In this study, we show that an UV initiated radical reaction can be used to synthesize symmetrically and unsymmetrically substituted BCP sulfides by reaction of [1.1.1]propellane (1) with disulfides.	Disulfides	188-198	opsin 1, short wave sensitive	Homo sapiens	133-136
9512538-5	1998	We conclude that the leucine zipper motif is required to maintain two molecules of TB-RBP as a dimer which is stabilized by a disulfide bond involving cysteine 225.	Disulfides	126-135	translin	Homo sapiens	83-89
31293664-7	2019	Depending on the ratio of 1 to the disulfide, only the BCP product (with up to 98% yield) or a mixture of BCP and [2]staffane can be obtained.	Disulfides	35-44	opsin 1, short wave sensitive	Homo sapiens	55-58
9516427-3	1998	Here we show that class III (SemD) and class IV semaphorins (SemB) form homodimers linked by intermolecular disulfide bridges.	Disulfides	108-117	semaphorin 3A	Homo sapiens	29-33
30857829-8	2019	Furthermore, our study revealed that disulfide bond was essential moiety for inhibition activity of PEN-A on Hsp90.	Disulfides	37-46	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	100-103
9508767-3	1998	Specifically, we have studied the role of a candidate structural motif implicated in the sorting of CgB, the highly conserved NH2-terminal disulfide- bonded loop.	Disulfides	139-148	chromogranin B	Homo sapiens	100-103
30857829-8	2019	Furthermore, our study revealed that disulfide bond was essential moiety for inhibition activity of PEN-A on Hsp90.	Disulfides	37-46	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
9508767-9	1998	In conclusion, our data show that (a) the disulfide-bonded loop is essential for sorting of CgB to ISG and (b) the lack of this structural motif can be compensated by coexpression of loop-bearing CgB.	Disulfides	42-51	chromogranin B	Homo sapiens	92-95
9508767-9	1998	In conclusion, our data show that (a) the disulfide-bonded loop is essential for sorting of CgB to ISG and (b) the lack of this structural motif can be compensated by coexpression of loop-bearing CgB.	Disulfides	42-51	chromogranin B	Homo sapiens	196-199
9514162-7	1998	Moreover, two-dimensional gel analysis showed that BiP associated especially well with intracellular Tg containing mispaired disulfide bonds, thought to represent early Tg folding intermediates.	Disulfides	125-134	thyroglobulin	Homo sapiens	101-103
30862546-8	2019	In contrast, Prx1 and Prx2 were present in neutrophils from human blood as disulfides, and PMA or S. aureus caused no further oxidation.	Disulfides	75-85	peroxiredoxin 1	Homo sapiens	13-17
9514721-1	1998	Protein disulfide isomerase (PDI) catalyzes protein folding linked to disulfide bond formation in secreted proteins.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
30658903-3	2019	In vitro, electrophilic lipids, including 15-deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2) and 4-hydroxynonenal (HNE), directly bind to vimentin, whereas the oxidant diamide induces disulfide bond formation.	Disulfides	181-190	vimentin	Homo sapiens	135-143
30658903-4	2019	Mutation of the single vimentin cysteine residue (Cys328) blunts disulfide formation and reduces lipoxidation by 15d-PGJ2, but not HNE.	Disulfides	65-74	vimentin	Homo sapiens	23-31
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	90-99	thioredoxin	Homo sapiens	4-15
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	90-99	thioredoxin	Homo sapiens	40-51
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	90-99	thioredoxin	Homo sapiens	53-56
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	171-180	thioredoxin	Homo sapiens	4-15
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	171-180	thioredoxin	Homo sapiens	40-51
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	171-180	thioredoxin	Homo sapiens	53-56
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	171-180	thioredoxin	Homo sapiens	4-15
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	171-180	thioredoxin	Homo sapiens	40-51
30367780-2	2019	The thioredoxin family of proteins like thioredoxin (Trx), glutaredoxin (Grx) and protein disulfide isomerase, are involved in the formation, transfer or isomerization of disulfide bonds through a characteristic thiol-disulfide exchange reaction.	Disulfides	171-180	thioredoxin	Homo sapiens	53-56
2532140-4	1989	The delta-TCS1 determinant was expressed on both nondisulfide- and disulfide-linked TcR gamma/delta.	Disulfides	52-61	telomerase reverse transcriptase	Homo sapiens	10-14
9605517-2	1998	In this report we have characterized tissue-derived STC in humans and found it to be a glycosylated, disulfide-linked dimer, with similar physical and chemical properties to baculovirus-expressed hormone.	Disulfides	101-110	stanniocalcin 1	Homo sapiens	52-55
2813393-7	1989	The results suggest that the lutropin/choriogonadotropin receptor from rat ovary exists in two molecular forms, and the higher molecular weight form appears to be composed of disulfide-linked Mr 92,000 subunit, which comprises the hormone-binding domain.	Disulfides	175-184	luteinizing hormone/choriogonadotropin receptor	Homo sapiens	29-65
30995786-1	2019	Mouse activating Nkrp1 proteins are commonly described as type II transmembrane receptors with disulfide-linked homodimeric structure.	Disulfides	95-104	killer cell lectin-like receptor subfamily B member 1C	Mus musculus	17-22
9446787-2	1998	Here we show that i-Tg, multimerized through formation of disulfide and dityrosine bonds, has a higher iodine content than soluble Tg and no thyroid hormones.	Disulfides	58-67	thyroglobulin	Homo sapiens	20-22
30948772-1	2019	Human immunodeficiency virus (HIV-1) entry is initiated by the binding between the viral envelope glycoprotein gp120 and the host receptor CD4, and followed by reduction of structural disulfides of gp120 and CD4.	Disulfides	184-194	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	198-203
30948772-2	2019	The host thioredoxin-1 (Trx1) efficiently reduces disulfides of gp120 and CD4 in vitro, and recently CD4-dependent HIV-1 entry was shown to be inhibited by anti-Trx1-antibodies, indicating a central role for Trx1.	Disulfides	50-60	thioredoxin	Homo sapiens	24-28
30948772-2	2019	The host thioredoxin-1 (Trx1) efficiently reduces disulfides of gp120 and CD4 in vitro, and recently CD4-dependent HIV-1 entry was shown to be inhibited by anti-Trx1-antibodies, indicating a central role for Trx1.	Disulfides	50-60	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	64-69
30948772-2	2019	The host thioredoxin-1 (Trx1) efficiently reduces disulfides of gp120 and CD4 in vitro, and recently CD4-dependent HIV-1 entry was shown to be inhibited by anti-Trx1-antibodies, indicating a central role for Trx1.	Disulfides	50-60	thioredoxin	Homo sapiens	161-165
30948772-2	2019	The host thioredoxin-1 (Trx1) efficiently reduces disulfides of gp120 and CD4 in vitro, and recently CD4-dependent HIV-1 entry was shown to be inhibited by anti-Trx1-antibodies, indicating a central role for Trx1.	Disulfides	50-60	thioredoxin	Homo sapiens	161-165
2553123-6	1989	The two subunits of C2 are disulfide bridge linked; the active center of the cholinesterase subunit is partly masked by the albumin molecule.	Disulfides	27-36	butyrylcholinesterase	Homo sapiens	77-91
9562549-7	1998	CONCLUSIONS: These results indicate that the heat-denatured RNase A and cytochrome c are substantially unfolded according to the criteria of solution X-ray scattering, although the heat-denatured RNase A remains compact because of the presence of the disulfide bonds.	Disulfides	251-260	LOC104968582	Bos taurus	72-84
2477449-3	1989	That all three mAb recognized the OH6 TCR was confirmed by immunoprecipitation studies in which each antibody precipitated a 90 kDa disulfide-linked heterodimer characteristic of the TCR.	Disulfides	132-141	T cell receptor alpha variable 6-3	Mus musculus	38-41
2477449-3	1989	That all three mAb recognized the OH6 TCR was confirmed by immunoprecipitation studies in which each antibody precipitated a 90 kDa disulfide-linked heterodimer characteristic of the TCR.	Disulfides	132-141	T cell receptor alpha variable 6-3	Mus musculus	183-186
9562551-3	1998	RESULTS: In this study, we investigate the refolding of chemically denatured, disulfide-intact ribonuclease A (RNase A) by monitoring compaction and secondary structure formation using stopped-flow dynamic light scattering and stopped-flow CD, respectively.	Disulfides	78-87	ribonuclease A family member 1, pancreatic	Homo sapiens	95-109
30894168-11	2019	The vimentin target was validated to reveal that ajoene and dansyl-ajoene covalently bind to recombinant vimentin via a disulfide linkage at Cys-328.	Disulfides	120-129	vimentin	Homo sapiens	4-12
30894168-11	2019	The vimentin target was validated to reveal that ajoene and dansyl-ajoene covalently bind to recombinant vimentin via a disulfide linkage at Cys-328.	Disulfides	120-129	vimentin	Homo sapiens	105-113
9562551-3	1998	RESULTS: In this study, we investigate the refolding of chemically denatured, disulfide-intact ribonuclease A (RNase A) by monitoring compaction and secondary structure formation using stopped-flow dynamic light scattering and stopped-flow CD, respectively.	Disulfides	78-87	ribonuclease A family member 1, pancreatic	Homo sapiens	111-118
9523269-0	1998	Construction of disulfide-constrained random peptide libraries displayed on phage coat protein VIII.	Disulfides	16-25	cytochrome c oxidase subunit 8A	Homo sapiens	95-99
30586735-3	2019	Here, we established the role of platelet-derived protein disulfide isomerase (PDI) in reducing the allosteric disulfide bonds in GPIbalpha and enhancing the ligand-binding activity under thromboinflammatory conditions.	Disulfides	58-67	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	79-82
30586735-9	2019	PDI directly bound to the extracellular domain of GPIbalpha on the platelet surface and reduced the Cys4-Cys17 and Cys209-Cys248 disulfide bonds.	Disulfides	129-138	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	0-3
30586735-12	2019	CONCLUSIONS: Our results demonstrate that PDI-facilitated cleavage of the allosteric disulfide bonds tightly regulates GPIbalpha function, promoting platelet-neutrophil interactions, vascular occlusion, and tissue damage under thromboinflammatory conditions.	Disulfides	85-94	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	42-45
31459612-7	2019	Remarkably, these disulfide-bonded species of FapC DeltaR1R2R3 also significantly delay the fibrillation of human alpha-synuclein, a key protein in Parkinson"s disease pathology.	Disulfides	18-27	synuclein alpha	Homo sapiens	114-129
2668279-1	1989	Protein disulfide isomerase (PDI) is a multifunctional microsomal enzyme that participates in the formation of protein disulfide bonds.	Disulfides	8-17	protein-disulfide isomerase	Escherichia coli	29-32
2668279-2	1989	PDI catalyzes the reduction of protein disulfide bonds in the presence of excess reduced glutathione and has been implicated in the reductive degradation of insulin; E. coli thioredoxin is homologous to two regions in PDI and can also degrade insulin.	Disulfides	39-48	protein-disulfide isomerase	Escherichia coli	0-3
2752977-11	1989	These similarities and the ability of hamster PL-II to form a disulfide-bonded complex with alpha 2-macroglobulin in vitro suggest that the major circulating form of PL-II in the hamster may be a disulfide-bonded complex of one or more PL monomers with alpha 2-macroglobulin or a related plasma protein.	Disulfides	196-205	alpha-2-macroglobulin	Homo sapiens	92-113
2745422-9	1989	We conclude that boar acrosin is synthesized as a single-chain polypeptide with the regions corresponding to the light and heavy chains covalently connected by two disulfide bonds, and that the single-chain molecule is autoactivated by cleavage of the Arg23-Val24 bond after removal of the COOH-terminal 14-residue segment, resulting in the formation of the light and heavy chains.	Disulfides	164-173	acrosin	Homo sapiens	22-29
30657688-4	2019	In this method, the O-GlcNAc moiety on peptides was labeled with UDP-GalNAz followed by copper-free azide-alkyne cycloaddition with a multifunctional reagent bearing a terminal cyclooctyne, a disulfide bridge, and a biotin handle.	Disulfides	192-201	O-linked N-acetylglucosamine (GlcNAc) transferase	Homo sapiens	20-28
9407079-1	1997	A catalyst of disulfide formation and isomerization during protein folding, protein-disulfide isomerase (PDI) has two catalytic sites housed in two domains homologous to thioredoxin, one near the N terminus and the other near the C terminus.	Disulfides	14-23	prolyl 4-hydroxylase subunit beta	Homo sapiens	76-103
9407079-1	1997	A catalyst of disulfide formation and isomerization during protein folding, protein-disulfide isomerase (PDI) has two catalytic sites housed in two domains homologous to thioredoxin, one near the N terminus and the other near the C terminus.	Disulfides	14-23	prolyl 4-hydroxylase subunit beta	Homo sapiens	105-108
2544589-4	1989	The study shows that the three disulfide linkages of AT-III can be sequentially reduced, with Cys8-Cys128 being the most sensitive, followed by Cys21-Cys95, while Cys247-Cys430 is the most resistant to the mild reduction conditions.	Disulfides	31-40	serpin family C member 1	Homo sapiens	53-59
9487987-1	1997	Amylin, calcitonin (CT) and calcitonin gene-related peptide (CGRP) share limited structural homology including amino-terminal ring structures linked by a disulfide bridge and amidated carboxy-termini.	Disulfides	154-163	islet amyloid polypeptide	Homo sapiens	0-6
29959143-6	2019	A novel anti-CLL-1-ADC, with a highly potent pyrrolobenzodiazepine (PBD) dimer conjugated through a self-immolative disulfide linker, was developed.	Disulfides	116-125	C-type lectin domain family 12 member A	Homo sapiens	13-18
9353278-7	1997	Furthermore, the disulfide loop in the Gla domain of prothrombin is not required for complete carboxylation.	Disulfides	17-26	prothrombin	Cricetulus griseus	53-64
30221761-3	2019	In the cytosol, two NADPH-dependent enzymes, glutathione reductase and thioredoxin reductase, as well as a recently identified NADPH-independent system that uses catabolism of methionine to maintain pools of reduced glutathione, supply disulfide reducing power.	Disulfides	236-245	peroxiredoxin 5	Homo sapiens	71-92
30537892-2	2019	After characterization of the chemical structure of TG-DPU using proton nuclear magnetic resonance spectroscopy, bone morphogenetic protein (BMP-2) was loaded in the TG-DPU under oxidative conditions to form disulfides between the free thiol of TG-DPU and BMP-2.	Disulfides	208-218	bone morphogenetic protein 1	Homo sapiens	113-139
2527159-1	1989	Immunohistochemistry has been used to investigate disulfide- and non-disulfide-linked forms of the T cell receptor gamma/delta heterodimer (TcR gamma/delta) in blood and intestinal epithelium of normal human small intestine, intestine of patients with untreated coeliac disease (in whom T cells expressing TcR gamma/delta are disproportionately raised), intestine of patients with tropical malabsorption, and in the human fetus.	Disulfides	50-59	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	140-143
2527159-2	1989	In blood from adult volunteers, 90% of T cells expressing TcR gamma/delta use the disulfide-linked form.	Disulfides	82-91	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	58-61
2527159-3	1989	In contrast in the epithelium in normal small intestine, coeliac disease and tropical malabsorption, most of the T cells expressing TcR gamma/delta use the non-disulfide-linked form.	Disulfides	160-169	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	132-135
2527159-4	1989	This is especially prominent in untreated coeliac disease where the increase in TcR gamma/delta T cells is mainly restricted to those using the non-disulfide-linked form.	Disulfides	148-157	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	80-83
9463780-1	1997	The CD28 molecule, a disulfide-linked homodimer expressed on peripheral T cells and thymocytes, mediates an essential costimulatory signal following engagement of the T cell receptor (TCR).	Disulfides	21-30	CD28 molecule	Homo sapiens	4-8
2793307-2	1989	The crystal structure analysis of the cyclic biscystine peptide [Boc-Cys1-Ala2-Cys3-NHCH3]2 with two disulfide bridges confirms the antiparallel beta-sheet conformation for the molecule as proposed for the conformation in solution.	Disulfides	101-110	cystin 1	Homo sapiens	69-73
30399388-2	2019	In the present study, we investigated the effects of protein disulfide-isomerase A3 (PDIA3), an ER-resident chaperone that catalyzes disulfide-bond formation in a subset of glycoproteins, against oxidative damage in the hypoxic HT22 cell line and against ischemic damage in the gerbil hippocampus.	Disulfides	61-70	protein disulfide isomerase associated 3	Mus musculus	85-90
9352906-8	1997	Analysis of the activity of mutant forms of DsbC in which either or both of these cysteines have been altered further supports the role of DsbC as a disulfide bond isomerase.	Disulfides	149-158	putative protein DsbC	Escherichia coli	44-48
30431279-2	2018	It has three pairs of intramolecular disulfide bonds which can break under reducing conditions to convert hBD-3 into the linear analog form.	Disulfides	37-46	defensin beta 103B	Homo sapiens	106-111
2543671-8	1989	It is concluded that the two disulfide-linked Epo-binding proteins which can be independently cross-linked to Epo form a single ligand binding site.	Disulfides	29-38	erythropoietin	Mus musculus	46-49
9352906-8	1997	Analysis of the activity of mutant forms of DsbC in which either or both of these cysteines have been altered further supports the role of DsbC as a disulfide bond isomerase.	Disulfides	149-158	putative protein DsbC	Escherichia coli	139-143
2543671-8	1989	It is concluded that the two disulfide-linked Epo-binding proteins which can be independently cross-linked to Epo form a single ligand binding site.	Disulfides	29-38	erythropoietin	Mus musculus	110-113
2785850-2	1989	OKT1-SAP comprised the OKT1 (CD5) monoclonal antibody disulfide linked to saporin-6 (SAP) ribosome-inactivating protein from the plant Saponaria officinalis.	Disulfides	54-63	CD5 molecule	Homo sapiens	29-32
2466831-12	1989	These findings indicate that "F" alpha 2M interacts with IL-1 beta through a thiol-disulfide exchange reaction.	Disulfides	83-92	alpha-2-macroglobulin	Homo sapiens	33-41
30568854-9	2018	In addition, RIP-MD also computes interactions based on distances between Calphas and disulfide bridges.	Disulfides	86-95	receptor interacting serine/threonine kinase 1	Homo sapiens	13-16
30496416-4	2018	By an oligonucleotide hybridization approach, double-stranded fragments encoding any EGF-LD can be first rapidly cloned into the prokaryotic vector pET-25b to promote its targeting to periplasm and formation of the three conserved disulfide bonds.	Disulfides	231-240	epidermal growth factor	Homo sapiens	85-88
9385634-1	1997	Lipoprotein(a) [Lp(a)] is a low-density lipoprotein complex consisting of apolipoprotein(a) [apo(a)] disulfide-linked to apolipoprotein B-100.	Disulfides	101-110	lipoprotein(a)	Homo sapiens	0-14
30591932-3	2018	As a critical member of the PDI family, thioredoxin domain containing protein 5 (TXNDC5) assists the folding of newly synthesized peptides to their mature form through series of disulfide bond exchange reactions.	Disulfides	178-187	thioredoxin domain containing 5	Homo sapiens	40-79
30591932-3	2018	As a critical member of the PDI family, thioredoxin domain containing protein 5 (TXNDC5) assists the folding of newly synthesized peptides to their mature form through series of disulfide bond exchange reactions.	Disulfides	178-187	thioredoxin domain containing 5	Homo sapiens	81-87
2924822-0	1989	Raman spectroscopy of calf lens gamma-II crystallin: direct evidence for the formation of mixed disulfide bonds with 2-mercaptoethanol and glutathione.	Disulfides	96-105	G protein subunit gamma 7	Bos taurus	32-40
2784209-1	1989	BB3 and delta-TCS1 monoclonal antibodies identify two distinct nonoverlapping populations of T-cell receptor (TcR) gamma/delta (TcR-1)-positive cells, which express a disulfide-linked and a nondisulfide-linked form of TcR, respectively.	Disulfides	167-176	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	93-108
9385634-1	1997	Lipoprotein(a) [Lp(a)] is a low-density lipoprotein complex consisting of apolipoprotein(a) [apo(a)] disulfide-linked to apolipoprotein B-100.	Disulfides	101-110	lipoprotein(a)	Homo sapiens	16-21
2784209-1	1989	BB3 and delta-TCS1 monoclonal antibodies identify two distinct nonoverlapping populations of T-cell receptor (TcR) gamma/delta (TcR-1)-positive cells, which express a disulfide-linked and a nondisulfide-linked form of TcR, respectively.	Disulfides	167-176	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	110-113
30021898-4	2018	The introduction of an artificial disulfide bond linking the gp120 and gp41 subunits (SOS) in combination with the I559P (IP) change has allowed structural characterization of soluble gp140 (sgp140) trimers.	Disulfides	34-43	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	61-66
9385634-1	1997	Lipoprotein(a) [Lp(a)] is a low-density lipoprotein complex consisting of apolipoprotein(a) [apo(a)] disulfide-linked to apolipoprotein B-100.	Disulfides	101-110	lipoprotein(a)	Homo sapiens	74-91
30104382-0	2018	Interleukin 4 is inactivated via selective disulfide-bond reduction by extracellular thioredoxin.	Disulfides	43-52	thioredoxin	Homo sapiens	85-96
2467818-6	1989	On resting cells, CD27 is a disulfide-linked homodimer with subunits of 55 kDa molecular mass.	Disulfides	28-37	CD27 molecule	Homo sapiens	18-22
9346903-7	1997	We therefore hypothesized that the small subunit of MTP, protein-disulfide isomerase (PDI), plays a role in apoB secretion by facilitating correct disulfide bond formation.	Disulfides	65-74	prolyl 4-hydroxylase subunit beta	Homo sapiens	86-89
2975598-7	1988	Biochemical analysis demonstrated that the predominant form of the gamma/delta TcR in adult peripheral blood is a disulfide-linked heterodimer, indicating preferential use of the C gamma 1 gene.	Disulfides	114-123	T cell receptor alpha variable 6-3	Mus musculus	79-82
30104382-2	2018	Recently, we showed that TRX activates extracellular transglutaminase 2 via reduction of an allosteric disulfide bond.	Disulfides	103-112	thioredoxin	Homo sapiens	25-28
30104382-5	2018	To test this hypothesis, the C35S mutant of human TRX was shown to form a mixed disulfide bond with recombinant IL-4 but not IL-13.	Disulfides	80-89	thioredoxin	Homo sapiens	50-53
30104382-7	2018	Mass spectrometry identified the C46-C99 bond of IL-4 as the target of TRX, consistent with the essential role of this disulfide bond in IL-4 activity.	Disulfides	119-128	thioredoxin	Homo sapiens	71-74
30104382-9	2018	By establishing that IL-4 is posttranslationally regulated by TRX-promoted reduction of a disulfide bond, our findings highlight a novel regulatory mechanism of the type 2 immune response that is specific to IL-4 over IL-13.	Disulfides	90-99	thioredoxin	Homo sapiens	62-65
9342327-7	1997	Disulfide bond formation of beta-lactamase was impaired under these conditions.	Disulfides	0-9	beta-lactamase	Escherichia coli	28-42
31544879-9	2018	We present a solution for the second challenge-correct pairing of heavy and light chains of bispecific IgGs; an engineered (artificial) disulfide bond between the antibodies" variable domains that asymmetrically replaces the natural disulfide bond between CH1 and CL.	Disulfides	136-145	SUN domain containing ossification factor	Homo sapiens	256-259
3194393-7	1988	The four cysteinyl residues (positions 66, 106, 119, and 160) responsible for intramolecular disulfide bridges in beta-lactoglobulins are all conserved in PP14.	Disulfides	93-102	progestagen associated endometrial protein	Homo sapiens	155-159
9330225-1	1997	Human neutrophil elastase cleaves angiogenin at the Ile-29/Met-30 peptide bond to produce two major disulfide-linked fragments with apparent molecular weights of 10,000 and 4000, respectively.	Disulfides	100-109	elastase, neutrophil expressed	Homo sapiens	6-25
3264877-3	1988	The 4-kb CSF-1 cDNA product was synthesized as an integral transmembrane glycoprotein that was assembled into disulfide-linked dimers and rapidly underwent proteolytic cleavage to generate a soluble growth factor.	Disulfides	110-119	colony stimulating factor 1	Homo sapiens	9-14
31544879-9	2018	We present a solution for the second challenge-correct pairing of heavy and light chains of bispecific IgGs; an engineered (artificial) disulfide bond between the antibodies" variable domains that asymmetrically replaces the natural disulfide bond between CH1 and CL.	Disulfides	233-242	SUN domain containing ossification factor	Homo sapiens	256-259
31544879-13	2018	When the artificial disulfide bond links the CH1 with the CL domain, effective H-L chain pairing also occurs, but in some cases, wrong H-L pairing is not totally prevented.	Disulfides	20-29	SUN domain containing ossification factor	Homo sapiens	45-48
29878755-9	2018	Applying this workflow, we successfully mapped the complex disulfide bonds of tertiapin and the epidermal growth factor (EGF) family members transforming growth factor alpha (TGFalpha) and EGF.	Disulfides	59-68	epidermal growth factor	Homo sapiens	96-119
29878755-9	2018	Applying this workflow, we successfully mapped the complex disulfide bonds of tertiapin and the epidermal growth factor (EGF) family members transforming growth factor alpha (TGFalpha) and EGF.	Disulfides	59-68	epidermal growth factor	Homo sapiens	121-124
29988369-1	2018	SLC7A5, known as LAT1, belongs to the APC superfamily and forms a heterodimeric amino acid transporter interacting with the glycoprotein CD98 (SLC3A2) through a conserved disulfide.	Disulfides	171-180	solute carrier family 7 member 5	Homo sapiens	0-6
29988369-1	2018	SLC7A5, known as LAT1, belongs to the APC superfamily and forms a heterodimeric amino acid transporter interacting with the glycoprotein CD98 (SLC3A2) through a conserved disulfide.	Disulfides	171-180	solute carrier family 7 member 5	Homo sapiens	17-21
29988369-1	2018	SLC7A5, known as LAT1, belongs to the APC superfamily and forms a heterodimeric amino acid transporter interacting with the glycoprotein CD98 (SLC3A2) through a conserved disulfide.	Disulfides	171-180	solute carrier family 3 member 2	Homo sapiens	137-141
29988369-1	2018	SLC7A5, known as LAT1, belongs to the APC superfamily and forms a heterodimeric amino acid transporter interacting with the glycoprotein CD98 (SLC3A2) through a conserved disulfide.	Disulfides	171-180	solute carrier family 3 member 2	Homo sapiens	143-149
2973066-1	1988	The receptor for antigen on the surface of T lymphocytes consists of a variable disulfide-bridged hetero-dimer (TCR-alpha/beta or -gamma/delta) associated with invariant CD3 proteins (CD3-gamma, -delta, -epsilon, and -zeta).	Disulfides	80-89	T cell receptor alpha chain	Mus musculus	112-121
2845582-2	1988	The CD3-zeta chains are either disulfide-linked homodimers (CD3-zeta 2) or disulfide-linked heterodimers with eta (CD3-zeta eta).	Disulfides	31-40	CD247 molecule	Homo sapiens	4-12
2845582-2	1988	The CD3-zeta chains are either disulfide-linked homodimers (CD3-zeta 2) or disulfide-linked heterodimers with eta (CD3-zeta eta).	Disulfides	75-84	CD247 molecule	Homo sapiens	4-12
3146023-1	1988	The conformation of the interchain disulfide bond between the light and the heavy chains of human immunoglobulin G4 (IgG4) was modeled based on the known structure of a human IgG1 Fab.	Disulfides	35-44	FA complementation group B	Homo sapiens	180-183
3261962-11	1988	Pulse-chase labeling showed that the first detectable form of PPH had a Mr 90,000 which corresponded to the high-mannose precursor as assessed by its sensitivity to endo-beta-N-acetylglucosaminidase H. Within 15 min of chase and prior to complex glycosylation, dimerization due to the formation of interchain disulfide bonds occurred (Mr 180,000).	Disulfides	309-318	enolase 1	Homo sapiens	62-65
9330225-1	1997	Human neutrophil elastase cleaves angiogenin at the Ile-29/Met-30 peptide bond to produce two major disulfide-linked fragments with apparent molecular weights of 10,000 and 4000, respectively.	Disulfides	100-109	angiogenin	Homo sapiens	34-44
3136023-3	1988	Similar to the L chain, H1 and H2 apparently carry intramolecular disulfide bonds.	Disulfides	66-75	H1.5 linker histone, cluster member	Homo sapiens	15-33
9350326-5	1997	In vivo, p73/Ds-1 and p54/Ds-1 are therefore likely to be present both in free and complexed form, while all of p92/Ds-2 and p40/Ds-2 form disulfide-bonded complexes.	Disulfides	139-148	tumor protein p73	Canis lupus familiaris	9-12
3413716-5	1988	The 58 kDa form was established to be a disulfide-linked heterodimer composed of TF and the alpha chain of hemoglobin.	Disulfides	40-49	coagulation factor III, tissue factor	Homo sapiens	81-83
29746088-1	2018	alpha-Conotoxins are disulfide-bonded peptides from cone snail venoms and are characterized by their affinity for nicotinic acetylcholine receptors (nAChR).	Disulfides	21-30	cholinergic receptor, nicotinic, alpha polypeptide 7	Mus musculus	114-147
29746088-1	2018	alpha-Conotoxins are disulfide-bonded peptides from cone snail venoms and are characterized by their affinity for nicotinic acetylcholine receptors (nAChR).	Disulfides	21-30	cholinergic receptor, nicotinic, alpha polypeptide 7	Mus musculus	149-154
9268305-6	1997	Furthermore, the ring-open intermolecular disulfide form of DTTox, 2-hydroxyethyl disulfide, was only a weak inducer of grp78 and gadd153 but was a strong inducer of hsp70 mRNA and a potent oxidant that lowered the NADPH/NADP+ ratio and depleted reduced glutathione (GSH).	Disulfides	42-51	heat shock protein family A (Hsp70) member 5	Sus scrofa	120-125
29442809-6	2018	Even if cystamine (a disulfide compound) was contained in SLN, the release degree at 25  C was not significantly affected by dithiothreitol (DTT, a reducing agent).	Disulfides	21-30	sarcolipin	Homo sapiens	58-61
2833758-8	1988	If similar material is boiled in 2% NaDodSO4 in the absence of a sulfhydryl reducing agent, the tau immunoreactivity is removed less efficiently, suggesting that tau epitopes are bound to the ubiquitin reactive material in a manner partially dependent on covalent disulfide bridges.	Disulfides	264-273	microtubule associated protein tau	Homo sapiens	162-165
9254601-4	1997	In vitro, DsbC and DsbA have an equivalent kcat for disulfide isomerization with the model substrate, misfolded insulin-like growth factor-1.	Disulfides	52-61	putative protein DsbC	Escherichia coli	10-14
3125251-4	1988	Moreover, the CH1 domain contains the H-L disulfide bond identical to alpha 1.	Disulfides	42-51	SUN domain containing ossification factor	Homo sapiens	14-17
29450858-8	2018	Interestingly, hepcidin peptides ionized from acidic solutions at elevated ESI voltages undergo gas-phase compaction, ostensibly due to partial disulfide ISR.	Disulfides	144-153	hepcidin antimicrobial peptide	Homo sapiens	15-23
9254601-9	1997	A dsbC deletion strain showed decreases in the production of some, but not all, heterologous proteins containing multiple disulfide bonds.	Disulfides	122-131	putative protein DsbC	Escherichia coli	2-6
3125251-4	1988	Moreover, the CH1 domain contains the H-L disulfide bond identical to alpha 1.	Disulfides	42-51	adrenoceptor alpha 1D	Homo sapiens	70-77
9252376-1	1997	Interleukin-5 (IL-5), a disulfide-linked homodimer, can be induced to fold as a biological active monomer by extending the loop between its third and fourth helices (Dickason, R. R., and Huston, D. P. (1996) Nature 379, 652-655).	Disulfides	24-33	interleukin 5	Homo sapiens	0-13
2452651-0	1988	Subunits of human alpha 2-macroglobulin produced by specific reduction of interchain disulfide bonds with thioredoxin.	Disulfides	85-94	alpha-2-macroglobulin	Homo sapiens	18-39
29420254-8	2018	This involves an initial sulfenylation of the active site thiol followed by the formation of an intrachain disulfide with a resolving thiol group and completed by the reduction of this disulfide by a thioredoxin-like protein to regenerate the active site thiol.	Disulfides	107-116	thioredoxin	Homo sapiens	200-211
29420254-8	2018	This involves an initial sulfenylation of the active site thiol followed by the formation of an intrachain disulfide with a resolving thiol group and completed by the reduction of this disulfide by a thioredoxin-like protein to regenerate the active site thiol.	Disulfides	185-194	thioredoxin	Homo sapiens	200-211
2452651-0	1988	Subunits of human alpha 2-macroglobulin produced by specific reduction of interchain disulfide bonds with thioredoxin.	Disulfides	85-94	thioredoxin	Homo sapiens	106-117
9252376-1	1997	Interleukin-5 (IL-5), a disulfide-linked homodimer, can be induced to fold as a biological active monomer by extending the loop between its third and fourth helices (Dickason, R. R., and Huston, D. P. (1996) Nature 379, 652-655).	Disulfides	24-33	interleukin 5	Homo sapiens	15-19
2452651-1	1988	Disulfide bonds in alpha 2-macroglobulin (alpha 2M) were reduced with the thioredoxin system from Escherichia coli.	Disulfides	0-9	alpha-2-macroglobulin	Homo sapiens	19-40
9252380-3	1997	We now demonstrate reduction of one or more disulfide bonds in the serine proteinase, plasmin, by a reductase secreted by Chinese hamster ovary or HT1080 cells.	Disulfides	44-53	plasminogen	Homo sapiens	86-93
2452651-1	1988	Disulfide bonds in alpha 2-macroglobulin (alpha 2M) were reduced with the thioredoxin system from Escherichia coli.	Disulfides	0-9	alpha-2-macroglobulin	Homo sapiens	42-50
2452651-1	1988	Disulfide bonds in alpha 2-macroglobulin (alpha 2M) were reduced with the thioredoxin system from Escherichia coli.	Disulfides	0-9	thioredoxin	Homo sapiens	74-85
2452651-2	1988	Under the conditions selected, 3.5-4.1 disulfide bonds were cleaved in each alpha 2M molecule, as determined by the consumption of NADPH during the reaction and by the incorporation of iodo[3H]acetate into the reaction product.	Disulfides	39-48	alpha-2-macroglobulin	Homo sapiens	76-84
2452651-3	1988	This extent of disulfide bond reduction, approximately corresponding to that expected from specific cleavage of all four interchain disulfide bonds of the protein, coincided with the nearly complete dissociation of the intact alpha 2M molecule to a species migrating as an alpha 2M subunit in gel electrophoresis, under both denaturing and nondenaturing conditions.	Disulfides	15-24	alpha-2-macroglobulin	Homo sapiens	226-234
2452651-3	1988	This extent of disulfide bond reduction, approximately corresponding to that expected from specific cleavage of all four interchain disulfide bonds of the protein, coincided with the nearly complete dissociation of the intact alpha 2M molecule to a species migrating as an alpha 2M subunit in gel electrophoresis, under both denaturing and nondenaturing conditions.	Disulfides	15-24	alpha-2-macroglobulin	Homo sapiens	273-281
2452651-3	1988	This extent of disulfide bond reduction, approximately corresponding to that expected from specific cleavage of all four interchain disulfide bonds of the protein, coincided with the nearly complete dissociation of the intact alpha 2M molecule to a species migrating as an alpha 2M subunit in gel electrophoresis, under both denaturing and nondenaturing conditions.	Disulfides	132-141	alpha-2-macroglobulin	Homo sapiens	226-234
29495280-4	2018	The authors used the scrambled disulfide bond technique to generate conformationally-altered isomers of the catalytic domain of mouse PCSK9.	Disulfides	31-40	proprotein convertase subtilisin/kexin type 9	Mus musculus	134-139
29305423-9	2018	We conclude that, to the best of our knowledge, the disulfide bond switch in human TG2 represents the first example of a post-translational redox regulatory mechanism that is reversibly and allosterically modulated by two distinct proteins (ERp57 and TRX).	Disulfides	52-61	thioredoxin	Homo sapiens	251-254
29298486-0	2018	Redox-Controlled Fluorescent Nanoswitch Based on Reversible Disulfide and Its Application in Butyrylcholinesterase Activity Assay.	Disulfides	60-69	butyrylcholinesterase	Homo sapiens	93-114
9252380-4	1997	Reduction of plasmin disulfide bond(s) triggered proteolysis of the enzyme, generating fragments with the domain structure of the angiogenesis inhibitor, angiostatin.	Disulfides	21-30	plasminogen	Homo sapiens	13-20
29298486-8	2018	The first design of reversible redox-controlled nanosiwtch based on disulfide expands the application of disulfide chemistry in sensing and clinical diagnostics, and this novel BChE assay enriches the detection methods for cholinesterase activity.	Disulfides	68-77	butyrylcholinesterase	Homo sapiens	177-181
29298486-8	2018	The first design of reversible redox-controlled nanosiwtch based on disulfide expands the application of disulfide chemistry in sensing and clinical diagnostics, and this novel BChE assay enriches the detection methods for cholinesterase activity.	Disulfides	105-114	butyrylcholinesterase	Homo sapiens	177-181
2896638-4	1988	Solvent shielding of the Cys2 amide proton, observed in variable temperature experiments, suggests an orientation of this amide proton toward the gem dimethyls of Pen7 with possible hydrogen bonding to the Thr6 carbonyl oxygen, and a dihedral angle of -110 degrees for the disulfide bond.	Disulfides	273-282	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	163-166
9252420-1	1997	Transcobalamin II-receptor (TC II-R) contains 10 half-cysteines, of which 8 are involved in intramolecular disulfide bonding.	Disulfides	107-116	transcobalamin 2	Homo sapiens	28-33
9252420-5	1997	Based on these results, we suggest that formation and maintenance of intramolecular disulfide bonds of TC II-R is important for its acquisition of ligand binding and post-trans-Golgi trafficking to basolateral surface membranes but not for its turnover and exit from the endoplasmic reticulum or trafficking through the Golgi.	Disulfides	84-93	transcobalamin 2	Homo sapiens	103-108
2832611-2	1988	Structural studies also show that the highly reactive sulfhydryl group of Cys102 is buried within a hydrophobic region in the monomer form of yeast iso-1-cytochrome c. Dimerization of yeast iso-1-cytochrome c through disulfide bond formation between two such residues would require a substantial conformational change in the C-terminal helix of this protein.	Disulfides	217-226	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	148-153
2832611-2	1988	Structural studies also show that the highly reactive sulfhydryl group of Cys102 is buried within a hydrophobic region in the monomer form of yeast iso-1-cytochrome c. Dimerization of yeast iso-1-cytochrome c through disulfide bond formation between two such residues would require a substantial conformational change in the C-terminal helix of this protein.	Disulfides	217-226	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	190-195
29476522-8	2018	By fine-tuning the collision energy for optimal fragmentation of each selected precursor ions, the full sequence of several novel inter- and intramolecular disulfide bond containing ant defensive peptides can be established.	Disulfides	156-165	solute carrier family 25 member 6	Homo sapiens	182-185
9202220-1	1997	In this study, site-directed mutagenesis and biochemical strategies have been used to establish whether disulfide bonding between extracellular Cys residues contributes to the structural integrity of the GnRH receptor (GnRH-R) and, if so, to delineate the nature of the bonding patterns involved.	Disulfides	104-113	gonadotropin releasing hormone receptor	Homo sapiens	204-217
9202220-1	1997	In this study, site-directed mutagenesis and biochemical strategies have been used to establish whether disulfide bonding between extracellular Cys residues contributes to the structural integrity of the GnRH receptor (GnRH-R) and, if so, to delineate the nature of the bonding patterns involved.	Disulfides	104-113	gonadotropin releasing hormone receptor	Homo sapiens	219-225
9202220-12	1997	This study demonstrates that GnRH-R residues Cys114 and Cys195 have a disulfide bonding interaction role essential for the maintenance of receptor function.	Disulfides	70-79	gonadotropin releasing hormone receptor	Homo sapiens	29-35
28917053-1	2018	Thioredoxin reductases are important oxidoreductases that keep the active site disulfide/dithiol motif of thioredoxins reduced using NADPH, thereby supporting many thioredoxin-dependent reductive pathways in cells.	Disulfides	79-88	thioredoxin	Homo sapiens	0-11
28917053-1	2018	Thioredoxin reductases are important oxidoreductases that keep the active site disulfide/dithiol motif of thioredoxins reduced using NADPH, thereby supporting many thioredoxin-dependent reductive pathways in cells.	Disulfides	79-88	thioredoxin	Homo sapiens	106-117
3676278-8	1987	5"-[p-(Fluorosulfonyl)benzoyl]adenosine (FSBA) inactivates glycine methyltransferase by forming 1 disulfide/subunit [Fujioka, M., &amp; Ishiguro, Y.	Disulfides	98-107	glycine N-methyltransferase	Rattus norvegicus	59-84
9314100-0	1997	Interheavy disulfide bridge in immunoglobulin G (IgG) reacting with dithionitrobenzoate.	Disulfides	11-20	immunoglobulin heavy variable V1-62	Mus musculus	49-52
29127146-4	2017	IFN-gamma-inducible lysosomal thiol reductase (GILT), which facilitates disulfide bond-containing Ag processing, was found to be upregulated in macrophages from Ncf1 mutant mice.	Disulfides	72-81	interferon gamma inducible protein 30	Mus musculus	0-45
9314100-2	1997	Immunoglobulin G (IgG) of many species contains "labile" disulfide bonds (SS*), which within 24 h undergo a disulfide exchange with dithionitrobenzoic acid (NBSSBN).	Disulfides	57-66	immunoglobulin heavy variable V1-62	Mus musculus	18-21
29127146-4	2017	IFN-gamma-inducible lysosomal thiol reductase (GILT), which facilitates disulfide bond-containing Ag processing, was found to be upregulated in macrophages from Ncf1 mutant mice.	Disulfides	72-81	interferon gamma inducible protein 30	Mus musculus	47-51
29127146-4	2017	IFN-gamma-inducible lysosomal thiol reductase (GILT), which facilitates disulfide bond-containing Ag processing, was found to be upregulated in macrophages from Ncf1 mutant mice.	Disulfides	72-81	neutrophil cytosolic factor 1	Mus musculus	161-165
29247216-7	2017	Finally, our results show that although both VKOR and VKORL form disulfide-linked oligomers, the cysteine residues involved in the oligomerization appear to be different.	Disulfides	65-74	vitamin K epoxide reductase complex subunit 1	Homo sapiens	45-49
3036867-1	1987	The human cell surface antigen 4F2 is a disulfide-linked heterodimer consisting of a glycosylated heavy chain and a nonglycosylated light chain.	Disulfides	40-49	solute carrier family 3 member 2	Homo sapiens	31-34
3606128-3	1987	FTR possesses a catalytically active dithiol group localized on the 13 kDa (similar) subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin m. The reduced thioredoxin m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive (S-S) to an active (SH) form.	Disulfides	241-250	thioredoxin	Homo sapiens	259-270
3606128-3	1987	FTR possesses a catalytically active dithiol group localized on the 13 kDa (similar) subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin m. The reduced thioredoxin m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive (S-S) to an active (SH) form.	Disulfides	241-250	thioredoxin	Homo sapiens	286-297
9314100-2	1997	Immunoglobulin G (IgG) of many species contains "labile" disulfide bonds (SS*), which within 24 h undergo a disulfide exchange with dithionitrobenzoic acid (NBSSBN).	Disulfides	108-117	immunoglobulin heavy variable V1-62	Mus musculus	18-21
3039346-4	1987	CSF-1 was synthesized as an integral transmembrane glycoprotein that was rapidly dimerized through disulfide bonds.	Disulfides	99-108	colony stimulating factor 1	Homo sapiens	0-5
29030430-7	2017	A disulfide linkage is present in IL1RN, but is not in IL-1beta because of natural C117F mutation.	Disulfides	2-11	interleukin 1 receptor antagonist	Homo sapiens	34-39
29030430-12	2017	Also, deletion of the disulfide linkage in IL1RN by the C116F mutation did not make it agonistic.	Disulfides	22-31	interleukin 1 receptor antagonist	Homo sapiens	43-48
9171381-5	1997	We recently demonstrated that VirB7 and VirB9 form a protein complex linked by a disulfide bond between cysteine 24 of VirB7 and cysteine 262 of VirB9 (L. Anderson, A. Hertzel, and A. Das, Proc.	Disulfides	81-90	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	30-35
3607517-2	1987	Neurite extension factor (NEF) is a disulfide-bonded dimer of a protein closely related to S100 beta, a calcium-binding protein made by glial cells.	Disulfides	36-45	S100 protein, beta polypeptide, neural	Mus musculus	91-100
3027700-3	1987	The recombinant fibronectins (deminectins) are processed and secreted by the cells and form disulfide-bonded dimers with themselves and with endogenous fibronectin subunits.	Disulfides	92-101	fibronectin 1	Mus musculus	16-27
28904203-10	2017	Taken together, our data revealed that all the three conserved regions are involved in P33 activity and are crucial for virus morphogenesis and peroral infectivity.IMPORTANCE Sulfhydryl oxidase catalyzes disulfide bond formation of substrate proteins.	Disulfides	204-213	inhibitor of growth family member 1	Homo sapiens	87-90
9171381-5	1997	We recently demonstrated that VirB7 and VirB9 form a protein complex linked by a disulfide bond between cysteine 24 of VirB7 and cysteine 262 of VirB9 (L. Anderson, A. Hertzel, and A. Das, Proc.	Disulfides	81-90	type IV secretion system protein VirB9	Agrobacterium tumefaciens	40-45
9171381-5	1997	We recently demonstrated that VirB7 and VirB9 form a protein complex linked by a disulfide bond between cysteine 24 of VirB7 and cysteine 262 of VirB9 (L. Anderson, A. Hertzel, and A. Das, Proc.	Disulfides	81-90	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	119-124
9171381-5	1997	We recently demonstrated that VirB7 and VirB9 form a protein complex linked by a disulfide bond between cysteine 24 of VirB7 and cysteine 262 of VirB9 (L. Anderson, A. Hertzel, and A. Das, Proc.	Disulfides	81-90	type IV secretion system protein VirB9	Agrobacterium tumefaciens	145-150
3771543-2	1986	Napin is composed of two polypeptide chains with molecular weights of 9000 and 4000 that are held together by disulfide bonds.	Disulfides	110-119	napin	Brassica napus	0-5
9144160-6	1997	A probable explanation is that MAO-generated H2O2 oxidizes glutathione to glutathione disulfide (GSSG), which undergoes thiol-disulfide interchange to form protein mixed disulfides, thereby interfering reversibly with thiol-dependent enzymatic function.	Disulfides	170-180	monoamine oxidase A	Rattus norvegicus	31-34
9192723-1	1997	We purified and characterized glutaredoxin (thioltransferase), which catalyzes thiol/disulfide exchange reaction, for the first time in plants.	Disulfides	85-94	glutaredoxin	Homo sapiens	30-42
3463991-6	1986	Reduced thioredoxin was optimal for catalyzing disulfide interchange in scrambled RNase, whereas oxidized thioredoxin was required for reactivation of the reduced, denatured species.	Disulfides	47-56	thioredoxin	Homo sapiens	8-19
3463991-8	1986	Addition of reduced thioredoxin after initiating refolding of reduced denatured RNase with oxidized glutathione effected a rapid reactivation of RNase, suggesting a two-step model for protein refolding in which the monothiol catalyzes the rapid initial formation of protein disulfides and thioredoxin catalyzes the second step of disulfide interchange.	Disulfides	274-284	thioredoxin	Homo sapiens	20-31
3463991-8	1986	Addition of reduced thioredoxin after initiating refolding of reduced denatured RNase with oxidized glutathione effected a rapid reactivation of RNase, suggesting a two-step model for protein refolding in which the monothiol catalyzes the rapid initial formation of protein disulfides and thioredoxin catalyzes the second step of disulfide interchange.	Disulfides	274-283	thioredoxin	Homo sapiens	20-31
28663059-6	2017	Furthermore, the likely conformational change of homo-dimerized hEb through a single disulfide bond, as well as the ability to trigger clathrin-mediated endocytosis may play important roles for inducing lamellipodia outspread in MDA-MB-231 cells.	Disulfides	85-94	transcription factor 12	Homo sapiens	64-67
28874874-0	2017	3-Mercaptopyruvate sulfurtransferase produces potential redox regulators cysteine- and glutathione-persulfide (Cys-SSH and GSSH) together with signaling molecules H2S2, H2S3 and H2S.	Disulfides	163-167	mercaptopyruvate sulfurtransferase	Mus musculus	0-36
28874874-4	2017	Here, we show that 3-mercaptopyruvate sulfurtransferase (3MST) produces Cys-SSH and GSSH together with the potential signaling molecules hydrogen per- and tri-sulfide (H2S2 and H2S3).	Disulfides	168-172	mercaptopyruvate sulfurtransferase	Mus musculus	19-55
3701066-0	1986	Location of the interchain disulfide bonds of the fourth component of human complement (C4): evidence based on the liberation of fragments secondary to thiol-disulfide interchange reactions.	Disulfides	27-36	complement C4A (Rodgers blood group)	Homo sapiens	76-90
9182804-0	1997	Disulfide-linked head-to-head multimerization in the mechanism of ion channel clustering by PSD-95.	Disulfides	0-9	discs large MAGUK scaffold protein 4	Rattus norvegicus	92-98
2868714-3	1986	The properties of the technique are illustrated by an investigation of cleavage reactions of the disulfide bonds in bovine insulin, cyclic somatostatin, and conotoxin G1 utilizing the reducing agent dithiothreitol.	Disulfides	97-106	insulin	Bos taurus	123-169
2870441-0	1986	Alpha-1 and alpha-2 adrenoceptor binding in cerebral cortex: role of disulfide and sulfhydryl groups.	Disulfides	69-78	adrenoceptor alpha 1D	Homo sapiens	0-7
28659344-6	2017	Here, by manipulating activity and levels of the Trx1/TrxR system and by using a Trx1-Trap assay, we demonstrate that Trx1 modulates cGMP synthesis through an association between Trx1 and GC1 via a mixed disulfide.	Disulfides	204-213	solute carrier family 25 member 22	Homo sapiens	188-191
28737377-4	2017	However, contrary to this, the elevated levels of TrxR cause the breakage of disulfide bonds and consequently abolishes the FRET pair through the release of the naphthalimide moiety from the surface of CDs.	Disulfides	77-86	peroxiredoxin 5	Homo sapiens	50-54
28628095-3	2017	Upon reacting with H2O2, Orp1 catalytic cysteine oxidizes to a sulfenic acid, which then engages into either an intermolecular disulfide with Yap1, leading to Yap1 activation, or an intramolecular disulfide that commits the enzyme into its peroxidatic cycle.	Disulfides	127-136	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	25-29
28628095-3	2017	Upon reacting with H2O2, Orp1 catalytic cysteine oxidizes to a sulfenic acid, which then engages into either an intermolecular disulfide with Yap1, leading to Yap1 activation, or an intramolecular disulfide that commits the enzyme into its peroxidatic cycle.	Disulfides	197-206	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	25-29
9182804-2	1997	We report that channel clustering depends on a conserved N-terminal domain of PSD-95 that mediates multimerization and disulfide linkage of PSD-95 protomers.	Disulfides	119-128	discs large MAGUK scaffold protein 4	Rattus norvegicus	78-84
28628095-5	2017	We show that the Yap1-binding protein Ybp1 brings together Orp1 and Yap1 into a ternary complex that selectively activates condensation of the Orp1 sulfenylated cysteine with one of the six Yap1 cysteines while inhibiting Orp1 intramolecular disulfide formation.	Disulfides	242-251	Ybp1p	Saccharomyces cerevisiae S288C	38-42
28628095-5	2017	We show that the Yap1-binding protein Ybp1 brings together Orp1 and Yap1 into a ternary complex that selectively activates condensation of the Orp1 sulfenylated cysteine with one of the six Yap1 cysteines while inhibiting Orp1 intramolecular disulfide formation.	Disulfides	242-251	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	59-63
9182804-2	1997	We report that channel clustering depends on a conserved N-terminal domain of PSD-95 that mediates multimerization and disulfide linkage of PSD-95 protomers.	Disulfides	119-128	discs large MAGUK scaffold protein 4	Rattus norvegicus	140-146
28628095-5	2017	We show that the Yap1-binding protein Ybp1 brings together Orp1 and Yap1 into a ternary complex that selectively activates condensation of the Orp1 sulfenylated cysteine with one of the six Yap1 cysteines while inhibiting Orp1 intramolecular disulfide formation.	Disulfides	242-251	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	143-147
2996534-4	1985	The obtained results indicate that the disulfide linkage stabilizes the bioactive conformation of ANF peptides but is not an absolute requirement for biological activity.	Disulfides	39-48	natriuretic peptide A	Bos taurus	98-101
28628095-5	2017	We show that the Yap1-binding protein Ybp1 brings together Orp1 and Yap1 into a ternary complex that selectively activates condensation of the Orp1 sulfenylated cysteine with one of the six Yap1 cysteines while inhibiting Orp1 intramolecular disulfide formation.	Disulfides	242-251	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	143-147
9182804-6	1997	PSD-95 and its relative chapsyn-110 exist as disulfide-linked complexes in rat brain, consistent with head-to-head multimerization of these proteins in vivo.	Disulfides	45-54	discs large MAGUK scaffold protein 4	Rattus norvegicus	0-6
9099671-0	1997	Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds.	Disulfides	79-88	putative protein DsbC	Escherichia coli	46-50
28746849-2	2017	Recent studies have proposed that activation of several tumor necrosis factor receptors, including Death Receptor 5, involves a scissorlike opening of the disulfide-linked transmembrane (TM) dimer.	Disulfides	155-164	TNF receptor superfamily member 10b	Homo sapiens	99-115
18640546-4	1985	The apparent molecular weights of P81, P53, and P49 changed significantly according to the composition of the lysis buffer used, suggesting that the differences in their molecular weights were due to conformational changes produced by reduction of their intramolecular disulfide bonds.	Disulfides	269-278	ezrin	Homo sapiens	34-37
2413884-13	1985	These data support a critical role for disulfide linkages in maintaining the native conformation of IFN alpha-2 and provide a potential basis for predicting the location of functionally important domains.	Disulfides	39-48	interferon alpha 2	Mus musculus	100-111
9099671-3	1997	Biochemical evidence indicates that DsbC has disulfide isomerization activity.	Disulfides	45-54	putative protein DsbC	Escherichia coli	36-40
9099671-8	1997	Overproduction of DsbC stimulated the formation of the correct disulfide bond.	Disulfides	63-72	putative protein DsbC	Escherichia coli	18-22
28247497-7	2017	The intramolecular disulfide bridge motifs of SsmTX-I was Cys1-Cys3 and Cys2-Cys4.	Disulfides	19-28	cystin 1	Homo sapiens	58-62
9099671-12	1997	In contrast, DsbC stimulates the formation of correct disulfide bonds and corrects previously introduced aberrant ones.	Disulfides	54-63	putative protein DsbC	Escherichia coli	13-17
9099671-13	1997	Thus, DsbC acts to isomerize disulfide bonds in vivo.	Disulfides	29-38	putative protein DsbC	Escherichia coli	6-10
28160557-5	2017	It is overexpressed in a variety of tumor types and it plays a role in disulfide bond formation in collaboration with PDI.	Disulfides	71-80	peptidyl arginine deiminase 1	Homo sapiens	118-121
4027217-6	1985	Electron spin resonance studies using a novel disulfide spin-label that is covalently linked to rhodopsin indicate that the apparent arrest of the protein at the metarhodopsin I stage is not due to simple aggregation of the protein in this short-chain, saturated lipid bilayer but must be understood in terms of the effect of the lipid host on the conformational energies of individual protein molecules.	Disulfides	46-55	rhodopsin	Bos taurus	96-105
9143327-9	1997	These findings indicate that some cysteines may preserve the catalytic activity of OXO by maintaining the integrity of its tertiary structure via disulfide bond formation.	Disulfides	146-155	LOC548260	Hordeum vulgare	83-86
3884381-1	1985	The insulin disulfide reducing thioredoxin system from E. coli was used to investigate a possible mechanism of degradation for the two somatomedins, insulin-like growth factor I and II (IGF-I and -II).	Disulfides	12-21	thioredoxin	Homo sapiens	31-42
28044432-8	2017	The oxidation and reduction of redox-active disulfides are mediated by cellular reactive oxygen species and activity of reductases, such as glutaredoxin and thioredoxin.	Disulfides	44-54	thioredoxin	Homo sapiens	157-168
9094311-1	1997	BACKGROUND: Protein disulfide isomerase (PDI), a multifunctional protein of the endoplasmic reticulum, catalyzes the formation, breakage and rearrangement of disulfide bonds during protein folding.	Disulfides	20-29	prolyl 4-hydroxylase subunit beta	Homo sapiens	41-44
28218242-2	2017	Using PDI variants that form mixed disulfide complexes with their substrates, we identify by kinetic trapping multiple substrate proteins, including vitronectin.	Disulfides	35-44	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	6-9
28218242-4	2017	The released PDI reduces disulfide bonds on plasma vitronectin, enabling vitronectin to bind to alphaVbeta3 and alphaIIbbeta3.	Disulfides	25-34	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	13-16
27936768-5	2017	Chemical cross-linking and coimmunoprecipitation experiments revealed that OATP1B1 may form homo-oligomers, possibly through disulfide bonds.	Disulfides	125-134	solute carrier organic anion transporter family member 1B1	Homo sapiens	75-82
27980120-5	2017	The molecules were then reduced and re-oxidized in a controlled manner to allow the formation of the proper hepcidin disulfide bridges.	Disulfides	117-126	hepcidin antimicrobial peptide	Homo sapiens	108-116
28076818-0	2017	One-Way Allosteric Communication between the Two Disulfide Bonds in Tissue Factor.	Disulfides	49-58	coagulation factor III, tissue factor	Homo sapiens	68-81
28076818-2	2017	TF contains two disulfide bonds, one each in the N-terminal and C-terminal extracellular domains.	Disulfides	16-25	coagulation factor III, tissue factor	Homo sapiens	0-2
28076818-4	2017	The redox state of this disulfide has been proposed to regulate TF encryption/decryption.	Disulfides	24-33	coagulation factor III, tissue factor	Homo sapiens	64-66
27664222-2	2017	Oxs1 and Pap1 form a complex when cells are exposed to diamide or Cd that causes disulfide stress.	Disulfides	81-90	phosphatidic acid phosphatase 1	Arabidopsis thaliana	9-13
27960036-12	2017	Similarly, inserting a disulfide bridge that stabilizes the LEM folded state impairs emerin N-terminal region self-assembly, whereas reducing this disulfide bridge triggers self-assembly.	Disulfides	23-32	emerin	Homo sapiens	85-91
27960424-2	2016	TP1, consisting of the antineoplastic camptothecin analogue SN-38, and the fluorescent dye rhodol green have been covalently conjugated through a disulfide bond.	Disulfides	146-155	transition protein 1	Homo sapiens	0-3
27732889-0	2016	Two fibrinogen-like proteins, FGL1 and FGL2 are disulfide-linked subunits of oligomers that specifically bind nonviable spermatozoa.	Disulfides	48-57	fibrinogen like 2	Homo sapiens	39-43
27609313-9	2016	In addition, the CRD contained two intradomain disulfide bridges (Cys49-Cys85 and Cys84-Cys97) and one interdomain disulfide bridge to FAS1-2 (Cys74-Cys339).	Disulfides	115-124	Fas cell surface death receptor	Homo sapiens	135-141
27609313-11	2016	The cysteine residues in FAS1-3 (Cys473 and Cys478) were shown to form an intradomain disulfide bridge.	Disulfides	86-95	Fas cell surface death receptor	Homo sapiens	25-31
27609313-12	2016	Finally, an interdomain disulfide bridge between FAS1-1 and FAS1-2 (Cys214-Cys317) was identified.	Disulfides	24-33	Fas cell surface death receptor	Homo sapiens	49-55
27609313-12	2016	Finally, an interdomain disulfide bridge between FAS1-1 and FAS1-2 (Cys214-Cys317) was identified.	Disulfides	24-33	Fas cell surface death receptor	Homo sapiens	60-66
27609313-13	2016	The interdomain disulfide bonds indicate that the NH2 terminus of TGFBIp (CRD, FAS1-1, and FAS1-2) adopts a compact globular fold, leaving FAS1-3 and FAS1-4 exposed.	Disulfides	16-25	Fas cell surface death receptor	Homo sapiens	91-97
27609313-13	2016	The interdomain disulfide bonds indicate that the NH2 terminus of TGFBIp (CRD, FAS1-1, and FAS1-2) adopts a compact globular fold, leaving FAS1-3 and FAS1-4 exposed.	Disulfides	16-25	Fas cell surface death receptor	Homo sapiens	91-95
28989532-0	2016	Disulfide Bond Characterization of Endogenous IgG3 Monoclonal Antibodies Using LC-MS: An Investigation of IgG3 Disulfide-mediated Isoforms.	Disulfides	0-9	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	46-50
28989532-0	2016	Disulfide Bond Characterization of Endogenous IgG3 Monoclonal Antibodies Using LC-MS: An Investigation of IgG3 Disulfide-mediated Isoforms.	Disulfides	0-9	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	106-110
28989532-0	2016	Disulfide Bond Characterization of Endogenous IgG3 Monoclonal Antibodies Using LC-MS: An Investigation of IgG3 Disulfide-mediated Isoforms.	Disulfides	111-120	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	46-50
28989532-0	2016	Disulfide Bond Characterization of Endogenous IgG3 Monoclonal Antibodies Using LC-MS: An Investigation of IgG3 Disulfide-mediated Isoforms.	Disulfides	111-120	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	106-110
28989532-6	2016	However, no studies have been carried out so far to investigate whether different IgG3 isoforms exist due to alternative disulfide connectivity.	Disulfides	121-130	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	82-86
28989532-7	2016	In an effort to investigate the presence of disulfide-mediated isoforms in IgG3, we employed a bottom-up mass spectrometry approach to accurately determine the disulfide bond linkages in endogenous human IgG3 monoclonal antibody and our results show that no such alternative disulfide bonds exist.	Disulfides	44-53	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	75-79
28989532-7	2016	In an effort to investigate the presence of disulfide-mediated isoforms in IgG3, we employed a bottom-up mass spectrometry approach to accurately determine the disulfide bond linkages in endogenous human IgG3 monoclonal antibody and our results show that no such alternative disulfide bonds exist.	Disulfides	44-53	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	204-208
28989532-7	2016	In an effort to investigate the presence of disulfide-mediated isoforms in IgG3, we employed a bottom-up mass spectrometry approach to accurately determine the disulfide bond linkages in endogenous human IgG3 monoclonal antibody and our results show that no such alternative disulfide bonds exist.	Disulfides	160-169	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	204-208
28989532-7	2016	In an effort to investigate the presence of disulfide-mediated isoforms in IgG3, we employed a bottom-up mass spectrometry approach to accurately determine the disulfide bond linkages in endogenous human IgG3 monoclonal antibody and our results show that no such alternative disulfide bonds exist.	Disulfides	160-169	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	204-208
27307043-4	2016	Mutational analyses and functional assays have identified residues of the receptor subunit IL-1Rrp2 needed for cytokine recognition, stable protein expression, disulfide bond formation and glycosylation that are critical for signal transduction.	Disulfides	160-169	interleukin 1 receptor like 2	Homo sapiens	91-99
26947058-7	2016	Mass spectrometry in VDAC3 revealed that a disulfide bridge can be formed and other cysteine oxidations are also detectable.	Disulfides	43-52	voltage dependent anion channel 3	Homo sapiens	21-26
27442017-5	2016	Moreover, mass spectrometry revealed some disulfide heterogeneity in the expressed proteins, particularly in V1V2-C1 region and most prominently in the TV1 gp120 dimers.	Disulfides	42-51	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	156-161
27091403-4	2016	A population of Cox26 was observed to exist in a disulfide bond partnership with the Cox2 subunit of complex IV.	Disulfides	49-58	Cox26p	Saccharomyces cerevisiae S288C	16-21
27105780-3	2016	Here a cap-closed variant of human intestinal fatty acid binding protein was generated by mutagenesis, in which the helical cap is locked to the beta-barrel by a disulfide linkage.	Disulfides	162-171	glutamic-oxaloacetic transaminase 2	Homo sapiens	46-72
27222580-6	2016	ATIII has three disulfide bonds, two near the N terminus and one near the C terminus.	Disulfides	16-25	serpin family C member 1	Homo sapiens	0-5
27222580-7	2016	Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state.	Disulfides	74-83	serpin family C member 1	Homo sapiens	15-20
27222580-7	2016	Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state.	Disulfides	139-148	serpin family C member 1	Homo sapiens	15-20
27222580-7	2016	Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state.	Disulfides	185-195	serpin family C member 1	Homo sapiens	15-20
27029462-12	2016	We show that Escherichia coli Trx83 with a truncated Trx fold induces PBMC proliferation, but only in the disulfide-reduced form.	Disulfides	106-115	thioredoxin	Homo sapiens	30-33
27067900-0	2016	An HLA-B27 Homodimer Specific Antibody Recognizes a Discontinuous Mixed-Disulfide Epitope as Identified by Affinity-Mass Spectrometry.	Disulfides	72-81	major histocompatibility complex, class I, B	Homo sapiens	3-10
27067900-6	2016	The epitope was identified by proteolytic epitope excision and MALDI mass spectrometry, and shown to comprise a discontinuous Cys-203- 257-Cys mixed-disulfide peptide structure that is not accessible in HLA-B27 heterotrimers due to protection by noncovalently linked beta2-microglobulin.	Disulfides	149-158	major histocompatibility complex, class I, B	Homo sapiens	203-210
27067900-6	2016	The epitope was identified by proteolytic epitope excision and MALDI mass spectrometry, and shown to comprise a discontinuous Cys-203- 257-Cys mixed-disulfide peptide structure that is not accessible in HLA-B27 heterotrimers due to protection by noncovalently linked beta2-microglobulin.	Disulfides	149-158	beta-2-microglobulin	Homo sapiens	267-286
27166796-5	2016	We report the successful expression of active human sialyltransferases ST3Gal1 and ST6Gal1 in commercial Escherichia coli strains designed for production of disulfide-containing proteins.	Disulfides	157-166	ST3 beta-galactoside alpha-2,3-sialyltransferase 1	Homo sapiens	71-78
27061576-0	2016	Oxidation of the N-terminal domain of the wheat metallothionein Ec -1 leads to the formation of three distinct disulfide bridges.	Disulfides	111-120	metallothionein-like protein 1	Triticum aestivum	48-63
27128442-9	2016	Two N-terminal PAN cysteines, Cys68 and Cys87, were shown to form a disulfide bridge and Cys340, localized in a C-terminal putative transactivation domain, can be S-glutathionylated.	Disulfides	68-77	bZIP transcription factor family protein	Arabidopsis thaliana	15-18
26948310-5	2016	CCl4 affected the formation of disulfide bonds through excessive hyper-oxidation of protein disulfide isomerase (PDI).	Disulfides	31-40	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	84-111
26948310-5	2016	CCl4 affected the formation of disulfide bonds through excessive hyper-oxidation of protein disulfide isomerase (PDI).	Disulfides	31-40	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	113-116
26944735-0	2016	Characterization of post-translational modifications in full-length human BMP-1 confirms the presence of a rare vicinal disulfide linkage in the catalytic domain and highlights novel features of the EGF domain.	Disulfides	120-129	bone morphogenetic protein 1	Homo sapiens	74-79
26944735-2	2016	Previous structural studies on the refolded catalytic domain of BMP-1 produced in E. coli have suggested the existence of a rare vicinal disulfide linkage near the active site.	Disulfides	137-146	bone morphogenetic protein 1	Homo sapiens	64-69
26944735-4	2016	Ten disulfide linkages of BMP-1, including the vicinal disulfide linkage C185-C186 could be unambiguously identified.	Disulfides	4-13	bone morphogenetic protein 1	Homo sapiens	26-31
26865631-11	2016	Disulfide cross-linking with directions opposing or along the bending angle of the beta2,3-sheet toward the alpha2-helix led to loss-of-function and gain-of-function of P2X4 receptors, respectively.	Disulfides	0-9	neuronal differentiation 1	Homo sapiens	83-90
26940996-0	2016	Intermolecular disulfide bond in the dimerization of S-periaxin mediated by Cys88 and Cys139.	Disulfides	15-24	periaxin	Homo sapiens	55-63
26940996-4	2016	In this paper, S-periaxin was reported to be homodimerized through the formation of intermolecular disulfide bonds with its Cys88 and Cys139 residues under mild oxidation conditions.	Disulfides	99-108	periaxin	Homo sapiens	17-25
26315306-1	2016	Selenoprotein M (SelM) may function as thiol disulfide oxidoreductase that participates in the formation of disulfide bonds and can be implicated in calcium responses.	Disulfides	45-54	selenoprotein M	Gallus gallus	0-15
26315306-1	2016	Selenoprotein M (SelM) may function as thiol disulfide oxidoreductase that participates in the formation of disulfide bonds and can be implicated in calcium responses.	Disulfides	45-54	selenoprotein M	Gallus gallus	17-21
26772871-4	2016	We used a redox sensitive green fluorescent protein (GFP) fused to the N- or C-terminus to show that these regions face the cytosol, and introduction of glycosylation sites along with mixed disulfide formation with thioredoxin-like transmembrane protein (TMX) to demonstrate ER localization of the major loop.	Disulfides	190-199	thioredoxin	Homo sapiens	215-226
26806159-0	2016	A computational study of ion current modulation in hVDAC3 induced by disulfide bonds.	Disulfides	69-78	voltage dependent anion channel 3	Homo sapiens	51-57
26806159-11	2016	The results show how VDAC3 is able to modulate its pore size and current by exploiting the mobility of the N-terminal and forming, upon external stimuli, disulfide bridges with cysteine residues located on the barrel and exposed to the inter-membrane space.	Disulfides	154-163	voltage dependent anion channel 3	Homo sapiens	21-26
26917556-5	2016	CAH1 pre-protein undergoes extensive post-translational modification in the endomembrane system, including glycosylation, disulfide bond formation and proteolytic removal of a peptide "spacer" region, resulting in a mature, heterotetrameric enzyme with two large and two small subunits.	Disulfides	122-131	carbonic anhydrase 1	Arabidopsis thaliana	0-4
26964514-6	2016	Additionally, recombinant human (rh) APE1/Ref-1 with reducing activity induced a conformational change in rh TNF-alpha receptor 1 (TNFR1) by thiol-disulfide exchange.	Disulfides	147-156	TNF receptor superfamily member 1A	Homo sapiens	109-129
26964514-6	2016	Additionally, recombinant human (rh) APE1/Ref-1 with reducing activity induced a conformational change in rh TNF-alpha receptor 1 (TNFR1) by thiol-disulfide exchange.	Disulfides	147-156	TNF receptor superfamily member 1A	Homo sapiens	131-136
26714232-5	2016	The partially reduced AuIB (P2-8 ), with the disulfide bond between cysteine 2, 8 broken, shows significantly perturbed secondary structural features with almost total loss in helicity.	Disulfides	45-54	transmembrane p24 trafficking protein 5	Homo sapiens	28-32
26809098-0	2016	A soluble form of the interleukin-6 family signal transducer gp130 is dimerized via a C-terminal disulfide bridge resulting from alternative mRNA splicing.	Disulfides	97-106	interleukin 6 cytokine family signal transducer	Homo sapiens	61-66
26601956-7	2016	The latter reaction occurred via the sulfenic acid, which reacted sufficiently rapidly (k = 500 m(-1) s(-1)) for physiological concentrations of GSH to inhibit Prx disulfide formation and protect against hyperoxidation to the sulfinic acid.	Disulfides	164-173	periaxin	Mus musculus	160-163
25827171-0	2016	Do Beta 2-Glycoprotein I Disulfide Bonds Protect the Human Retina in the Setting of Age-Related Macular Degeneration?	Disulfides	25-34	apolipoprotein H	Homo sapiens	3-24
27538701-5	2016	The study of molecular characteristics of PDI in some cereal species have shown that this enzyme participates in the maturation of secretory proteins and also in the formation of albuminous substances in endosperm, in the mechanism of formation of disulfide bonds and polymerization of gluten polypeptides in wheat.	Disulfides	248-257	protein disulfide-isomerase	Triticum aestivum	42-45
26407725-0	2015	VDAC3 gating is activated by suppression of disulfide-bond formation between the N-terminal region and the bottom of the pore.	Disulfides	44-53	voltage dependent anion channel 3	Homo sapiens	0-5
26407725-6	2015	However, gating of VDAC3 was evoked by dithiothreitol (DTT) and S-nitrosoglutathione (GSNO), which are thought to suppress disulfide-bond formation.	Disulfides	123-132	voltage dependent anion channel 3	Homo sapiens	19-24
26367013-7	2015	From the findings of the present study, it appears that the tandem repeats of two small domains with no disulfide bonds and with a destabilizing cavity function as the evolutionary strategy of the wide-type c-Myb DNA-binding domain to produce an appropriate fraction of the locally fluctuating state at 37  C, which is more amenable to DNA-binding.	Disulfides	104-113	MYB proto-oncogene, transcription factor	Homo sapiens	207-212
3838304-9	1985	In particular, a disulfide bond which links the COOH-terminal (reactive site) region of antithrombin III to the remainder of the molecule and is important for the heparin-induced conformational change in the protein and high affinity binding of heparin does not appear to exist in heparin cofactor II.	Disulfides	17-26	serpin family C member 1	Homo sapiens	88-104
2985098-7	1985	So far no information has been obtained in which compartment and at what stage of posttranslational events the dimerization occurs by formation of the single disulfide bond at position Cys6 in the mature apo AII structure, leading to the symmetrical molecule.	Disulfides	158-167	apolipoprotein A2	Homo sapiens	204-211
2416557-2	1985	A half-molecular fragment of alpha 2-macroglobulin has been prepared by reducing and alkylating the inter-subunit disulfide bonds in the tetrameric alpha 2-macroglobulin molecule with 1 mM dithiothreitol (40 min) and 3 mM iodoacetamide (40 min).	Disulfides	114-123	alpha-2-macroglobulin	Homo sapiens	29-50
2416557-2	1985	A half-molecular fragment of alpha 2-macroglobulin has been prepared by reducing and alkylating the inter-subunit disulfide bonds in the tetrameric alpha 2-macroglobulin molecule with 1 mM dithiothreitol (40 min) and 3 mM iodoacetamide (40 min).	Disulfides	114-123	alpha-2-macroglobulin	Homo sapiens	148-169
6510521-3	1984	The presence of intramolecular disulfide bonds, connecting half-cystine residues 126/130 and 165/170, was proved in fragments CB2 and CB3.	Disulfides	31-40	cannabinoid receptor 2	Homo sapiens	126-129
6334307-5	1984	We suggest that the conservation of cysteine residues, which form the disulfide bonds present in the active EGF molecule, may extend to conservation of disulfide bonds in these other proteins.	Disulfides	70-79	epidermal growth factor	Homo sapiens	108-111
6334307-5	1984	We suggest that the conservation of cysteine residues, which form the disulfide bonds present in the active EGF molecule, may extend to conservation of disulfide bonds in these other proteins.	Disulfides	152-161	epidermal growth factor	Homo sapiens	108-111
6589623-10	1984	In plasma, the heavy and light chains of protein C are linked together by a disulfide bond.	Disulfides	76-85	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	41-50
6203904-8	1984	Most likely, Cys-6 of CB9 is bound to the corresponding residue in CB9 from another subunit, thus forming an interchain disulfide bridge in alpha 2-macroglobulin.	Disulfides	120-129	alpha-2-macroglobulin	Homo sapiens	140-161
6203905-6	1984	CB2 contains two glucosamine-based carbohydrate groups attached to Asn-23 and Asn-38, and one internal disulfide bridge connecting Cys-16 with Cys-54.	Disulfides	103-112	cannabinoid receptor 2	Homo sapiens	0-3
6334690-2	1984	In vitro hepatocyte-uptake studies with antithrombin III-proteinase complexes confirmed the hepatocyte uptake and degradation of these complexes, and demonstrated the formation of a disulfide interchange product between the ligand and a cellular protein.	Disulfides	182-191	serpin family C member 1	Homo sapiens	40-56
6390091-0	1984	Enzymatic reduction-oxidation of protein disulfides by thioredoxin.	Disulfides	41-51	thioredoxin	Homo sapiens	55-66
6198647-7	1984	The 125I-PDGF-alpha 2M complex or 125I-PDGF-plasma binding protein complex was not dissociated by 8 M urea, 1 M acetic acid, 0.1 M NaOH, or 1% NaDodSO4 but was dissociated by 2-mercaptoethanol, suggesting that the covalent binding of 125I-PDGF to alpha 2M occurs through a disulfide/sulfhydryl exchange reaction.	Disulfides	273-282	alpha-2-macroglobulin	Homo sapiens	14-22
6197087-1	1983	Native bovine seminal ribonuclease is a dimeric protein, whose identical subunits (Mr 14500), linked through two disulfide bridges, can be dissociated by a selective reduction procedure.	Disulfides	113-122	seminal ribonuclease	Bos taurus	14-34
6313454-8	1983	The high-affinity IGF-II receptor in fibroblasts affinity labeled with 125I-IGF-II or 125I-IGF-I consists of a single polypeptide not disulfide linked to any other membrane component.	Disulfides	134-143	insulin like growth factor 2 receptor	Homo sapiens	18-33
6313454-8	1983	The high-affinity IGF-II receptor in fibroblasts affinity labeled with 125I-IGF-II or 125I-IGF-I consists of a single polypeptide not disulfide linked to any other membrane component.	Disulfides	134-143	insulin like growth factor 2	Homo sapiens	18-24
6411612-3	1983	It is inferred from circular dichroism studies that there are changes in the aromatic residues and the disulfides as well as in the folding of peptide backbone of Fab mu.	Disulfides	103-113	FA complementation group B	Homo sapiens	163-166
6185576-4	1983	In the present study, we show that B10.BR GT-TSF1 is composed of separate I-Jk and idiotype-bearing chains linked by disulfide bond(s).	Disulfides	117-126	serine/threonine kinase 16	Mus musculus	45-49
6830263-0	1983	Localization of the disulfide bond in human antithrombin III required for heparin-accelerated thrombin inactivation.	Disulfides	20-29	serpin family C member 1	Homo sapiens	44-60
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Disulfides	39-48	serpin family C member 1	Homo sapiens	57-73
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Disulfides	39-48	serpin family C member 1	Homo sapiens	150-166
6191200-4	1982	A peptic fragment containing a disulfide loop was found to possess antigenic activity in both bovine and goat alpha-lactalbumin.	Disulfides	31-40	alpha-lactalbumin	Capra hircus	110-127
6177771-1	1982	The monoclonal antibody 4F2 recognizes a disulfide-linked ricin-binding glycoprotein complex (Mr congruent to 125,000) composed of a sialylated heavy subunit (Mr congruent to 85,000 on T cell lines) and an unsialylated light subunit (Mr congruent to 41,000).	Disulfides	41-50	solute carrier family 3 member 2	Homo sapiens	24-27
7061512-12	1982	Reduction of the interchain disulfide bonds of the Fab fragments abolished their ability to polymerize, probably by inducing a conformational change a considerable distance away in the variable domains of the molecules.	Disulfides	28-37	FA complementation group B	Homo sapiens	51-54
7105432-6	1982	DBH is a tetrameric glycoprotein consisting of 2 non-covalently joined dimeric subunits, each of which is 2 disulfide linked monomers; interspecies molecular weight differences were noted.	Disulfides	108-117	dopamine beta-hydroxylase	Homo sapiens	0-3
7284322-0	1981	Immunospecific targeting of liposomes to cells: a novel and efficient method for covalent attachment of Fab" fragments via disulfide bonds.	Disulfides	123-132	FA complementation group B	Homo sapiens	104-107
6270681-12	1981	The major labeled thymocyte membrane protein consisting of disulfide-bonded subunits was identified as the Ly-2/3 antigen.	Disulfides	59-68	lymphocyte antigen 23	Mus musculus	107-113
6270681-15	1981	A third disulfide-bonded homodimer, which was heterogeneous in apparent Mr, appeared to be part of the Ly-2/3 complex.	Disulfides	8-17	lymphocyte antigen 23	Mus musculus	103-109
6101236-2	1981	Analysis by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and gas/liquid chromatography indicated that the C3d-binding glycoprotein consisted of a single polypeptide chain with extensive intrachain disulfide bonds, a molecular weight of 72,000, and several different bound carbohydrates.	Disulfides	210-219	endogenous retrovirus group K member 13	Homo sapiens	119-122
7430640-1	1980	The toxic A chain of ricin and the Fab" fragment of antibody directed against human immunoglobulin (Ig) have been disulfide linked via their intrinsic sulfhydryl groups.	Disulfides	114-123	FA complementation group B	Homo sapiens	35-38
6256086-1	1980	We have prepared a 2-pyridyl-dithiopropionate derivative of epidermal growth factor (EGF) and conjugated the derivative by disulfide interchange to the A chain of ricin (RTA) or to fragment A of diphtheria toxin (DTA).	Disulfides	123-132	epidermal growth factor	Mus musculus	60-83
6256086-1	1980	We have prepared a 2-pyridyl-dithiopropionate derivative of epidermal growth factor (EGF) and conjugated the derivative by disulfide interchange to the A chain of ricin (RTA) or to fragment A of diphtheria toxin (DTA).	Disulfides	123-132	epidermal growth factor	Mus musculus	85-88
6766924-13	1980	Activation of prekallikrein by Hageman factor was found to involve cleavage of the single peptide bond on the disulfide-bridged polypeptide chain, and no change of molecular weight was observed during the activation.	Disulfides	110-119	coagulation factor XII	Bos taurus	31-45
534646-0	1979	Intrachain disulfide bridges of bovine seminal ribonuclease.	Disulfides	11-20	seminal ribonuclease	Bos taurus	39-59
534646-1	1979	The pairing of the four intrachain disulfide bonds of bovine seminal ribonuclease, a dimeric protein isolated from bovine seminal plasma, has been established by the isolation and characterization of the cystine peptides obtained from a thermolytic-tryptic hydrolysate of the protein.	Disulfides	35-44	seminal ribonuclease	Bos taurus	61-81
454621-6	1979	Evidence is presented that disulfide-disulfide interchange enzyme is a different activity from the previously described protein disulfide isomerase and thiol transferase.	Disulfides	27-36	protein disulfide-isomerase	Oryctolagus cuniculus	120-147
454621-6	1979	Evidence is presented that disulfide-disulfide interchange enzyme is a different activity from the previously described protein disulfide isomerase and thiol transferase.	Disulfides	37-46	protein disulfide-isomerase	Oryctolagus cuniculus	120-147
738998-0	1978	Formation of interchain disulfide bonds in Bence Jones proteins and Fab(t) fragments of immunoglobulin G through thiol-disulfide interchange.	Disulfides	24-33	FA complementation group B	Homo sapiens	68-71
738998-0	1978	Formation of interchain disulfide bonds in Bence Jones proteins and Fab(t) fragments of immunoglobulin G through thiol-disulfide interchange.	Disulfides	119-128	FA complementation group B	Homo sapiens	68-71
738998-1	1978	The formation of interchain disulfide bonds from partially reduced Bence Jones protein (Nag, type lambda) and Fab(t) fragments of IgG1 myeloma proteins was studied in the presence of various disulfide reagents.	Disulfides	28-37	FA complementation group B	Homo sapiens	110-113
738998-8	1978	For Fab(t), on the other hand, both intermediates equally can form the inter Fd-L disulfide bond.	Disulfides	82-91	FA complementation group B	Homo sapiens	4-7
722075-12	1978	However, the I-A alpha and beta chains tend to associate through disulfide bonds during detergent lysis; the presence of alkylating agents during cell lysis prevents this association, and only free alpha and beta chains are observed under nonreducing conditions.	Disulfides	65-74	protein tyrosine phosphatase, receptor type, N	Mus musculus	13-22
281700-2	1978	Sequence analyses performed by automated methods and by sequential digestion with leucine aminopeptidase and carboxypeptidase Y demonstrate that blastokinin is a dimer of identical 69-amino acid subunits held together in parallel orientation by two disulfide bridges at positions 3 and 68.	Disulfides	249-258	secretoglobin family 1A member 1	Homo sapiens	145-156
211503-2	1978	The labeled gp70 molecules in these cells were linked to a protein of approximately 15,000 daltons via native disulfide bonding.	Disulfides	110-119	embigin	Mus musculus	12-16
17603-1	1977	Purification of thioredoxin reductase from calf liver and thymus and studies of its function in disulfide reduction.	Disulfides	96-105	peroxiredoxin 5	Bos taurus	16-37
190236-3	1977	Utilizing methyl-5-bromovalerimidate, a disulfide cross-linked conjugate of human placental lactogen (hPL) and diphtheria toxin fragment A (toxin A) was synthesized.	Disulfides	40-49	galectin 1	Homo sapiens	102-105
190236-6	1977	The S-sulfonated hPL reacted readily with the-SH gorup of reduced toxin A to form a 1 mol/mol of disulfide conjugate in high yield.	Disulfides	97-106	galectin 1	Homo sapiens	17-20
809280-0	1975	Purification of alpha1-antitrypsin from plasma through thiol-disulfide interchange.	Disulfides	61-70	serpin family A member 1	Canis lupus familiaris	16-34
809280-4	1975	The plasma proteins, alpha1-antitrypsin and prealbumin have the greatest affinity for the interchange reaction with mixed disulfides.	Disulfides	122-132	serpin family A member 1	Canis lupus familiaris	21-39
809280-5	1975	The disulfide link between alpha1-antitrypsin and nu-chain is sensitive to excess Nbs, and is selectively cleaved in the presence of 5,5"-dithiobis(2-nitrobenzoate) (Nbs2) which accepts the sulfhydryl group of alpha1-antitrypsin.	Disulfides	4-13	serpin family A member 1	Canis lupus familiaris	27-45
809280-5	1975	The disulfide link between alpha1-antitrypsin and nu-chain is sensitive to excess Nbs, and is selectively cleaved in the presence of 5,5"-dithiobis(2-nitrobenzoate) (Nbs2) which accepts the sulfhydryl group of alpha1-antitrypsin.	Disulfides	4-13	serpin family A member 1	Canis lupus familiaris	210-228
809280-9	1975	The alpha1-antitrypsin is harvested from this procedure as a mixed disulfide with Nbs.	Disulfides	67-76	serpin family A member 1	Canis lupus familiaris	4-22
1058492-8	1975	Reduction of the interchain disulfide bonds of the antibodies abolished the antigen-induced spectral changes due to the presence of the Fc portion in the molecule, but not the changes observed in Fab, suggesting that the disulfide bonds at the hinge region of the antibody are required for the transmission of the conformational change from the Fab to the Fc.	Disulfides	28-37	FA complementation group B	Homo sapiens	345-348
1058492-8	1975	Reduction of the interchain disulfide bonds of the antibodies abolished the antigen-induced spectral changes due to the presence of the Fc portion in the molecule, but not the changes observed in Fab, suggesting that the disulfide bonds at the hinge region of the antibody are required for the transmission of the conformational change from the Fab to the Fc.	Disulfides	221-230	FA complementation group B	Homo sapiens	345-348
47881-14	1975	Recovery of the affinity by papain digestion strongly suggested that cleavage of disulfide bonds in the Fab portion of the molecules induced conformational changes in the Fc portion which is involved in binding to the target cells.	Disulfides	81-90	FA complementation group B	Homo sapiens	104-107
1178941-0	1975	Spontaneous dissociation of an IgG-3 paraprotein through disulfide interchange.	Disulfides	57-66	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	31-36
33460768-6	2021	Through proteomic approaches, ZAP70 is identified as the key interacting protein of NPGPx through disulfide bonding.	Disulfides	98-107	zeta-chain (TCR) associated protein kinase	Mus musculus	30-35
33389495-11	2021	The results obtained show that CTX inactivates the pkBADH due to oxidation of the catalytic cysteine or because it oxidizes catalytic and neighborhood cysteine, forming a disulfide bridge with a concomitant decrease in the activity of the enzyme.	Disulfides	171-180	cytochrome P450 family 27 subfamily A member 1	Homo sapiens	31-34
33620491-5	2021	LTO1 contains thioredoxin (TRX)-like and VKOR domains which are related to the disulfide-bond-formation (Dsb) system in bacteria.	Disulfides	79-88	NAD(P)H dehydrogenase (quinone)s	Arabidopsis thaliana	0-4
33541434-0	2021	Protein disulfide isomerase ERp57 protects early muscle denervation in experimental ALS.	Disulfides	8-17	protein disulfide isomerase associated 3	Mus musculus	28-33
33541434-5	2021	ERp57 catalyzes disulfide bond formation and isomerization in the endoplasmic reticulum (ER), constituting a central component of protein quality control mechanisms.	Disulfides	16-25	protein disulfide isomerase associated 3	Mus musculus	0-5
33185461-2	2021	In the myocardium, type-1 protein kinase A (PKARIalpha) can be reversibly oxidized, forming interprotein disulfide bonds within the holoenzyme complex.	Disulfides	105-114	protein kinase, cAMP dependent regulatory, type I, alpha	Mus musculus	44-54
33372514-7	2021	With the disulfide bond-mediated GSH depletion and DOX-mediated reactive oxygen species (ROS) production, treatment with DOX@PssP-Hh NPs prominently reduced glutathione peroxidase 4 (GPX4) level and would lead to enhanced oxidative stresses.	Disulfides	9-18	glutathione peroxidase 4	Homo sapiens	157-181
33372514-7	2021	With the disulfide bond-mediated GSH depletion and DOX-mediated reactive oxygen species (ROS) production, treatment with DOX@PssP-Hh NPs prominently reduced glutathione peroxidase 4 (GPX4) level and would lead to enhanced oxidative stresses.	Disulfides	9-18	glutathione peroxidase 4	Homo sapiens	183-187
33220304-9	2021	Reduction of the Cys1-Cys7 disulfide bond resulted in faster fibrillation with involvement of different hCT residues as indicated by pulsed HDX-MS.	Disulfides	27-36	cystin 1	Homo sapiens	17-21
33301305-0	2020	Substituting the Thiol Ester of Human A2M or C3 with a Disulfide Produces Native Proteins with Altered Proteolysis-Induced Conformational Changes.	Disulfides	55-64	alpha-2-macroglobulin	Homo sapiens	38-47
33301305-2	2020	Here, we have characterized the human alpha2-macroglobulin (A2M) and complement component C3 mutants A2M Q975C and C3 Q1013C, which replace the CGEQ thiol ester motifs of the original proteins with the disulfide-forming sequence CGEC.	Disulfides	202-211	alpha-2-macroglobulin	Homo sapiens	38-58
32992250-0	2020	Disulfide bridge cross-linking between protein and the RNA backbone as a tool to study RNase H1.	Disulfides	0-9	ribonuclease H1	Homo sapiens	87-95
33263168-4	2020	Multimerin1 (MMRN1) is a di-sulfide linked homo-polymeric glycoprotein from EMILIN family.	Disulfides	25-35	multimerin 1	Homo sapiens	0-11
33263168-4	2020	Multimerin1 (MMRN1) is a di-sulfide linked homo-polymeric glycoprotein from EMILIN family.	Disulfides	25-35	multimerin 1	Homo sapiens	13-18
32997205-6	2020	Additionally, glucose 6-phosphate dehydrogenase (G6PD) activity and an increased (>= 300%) lactate/pyruvate molar ratio (lac/pyr) during production cell culture correlated to disulfide reduction risk, suggesting a metabolic shift to the pentose phosphate pathway (PPP).	Disulfides	175-184	glucose-6-phosphate 1-dehydrogenase	Cricetulus griseus	14-47
32997205-6	2020	Additionally, glucose 6-phosphate dehydrogenase (G6PD) activity and an increased (>= 300%) lactate/pyruvate molar ratio (lac/pyr) during production cell culture correlated to disulfide reduction risk, suggesting a metabolic shift to the pentose phosphate pathway (PPP).	Disulfides	175-184	glucose-6-phosphate 1-dehydrogenase	Cricetulus griseus	49-53
33087733-9	2020	In the meantime, the protein levels of glutathione peroxidase 4 (GPX4), which plays an essential role in the disulfide bond formation during spermatogenesis, were significantly increased in the testis and caput epididymis of the DKO mice compared with the WT mice.	Disulfides	109-118	glutathione peroxidase 4	Mus musculus	39-63
33087733-9	2020	In the meantime, the protein levels of glutathione peroxidase 4 (GPX4), which plays an essential role in the disulfide bond formation during spermatogenesis, were significantly increased in the testis and caput epididymis of the DKO mice compared with the WT mice.	Disulfides	109-118	glutathione peroxidase 4	Mus musculus	65-69
33060708-3	2020	Mammalian Prdx"s are classified according to the number of Cys implicated in their catalytic activity by the formation of either inter-molecular (typical 2-Cys, Prdx1-4) or intra-molecular (atypical 2-Cys, Prdx5) disulfide bond, or non-covalent interactions (1-Cys, Prdx6).	Disulfides	213-222	peroxiredoxin 1	Homo sapiens	10-14
33054088-2	2020	The extracellular allosteric disulfide bond Cys186-Cys209 of human tissue factor shows high evolutionary conservation and in vitro evidence suggests that it significantly contributes to tissue factor procoagulant activity.	Disulfides	29-38	coagulation factor III, tissue factor	Homo sapiens	67-80
33054088-2	2020	The extracellular allosteric disulfide bond Cys186-Cys209 of human tissue factor shows high evolutionary conservation and in vitro evidence suggests that it significantly contributes to tissue factor procoagulant activity.	Disulfides	29-38	coagulation factor III, tissue factor	Homo sapiens	186-199
26311893-6	2015	The further addition of a disulfide bond (SOS) to link the gp120 and gp41 subunits in the uncleaved gp140-FL20-SOSIP protein increases native-like trimer formation to ~20 to 30%.	Disulfides	26-35	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	59-64
26311893-7	2015	Analysis of the disulfide bond content shows that misfolded gp120 subunits are abundant in uncleaved CZA97.012 gp140UNC-Fd-His proteins but very rare in native-like trimer populations.	Disulfides	16-25	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	60-65
26349060-1	2015	Extracellular high-mobility group box 1 (HMGB1) (disulfide form), via activation of toll-like receptor 4 (TLR4)-dependent signaling, is a strong driver of pathologic inflammation in both acute and chronic conditions.	Disulfides	49-58	toll like receptor 4	Homo sapiens	84-104
26349060-1	2015	Extracellular high-mobility group box 1 (HMGB1) (disulfide form), via activation of toll-like receptor 4 (TLR4)-dependent signaling, is a strong driver of pathologic inflammation in both acute and chronic conditions.	Disulfides	49-58	toll like receptor 4	Homo sapiens	106-110
26349060-4	2015	Here we report that the first-generation HIV-PI saquinavir (SQV), as well as a newly identified mammalian protease inhibitor STO33438 (334), potently block disulfide HMGB1-induced TLR4 activation, as assayed by the production of TNF-alpha by human monocyte-derived macrophages (THP-1).	Disulfides	156-165	toll like receptor 4	Homo sapiens	180-184
26349060-10	2015	Disulfide HMGB1 drives pathologic inflammation in many models by activating signaling through TLR4.	Disulfides	0-9	toll like receptor 4	Homo sapiens	94-98
26349060-11	2015	Cell-based screening identified the mammalian protease cathepsin V as a novel therapeutic target to inhibit TLR4-mediated inflammation induced by extracellular HMGB1 (disulfide form).	Disulfides	167-176	toll like receptor 4	Homo sapiens	108-112
26349060-12	2015	We identified two protease inhibitors (PIs) that block cathepsin V and thereby inhibit disulfide HMGB1-induced TLR4 activation: saquinavir (SQV), a first-generation PI targeting viral HIV protease and STO33438 (334), targeting mammalian proteases.	Disulfides	87-96	toll like receptor 4	Homo sapiens	111-115
26513450-7	2015	This is because disulfide bonds are stable in most blood pools but are efficiently cleaved by cellular thiols, including glutathione (GSH) and thioredoxin (Trx), which are generally found at elevated levels in tumors.	Disulfides	16-25	thioredoxin	Homo sapiens	143-154
26513450-7	2015	This is because disulfide bonds are stable in most blood pools but are efficiently cleaved by cellular thiols, including glutathione (GSH) and thioredoxin (Trx), which are generally found at elevated levels in tumors.	Disulfides	16-25	thioredoxin	Homo sapiens	156-159
26417924-2	2015	TrxR catalyzes disulfide reduction in Trx with NADPH as cofactor.	Disulfides	15-24	thioredoxin	Homo sapiens	0-3
26417924-3	2015	Because Trx is an antioxidant, oxidative stress results in an increase in Trx, which has a reduced disulfide component.	Disulfides	99-108	thioredoxin	Homo sapiens	8-11
26417924-3	2015	Because Trx is an antioxidant, oxidative stress results in an increase in Trx, which has a reduced disulfide component.	Disulfides	99-108	thioredoxin	Homo sapiens	74-77
26303832-0	2015	In Vivo Formation of the Protein Disulfide Bond That Enhances the Thermostability of Diphosphomevalonate Decarboxylase, an Intracellular Enzyme from the Hyperthermophilic Archaeon Sulfolobus solfataricus.	Disulfides	33-42	hypothetical protein	Saccharolobus solfataricus	85-118
26267866-5	2015	A variant of full-length PABPN1 with a stabilizing disulfide bond at position 185/201 in the RNP domain fibrillized in a redox-sensitive manner suggesting that the integrity of the RNP domain may contribute to fibril formation.	Disulfides	51-60	poly(A) binding protein nuclear 1	Homo sapiens	25-31
26068405-5	2015	Unraveling of the helical structure and formation of disulfide bonds due to oxidation were implicated in the altered myosin cross-linking pattern during subsequent TGase reactions.	Disulfides	53-62	myosin heavy chain 14	Homo sapiens	117-123
33019770-1	2020	Ly-6/uPAR or three-finger proteins (TFPs) contain a disulfide-stabilized beta-structural core and three protruding loops (fingers).	Disulfides	52-61	plasminogen activator, urokinase receptor	Homo sapiens	5-9
32522853-7	2020	Shedding of gp120, known to severely complicate structural studies, can be prevented by using the uncleaved gp160JR-FL precursor with alterations in the protease cleavage site (R508S/R511S), or by introducing a disulfide bridge between gp120 and gp41 designated "SOS" (A501C/T605C).	Disulfides	211-220	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	12-17
9293773-0	1997	Beta 2-microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins.	Disulfides	72-81	calnexin	Homo sapiens	25-33
31584633-1	2020	AIMS: Thioredoxin 1 (Trx1) is an evolutionarily conserved oxidoreductase that cleaves disulfide bonds in oxidized substrate proteins such as mechanistic target of rapamycin (mTOR) and maintains nuclear-encoded mitochondrial gene expression.	Disulfides	86-95	mechanistic target of rapamycin kinase	Mus musculus	141-172
31584633-1	2020	AIMS: Thioredoxin 1 (Trx1) is an evolutionarily conserved oxidoreductase that cleaves disulfide bonds in oxidized substrate proteins such as mechanistic target of rapamycin (mTOR) and maintains nuclear-encoded mitochondrial gene expression.	Disulfides	86-95	mechanistic target of rapamycin kinase	Mus musculus	174-178
32593213-4	2020	A disulfide isomerase, anterior gradient 2 (AGR2), has been shown to increase hypoxia-inducible factor 1, alpha subunit (HIF-1alpha) stability in breast cancer.	Disulfides	2-11	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	23-42
32593213-4	2020	A disulfide isomerase, anterior gradient 2 (AGR2), has been shown to increase hypoxia-inducible factor 1, alpha subunit (HIF-1alpha) stability in breast cancer.	Disulfides	2-11	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	44-48
9126607-1	1997	The gene from Bacteroides fragilis encoding a metallo-beta-lactamase, ccrA, was expressed in Escherichia coli BL21(DE3) containing the wild-type disulfide bond-catalyzing system dsb as an active, soluble enzyme in quantities exceeding 100 mg/liter using both rich and minimal media.	Disulfides	145-154	cfiA	Bacteroides fragilis	70-74
32434885-12	2020	Enzyme activity of P33 is related to infectious BV production, occlusion-derived virus (ODV) envelopment, occlusion body morphogenesis, and oral infectivity, suggesting that P33 is involved in disulfide bond formation of multiple proteins.	Disulfides	193-202	inhibitor of growth family member 1	Homo sapiens	19-22
32434885-12	2020	Enzyme activity of P33 is related to infectious BV production, occlusion-derived virus (ODV) envelopment, occlusion body morphogenesis, and oral infectivity, suggesting that P33 is involved in disulfide bond formation of multiple proteins.	Disulfides	193-202	inhibitor of growth family member 1	Homo sapiens	174-177
32434885-15	2020	In this study, we identified PIF5 as the first substrate of P33, which is fundamental for revealing the complete disulfide bond formation pathway in baculovirus.	Disulfides	113-122	inhibitor of growth family member 1	Homo sapiens	60-63
9522125-1	1997	Feline Interleukin-12 (IL-12) is a heterodimeric glycoprotein consisting of two disulfide linked subunits of about 40 kD (p40) and 35 kD (p35).	Disulfides	80-89	interleukin 9	Homo sapiens	122-125
32561649-4	2020	The simplest form, Hp 1-1, forms dimers consisting of two alpha1beta units, connected by disulfide bridges.	Disulfides	89-98	chromobox 5	Homo sapiens	19-25
9080194-3	1997	The presence of four disulfide bonds and the existence of two cis peptide bonds preceding prolines in the native state have complicated the analysis of the folding pathway of RNase A.	Disulfides	21-30	ribonuclease A family member 1, pancreatic	Homo sapiens	175-182
8980650-2	1996	Newly synthesized 31 kDa monomers of the B-chain (p31) dimerized rapidly via disulfide bonds to a p54 species (t1/2 &lt; 30 min).	Disulfides	77-86	interferon induced protein with tetratricopeptide repeats 2	Homo sapiens	98-101
32330361-2	2020	AspH is overexpressed on the cell surface of invasive cancer cells and accepts epidermal growth factor-like domain (EGFDs) substrates with a non-canonical ( i.e. Cys 1-2, 3-4, 5-6) disulfide pattern.	Disulfides	181-190	aspartate beta-hydroxylase	Homo sapiens	0-4
9010926-5	1996	The disulfide pattern in domain 1 of IL-7R is predicted to deviate from that observed in hGHR in that the C"-E disulfide (hGHR) is replaced by a C-C" cross-link.	Disulfides	4-13	interleukin 7 receptor	Homo sapiens	37-42
32734266-4	2020	A compact myosin gel network with thin cross-linked strands and small regular cavities formed at the age of 30 days, which was resulted from the higher content of hydrophobic interactions and disulfide bonds.	Disulfides	192-201	myosin heavy chain 14	Homo sapiens	10-16
8917542-1	1996	Biochemical studies have shown that the periplasmic protein disulfide oxidoreductase DsbC can isomerize aberrant disulfide bonds.	Disulfides	60-69	putative protein DsbC	Escherichia coli	85-89
32597324-5	2021	We found that proprotein dimers of Activin isoforms differ at intrachain disulfide bonds, which support prior evidence of varying pro-domain stability and isoform preference.	Disulfides	73-82	inhibin subunit beta E	Homo sapiens	35-42
8917542-2	1996	Here we present the first evidence for an in vivo role of DsbC in disulfide bond isomerization.	Disulfides	66-75	putative protein DsbC	Escherichia coli	58-62
8917542-3	1996	Furthermore, our data suggest that the enzymes DsbA and DsbC play distinct roles in the cell in disulfide bond formation and isomerization, respectively.	Disulfides	96-105	putative protein DsbC	Escherichia coli	56-60
8917542-4	1996	We have shown that mutants in dsbC display a defect in disulfide bond formation specific for proteins with multiple disulfide bonds.	Disulfides	55-64	putative protein DsbC	Escherichia coli	30-34
8917542-4	1996	We have shown that mutants in dsbC display a defect in disulfide bond formation specific for proteins with multiple disulfide bonds.	Disulfides	116-125	putative protein DsbC	Escherichia coli	30-34
8917542-7	1996	We propose that DipZ, a cytoplasmic membrane protein with a thioredoxin-like domain, and thioredoxin, the product of the trxA gene, are components of a pathway for maintaining DsbC active as a protein disulfide bond isomerase.	Disulfides	201-210	putative protein DsbC	Escherichia coli	176-180
32575755-5	2020	To advance our understanding of the impact of ubiquitination on tau protein aggregation and function, we applied disulfide-coupling chemistry to modify tau protein at position 353 with Lys48- or Lys63-linked di-ubiquitin, two representative polyubiquitin chains that differ in topology and structure.	Disulfides	113-122	microtubule associated protein tau	Homo sapiens	152-155
32107312-3	2020	Recent structural work has revealed that AspH accepts substrates with a noncanonical EGFD disulfide connectivity (i.e. the Cys 1-2, 3-4, 5-6 disulfide pattern).	Disulfides	90-99	aspartate beta-hydroxylase	Homo sapiens	41-45
32107312-3	2020	Recent structural work has revealed that AspH accepts substrates with a noncanonical EGFD disulfide connectivity (i.e. the Cys 1-2, 3-4, 5-6 disulfide pattern).	Disulfides	141-150	aspartate beta-hydroxylase	Homo sapiens	41-45
32107312-4	2020	We developed stable cyclic thioether analogues of the noncanonical EGFD AspH substrates to avoid disulfide shuffling.	Disulfides	97-106	aspartate beta-hydroxylase	Homo sapiens	72-76
8900156-5	1996	Native disulfide-linked homodimers of CD28 and CTLA-4 bound with two kinetically distinct binding sites, one of high avidity and slow dissociation and one of low avidity and more rapid dissociation.	Disulfides	7-16	CD28 molecule	Homo sapiens	38-42
8816823-5	1996	Tunicate GnRH-I (pGlu-His-Trp-Ser-Asp-Tyr-Phe-Lys-Pro-Gly-NH2) has 60% of its residues conserved, compared with mammalian GnRH, whereas tunicate GnRH-II (pGlu-His-Trp-Ser-Leu-Cys-His-Ala-Pro-Gly-NH2) is unusual in that it was isolated as a disulfide-linked dimer.	Disulfides	240-249	gonadotropin releasing hormone 1	Homo sapiens	9-13
32269095-2	2020	In peripheral APCs, gamma-IFN-inducible lysosomal thiol reductase (GILT) is critical for MHC class II-restricted presentation of disulfide bond-containing proteins, including the self-antigen and melanoma Ag tyrosinase-related protein 1 (TRP1).	Disulfides	129-138	interferon gamma inducible protein 30	Mus musculus	20-65
32269095-2	2020	In peripheral APCs, gamma-IFN-inducible lysosomal thiol reductase (GILT) is critical for MHC class II-restricted presentation of disulfide bond-containing proteins, including the self-antigen and melanoma Ag tyrosinase-related protein 1 (TRP1).	Disulfides	129-138	interferon gamma inducible protein 30	Mus musculus	67-71
8902616-0	1996	A role of PDI in the reductive cleavage of mixed disulfides.	Disulfides	49-59	prolyl 4-hydroxylase subunit beta	Homo sapiens	10-13
32318934-4	2020	To solve this problem, we proposed the redirection of hEGF into the thylakoid lumen where the environment could improve disulfide bonds formation stabilizing the functional conformation of the protein.	Disulfides	120-129	epidermal growth factor	Homo sapiens	54-58
32369015-0	2020	Keratin 14-dependent disulfides regulate epidermal homeostasis and barrier function via 14-3-3sigma and YAP1.	Disulfides	21-31	keratin 14	Mus musculus	0-10
32369015-2	2020	Recent studies evidenced a role for K14-dependent disulfide bonding in the organization and dynamics of keratin IFs in skin keratinocytes.	Disulfides	50-59	keratin 14	Mus musculus	36-39
8902616-1	1996	We previously reported that protein disulfide isomerase (PDI) can dissociate the glutathione molecule in vitro from the mutant human lysozyme (hLZM) C77A-a, which is modified with glutathione at Cys95; however, it seems structurally difficult for PDI to attack either the disulfide bond or the side chain of the cysteine residue of a mixed disulfide.	Disulfides	36-45	prolyl 4-hydroxylase subunit beta	Homo sapiens	57-60
32369015-3	2020	Here we report that knock-in mice harboring a cysteine-to-alanine substitution at Krt14"s codon 373 (C373A) exhibit alterations in disulfide-bonded K14 species and a barrier defect secondary to enhanced proliferation, faster transit time and altered differentiation in epidermis.	Disulfides	131-140	keratin 14	Mus musculus	82-87
32369015-3	2020	Here we report that knock-in mice harboring a cysteine-to-alanine substitution at Krt14"s codon 373 (C373A) exhibit alterations in disulfide-bonded K14 species and a barrier defect secondary to enhanced proliferation, faster transit time and altered differentiation in epidermis.	Disulfides	131-140	keratin 14	Mus musculus	148-151
8902616-1	1996	We previously reported that protein disulfide isomerase (PDI) can dissociate the glutathione molecule in vitro from the mutant human lysozyme (hLZM) C77A-a, which is modified with glutathione at Cys95; however, it seems structurally difficult for PDI to attack either the disulfide bond or the side chain of the cysteine residue of a mixed disulfide.	Disulfides	36-45	prolyl 4-hydroxylase subunit beta	Homo sapiens	247-250
8902616-1	1996	We previously reported that protein disulfide isomerase (PDI) can dissociate the glutathione molecule in vitro from the mutant human lysozyme (hLZM) C77A-a, which is modified with glutathione at Cys95; however, it seems structurally difficult for PDI to attack either the disulfide bond or the side chain of the cysteine residue of a mixed disulfide.	Disulfides	272-281	prolyl 4-hydroxylase subunit beta	Homo sapiens	28-55
32260357-3	2020	As a hallmark, TFF1 contains seven cysteine residues with three disulfide bonds stabilizing the conserved TFF domain.	Disulfides	64-73	trefoil factor 1	Mus musculus	15-19
8902616-1	1996	We previously reported that protein disulfide isomerase (PDI) can dissociate the glutathione molecule in vitro from the mutant human lysozyme (hLZM) C77A-a, which is modified with glutathione at Cys95; however, it seems structurally difficult for PDI to attack either the disulfide bond or the side chain of the cysteine residue of a mixed disulfide.	Disulfides	272-281	prolyl 4-hydroxylase subunit beta	Homo sapiens	57-60
32260401-0	2020	Molecular Dynamics Simulation and Kinetic Study of Fluoride Binding to V21C/V66C Myoglobin with a Cytoglobin-like Disulfide Bond.	Disulfides	114-123	myoglobin	Homo sapiens	81-90
8902616-4	1996	For all of the modifications we tested, a negative correlation was found between the initial rate and the acceleration ratio of the reductive cleavage of mixed disulfides with PDI.	Disulfides	160-170	prolyl 4-hydroxylase subunit beta	Homo sapiens	176-179
32260401-2	2020	In the absence of structural evidence for cytoglobin (Cgb) with an intramolecular disulfide bond, we recently designed a de novo disulfide bond in myoglobin (Mb) based on structural alignment (i.e., V21C/V66C Mb double mutant).	Disulfides	129-138	myoglobin	Homo sapiens	147-156
8892059-3	1996	In contrast to other subfamily members which fold unimolecularly into a single helical bundle, IL-5 forms a pair of helical bundles by the interdigitation of two identical monomers covalently linked by a pair of intermolecular disulfide bonds.	Disulfides	227-236	interleukin 5	Homo sapiens	95-99
8892059-8	1996	Fluorescent labeling studies further revealed that the cysteines of mono5 contained free sulfhydryl groups, thereby demonstrating that the role of the disulfide bonds of IL-5 is the structural maintenance of other functional domains.	Disulfides	151-160	interleukin 5	Homo sapiens	170-174
32018094-3	2020	We present bis(vinylsulfonyl)piperazines (BVP) as efficient linkers to selectively re-bridge disulfides at the antigen-binding fragment (Fab) regions and produce highly homogeneous conjugates with a loading of two drugs without disulfide scrambling.	Disulfides	93-103	FA complementation group B	Homo sapiens	137-140
32018094-3	2020	We present bis(vinylsulfonyl)piperazines (BVP) as efficient linkers to selectively re-bridge disulfides at the antigen-binding fragment (Fab) regions and produce highly homogeneous conjugates with a loading of two drugs without disulfide scrambling.	Disulfides	93-102	FA complementation group B	Homo sapiens	137-140
32065582-0	2020	EDEM2 stably disulfide-bonded to TXNDC11 catalyzes the first mannose trimming step in mammalian glycoprotein ERAD.	Disulfides	13-22	thioredoxin domain containing 11	Homo sapiens	33-40
32065582-4	2020	Here, we found that EDEM2 was stably disulfide-bonded to TXNDC11, an endoplasmic reticulum protein containing five thioredoxin (Trx)-like domains.	Disulfides	37-46	thioredoxin domain containing 11	Homo sapiens	57-64
8812848-1	1996	Lipoprotein(a) is a macromolecular complex consisting of a low-density lipoprotein-like particle with an additional glycoprotein, apolipoprotein(a) [apo(a)], linked to apolipoprotein B-100 via a disulfide bond.	Disulfides	195-204	lipoprotein(a)	Homo sapiens	130-147
31852864-0	2020	Reinvestigation of Disulfide-bonded Oligomeric Forms of the Unfolded Protein Response Transducer ATF6.	Disulfides	19-28	activating transcription factor 6	Homo sapiens	97-101
31852864-6	2020	Furthermore, ATF6alpha monomer physically associates with another ATF6alpha monomer in the absence of disulfide bonding, which renders two C467 residues in close proximity so that formation of C467-dimer is much easier than that of C618-dimer.	Disulfides	102-111	activating transcription factor 6	Homo sapiens	13-22
31852864-8	2020	Thus, our analysis revealed that all forms of ATF6alpha, namely monomer, C618-dimer and C467-dimer, are activated by single reduction of a disulfide bond in response to ER stress, ensuring the rapidity of ATF6alpha activation.Key words: disulfide-bonded structure, endoplasmic reticulum, membrane-bound transcription factor, non-reducing SDS-PAGE, unfolded protein response.	Disulfides	139-148	activating transcription factor 6	Homo sapiens	46-55
31852864-8	2020	Thus, our analysis revealed that all forms of ATF6alpha, namely monomer, C618-dimer and C467-dimer, are activated by single reduction of a disulfide bond in response to ER stress, ensuring the rapidity of ATF6alpha activation.Key words: disulfide-bonded structure, endoplasmic reticulum, membrane-bound transcription factor, non-reducing SDS-PAGE, unfolded protein response.	Disulfides	139-148	activating transcription factor 6	Homo sapiens	205-214
8812848-1	1996	Lipoprotein(a) is a macromolecular complex consisting of a low-density lipoprotein-like particle with an additional glycoprotein, apolipoprotein(a) [apo(a)], linked to apolipoprotein B-100 via a disulfide bond.	Disulfides	195-204	lipoprotein(a)	Homo sapiens	149-155
31852864-8	2020	Thus, our analysis revealed that all forms of ATF6alpha, namely monomer, C618-dimer and C467-dimer, are activated by single reduction of a disulfide bond in response to ER stress, ensuring the rapidity of ATF6alpha activation.Key words: disulfide-bonded structure, endoplasmic reticulum, membrane-bound transcription factor, non-reducing SDS-PAGE, unfolded protein response.	Disulfides	237-246	activating transcription factor 6	Homo sapiens	46-55
31852864-8	2020	Thus, our analysis revealed that all forms of ATF6alpha, namely monomer, C618-dimer and C467-dimer, are activated by single reduction of a disulfide bond in response to ER stress, ensuring the rapidity of ATF6alpha activation.Key words: disulfide-bonded structure, endoplasmic reticulum, membrane-bound transcription factor, non-reducing SDS-PAGE, unfolded protein response.	Disulfides	237-246	activating transcription factor 6	Homo sapiens	205-214
8781546-11	1996	Selenoprotein P secretion was inhibited by dithiothreitol, suggesting that disulfide bond formation is necessary for secretion of the mature protein.	Disulfides	75-84	selenoprotein P	Rattus norvegicus	0-15
31992623-6	2020	Yeast-two hybrid analysis identified protein disulfide isomerase (PDI) as an Asp14 binding partner.	Disulfides	45-54	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	66-69
8663400-0	1996	Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis.	Disulfides	50-59	myelin basic protein	Homo sapiens	0-23
31963646-0	2020	Disulfide-Linked Peptides for Blocking BTLA/HVEM Binding.	Disulfides	0-9	B and T lymphocyte associated	Homo sapiens	39-43
8663400-6	1996	We introduced cysteines (G69C and S337C) by site-directed mutagenesis into each domain of MBP and found that they formed an interdomain disulfide cross-link that should hold the protein in a closed conformation.	Disulfides	136-145	myelin basic protein	Homo sapiens	90-93
8703948-0	1996	Catalysis of disulfide isomerization in thrombospondin 1 by protein disulfide isomerase.	Disulfides	13-22	prolyl 4-hydroxylase subunit beta	Homo sapiens	60-87
31866066-3	2020	NaV1.5 is distinguished from other sodium channels by a unique glycosyl moiety and loss of disulfide-bonding capability at the NaVbeta subunit-interaction sites.	Disulfides	91-100	sodium voltage-gated channel alpha subunit 5	Homo sapiens	0-6
8703948-3	1996	The recent identification of the enzyme, protein disulfide isomerase, on the platelet surface suggested that protein disulfide isomerase may catalyze disulfide isomerization in platelet thrombospondin 1.	Disulfides	49-58	prolyl 4-hydroxylase subunit beta	Homo sapiens	109-136
8703948-4	1996	Protein disulfide isomerase was found to form disulfide-linked complexes with thrombospondin 1, which is consistent with protein disulfide isomerase-mediated rearrangement of disulfide bonds in thrombospondin 1.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	121-148
8703948-4	1996	Protein disulfide isomerase was found to form disulfide-linked complexes with thrombospondin 1, which is consistent with protein disulfide isomerase-mediated rearrangement of disulfide bonds in thrombospondin 1.	Disulfides	46-55	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
31272904-3	2020	We have previously shown that most serum periostin exists in the oligomeric form by intermolecular disulfide bonds.	Disulfides	99-108	periostin	Homo sapiens	41-50
8703948-4	1996	Protein disulfide isomerase was found to form disulfide-linked complexes with thrombospondin 1, which is consistent with protein disulfide isomerase-mediated rearrangement of disulfide bonds in thrombospondin 1.	Disulfides	46-55	prolyl 4-hydroxylase subunit beta	Homo sapiens	121-148
8703948-7	1996	The rate of protein disulfide isomerase-catalyzed disulfide interchange in thrombospondin 1 increased linearly with protein disulfide isomerase concentration and the K(m) for reduced glutathione was 0.4 +/- 0.2 mM.	Disulfides	20-29	prolyl 4-hydroxylase subunit beta	Homo sapiens	116-143
8755505-0	1996	Intermolecular disulfide bonds stabilize VirB7 homodimers and VirB7/VirB9 heterodimers during biogenesis of the Agrobacterium tumefaciens T-complex transport apparatus.	Disulfides	15-24	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	41-46
31124420-5	2020	Thioredoxin and glutathione systems are two main cellular disulfide reductase systems maintaining cellular ROS level.	Disulfides	58-67	thioredoxin	Homo sapiens	0-11
8755505-0	1996	Intermolecular disulfide bonds stabilize VirB7 homodimers and VirB7/VirB9 heterodimers during biogenesis of the Agrobacterium tumefaciens T-complex transport apparatus.	Disulfides	15-24	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	62-67
8755505-0	1996	Intermolecular disulfide bonds stabilize VirB7 homodimers and VirB7/VirB9 heterodimers during biogenesis of the Agrobacterium tumefaciens T-complex transport apparatus.	Disulfides	15-24	type IV secretion system protein VirB9	Agrobacterium tumefaciens	68-73
8755505-2	1996	Here, we report that stabilization of VirB7 itself is correlated with its ability to form disulfide cross-linked homodimers via a reactive Cys-24 residue.	Disulfides	90-99	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	38-43
31727737-0	2019	The impact of thioredoxin reduction of allosteric disulfide bonds on the therapeutic potential of monoclonal antibodies.	Disulfides	50-59	thioredoxin	Homo sapiens	14-25
8755505-5	1996	We further report that VirB7-dependent stabilization of VirB9 is correlated with the ability of these two proteins to dimerize via formation of a disulfide bridge between reactive Cys-24 and Cys-262 residues, respectively.	Disulfides	146-155	type IV secretion system lipoprotein VirB7	Agrobacterium tumefaciens	23-28
31727737-3	2019	Increased levels of oxidative stress associated with several diseases are counteracted by the activities of various oxidoreductase enzymes, such as thioredoxin (Trx), which also reduces allosteric disulfide bonds in proteins, including mAbs.	Disulfides	197-206	thioredoxin	Homo sapiens	148-159
31727737-3	2019	Increased levels of oxidative stress associated with several diseases are counteracted by the activities of various oxidoreductase enzymes, such as thioredoxin (Trx), which also reduces allosteric disulfide bonds in proteins, including mAbs.	Disulfides	197-206	thioredoxin	Homo sapiens	161-164
31727737-5	2019	We found that Trx reduces the interchain disulfide bonds of the mAbs, after which they remain intact but have altered function.	Disulfides	41-50	thioredoxin	Homo sapiens	14-17
31727737-9	2019	We also confirmed that without alkylation, Trx-reduced interchain disulfide bonds reoxidize, and ADCC activity is restored.	Disulfides	66-75	thioredoxin	Homo sapiens	43-46
31839995-5	2019	At the protein level, DDAs alter DR5 disulfide bonding to increase steady-state DR5 levels and oligomerization, leading to downstream caspase 8 and 3 activation.	Disulfides	37-46	TNF receptor superfamily member 10b	Homo sapiens	33-36
31839995-5	2019	At the protein level, DDAs alter DR5 disulfide bonding to increase steady-state DR5 levels and oligomerization, leading to downstream caspase 8 and 3 activation.	Disulfides	37-46	TNF receptor superfamily member 10b	Homo sapiens	80-83
8755505-5	1996	We further report that VirB7-dependent stabilization of VirB9 is correlated with the ability of these two proteins to dimerize via formation of a disulfide bridge between reactive Cys-24 and Cys-262 residues, respectively.	Disulfides	146-155	type IV secretion system protein VirB9	Agrobacterium tumefaciens	56-61
8663221-8	1996	In the absence of either PS or Ca2+, the plasmin-mediated fragmentation of FXaalpha was altered to include a FXabeta-like molecule and a species (40 kDa) with intact beta-heavy chain disulfide linked to a COOH-terminal fragment of the light chain starting at Tyr44.	Disulfides	183-192	plasminogen	Homo sapiens	41-48
31754768-3	2019	Comparison between normal and SERS spectra of ATP isomers supports the fact that additional disulfide- or hydrogen-bonding interactions are established in para-ATP solid crystal, but neither of ortho- nor meta-isomers.	Disulfides	92-101	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	30-34
28347082-2	2015	In this study, a GST inhibitor, ethacrynic acid (ECA), was designed to be coupled with methoxy poly(ethylene glycol)-poly(lactide) (MPEG-PLA) by disulfide bonds to prepare methoxy poly(ethylene glycol)-poly(lactide)-disulphide bond-mthacrynic acid (MPEG-PLA-SS-ECA) as a carrier material of the nanoparticles.	Disulfides	145-154	glutathione S-transferase kappa 1	Homo sapiens	17-20
8763963-1	1996	It has previously been shown that functional expression of CcrA, a metallo-beta-lactamase from Bacteroides fragilis, in Escherichia coli requires a mutation in either dsbA or dsbB, components of a periplasmic disulfide bond-catalyzing system.	Disulfides	209-218	cfiA	Bacteroides fragilis	59-63
26629401-7	2015	Over and under expression of Adrx in vitro enhances and reduces, respectively, the secretion of the disulfide-bonded proteins including adiponectin and collagen isoforms.	Disulfides	100-109	adiponectin, C1Q and collagen domain containing	Mus musculus	136-147
31393047-3	2019	OBJECTIVE: The purpose of the present study is to obtain direct evidence for ADAMTS13 to engage in thiol/disulfide exchange reactions.	Disulfides	105-114	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	77-85
31393047-10	2019	This suggests functionally relevant disulfide plasticity in ADAMTS13.	Disulfides	36-45	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	60-68
8763963-3	1996	This finding supports the hypothesis that DsbA creates aberrant disulfide bonds involving the Cys residues of CcrA.	Disulfides	64-73	cfiA	Bacteroides fragilis	110-114
31479228-4	2019	Here we present an NMR conformational characterization of p15PAF monoubiquitinated at both K15 and K24 via a disulfide bridge mimicking the isopeptide bond.	Disulfides	109-118	PCNA clamp associated factor	Homo sapiens	58-64
26187352-0	2015	Engineering of a disulfide loop instead of a Zn binding loop restores the anti-proliferative, anti-angiogenic and anti-tumor activities of the N-terminal fragment of endostatin: Mechanistic and therapeutic insights.	Disulfides	17-26	collagen type XVIII alpha 1 chain	Homo sapiens	166-176
8682311-1	1996	The Drosophila melanogaster try29F gene encodes a protein that shares all known features of serine proteases, like residues known to be involved in substrate specificity, catalysis and disulfide bond formation.	Disulfides	185-194	Trypsin 29F	Drosophila melanogaster	28-34
26085103-6	2015	In addition, a ternary complex consisting of Erv1, Mia40, and substrate, linked by disulfide bonds, was not detected in vitro.	Disulfides	83-92	growth factor, augmenter of liver regeneration	Homo sapiens	45-49
8670797-4	1996	If HA"s binding to CNX and CRT was inhibited using a glucosidase inhibitor, castanospermine (CST), the rate of disulfide formation and oligomerization was doubled but the overall efficiency of maturation of HA decreased due to aggregation and degradation.	Disulfides	111-120	calreticulin	Canis lupus familiaris	27-30
26172215-1	2015	The human CD99 protein is a 32-kDa type I transmembrane glycoprotein, while CD98 is a disulfide-linked 125-kDa heterodimeric type II transmembrane glycoprotein.	Disulfides	86-95	solute carrier family 3 member 2	Homo sapiens	76-80
31601022-11	2019	Finally, our sequence analysis of the N-terminal end of N-BChE revealed evolutionarily conserved amino acid residues that can be involved in disulfide bond formation and anchoring of N-BChE in the cell membrane.	Disulfides	141-150	butyrylcholinesterase	Homo sapiens	58-62
31418171-2	2019	HMGB1 has several redox states: reduced HMGB1 recruits inflammatory cells to injured tissues forming a heterocomplex with CXCL12 and signaling via its receptor CXCR4; disulfide-containing HMGB1 binds to TLR4 and promotes inflammatory responses.	Disulfides	167-176	toll like receptor 4	Homo sapiens	203-207
31085544-6	2019	For a diverse set of drug-linker conjugates, we determined that TRX in the presence of TRX-reductase and NADPH generated the cleaved products that are consistent with catalytic disulfide cleavage and linker immolation.	Disulfides	177-186	thioredoxin	Homo sapiens	64-67
8668334-5	1996	The DeltaV-TCRbeta chain appears at the cell surface as a disulfide-linked DeltaV-TCRbeta/pTalpha dimer in association with CD3gamma and -episilon, but not with CD3delta.	Disulfides	58-67	pre T cell antigen receptor alpha	Mus musculus	90-97
31085544-6	2019	For a diverse set of drug-linker conjugates, we determined that TRX in the presence of TRX-reductase and NADPH generated the cleaved products that are consistent with catalytic disulfide cleavage and linker immolation.	Disulfides	177-186	thioredoxin	Homo sapiens	87-90
31085544-8	2019	Collectively, these in vitro experiments demonstrate that TRX as well as GRX can catalyze the cleavage of disulfide bonds in both small molecules and linkers of ADCs.	Disulfides	106-115	thioredoxin	Homo sapiens	58-61
26523134-4	2015	The inclusion of thiols from a pair of cysteine residues in the ELP sequence allows disulfide bond formation upon exposure to UV light, leading to the formation of a highly elastic hydrogel.	Disulfides	84-93	diazepam binding inhibitor-like 5	Rattus norvegicus	64-67
26075496-10	2015	This highly conserved pseudogene-derived variant in the TNX fibrinogen-like domain is predicted to be deleterious and disulfide bonded, results in reduced dermal elastin and fibrillin-1 staining and altered TGF-beta1 binding, and represents a novel TNXA/TNXB chimera.	Disulfides	118-127	tenascin XB	Homo sapiens	56-59
26075496-10	2015	This highly conserved pseudogene-derived variant in the TNX fibrinogen-like domain is predicted to be deleterious and disulfide bonded, results in reduced dermal elastin and fibrillin-1 staining and altered TGF-beta1 binding, and represents a novel TNXA/TNXB chimera.	Disulfides	118-127	fibrillin 1	Homo sapiens	174-185
26075496-10	2015	This highly conserved pseudogene-derived variant in the TNX fibrinogen-like domain is predicted to be deleterious and disulfide bonded, results in reduced dermal elastin and fibrillin-1 staining and altered TGF-beta1 binding, and represents a novel TNXA/TNXB chimera.	Disulfides	118-127	tenascin XB	Homo sapiens	254-258
25935706-2	2015	For selective cancer cell targeting, here the coupling of a synthetic cytolysin to the hY1-receptor preferring peptide [F(7),P(34)]-neuropeptide Y (NPY) using a labile disulfide linker is described.	Disulfides	168-177	perforin 1	Homo sapiens	70-79
31349481-3	2019	The primary gatekeeper was achieved by capping beta-CD via a disulfide linkage.	Disulfides	61-70	Rho GTPase activating protein 31	Homo sapiens	52-54
8744943-0	1996	Identification of the cysteine residues involved in the class I disulfide bonds of the human insulin receptor: properties of insulin receptor monomers.	Disulfides	64-73	insulin receptor	Homo sapiens	93-109
31436417-7	2019	The on-rate for hydrogen disulfide binding to ferric IDO1 was found to be >106 M-1 s-1 at pH 7 using stopped-flow spectrometry.	Disulfides	16-34	indoleamine 2,3-dioxygenase 1	Homo sapiens	53-57
25957407-4	2015	But the sequences and innate properties of ABri and Abeta are quite different, notably ABri contains two cysteine residues that can form disulfide bonds.	Disulfides	137-146	integral membrane protein 2B	Homo sapiens	43-47
25957407-4	2015	But the sequences and innate properties of ABri and Abeta are quite different, notably ABri contains two cysteine residues that can form disulfide bonds.	Disulfides	137-146	integral membrane protein 2B	Homo sapiens	87-91
25957407-8	2015	ABri was more prone to form inter-molecular disulfide bonds than Bri and the formation of covalently stabilized ABri oligomers was associated with toxicity.	Disulfides	44-53	integral membrane protein 2B	Homo sapiens	0-4
25957407-8	2015	ABri was more prone to form inter-molecular disulfide bonds than Bri and the formation of covalently stabilized ABri oligomers was associated with toxicity.	Disulfides	44-53	integral membrane protein 2B	Homo sapiens	1-4
25957407-9	2015	These results suggest that extension of the C-terminal of Bri causes a shift in the type of disulfide bonds formed and that structures built from covalently cross-linked oligomers can interact with neurons and compromise their function and viability.	Disulfides	92-101	integral membrane protein 2B	Homo sapiens	58-61
8744943-1	1996	The cysteine residues involved in the class I disulfide bonds between the alpha subunits in the (alpha beta)2 dimer of the human insulin receptor have been identified by labeling with N-ethylmaleimide and by site-directed mutagenesis.	Disulfides	46-55	insulin receptor	Homo sapiens	129-145
8613985-1	1996	The solution structure and the disulfide pairings of a 36-residue proteinase inhibitor isolated from the insect Locusta migratoria have been determined using NMR spectroscopy and simulated annealing calculations.	Disulfides	31-40	endogenous retrovirus group K member 18	Homo sapiens	66-76
25926547-3	2015	Thioredoxin system not only plays a crucial role as thiol/disulfide redox controller, it is also essential for certain organisms as the only system ensuring the redox homeostasis.	Disulfides	58-67	thioredoxin	Homo sapiens	0-11
25956655-5	2015	It is composed by two main proteins: Mia40 is the oxidoreductase that catalyzes the formation of the disulfide bonds in the substrate, while ALR reoxidizes Mia40 after the import.	Disulfides	101-110	growth factor, augmenter of liver regeneration	Homo sapiens	141-144
25944298-5	2015	In this study, three gp120 (strain JR-FL) variants were constructed, in which deletions of single outer-domain disulfide bonds were expected to introduce local conformational flexibility and promote presentation of additional CD4(+) T-cell epitopes.	Disulfides	111-120	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	21-26
25944298-6	2015	Following mucosal immunization of C57BL/6 mice with wild-type or variant gp120 lacking the V3-flanking disulfide bond, the typical pattern of dominant epitopes was observed, suggesting that the disulfide bond posed no barrier to antigen presentation.	Disulfides	103-112	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	73-78
25944298-6	2015	Following mucosal immunization of C57BL/6 mice with wild-type or variant gp120 lacking the V3-flanking disulfide bond, the typical pattern of dominant epitopes was observed, suggesting that the disulfide bond posed no barrier to antigen presentation.	Disulfides	194-203	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	73-78
33654871-10	2019	However, conjugation of a Fab with a dye using the chemical cross-linking agent SMCC (succinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate) requires reduction of the interchain disulfide bond within the Fab fragment, which can decrease the structural stability of the Fab and weaken its antigen-binding capability.	Disulfides	184-193	FA complementation group B	Homo sapiens	26-29
33654871-10	2019	However, conjugation of a Fab with a dye using the chemical cross-linking agent SMCC (succinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate) requires reduction of the interchain disulfide bond within the Fab fragment, which can decrease the structural stability of the Fab and weaken its antigen-binding capability.	Disulfides	184-193	FA complementation group B	Homo sapiens	210-213
33654871-10	2019	However, conjugation of a Fab with a dye using the chemical cross-linking agent SMCC (succinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate) requires reduction of the interchain disulfide bond within the Fab fragment, which can decrease the structural stability of the Fab and weaken its antigen-binding capability.	Disulfides	184-193	FA complementation group B	Homo sapiens	210-213
8613985-6	1996	The proteinase binding loop is located in the carboxy-terminal part of the molecule, between two cysteine residues involved in disulfide bridges.	Disulfides	127-136	endogenous retrovirus group K member 18	Homo sapiens	4-14
31325422-5	2019	In this study, we aimed to dimerize the truncated BChE mutant protein expressed in a prokaryotic system (E. coli) in order to further improve its thermal stability by introducing a pair of cross-subunit disulfide bonds to the BChE-M47 structure.	Disulfides	203-212	butyrylcholinesterase	Homo sapiens	50-54
25573276-4	2015	A structure-based sequence alignment predicts that the C-terminal domain 15 contains three out of the four conserved residues identified as essential for carbohydrate recognition by domains 3, 5 and 9 of the CI-MPR, but lacks two cysteine residues that are predicted to form a disulfide bond.	Disulfides	277-286	insulin like growth factor 2 receptor	Homo sapiens	208-214
8621668-0	1996	Porcine submaxillary mucin forms disulfide-bonded dimers between its carboxyl-terminal domains.	Disulfides	33-42	LOC100508689	Homo sapiens	21-26
25873657-1	2015	In plants, the presence of thioredoxin (Trx), peroxiredoxin (Prx), and sulfiredoxin (Srx) has been reported as a component of a redox system involved in the control of dithiol-disulfide exchanges of target proteins, which modulate redox signalling during development and stress adaptation.	Disulfides	176-185	thioredoxin	Homo sapiens	27-38
25873657-1	2015	In plants, the presence of thioredoxin (Trx), peroxiredoxin (Prx), and sulfiredoxin (Srx) has been reported as a component of a redox system involved in the control of dithiol-disulfide exchanges of target proteins, which modulate redox signalling during development and stress adaptation.	Disulfides	176-185	thioredoxin	Homo sapiens	40-43
31325422-5	2019	In this study, we aimed to dimerize the truncated BChE mutant protein expressed in a prokaryotic system (E. coli) in order to further improve its thermal stability by introducing a pair of cross-subunit disulfide bonds to the BChE-M47 structure.	Disulfides	203-212	butyrylcholinesterase	Homo sapiens	226-230
31325422-6	2019	Specifically, the E377C/A516C mutations were designed and introduced to BChE-M47, and the obtained new protein entity, denoted as BChE-M48, with a pair of cross-subunit disulfide bonds indeed exists as a dimer with significantly improved thermostability and unaltered catalytic activity and reactivity compared to BChE-M47.	Disulfides	169-178	butyrylcholinesterase	Homo sapiens	72-76
31325422-6	2019	Specifically, the E377C/A516C mutations were designed and introduced to BChE-M47, and the obtained new protein entity, denoted as BChE-M48, with a pair of cross-subunit disulfide bonds indeed exists as a dimer with significantly improved thermostability and unaltered catalytic activity and reactivity compared to BChE-M47.	Disulfides	169-178	butyrylcholinesterase	Homo sapiens	130-134
31325422-6	2019	Specifically, the E377C/A516C mutations were designed and introduced to BChE-M47, and the obtained new protein entity, denoted as BChE-M48, with a pair of cross-subunit disulfide bonds indeed exists as a dimer with significantly improved thermostability and unaltered catalytic activity and reactivity compared to BChE-M47.	Disulfides	169-178	butyrylcholinesterase	Homo sapiens	130-134
25637034-5	2015	Formation of oxidized PTEN was abolished when the active site Cys(124) or nearby Cys(71) was replaced with Ser suggesting that Cys(124) and Cys(71) are involved in the formation of an intramolecular disulfide bond.	Disulfides	199-208	phosphatase and tensin homolog	Homo sapiens	22-26
8621668-1	1996	COS-7 cells transfected with three different expression vectors encoding the 240-amino acid residue, disulfide-rich domain at the carboxyl terminus of porcine submaxillary mucin have been used to determine the possible function of the domain in forming higher oligomers of the mucin polypeptide chain.	Disulfides	101-110	LOC100508689	Homo sapiens	172-177
8612734-5	1996	Improper disulfide bond formation and/or lack of post-translational events in insect cells, may affect the conformation and/or lack of post-translational events in insect cells, may affect the conformation of PR3, precluding its reactivity with sera from WG patients.	Disulfides	9-18	proteinase 3	Homo sapiens	209-212
31044600-6	2019	These residues form a disulfide bond, which likely plays a structural role and influences conformational stability and activity of the Oma1 high-mass complex.	Disulfides	22-31	OMA1 zinc metallopeptidase	Homo sapiens	135-139
31044600-9	2019	Conclusion: Disulfide bonds formed by IMS-exposed residues Cys272 and Cys332 play an important evolutionarily conserved role in the regulation of Oma1 function.	Disulfides	12-21	OMA1 zinc metallopeptidase	Homo sapiens	146-150
25856548-4	2015	We devise a free-energy calculation scheme, which makes use of the Crooks Gaussian intersection method to estimate the redox potential of thiol/disulfide pairs in 12 proteins belonging to the thioredoxin superfamily, namely, thioredoxins, glutaredoxins, and thiol-disulfide oxidoreductases in disulfide bond formation systems.	Disulfides	144-153	thioredoxin	Homo sapiens	192-203
8838095-1	1996	The high-affinity receptor for IgE (Fc epsilon R I) has a tetrameric structure composed of one alpha, one beta and two disulfide-linked gamma subunits (alpha beta gamma 2), of which alpha subunit binds IgE with high affinity and beta, gamma subunits transduce intracellular activation signals.	Disulfides	119-128	Fc epsilon receptor Ia	Homo sapiens	36-50
25856548-4	2015	We devise a free-energy calculation scheme, which makes use of the Crooks Gaussian intersection method to estimate the redox potential of thiol/disulfide pairs in 12 proteins belonging to the thioredoxin superfamily, namely, thioredoxins, glutaredoxins, and thiol-disulfide oxidoreductases in disulfide bond formation systems.	Disulfides	264-273	thioredoxin	Homo sapiens	192-203
25645953-8	2015	N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters.	Disulfides	170-179	CDGSH iron sulfur domain 1	Homo sapiens	109-117
25645953-8	2015	N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters.	Disulfides	170-179	CDGSH iron sulfur domain 1	Homo sapiens	276-284
31391482-5	2019	To create therapeutic proteins derived from a disulfide-rich scaffold, we selected human serine protease inhibitor Kazal type 2 (SPINK2) through a scaffold screening, as a protein scaffold with requirements for therapeutic proteins.	Disulfides	46-55	serine peptidase inhibitor Kazal type 2	Homo sapiens	89-127
31391482-5	2019	To create therapeutic proteins derived from a disulfide-rich scaffold, we selected human serine protease inhibitor Kazal type 2 (SPINK2) through a scaffold screening, as a protein scaffold with requirements for therapeutic proteins.	Disulfides	46-55	serine peptidase inhibitor Kazal type 2	Homo sapiens	129-135
31100280-0	2019	An evolutionary perspective on the first disulfide bond in members of the cholinesterase-carboxylesterase (COesterase) family: Possible outcomes for cholinesterase expression in prokaryotes.	Disulfides	41-50	butyrylcholinesterase	Homo sapiens	74-88
25688043-7	2015	Our data show for the first time that a disulfide bridge between Cys243 and Cys249 on PRK is required to form the PRK-GAPDH-CP12 complex.	Disulfides	40-49	uncharacterized protein	Chlamydomonas reinhardtii	86-89
8727481-1	1996	Previous theoretical analysis of the primary structure of lung surfactant protein SP-B indicates a disulfide-linked, hydrophobic midsequence that forms a hairpin-like motif.	Disulfides	99-108	surfactant protein B	Homo sapiens	82-86
25091901-2	2015	In protein disulfide isomerase-first (PDI-first) pathways of oxidative protein folding, PDI is the immediate oxidant of reduced client proteins and then addresses disulfide mispairings in a second isomerization phase.	Disulfides	11-20	peptidyl arginine deiminase 1	Homo sapiens	38-41
31100280-0	2019	An evolutionary perspective on the first disulfide bond in members of the cholinesterase-carboxylesterase (COesterase) family: Possible outcomes for cholinesterase expression in prokaryotes.	Disulfides	41-50	butyrylcholinesterase	Homo sapiens	149-163
31100280-12	2019	Surprisingly however, crystal structures of the optimized cholinesterase variants expressed in bacteria revealed co-existing formed and unformed states of the first disulfide bond.	Disulfides	165-174	butyrylcholinesterase	Homo sapiens	58-72
25091901-2	2015	In protein disulfide isomerase-first (PDI-first) pathways of oxidative protein folding, PDI is the immediate oxidant of reduced client proteins and then addresses disulfide mispairings in a second isomerization phase.	Disulfides	11-20	peptidyl arginine deiminase 1	Homo sapiens	88-91
8727481-2	1996	Here, we experimentally investigate the secondary structure of the disulfide-stabilized bend region by synthesizing two 12-residue analogs of the SP-B midsequence.	Disulfides	67-76	surfactant protein B	Homo sapiens	146-150
25487639-0	2015	Thioether analogues of disulfide-bridged cyclic peptides targeting death receptor 5: conformational analysis, dimerisation and consequences for receptor activation.	Disulfides	23-32	TNF receptor superfamily member 10b	Homo sapiens	67-83
25487639-2	2015	We report the effect of replacing the disulfide bridge with a lanthionine linkage in a 16-mer cyclic peptide that binds to death receptor 5 (DR5, TRAIL-R2).	Disulfides	38-47	TNF receptor superfamily member 10b	Homo sapiens	123-139
25487639-2	2015	We report the effect of replacing the disulfide bridge with a lanthionine linkage in a 16-mer cyclic peptide that binds to death receptor 5 (DR5, TRAIL-R2).	Disulfides	38-47	TNF receptor superfamily member 10b	Homo sapiens	141-144
25487639-2	2015	We report the effect of replacing the disulfide bridge with a lanthionine linkage in a 16-mer cyclic peptide that binds to death receptor 5 (DR5, TRAIL-R2).	Disulfides	38-47	TNF receptor superfamily member 10b	Homo sapiens	146-154
25487639-3	2015	Upon covalent oligomerisation, the disulfide-bridged peptide has previously shown similar behaviour to that of TNF-related apoptosis inducing ligand (TRAIL), by selectively triggering the DR5 cell death pathway.	Disulfides	35-44	TNF receptor superfamily member 10b	Homo sapiens	188-191
25487639-6	2015	The same holds true for dimeric versions of these peptides: the thioether is able to induce DR5-mediated apoptosis of BJAB lymphoma and tumorigenic BJELR cells, albeit to a slightly lower extent compared to its disulfide homologue.	Disulfides	211-220	TNF receptor superfamily member 10b	Homo sapiens	92-95
25559892-0	2015	MD-2 is required for disulfide HMGB1-dependent TLR4 signaling.	Disulfides	21-30	lymphocyte antigen 96	Mus musculus	0-4
25559892-4	2015	Here we demonstrate that the extracellular TLR4 adaptor, myeloid differentiation factor 2 (MD-2), binds specifically to the cytokine-inducing disulfide isoform of HMGB1, to the exclusion of other isoforms.	Disulfides	142-151	lymphocyte antigen 96	Mus musculus	57-89
25559892-4	2015	Here we demonstrate that the extracellular TLR4 adaptor, myeloid differentiation factor 2 (MD-2), binds specifically to the cytokine-inducing disulfide isoform of HMGB1, to the exclusion of other isoforms.	Disulfides	142-151	lymphocyte antigen 96	Mus musculus	91-95
31055076-3	2019	We developed novel disulfide-crosslinked CLL1-targeting micelles (DC-CTM), which can deliver high concentrations of daunorubicin (DNR) into both bulk leukemia cells and LSCs.	Disulfides	19-28	C-type lectin domain family 12 member A	Homo sapiens	41-45
31177768-0	2019	Fluorophore-Dependent Cleavage of Disulfide Bond Leading to a Highly Selective Fluorescent Probe of Thioredoxin.	Disulfides	34-43	thioredoxin	Homo sapiens	100-111
31177768-5	2019	In addition, our discovery, i.e., the preference reduction of simple disulfide bonds by Trx over glutathione, also advances the development of disulfide cleavage-based probes, prodrugs, and theranostic agents.	Disulfides	69-78	thioredoxin	Homo sapiens	88-91
31177768-5	2019	In addition, our discovery, i.e., the preference reduction of simple disulfide bonds by Trx over glutathione, also advances the development of disulfide cleavage-based probes, prodrugs, and theranostic agents.	Disulfides	143-152	thioredoxin	Homo sapiens	88-91
31209055-8	2019	Outside the membrane this symmetry is broken by the disulfide-bridged dimerization of the extracellular Ig domains of Igalpha and Igbeta.	Disulfides	52-61	chemokine (C-X-C motif) ligand 9	Mus musculus	104-106
31209055-8	2019	Outside the membrane this symmetry is broken by the disulfide-bridged dimerization of the extracellular Ig domains of Igalpha and Igbeta.	Disulfides	52-61	CD79b molecule	Homo sapiens	130-136
31117586-1	2019	Different reactivity of homologous disulfides toward Pd2+ was previously reported: stepwise complexation to Pd2+ for l-cystine and cystamine ligands, while for dl-homocystine and 3,3"-dithiodipropionic acid, disulfide"s disproportionation toward thiolate and sulfinic acid complexes is observed.	Disulfides	35-45	PAF1 homolog, Paf1/RNA polymerase II complex component	Homo sapiens	53-56
25383757-4	2015	The bacteria characteristically have two cysteine residues on the Lon protease (P) domain surface that unusually form a disulfide bond.	Disulfides	120-129	lon peptidase 1, mitochondrial	Homo sapiens	66-69
7489981-1	1995	Human hepatocyte growth factor (hHGF), which is now known to be the same protein as the scatter factor and the tumor cytotoxic factor, is a heterodimeric protein with one heavy chain and one light chain linked together by a disulfide bond, and is thought to be involved in liver regeneration.	Disulfides	224-233	hepatocyte growth factor	Homo sapiens	6-30
25924479-3	2015	Results show that the molecular mass and amino acid sequence were consistent with theory; the disulfide bonds of 4 lots of interferon were Cys1-Cys98/Cys29-Cys138, 1 lot was Cys29-Cys139/Cys86-Cys99; N-terminal "+Met", acetyl N-terminal and Met oxidation were identified in part of the sample.	Disulfides	94-103	cystin 1	Homo sapiens	139-143
31117586-1	2019	Different reactivity of homologous disulfides toward Pd2+ was previously reported: stepwise complexation to Pd2+ for l-cystine and cystamine ligands, while for dl-homocystine and 3,3"-dithiodipropionic acid, disulfide"s disproportionation toward thiolate and sulfinic acid complexes is observed.	Disulfides	35-45	PAF1 homolog, Paf1/RNA polymerase II complex component	Homo sapiens	108-111
31026770-4	2019	The oxidation is catalyzed by peroxiredoxin I (PrxI) and PrxII, which are first oxidized by H2O2 and then transfer their disulfide oxidation state to HMGB1.	Disulfides	121-130	peroxiredoxin 1	Mus musculus	30-45
31026770-4	2019	The oxidation is catalyzed by peroxiredoxin I (PrxI) and PrxII, which are first oxidized by H2O2 and then transfer their disulfide oxidation state to HMGB1.	Disulfides	121-130	peroxiredoxin 1	Mus musculus	47-51
31026770-5	2019	The disulfide form of HMGB1 showed higher affinity for nuclear exportin CRM1 compared with the reduced form.	Disulfides	4-13	exportin 1	Mus musculus	72-76
30853337-9	2019	Although the disulfide-bonded form of homocysteine (HSSH) modified PTP1B to form an inactive S-homocysteinylated PTP1B, HcySH-induced increase in the activities of cellular thioredoxin and thioredoxin reductase, components of thioredoxin system, could recover active PTP1B from S-homocysteinylated PTP1B.	Disulfides	13-22	thioredoxin	Homo sapiens	173-184
30853337-9	2019	Although the disulfide-bonded form of homocysteine (HSSH) modified PTP1B to form an inactive S-homocysteinylated PTP1B, HcySH-induced increase in the activities of cellular thioredoxin and thioredoxin reductase, components of thioredoxin system, could recover active PTP1B from S-homocysteinylated PTP1B.	Disulfides	13-22	thioredoxin	Homo sapiens	189-200
30853337-9	2019	Although the disulfide-bonded form of homocysteine (HSSH) modified PTP1B to form an inactive S-homocysteinylated PTP1B, HcySH-induced increase in the activities of cellular thioredoxin and thioredoxin reductase, components of thioredoxin system, could recover active PTP1B from S-homocysteinylated PTP1B.	Disulfides	13-22	thioredoxin	Homo sapiens	189-200
25264323-1	2014	Human IgG2 consists of disulfide-mediated structural isoforms, classified by the number of Fab arms disulfide-linked to the heavy chain hinge.	Disulfides	100-109	FA complementation group B	Homo sapiens	91-94
7489981-1	1995	Human hepatocyte growth factor (hHGF), which is now known to be the same protein as the scatter factor and the tumor cytotoxic factor, is a heterodimeric protein with one heavy chain and one light chain linked together by a disulfide bond, and is thought to be involved in liver regeneration.	Disulfides	224-233	hepatocyte growth factor	Homo sapiens	32-36
7499374-8	1995	It was found that NAD+ binding influences the interaction between the flavin and the reduced disulfide in the 2"-F-arabino-FAD-lipoamide dehydrogenase, presumably by altering the relative oxidation-reduction potentials.	Disulfides	93-102	dihydrolipoamide dehydrogenase	Homo sapiens	127-150
31177460-0	2019	Effect of Interchain Disulfide Crosslinking in the Tropomyosin Molecule on Actin-Myosin Interaction in the Atrial Myocardium.	Disulfides	21-30	myosin heavy chain 14	Homo sapiens	81-87
30942563-3	2019	The molecular structure of the complete extracellular domain (ECD) of DSC2 was recently described, revealing three disulfide bridges, four N-glycosylation sites, and four O-mannosylation sites.	Disulfides	115-124	desmocollin 2	Homo sapiens	70-74
30942563-5	2019	Here, we generated a set of DSC2 mutants, in which we systematically exchanged all N-glycosylation sites, O-mannosylation sites, and disulfide bridges within the ECD and investigated the resulting subcellular localization by confocal laser scanning microscopy.	Disulfides	133-142	desmocollin 2	Homo sapiens	28-32
25274631-4	2014	The dual role of TlpA was documented best with high-resolution crystal structures of the kinetically trapped TlpA-ScoI and TlpA-CoxB mixed disulfide intermediates.	Disulfides	139-148	cysteine rich protein 3	Homo sapiens	17-21
25274631-7	2014	The reduction of CoxB by TlpA via disulfide exchange proved to be very fast, with a rate constant of 8.4 x 10(4) M(-1) s(-1) that is similar to that found previously for ScoI reduction.	Disulfides	34-43	cysteine rich protein 3	Homo sapiens	25-29
32261800-9	2014	Cell viability assay results showed that OEI-SeSex has a similar cell viability profile as disulfide bond conjugated OEI800 (OEI-SSx), which is much less toxic than PEI25k.	Disulfides	91-100	SSX family member 2B	Homo sapiens	129-132
15251573-1	1995	The major apoproteins of Lp(a)--apo(a) and apo B-100--are linked by only one intermolecular disulfide bond.	Disulfides	92-101	lipoprotein(a)	Homo sapiens	25-30
25179300-4	2014	Recombinant preparation of the biologically active LIF protein is quite difficult due to its hydrophobic nature and three disulfide bonds.	Disulfides	122-131	LIF interleukin 6 family cytokine	Homo sapiens	51-54
30668797-4	2019	Here we tested whether the enzymes Erv1 and Mia40 of the yeast mitochondrial disulfide relay could be functionally replaced by corresponding components of other compartments.	Disulfides	77-86	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	35-39
30769283-6	2019	Here, we stapled the ends of this motif with a designed disulfide bond and evaluated its impact on the conformation, aggregation and toxicity of alpha-syn in different environments.	Disulfides	56-65	synuclein alpha	Homo sapiens	145-154
7577954-3	1995	Protein disulfide isomerase (PDI) facilitates the oxidation of a kinetically trapped state of RTEM-1 beta-lactamase in which two cysteines that form the single disulfide bond in the native protein are buried and approximately 500-fold less reactive than exposed cysteines.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
30670593-4	2019	Ficolin-3, the most abundant lectin pathway initiator in humans, circulates as disulfide-linked multimers of a monomer.	Disulfides	79-88	ficolin 3	Homo sapiens	0-9
30670593-5	2019	ERp57 attenuated ficolin-3 ligand recognition and complement activation by cleaving intermolecular disulfide bonds in large ficolin-3 multimers, thereby reducing multimer size and ligand-binding affinity.	Disulfides	99-108	ficolin 3	Homo sapiens	17-26
30670593-5	2019	ERp57 attenuated ficolin-3 ligand recognition and complement activation by cleaving intermolecular disulfide bonds in large ficolin-3 multimers, thereby reducing multimer size and ligand-binding affinity.	Disulfides	99-108	ficolin 3	Homo sapiens	124-133
30670593-6	2019	We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57.	Disulfides	27-36	ficolin 3	Homo sapiens	56-65
30670593-6	2019	We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57.	Disulfides	27-36	ficolin 3	Homo sapiens	176-185
30670593-6	2019	We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57.	Disulfides	27-36	ficolin 3	Homo sapiens	176-185
30670593-6	2019	We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57.	Disulfides	84-93	ficolin 3	Homo sapiens	176-185
30670593-6	2019	We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57.	Disulfides	84-93	ficolin 3	Homo sapiens	176-185
25242227-4	2014	The Thioredoxin Reductase-Thioredoxin system cleaves the interchain disulfide, and its inhibition prevents neurotoxicity, and may provide novel strategies for chemoprophylaxis and therapy.	Disulfides	68-77	peroxiredoxin 5	Homo sapiens	4-25
25242227-4	2014	The Thioredoxin Reductase-Thioredoxin system cleaves the interchain disulfide, and its inhibition prevents neurotoxicity, and may provide novel strategies for chemoprophylaxis and therapy.	Disulfides	68-77	thioredoxin	Homo sapiens	4-15
30670593-6	2019	We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57.	Disulfides	84-93	ficolin 3	Homo sapiens	176-185
7592581-1	1995	In the formation of the lipoprotein(a) (Lp(a)) particle, apolipoprotein(a) (apo(a)) and apolipoprotein B (apoB) are covalently linked via a disulfide bond in both humans and human-apo(a)/apoB transgenic mice.	Disulfides	140-149	lipoprotein(a)	Homo sapiens	24-38
30670593-6	2019	We used MS to identify the disulfide-bonding pattern in ficolin-3 multimers and the disulfide bonds targeted by ERp57 and found that Cys6 and Cys23 in the N-terminal region of ficolin-3 form the intermolecular disulfide bonds in ficolin-3 multimers that are reduced by ERp57.	Disulfides	84-93	ficolin 3	Homo sapiens	176-185
25106706-14	2014	Reactive cysteines within the structure of HSP90 are known to modulate its ATPase-dependent chaperone activity through disulfide formation and S-nitrosylation.	Disulfides	119-128	heat shock protein 90 alpha family class A member 1	Homo sapiens	43-48
7592581-1	1995	In the formation of the lipoprotein(a) (Lp(a)) particle, apolipoprotein(a) (apo(a)) and apolipoprotein B (apoB) are covalently linked via a disulfide bond in both humans and human-apo(a)/apoB transgenic mice.	Disulfides	140-149	lipoprotein(a)	Homo sapiens	40-45
7592581-1	1995	In the formation of the lipoprotein(a) (Lp(a)) particle, apolipoprotein(a) (apo(a)) and apolipoprotein B (apoB) are covalently linked via a disulfide bond in both humans and human-apo(a)/apoB transgenic mice.	Disulfides	140-149	lipoprotein(a)	Homo sapiens	57-74
25125675-1	2014	Endoglin, a 180-kDa disulfide-linked homodimeric transmembrane receptor protein mostly expressed in tumor-associated endothelial cells, is an endogenous binding partner of GAIP-interacting protein, C terminus (GIPC).	Disulfides	20-29	endoglin	Homo sapiens	0-8
7592581-1	1995	In the formation of the lipoprotein(a) (Lp(a)) particle, apolipoprotein(a) (apo(a)) and apolipoprotein B (apoB) are covalently linked via a disulfide bond in both humans and human-apo(a)/apoB transgenic mice.	Disulfides	140-149	lipoprotein(a)	Homo sapiens	76-82
25125675-1	2014	Endoglin, a 180-kDa disulfide-linked homodimeric transmembrane receptor protein mostly expressed in tumor-associated endothelial cells, is an endogenous binding partner of GAIP-interacting protein, C terminus (GIPC).	Disulfides	20-29	GIPC PDZ domain containing family member 1	Homo sapiens	172-208
25125675-1	2014	Endoglin, a 180-kDa disulfide-linked homodimeric transmembrane receptor protein mostly expressed in tumor-associated endothelial cells, is an endogenous binding partner of GAIP-interacting protein, C terminus (GIPC).	Disulfides	20-29	GIPC PDZ domain containing family member 1	Homo sapiens	210-214
25131860-2	2014	The function of human epididymis protein 4 (HE4), a 124-amino acid long polypeptide that has two whey acidic protein four-disulfide core (WFDC) domains, is not well studied.	Disulfides	122-131	WAP four-disulfide core domain 2	Homo sapiens	44-47
30718304-9	2019	On the basis of these results, I propose that the DeltacysL mutation causes phosphoadenosine phosphosulfate reductase to consume large amounts of reduced thioredoxin, inducing disulfide stress and activating Spx.	Disulfides	176-185	thioredoxin	Homo sapiens	154-165
30739449-5	2019	The decrease of hydrogen peroxide and increase of free thiol groups in wCat1-treated dough suggest that the decomposition of hydrogen peroxide by wCat1 likely promotes disulfide-bond formation and thus the cross-linking of dough proteins.	Disulfides	168-177	catalase-1	Triticum aestivum	71-76
30739449-5	2019	The decrease of hydrogen peroxide and increase of free thiol groups in wCat1-treated dough suggest that the decomposition of hydrogen peroxide by wCat1 likely promotes disulfide-bond formation and thus the cross-linking of dough proteins.	Disulfides	168-177	catalase-1	Triticum aestivum	146-151
25259790-6	2014	p35 and p40 but not p35 and EBI3 form an inter-chain disulfide bridge.	Disulfides	53-62	interleukin 12a	Mus musculus	0-3
7592581-1	1995	In the formation of the lipoprotein(a) (Lp(a)) particle, apolipoprotein(a) (apo(a)) and apolipoprotein B (apoB) are covalently linked via a disulfide bond in both humans and human-apo(a)/apoB transgenic mice.	Disulfides	140-149	lipoprotein(a)	Homo sapiens	180-186
7547904-6	1995	The differences in activity between PDI and its thioredoxin-like domains suggest that other features of the PDI molecule are also required for its complete range of thiol-disulfide exchange activities.	Disulfides	171-180	prolyl 4-hydroxylase subunit beta	Homo sapiens	36-39
24847059-2	2014	The ability of GPIHBP1 to bind LPL depends on the Ly6 domain, a three-fingered structure containing 10 cysteines and a conserved pattern of disulfide bond formation.	Disulfides	140-149	lipoprotein lipase	Homo sapiens	31-34
24846539-5	2014	The specificity of the autolytic cleavage reveals a strong preference for cysteine in the P1 position of HtrA1, explaining the lack of autolysis prior to disulfide reduction.	Disulfides	154-163	HtrA serine peptidase 1	Homo sapiens	105-110
24846539-6	2014	Significantly, the disulfides were reduced by thioredoxin, suggesting that autolysis of HtrA1 in vivo is linked to the endogenous redox balance and that the N-terminal domain acts as a redox-sensing switch.	Disulfides	19-29	thioredoxin	Homo sapiens	46-57
30742135-6	2019	Impeding intra-endosomal disulfide reduction by knocking down TRX-1 protects nematodes from infection by Corynebacterium diphtheriae, revealing the importance of this minor pool of endosomal TRX-1.	Disulfides	25-34	thioredoxin	Homo sapiens	62-67
30742135-6	2019	Impeding intra-endosomal disulfide reduction by knocking down TRX-1 protects nematodes from infection by Corynebacterium diphtheriae, revealing the importance of this minor pool of endosomal TRX-1.	Disulfides	25-34	thioredoxin	Homo sapiens	191-196
30742135-7	2019	TRX-1 also mediates endosomal disulfide reduction in human cells.	Disulfides	30-39	thioredoxin	Homo sapiens	0-5
24846539-6	2014	Significantly, the disulfides were reduced by thioredoxin, suggesting that autolysis of HtrA1 in vivo is linked to the endogenous redox balance and that the N-terminal domain acts as a redox-sensing switch.	Disulfides	19-29	HtrA serine peptidase 1	Homo sapiens	88-93
7547904-6	1995	The differences in activity between PDI and its thioredoxin-like domains suggest that other features of the PDI molecule are also required for its complete range of thiol-disulfide exchange activities.	Disulfides	171-180	prolyl 4-hydroxylase subunit beta	Homo sapiens	108-111
30762062-1	2019	Previous studies have led to opposing hypotheses about the requirement of intermolecular disulfide exchange in the binding of the iron regulatory peptide hepcidin to its receptor ferroportin.	Disulfides	89-98	hepcidin antimicrobial peptide	Homo sapiens	154-162
24752778-9	2014	Subsequent to identification of the transferrin receptor (TfR) as a component of a high molecular mass KLRG1 complex, they demonstrate that a fraction of mouse KLRG1 molecules undergoes disulfide-bonding with TfRs and colocalises with the latter at the cell surface.	Disulfides	186-195	killer cell lectin-like receptor subfamily G, member 1	Mus musculus	160-165
7574684-0	1995	Extracellular domain of neurotrophin receptor trkB: disulfide structure, N-glycosylation sites, and ligand binding.	Disulfides	52-61	neurotrophic receptor tyrosine kinase 2	Homo sapiens	46-50
30762062-2	2019	To clarify this issue, we used the diaminodiacid approach to replace the disulfide bonds in hepcidin with non-reducible thioether bonds.	Disulfides	73-82	hepcidin antimicrobial peptide	Homo sapiens	92-100
7656978-1	1995	The mutant T4 glutaredoxin where the active site residues Val15 and Tyr16 have been substituted by Gly and Pro, respectively, crystallizes in a form where the active site disulfide is accessible to reagents.	Disulfides	171-180	glutaredoxin	Homo sapiens	14-26
30401714-1	2019	Glutathione (GSH)/GSH reductase (GSR) and thioredoxin/thioredoxin reductase (TXNRD) are two major compensating thiol-dependent antioxidant pathways that maintain protein dithiol/disulfide balance.	Disulfides	178-187	thioredoxin	Homo sapiens	42-53
30401714-1	2019	Glutathione (GSH)/GSH reductase (GSR) and thioredoxin/thioredoxin reductase (TXNRD) are two major compensating thiol-dependent antioxidant pathways that maintain protein dithiol/disulfide balance.	Disulfides	178-187	peroxiredoxin 5	Homo sapiens	54-75
24700462-6	2014	The disulfide has a standard redox potential of -261 mV and is efficiently reduced by the protein reductant, thioredoxin, with a rate constant of 16,180 m(-1) s(-1).	Disulfides	4-13	thioredoxin	Homo sapiens	109-120
24700787-4	2014	The hEGF, featuring three native disulfide bonds, was expressed featuring additional sulfhydryl groups, in the form of cysteine residues, as orthogonal ligation sites at both the N and C termini.	Disulfides	33-42	epidermal growth factor	Homo sapiens	4-8
7642652-9	1995	Our data suggest that calnexin can promote disulfide bond formation in class I heavy chains but does not directly facilitate subsequent binding to beta 2m.	Disulfides	43-52	calnexin	Homo sapiens	22-30
24636989-4	2014	PDIA5 contributed to disulfide bond rearrangement in ATF6alpha under stress conditions, thereby leading to ATF6alpha export from the ER and activation of its target genes.	Disulfides	21-30	activating transcription factor 6	Homo sapiens	53-62
24636989-4	2014	PDIA5 contributed to disulfide bond rearrangement in ATF6alpha under stress conditions, thereby leading to ATF6alpha export from the ER and activation of its target genes.	Disulfides	21-30	activating transcription factor 6	Homo sapiens	107-116
30647818-12	2018	We analyzed cartilage-specific ERp57 knockout mice and demonstrated that the deficiency of this single protein disulfide isomerase, which is responsible for formation of disulfide bridges in ECM glycoproteins, is sufficient to induce ER stress and to cause an ER stress-related bone phenotype.	Disulfides	111-120	protein disulfide isomerase associated 3	Mus musculus	31-36
30545068-5	2018	Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems.	Disulfides	0-9	thioredoxin	Homo sapiens	76-87
30466386-2	2018	PDI plays a key role in the formation of disulfide bonds in newly formed proteins.	Disulfides	41-50	protein disulfide-isomerase	Triticum aestivum	0-3
24680680-5	2014	We demonstrate that adiponutrin is present in plasma as disulfide-bond dependent multimers, estimated to circulate at a concentration of 1.25-4 nM.	Disulfides	56-65	patatin like phospholipase domain containing 3	Homo sapiens	20-31
8846437-1	1995	Calcitonin, calcitonin gene related peptide, amylin, and adrenomedullin are structurally related polypeptides characterized by a six or seven amino acid ring structure linked by a disulfide bridge and an amidated C-terminus.	Disulfides	180-189	islet amyloid polypeptide	Homo sapiens	45-51
7627335-1	1995	Calcitonin, calcitonin gene-related peptide, adrenomedullin and amylin are structurally related peptides with N-terminal 6-7 amino acid ring structures linked by a disulfide bridge and with amidated C-termini.	Disulfides	164-173	islet amyloid polypeptide	Homo sapiens	64-70
24462249-3	2014	Whereas PDI catalyzes native disulfide bond formation by the cooperative action of two mutually facing redox-active sites on folding intermediates bound to the central cleft, ERp46 Trx domains are separated, act independently, and engage in rapid but promiscuous disulfide bond formation during early oxidative protein folding.	Disulfides	263-272	thioredoxin domain containing 5	Homo sapiens	175-180
29405790-6	2018	For HER2, a similar potency has been observed for a 12-amino-acid anti-HER2 peptide mimetic YCDGFYACYMDV-NH2 (AHNP, disulfide-bridged) and full-length trastuzumab.	Disulfides	116-125	erb-b2 receptor tyrosine kinase 2	Mus musculus	71-75
7539791-1	1995	In sera from pregnant women, pregnancy-associated plasma protein-A (PAPP-A) circulates as a disulfide-bound complex (approximately 474 kDa) with the proform of eosinophil major basic protein (proMBP) (Oxvig, C., Sand, O., Kristensen, T., Gleich, G. J., and Sottrup-Jensen, L. (1993) J. Biol.	Disulfides	92-101	pappalysin 1	Homo sapiens	29-66
7539791-1	1995	In sera from pregnant women, pregnancy-associated plasma protein-A (PAPP-A) circulates as a disulfide-bound complex (approximately 474 kDa) with the proform of eosinophil major basic protein (proMBP) (Oxvig, C., Sand, O., Kristensen, T., Gleich, G. J., and Sottrup-Jensen, L. (1993) J. Biol.	Disulfides	92-101	pappalysin 1	Homo sapiens	68-74
7539791-1	1995	In sera from pregnant women, pregnancy-associated plasma protein-A (PAPP-A) circulates as a disulfide-bound complex (approximately 474 kDa) with the proform of eosinophil major basic protein (proMBP) (Oxvig, C., Sand, O., Kristensen, T., Gleich, G. J., and Sottrup-Jensen, L. (1993) J. Biol.	Disulfides	92-101	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	160-190
24591711-3	2014	In the reduced state, thioredoxins control the structure and function of proteins by reducing disulfide bridges in the redox active site of a protein.	Disulfides	94-103	thioredoxin	Homo sapiens	22-34
7539791-1	1995	In sera from pregnant women, pregnancy-associated plasma protein-A (PAPP-A) circulates as a disulfide-bound complex (approximately 474 kDa) with the proform of eosinophil major basic protein (proMBP) (Oxvig, C., Sand, O., Kristensen, T., Gleich, G. J., and Sottrup-Jensen, L. (1993) J. Biol.	Disulfides	92-101	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	192-198
30236986-0	2018	SGIP1 dimerizes via intermolecular disulfide bond in muHD domain during cellular endocytosis.	Disulfides	35-44	SH3GL interacting endocytic adaptor 1	Homo sapiens	0-5
7539791-8	1995	Based on sequence analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and reaction with specific antibodies, one is shown to be a 2:2 disulfide-bound complex (approximately 200 kDa) between proMBP and angiotensinogen.	Disulfides	151-160	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	207-213
30236986-4	2018	In this study, we found that muHD domain of SGIP1 is capable of forming a stable dimer by an intermolecular disulfide bond formed by C632 in our crystal structure.	Disulfides	108-117	SH3GL interacting endocytic adaptor 1	Homo sapiens	44-49
7759526-0	1995	Thrombospondin 3 is a pentameric molecule held together by interchain disulfide linkage involving two cysteine residues.	Disulfides	70-79	thrombospondin 3	Homo sapiens	0-16
30068531-3	2018	We used proteomics to identify LMF1-binding partners necessary for LPL secretion in HEK293 cells and found these to include oxidoreductases and lectin chaperones, suggesting that LMF1 facilitates the formation of LPL"s five disulfide bonds.	Disulfides	224-233	lipoprotein lipase	Homo sapiens	67-70
30068531-3	2018	We used proteomics to identify LMF1-binding partners necessary for LPL secretion in HEK293 cells and found these to include oxidoreductases and lectin chaperones, suggesting that LMF1 facilitates the formation of LPL"s five disulfide bonds.	Disulfides	224-233	lipase maturation factor 1	Homo sapiens	179-183
30068531-3	2018	We used proteomics to identify LMF1-binding partners necessary for LPL secretion in HEK293 cells and found these to include oxidoreductases and lectin chaperones, suggesting that LMF1 facilitates the formation of LPL"s five disulfide bonds.	Disulfides	224-233	lipoprotein lipase	Homo sapiens	213-216
24375145-3	2014	In this study, we confirmed that the Corynebacterium glutamicum NrdH redoxin catalytically reduces the disulfides in the class Ib ribonucleotide reductases (RNR), insulin and 5,5"-dithiobis-(2-nitrobenzoic acid) (DTNB), by exclusively receiving electrons from thioredoxin reductase.	Disulfides	103-113	redoxin homolog NrdH	Corynebacterium glutamicum	64-68
24376157-3	2014	A student procedure is provided that illustrates the use of DockoMatic to create a homology model for the amino propeptide region (223 amino acids with two disulfide bonds) of collagen alpha1 (XI), followed by molecular docking of the commercial drug Arixtra( ) to the homology model of alpha1 (XI), and finally, analysis of the results of the docking experiment.	Disulfides	156-165	adrenoceptor alpha 1D	Homo sapiens	185-191
30068531-4	2018	In accordance with this role, we found that LPL aggregates in LMF1-deficient cells due to the formation of incorrect intermolecular disulfide bonds.	Disulfides	132-141	lipoprotein lipase	Homo sapiens	44-47
7759526-7	1995	TSP3 is held together by interchain disulfide linkage involving just two cysteine residues, Cys-245 and Cys-248.	Disulfides	36-45	thrombospondin 3	Homo sapiens	0-4
30068531-5	2018	Cells lacking LMF1 were hypersensitive to depletion of glutathione, but not DTT treatment, suggesting that LMF1 helps reduce the ER Accordingly, we found that loss of LMF1 results in a more oxidized ER Our data show that LMF1 has a broader role than simply folding lipases, and we identified fibronectin and the low-density lipoprotein receptor (LDLR) as novel LMF1 clients that contain multiple, non-sequential disulfide bonds.	Disulfides	412-421	lipase maturation factor 1	Homo sapiens	14-18
30068531-5	2018	Cells lacking LMF1 were hypersensitive to depletion of glutathione, but not DTT treatment, suggesting that LMF1 helps reduce the ER Accordingly, we found that loss of LMF1 results in a more oxidized ER Our data show that LMF1 has a broader role than simply folding lipases, and we identified fibronectin and the low-density lipoprotein receptor (LDLR) as novel LMF1 clients that contain multiple, non-sequential disulfide bonds.	Disulfides	412-421	lipase maturation factor 1	Homo sapiens	107-111
7648447-6	1995	The IL-2/IL-2R gamma c, but not the IL-2/IL-2R beta, complex exhibited enhanced mobility after SDS-polyacrylamide gel electrophoresis under nonreducing conditions, suggesting a more compact structure for gamma c as a result of intrachain disulfide bonds.	Disulfides	238-247	interleukin 2 receptor, gamma chain	Mus musculus	15-22
30068531-5	2018	Cells lacking LMF1 were hypersensitive to depletion of glutathione, but not DTT treatment, suggesting that LMF1 helps reduce the ER Accordingly, we found that loss of LMF1 results in a more oxidized ER Our data show that LMF1 has a broader role than simply folding lipases, and we identified fibronectin and the low-density lipoprotein receptor (LDLR) as novel LMF1 clients that contain multiple, non-sequential disulfide bonds.	Disulfides	412-421	lipase maturation factor 1	Homo sapiens	107-111
30068531-5	2018	Cells lacking LMF1 were hypersensitive to depletion of glutathione, but not DTT treatment, suggesting that LMF1 helps reduce the ER Accordingly, we found that loss of LMF1 results in a more oxidized ER Our data show that LMF1 has a broader role than simply folding lipases, and we identified fibronectin and the low-density lipoprotein receptor (LDLR) as novel LMF1 clients that contain multiple, non-sequential disulfide bonds.	Disulfides	412-421	lipase maturation factor 1	Homo sapiens	107-111
30068531-5	2018	Cells lacking LMF1 were hypersensitive to depletion of glutathione, but not DTT treatment, suggesting that LMF1 helps reduce the ER Accordingly, we found that loss of LMF1 results in a more oxidized ER Our data show that LMF1 has a broader role than simply folding lipases, and we identified fibronectin and the low-density lipoprotein receptor (LDLR) as novel LMF1 clients that contain multiple, non-sequential disulfide bonds.	Disulfides	412-421	low density lipoprotein receptor	Homo sapiens	312-344
30068531-5	2018	Cells lacking LMF1 were hypersensitive to depletion of glutathione, but not DTT treatment, suggesting that LMF1 helps reduce the ER Accordingly, we found that loss of LMF1 results in a more oxidized ER Our data show that LMF1 has a broader role than simply folding lipases, and we identified fibronectin and the low-density lipoprotein receptor (LDLR) as novel LMF1 clients that contain multiple, non-sequential disulfide bonds.	Disulfides	412-421	low density lipoprotein receptor	Homo sapiens	346-350
30068531-5	2018	Cells lacking LMF1 were hypersensitive to depletion of glutathione, but not DTT treatment, suggesting that LMF1 helps reduce the ER Accordingly, we found that loss of LMF1 results in a more oxidized ER Our data show that LMF1 has a broader role than simply folding lipases, and we identified fibronectin and the low-density lipoprotein receptor (LDLR) as novel LMF1 clients that contain multiple, non-sequential disulfide bonds.	Disulfides	412-421	lipase maturation factor 1	Homo sapiens	107-111
30068531-6	2018	We conclude that LMF1 is needed for secretion of some ER client proteins that require reduction of non-native disulfides during their folding.	Disulfides	110-120	lipase maturation factor 1	Homo sapiens	17-21
30111632-6	2018	Lack of structural restraint by disulfides, present in other related cytokines, is most likely reason for the low stability of IL-24.	Disulfides	32-42	interleukin 24	Homo sapiens	127-132
30030891-5	2018	We here review how TF is switched between its role in coagulation and cell signaling through thiol-disulfide exchange reactions in the context of physiologically relevant lipid microdomains.	Disulfides	99-108	coagulation factor III, tissue factor	Homo sapiens	19-21
24425871-7	2014	These interactions are sufficiently strong to maintain the structural integrity of IgG1 during its normal life span; for IgG2 and IgG3 the inter-heavy chain disulfide bonds are essential to prevent half-molecule dissociation, whereas the labile hinge disulfide bonds favor half-molecule exchange in vivo for IgG4.	Disulfides	157-166	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	130-134
24398688-3	2014	By studying channels expressed in Xenopus laevis oocytes, we show a novel disulfide-cross-linked dimer conopeptide, Vt3.1 that preferentially inhibits BK channels containing the beta4 subunit, which is most abundantly expressed in brain and important for neuronal functions.	Disulfides	74-83	basic helix-loop-helix family member e23 L homeolog	Xenopus laevis	178-183
24103200-8	2014	In a purified system, ABX shortened the initial lag phase during the reduction of insulin disulfide by Trx system.	Disulfides	90-99	thioredoxin	Homo sapiens	103-106
24351040-3	2014	TRFS-green displays a green fluorescence off-on change induced by the TrxR-mediated disulfide cleavage and subsequent intramolecular cyclization to liberate the masked naphthalimide fluorophore.	Disulfides	84-93	peroxiredoxin 5	Homo sapiens	70-74
7783756-12	1995	Thus, we propose that intrachain disulfide bond formation precedes the association of class I heavy chain with beta 2m and peptide, and that disulfide bond formation is required for efficient assembly, ligand binding and folding of the class I heavy chain.	Disulfides	33-42	beta-2 microglobulin	Mus musculus	111-118
25045530-6	2014	A disulfide-bonded CTLA-2alpha/cathepsin L complex was isolated, and a cathepsin L subunit with a molecular weight of 24,000 was identified as the interactive enzyme protein.	Disulfides	2-11	cathepsin L	Mus musculus	31-42
25045530-6	2014	A disulfide-bonded CTLA-2alpha/cathepsin L complex was isolated, and a cathepsin L subunit with a molecular weight of 24,000 was identified as the interactive enzyme protein.	Disulfides	2-11	cathepsin L	Mus musculus	71-82
30098457-9	2018	In the presence of hydrogen peroxide, GRPEL2 forms dimers through intermolecular disulfide bonds in which Cys87 is the thiol switch.	Disulfides	81-90	GrpE like 2, mitochondrial	Homo sapiens	38-44
30131247-6	2018	In addition, to make the CDCA1-siRNA efficiently targeting the PCa cells, pHLIP and CDCA1-siRNA were combined with disulfide bond to become effector molecules.	Disulfides	115-124	NUF2 component of NDC80 kinetochore complex	Homo sapiens	25-30
7721777-1	1995	The NH2-terminal region of pro-opiomelanocortin (POMC) is highly conserved across species, having two disulfide bridges that cause the formation of an amphipathic hairpin loop structure between the 2nd and 3rd cysteine residues (Cys8 to Cys20).	Disulfides	102-111	pro-opiomelanocortin-alpha	Mus musculus	27-47
24136556-0	2014	Identification of thioredoxin target disulfides using isotope-coded affinity tags.	Disulfides	37-47	thioredoxin	Homo sapiens	18-29
7721777-1	1995	The NH2-terminal region of pro-opiomelanocortin (POMC) is highly conserved across species, having two disulfide bridges that cause the formation of an amphipathic hairpin loop structure between the 2nd and 3rd cysteine residues (Cys8 to Cys20).	Disulfides	102-111	pro-opiomelanocortin-alpha	Mus musculus	49-53
29979586-1	2018	Many mutations that cause familial hypercholesterolemia localize to ligand-binding domain 5 (LA5) of the low-density lipoprotein receptor, motivating investigation of the folding and misfolding of this small, disulfide-rich, calcium-binding domain.	Disulfides	209-218	low density lipoprotein receptor	Homo sapiens	105-137
7721777-2	1995	The role that the NH2-terminal region of pro-opiomelanocortin plays in acting as a molecular sorting signal for the regulated secretory pathway was investigated by using site-directed mutagenesis either to disrupt one or more of the disulfide bridges or to delete the amphipathic loop entirely.	Disulfides	233-242	pro-opiomelanocortin-alpha	Mus musculus	41-61
30091702-3	2018	Disulfide crosslinks between cysteine-modified H2A.Z and/or H2A histones within nucleosomes were induced using a membrane-permeable oxidant.	Disulfides	0-9	H2A.Z variant histone 1	Homo sapiens	47-52
7721777-5	1995	Disruption of both disulfide bridges or the second disulfide bridge or removal of the amphipathic hairpin loop resulted in constitutive secretion of the mutant POMC from the cells and a lack of punctate secretory granule immunostaining within the cells.	Disulfides	19-28	pro-opiomelanocortin-alpha	Mus musculus	160-164
7721777-5	1995	Disruption of both disulfide bridges or the second disulfide bridge or removal of the amphipathic hairpin loop resulted in constitutive secretion of the mutant POMC from the cells and a lack of punctate secretory granule immunostaining within the cells.	Disulfides	51-60	pro-opiomelanocortin-alpha	Mus musculus	160-164
29569285-5	2018	Furthermore, we studied the effects of the disulfide bond on the PSGL-1 dimer using MD simulations.	Disulfides	43-52	selectin P ligand	Homo sapiens	65-71
29569285-6	2018	The disulfide bond was critical to form the leucine zipper structure, by which the disulfide bond further improved the stability of the PSGL-1 dimer.	Disulfides	4-13	selectin P ligand	Homo sapiens	136-142
29569285-6	2018	The disulfide bond was critical to form the leucine zipper structure, by which the disulfide bond further improved the stability of the PSGL-1 dimer.	Disulfides	83-92	selectin P ligand	Homo sapiens	136-142
29714059-5	2018	Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322.	Disulfides	116-125	microtubule associated protein tau	Homo sapiens	29-32
29714059-5	2018	Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322.	Disulfides	116-125	microtubule associated protein tau	Homo sapiens	88-91
24266532-7	2013	Treatment of the NEMO-reconstituted cells with H2O2 led to the formation of covalent dimers for wild-type NEMO and the five-Ala mutant, but not for the seven-Ala mutant, confirming that Cys54 and/or Cys347 can mediate interchain disulfide bonding.	Disulfides	229-238	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	17-21
24266532-9	2013	This conclusion was corroborated by the observation that the secondary structure content of NEMO and its thermal stability were independent of the presence or absence of interchain disulfide bonds.	Disulfides	181-190	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	92-96
24364984-7	2013	SiRNA-mediated knockdown of ATF6alpha and ERp57 during HDM administration in mice resulted in a decrease in components of HDM-induced ER stress, disulfide mediated oligomerization of Bak, and activation of caspase-3.	Disulfides	145-154	protein disulfide isomerase associated 3	Mus musculus	42-47
24364984-7	2013	SiRNA-mediated knockdown of ATF6alpha and ERp57 during HDM administration in mice resulted in a decrease in components of HDM-induced ER stress, disulfide mediated oligomerization of Bak, and activation of caspase-3.	Disulfides	145-154	BCL2-antagonist/killer 1	Mus musculus	183-186
24349312-1	2013	Human relaxin-3 is a neuropeptide that is structurally similar to human insulin with two chains (A and B) connected by three disulfide bonds.	Disulfides	125-134	relaxin 3	Homo sapiens	6-15
29714059-5	2018	Furthermore, we identified a tau-interacting protein, selenoprotein W, which attenuates tau accumulation by forming disulfide linkage between SelW Cys-37 and tau Cys-322.	Disulfides	116-125	microtubule associated protein tau	Homo sapiens	88-91
7721777-7	1995	Thus the sorting signal for POMC to the regulated secretory pathway appears to be encoded by a specific conformational motif comprised of a 13-amino acid amphipathic loop structure stabilized by a disulfide bridge, located at the NH2 terminus of the molecule.	Disulfides	197-206	pro-opiomelanocortin-alpha	Mus musculus	28-32
29858230-4	2018	We further show that ER oxidoreductin 1alpha (Ero1alpha), the pivotal sulfhydryl oxidase that catalyzes disulfide formation in the ER, is phosphorylated by Fam20C in the Golgi apparatus and retrograde-transported to the ER mediated by ERp44.	Disulfides	104-113	FAM20C golgi associated secretory pathway kinase	Homo sapiens	156-162
7599600-4	1995	The characteristic structural feature of the subfamily of periplasmic molecular chaperones with the accessory sequence (Caf1M subfamily) is the existence of exposed to a solvent Cys residues in F1 and G1 beta-strands which can form disulfide bond in the putative binding pocket.	Disulfides	232-241	F1 capsule protein	Yersinia pestis	120-125
29991649-4	2018	However, ATM also performs a redox-sensing function mediated through formation of ROS-dependent disulfide-linked dimers.	Disulfides	96-105	ATM serine/threonine kinase	Homo sapiens	9-12
24118938-1	2013	Protein disulfide isomerase (PDI) catalyzes disulfide bond oxidation, reduction and isomerization during protein synthesis in the endoplasmic reticulum (ER).	Disulfides	8-17	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	29-32
24062305-10	2013	In conclusion, reversible oxidation of the non-active site disulfide of Trx1 is suggested to play an important role in redox regulation and cell signaling via temporal inhibition of its protein-disulfide reductase activity for the transmission of oxidative signals under oxidative stress.	Disulfides	59-68	thioredoxin	Homo sapiens	72-76
7719935-2	1995	IL-12 is a disulfide-linked heterodimeric cytokine composed of a 35-kDa light chain (p35) and a 40-kDa heavy chain (p40).	Disulfides	11-20	interleukin 9	Homo sapiens	116-119
23913858-2	2013	Protein disulfide isomerase (PDI) is an oxidoreductase that mediates thiol/disulfide interchange reactions.	Disulfides	8-17	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	29-32
29784879-6	2018	This interaction, which depended on the redox activity of ERp46, involved formation of a disulfide bond between the cysteine residues of the ERp46 redox-active sites and the EDEM3 alpha-mannosidase domain.	Disulfides	89-98	thioredoxin domain containing 5	Homo sapiens	58-63
29784879-6	2018	This interaction, which depended on the redox activity of ERp46, involved formation of a disulfide bond between the cysteine residues of the ERp46 redox-active sites and the EDEM3 alpha-mannosidase domain.	Disulfides	89-98	thioredoxin domain containing 5	Homo sapiens	141-146
29784879-6	2018	This interaction, which depended on the redox activity of ERp46, involved formation of a disulfide bond between the cysteine residues of the ERp46 redox-active sites and the EDEM3 alpha-mannosidase domain.	Disulfides	89-98	ER degradation enhancing alpha-mannosidase like protein 3	Homo sapiens	174-179
7629027-0	1995	Functional consequences of substitution of the disulfide-bonded segment, Cys127-Cys150, located in the extracellular domain of the Na,K-ATPase beta subunit: Arg148 is essential for the functional expression of Na,K-ATPase.	Disulfides	47-56	ATPase Na+/K+ transporting subunit beta 1	Sus scrofa	131-155
29878755-9	2018	Applying this workflow, we successfully mapped the complex disulfide bonds of tertiapin and the epidermal growth factor (EGF) family members transforming growth factor alpha (TGFalpha) and EGF.	Disulfides	59-68	epidermal growth factor	Homo sapiens	189-192
23571504-2	2013	We demonstrated recently that hBD-1 shows activity against enteric commensals and Candida species only after its disulfide bonds have been reduced by thioredoxin (TRX) or a reducing environment.	Disulfides	113-122	thioredoxin	Homo sapiens	150-161
7723770-5	1995	The mutant subunits form a disulfide-bonded Fv molecule, which binds to the alpha-subunit of the IL2 receptor (IL2R alpha) with an affinity identical to that of humanized anti-Tac IgG.	Disulfides	27-36	interleukin 2 receptor subunit alpha	Homo sapiens	111-121
24002168-1	2013	Human calcitonin (hCT) is a 32-amino acid peptide hormone that contains an intrachain disulfide bridge between Cys1 and Cys7 and a proline amide at the C-terminus.	Disulfides	86-95	cystin 1	Homo sapiens	111-115
29763554-2	2018	Here, we used the high affinity, meditope-Fab interaction to template and drive the rapid, efficient, and stable site-specific formation of a disulfide bond.	Disulfides	142-151	FA complementation group B	Homo sapiens	42-45
7851394-1	1995	Glutaredoxin is generally a glutathione-dependent hydrogen donor for ribonucleotide reductase and also catalyses general glutathione (GSH)-disulfide-oxidoreduction reactions in the presence of NADPH and glutathione reductase.	Disulfides	139-148	glutaredoxin	Homo sapiens	0-12
29553725-1	2018	Two-cysteine peroxiredoxins (Prx) have a three-step catalytic cycle consisting of (1) reduction of peroxide and formation of sulfenic acid on the enzyme, (2) condensation of the sulfenic acid with a thiol to form disulfide, also known as resolution, and (3) reduction of the disulfide by a reductant protein.	Disulfides	213-222	peroxiredoxin 1	Homo sapiens	13-27
29553725-1	2018	Two-cysteine peroxiredoxins (Prx) have a three-step catalytic cycle consisting of (1) reduction of peroxide and formation of sulfenic acid on the enzyme, (2) condensation of the sulfenic acid with a thiol to form disulfide, also known as resolution, and (3) reduction of the disulfide by a reductant protein.	Disulfides	275-284	peroxiredoxin 1	Homo sapiens	13-27
30013808-2	2018	Here, improved MS detection sensitivity of hepcidin has been achieved by reducing the disulfide bonds in hepcidin, by which proton accessibility increased, compared to the intact hepcidin peptide.	Disulfides	86-95	hepcidin antimicrobial peptide	Homo sapiens	43-51
30013808-2	2018	Here, improved MS detection sensitivity of hepcidin has been achieved by reducing the disulfide bonds in hepcidin, by which proton accessibility increased, compared to the intact hepcidin peptide.	Disulfides	86-95	hepcidin antimicrobial peptide	Homo sapiens	105-113
30013808-2	2018	Here, improved MS detection sensitivity of hepcidin has been achieved by reducing the disulfide bonds in hepcidin, by which proton accessibility increased, compared to the intact hepcidin peptide.	Disulfides	86-95	hepcidin antimicrobial peptide	Homo sapiens	105-113
24003226-2	2013	The typical 2-Cys subclass of Prxs (human Prx1-4) utilizes a Cys sulfenic acid (Cys-SOH) intermediate and disulfide bond formation across two subunits during catalysis.	Disulfides	106-115	peroxiredoxin 1	Homo sapiens	42-48
23834247-2	2013	Mia40 uses its redox active CPC motif to shuttle disulfides between its client proteins (newly imported proteins) and the thiol oxidase Erv1.	Disulfides	49-59	growth factor, augmenter of liver regeneration	Homo sapiens	136-140
8540329-0	1995	Site-directed mutagenesis of a disulfide bridge in cathepsin D: expression, activation, purification, and characterization.	Disulfides	31-40	cathepsin D	Homo sapiens	51-62
23726996-6	2013	We propose that the S326C OGG1 catalytic impairment and its susceptibility to dimerization and disulfide bond formation in an oxidizing environment all concur to decrease repair capacity.	Disulfides	95-104	8-oxoguanine DNA glycosylase	Homo sapiens	26-30
29769573-3	2018	To improve the drug-like properties of natural IL-15, we create an IL-15-based molecule, named P22339, with the following characteristics: 1) building a complex of IL-15 and the Sushi domain of IL-15 receptor alpha chain to enhance the agonist activity of IL-15 via transpresentation; 2) through a rational structure-based design, creating a disulfide bond linking the IL-15/Sushi domain complex with an IgG1 Fc to augment its half-life.	Disulfides	342-351	interleukin-15	Macaca fascicularis	67-72
29769573-3	2018	To improve the drug-like properties of natural IL-15, we create an IL-15-based molecule, named P22339, with the following characteristics: 1) building a complex of IL-15 and the Sushi domain of IL-15 receptor alpha chain to enhance the agonist activity of IL-15 via transpresentation; 2) through a rational structure-based design, creating a disulfide bond linking the IL-15/Sushi domain complex with an IgG1 Fc to augment its half-life.	Disulfides	342-351	interleukin-15	Macaca fascicularis	67-72
29769573-3	2018	To improve the drug-like properties of natural IL-15, we create an IL-15-based molecule, named P22339, with the following characteristics: 1) building a complex of IL-15 and the Sushi domain of IL-15 receptor alpha chain to enhance the agonist activity of IL-15 via transpresentation; 2) through a rational structure-based design, creating a disulfide bond linking the IL-15/Sushi domain complex with an IgG1 Fc to augment its half-life.	Disulfides	342-351	interleukin-15	Macaca fascicularis	67-72
29769573-3	2018	To improve the drug-like properties of natural IL-15, we create an IL-15-based molecule, named P22339, with the following characteristics: 1) building a complex of IL-15 and the Sushi domain of IL-15 receptor alpha chain to enhance the agonist activity of IL-15 via transpresentation; 2) through a rational structure-based design, creating a disulfide bond linking the IL-15/Sushi domain complex with an IgG1 Fc to augment its half-life.	Disulfides	342-351	interleukin-15	Macaca fascicularis	67-72
7672822-1	1995	The mouse pre-T-cell receptor alpha (pT alpha) chain is a 33,000 M(r) glycoprotein expressed on the surface of immature thymocytes as a disulfide-linked heterodimer with the T-cell receptor beta (TCR beta) chain, and in association with proteins of the CD3 complex.	Disulfides	136-145	pre T cell antigen receptor alpha	Mus musculus	37-45
29342507-13	2018	Our results suggest that impaired ubiquitination of HLA-B27 may play a role in the accumulation of misfolded disulfide-linked dimers, the elimination of which can be enhanced by activation of autophagy.	Disulfides	109-118	major histocompatibility complex, class I, B	Homo sapiens	52-59
23966469-4	2013	Here we show that nonglycoprotein substrates are captured by BiP and then transferred to ERdj5 without going through the calnexin/EDEM1 pathway; after cleavage of disulfide bonds by ERdj5, the nonglycoproteins are transferred to the ERAD scaffold protein SEL1L by the aid of BiP for dislocation into the cytosol.	Disulfides	163-172	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	182-187
25702411-1	2013	Linear hepta-peptide Cys-Lys-Gly-Asp-Trp-Asp-Cys was synthesized first and then disulfide bond was formed between the Cys1 and Cys7 to develop cyclo-heptapeptide containing Lys-Gly-Asp-sequence.	Disulfides	80-89	cystin 1	Homo sapiens	118-122
7527811-1	1995	IL-12, a heterodimeric cytokine, consists of two disulfide-linked subunits, p40 and p35.	Disulfides	49-58	interleukin 9	Homo sapiens	76-79
23689258-8	2013	The soluble DsbA-like domain of LTO1 was found to have reduction, oxidation and isomerization activities, and could promote the formation of disulfide bonds in a lumenal protein, FKBP13.	Disulfides	141-150	NAD(P)H dehydrogenase (quinone)s	Arabidopsis thaliana	32-36
29488681-5	2018	SUMMARY: Background Rhodocytin, a disulfide-linked heterodimeric C-type lectin from Calloselasma rhodostoma consisting of alpha-subunits and beta-subunits, induces platelet aggregation through C-type lectin-like receptor 2 (CLEC-2).	Disulfides	34-43	C-type lectin domain family 1, member b	Mus musculus	224-230
7811279-1	1994	The involvement of cysteine 524 of the insulin receptor in an intermolecular (class I) disulfide bond between the two alpha-subunits was investigated using site-directed mutagenesis.	Disulfides	87-96	insulin receptor	Homo sapiens	39-55
29645029-0	2018	Regulation of both the structure and function by a de novo designed disulfide bond: a case study of heme proteins in myoglobin.	Disulfides	68-77	myoglobin	Homo sapiens	117-126
29645029-1	2018	A de novo designed intramolecular disulfide bond in myoglobin, resembling that in cytoglobin without structural evidence, was confirmed by an X-ray structure for the first time and was demonstrated to regulate both the structure and function of this protein, which fulfills the design of an artificial dehaloperoxidase, with an activity exceeding that of a native enzyme.	Disulfides	34-43	myoglobin	Homo sapiens	52-61
29421551-4	2018	The micelle (HA-SS-TOS, HSST) can highly specifically bind with CD44 receptor over-expressed tumor, and response selectively to high GSH level in the cells, inducing disulfide bond breakage and the release of the payload (paclitaxel, PTX).	Disulfides	166-175	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	24-28
23914919-1	2013	Selenoprotein S (SelS, VIMP) is an intrinsically disordered enzyme that utilizes selenocysteine to catalyze the reduction of disulfide bonds and peroxides.	Disulfides	125-134	selenoprotein S	Homo sapiens	0-15
23914919-1	2013	Selenoprotein S (SelS, VIMP) is an intrinsically disordered enzyme that utilizes selenocysteine to catalyze the reduction of disulfide bonds and peroxides.	Disulfides	125-134	selenoprotein S	Homo sapiens	17-21
23914919-1	2013	Selenoprotein S (SelS, VIMP) is an intrinsically disordered enzyme that utilizes selenocysteine to catalyze the reduction of disulfide bonds and peroxides.	Disulfides	125-134	selenoprotein S	Homo sapiens	23-27
32261169-4	2013	The confocal fluorescence microscopic observation revealed that the colocalization ratio of siRNAs to endosomes decreased for DMAE-COO-PRX in comparison with disulfide-introduced PRX (DMAE-SS-PRX).	Disulfides	158-167	periaxin	Homo sapiens	179-182
23207101-6	2013	Both HMGB1 containing a disulfide bond between C23 and C45, which induces chemokine and cytokine release by activating TLR4, and HMGB1 terminally oxidized to contain a cysteine sulfonate are inactive in recruiting leukocytes.	Disulfides	24-33	toll like receptor 4	Homo sapiens	119-123
29146339-4	2018	The result revealed that cysteine at head of myosin tended to form sulfinic and sulfonic acid, while the cysteine at coiled tail of myosin easily generated disulfide under same condition.	Disulfides	156-165	myosin heavy chain 14	Homo sapiens	132-138
29470989-7	2018	Increases in the dynamics of regions important for HIV gp120 and MHCII binding in D1 also result allosterically after reducing the D2 disulfide, which are likely a consequence of the structural changes that take place in D2, findings that advance our understanding of the mechanisms by which redox exchange of the CD4 disulfides regulates its function.	Disulfides	318-328	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	55-60
8001133-0	1994	An intermolecular disulfide bond stabilizes E2A homodimers and is required for DNA binding at physiological temperatures.	Disulfides	18-27	transcription factor 3	Homo sapiens	44-47
29167151-5	2018	Homology models of PCFT based on Glut5 fructose transporter structures in both inward- and outward- open conformations were constructed and predicted that two pairs of residues (T289-I304C and Q285-Q311C) from the 7th and 8th TMDs should be in sufficiently close proximity to form a disulfide bond when substituted with cysteines.	Disulfides	283-292	solute carrier family 46 member 1	Homo sapiens	19-23
29261301-3	2018	The currently available inhibitors of Trx1 and Grx1 are thiol-reactive electrophiles or disulfides that may suffer from low selectivity because of their thiol reactivity.	Disulfides	88-98	thioredoxin	Homo sapiens	38-42
29507626-3	2018	DESIGN: In this study, a sarcoma-targeting peptide-decorated disulfide-crosslinked polypeptide nanogel (STP-NG) was exploited for enhanced intracellular delivery of shikonin (SHK), an extract of a medicinal herb, to inhibit osteosarcoma progression with minimal systemic toxicity.	Disulfides	61-70	sedoheptulokinase	Homo sapiens	175-178
23922729-4	2013	Recent evidence suggests that laforin dimerization depends on redox conditions, suggesting that disulfide bonds are involved in laforin dimerization.	Disulfides	96-105	EPM2A glucan phosphatase, laforin	Homo sapiens	30-37
23922729-4	2013	Recent evidence suggests that laforin dimerization depends on redox conditions, suggesting that disulfide bonds are involved in laforin dimerization.	Disulfides	96-105	EPM2A glucan phosphatase, laforin	Homo sapiens	128-135
8001133-1	1994	It is demonstrated in this report that purified E2A helix-loop-helix (HLH) proteins spontaneously form homodimers that are linked by an intermolecular disulfide bond.	Disulfides	151-160	transcription factor 3	Homo sapiens	48-51
23880302-4	2013	Molecular dynamics trajectories have been exploited allowing successfully the formation of a full disulfide bridge network, which was expected based on the similarities between FRalpha and RfBP.	Disulfides	98-107	rabaptin, RAB GTPase binding effector protein 2	Homo sapiens	177-184
7983029-1	1994	Protein disulfide isomerase (PDI), a foldase of the endoplasmic recticulum, is a multifunctional protein that catalyzes the formation and isomerization of disulfide bonds during protein folding.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
29064673-3	2018	The eukaryotic disulfide donors are flavoenzymes, Ero1 in the endoplasmic reticulum and Erv1 in mitochondria.	Disulfides	15-24	growth factor, augmenter of liver regeneration	Homo sapiens	88-92
29064673-4	2018	In prokaryotes, disulfide generation is coupled to quinone reduction, catalyzed by intramembrane donor enzymes, DsbB and VKOR.	Disulfides	16-25	vitamin K epoxide reductase complex subunit 1	Homo sapiens	121-125
29064673-10	2018	Structural convergence between human VKOR and the disulfide donors is found to underlie cofactor reduction, disulfide generation, and electron transfer.	Disulfides	108-117	vitamin K epoxide reductase complex subunit 1	Homo sapiens	37-41
23628981-1	2013	Leukemia inhibitor factor (LIF) is a three disulfide bridge-containing cytokine with numerous regulatory effects.	Disulfides	43-52	LIF interleukin 6 family cytokine	Homo sapiens	27-30
7756992-3	1994	Models of the N domains of HGF/SF, HGF1/MSP, and plasminogen, characterized by the presence of 4 conserved Cys residues forming a loop in a loop, have been modeled based on disulfide-bond constraints.	Disulfides	173-182	hepatocyte growth factor	Homo sapiens	27-33
23875128-7	2013	The predicted 3D-structure showed mainly five alpha-helices, one 310 helix and two disulfide bonds at Cys1-Cys98 and Cys129-Cys138.	Disulfides	83-92	cystin 1	Homo sapiens	102-106
29303250-5	2018	We present updated LPL structural models generated by combining disulfide mapping, computational modeling, and data derived from single-molecule Forster resonance energy transfer (smFRET).	Disulfides	64-73	lipoprotein lipase	Homo sapiens	19-22
7827267-3	1994	Bis(cysteinyl)octapeptides related to the active sites of the oxidoreductases protein disulfide isomerase (PDI), thioredoxin reductase (trr), glutaredoxin (grx), and thioredoxin (trx) were analyzed for their propensity to form the intramolecular 14-membered disulfide ring in oxidation experiments.	Disulfides	86-95	prolyl 4-hydroxylase subunit beta	Homo sapiens	107-110
32291042-2	2018	ER lumen localised protein disulfide isomerase (PDI) catalyses the generation of disulfide bonds in conjugation with ER oxidoreductase1 (ERO1) during protein folding.	Disulfides	27-36	endoplasmic reticulum oxidoreductins 1	Arabidopsis thaliana	117-135
32291042-2	2018	ER lumen localised protein disulfide isomerase (PDI) catalyses the generation of disulfide bonds in conjugation with ER oxidoreductase1 (ERO1) during protein folding.	Disulfides	27-36	endoplasmic reticulum oxidoreductins 1	Arabidopsis thaliana	137-141
23744371-1	2013	The title compound, hexadecacarbonylbis{mu3-[(diphenylphosphanyl)methanediidyl]sulfanido}-mu4-disulfido(2-)-hexairon(4 Fe-Fe), [Fe6(C13H10PS)2(S2)(CO)16], contains two inversion-related [Fe3(Ph2PCS)(CO)8] subclusters linked by an equatorial disulfide bond [S-S = 2.1490 (9) A].	Disulfides	241-250	adaptor related protein complex 4 subunit mu 1	Homo sapiens	90-93
23662810-3	2013	Hepcidin is a small, disulfide-rich peptide synthesized by the liver, which plays a keystone role in regulating systemic iron metabolism in mammals.	Disulfides	21-30	hepcidin antimicrobial peptide	Homo sapiens	0-8
7929293-1	1994	Folding catalysts of the endoplasmic reticulum (ER), such as protein disulfide isomerase (PDI), accelerate the slow chemical steps, such as disulfide bond formation, that accompany protein folding.	Disulfides	69-78	prolyl 4-hydroxylase subunit beta	Homo sapiens	90-93
23809131-7	2013	A variety of experimental observations imply that decryption of leucocyte surface TF involves both a dithiol/disulfide switch and exposure of phosphatidylserine.	Disulfides	109-118	coagulation factor III, tissue factor	Homo sapiens	82-84
23809131-8	2013	The dithiol/disulfide switch appears to involve the Cys186-Cys209 disulfide bond in the membrane-proximal domain of TF, although this has not been demonstrated in vivo.	Disulfides	12-21	coagulation factor III, tissue factor	Homo sapiens	116-118
23809131-8	2013	The dithiol/disulfide switch appears to involve the Cys186-Cys209 disulfide bond in the membrane-proximal domain of TF, although this has not been demonstrated in vivo.	Disulfides	66-75	coagulation factor III, tissue factor	Homo sapiens	116-118
23291144-1	2013	Human IgG2 antibodies contain three types of disulfide isoforms, classified by the number of Fab arms having disulfide links to the heavy chain hinge region.	Disulfides	45-54	FA complementation group B	Homo sapiens	93-96
29089383-5	2017	We report 1) that hERG1a dominant-negative subunits suppress hERG1b currents (and vice versa), 2) that disulfide bonds form between single cysteine residues experimentally introduced into an extracellular loop of hERG1a and hERG1b subunits and produce hERG1a-hERG1b dimers, and 3) that hERG1a and hERG1b subunits tagged with fluorescent proteins that are FRET pairs exhibit robust energy transfer at the plasma membrane.	Disulfides	103-112	potassium voltage-gated channel subfamily H member 2	Homo sapiens	18-23
29179722-3	2017	Glucose transporter-1 (GLUT-1) and glutathione (GSH) overexpression in cancer cells was exploited to assemble aminoglucose (AG)-conjugated, redox-responsive nanomicelles from a single disulfide bond-bridged block polymer of polyethylene glycol and polylactic acid (AG-PEG-SS-PLA).	Disulfides	184-193	solute carrier family 2 (facilitated glucose transporter), member 1	Mus musculus	0-21
29179722-3	2017	Glucose transporter-1 (GLUT-1) and glutathione (GSH) overexpression in cancer cells was exploited to assemble aminoglucose (AG)-conjugated, redox-responsive nanomicelles from a single disulfide bond-bridged block polymer of polyethylene glycol and polylactic acid (AG-PEG-SS-PLA).	Disulfides	184-193	solute carrier family 2 (facilitated glucose transporter), member 1	Mus musculus	23-29
23291144-1	2013	Human IgG2 antibodies contain three types of disulfide isoforms, classified by the number of Fab arms having disulfide links to the heavy chain hinge region.	Disulfides	109-118	FA complementation group B	Homo sapiens	93-96
23291144-2	2013	In the IgG2-B form, both Fab arms have interchain disulfide bonds to the hinge region, and in IgG2-A, neither Fab arm are disulfide linked to the hinge.	Disulfides	50-59	FA complementation group B	Homo sapiens	25-28
7929293-4	1994	Depending on the ratio of PDI to substrate and order in which the components of the reaction are mixed, PDI can exhibit a foldase/chaperone activity, which increases the rate and extent of lysozyme refolding, or it can function as an anti-chaperone that promotes the formation of inactive, disulfide-linked lysozyme aggregates (Puig, A., and Gilbert, H.F. (1994) J. Biol.	Disulfides	290-299	prolyl 4-hydroxylase subunit beta	Homo sapiens	104-107
23395816-1	2013	Chitosan-disulfide-conjugated LMW-PEI (CS-ss-PEI) was designed to combine the biocompatibility of chitosan and the gene delivery ability of polyethylenimine (PEI) using bio-reducible disulfide for bone morphogenetic protein (BMP2) gene delivery in mediating osteogenic differentiation.	Disulfides	9-18	bone morphogenetic protein 1	Homo sapiens	197-223
7866298-4	1994	For the first time, we suggested thioltransferase can utilize cysteamine in stead of GSH during its thiol/disulfide exchange reaction activity.	Disulfides	106-115	glutaredoxin	Homo sapiens	33-49
23244515-7	2013	Central to redox signaling processes are the glutathione and thioredoxin systems controlling H(2)O(2) levels and, hence, the thiol/disulfide balance.	Disulfides	131-140	thioredoxin	Homo sapiens	61-72
23521534-5	2013	PDI catalyzes an isomerization of disulfide bridges within the thioredoxin motif C600XXC603 of the MPD and results in a drastic structural change between an active open state and an inactive closed conformation.	Disulfides	34-43	thioredoxin	Homo sapiens	63-74
29109267-4	2017	We screened a panel of CCL20 variants designed to form dimers stabilized by intermolecular disulfide bonds.	Disulfides	91-100	chemokine (C-C motif) ligand 20	Mus musculus	23-28
28939765-1	2017	Thioredoxin 1 (Trx1) is a 12-kDa oxidoreductase that catalyzes thiol-disulfide exchange reactions to reduce proteins with disulfide bonds.	Disulfides	69-78	thioredoxin	Homo sapiens	15-19
28939765-1	2017	Thioredoxin 1 (Trx1) is a 12-kDa oxidoreductase that catalyzes thiol-disulfide exchange reactions to reduce proteins with disulfide bonds.	Disulfides	122-131	thioredoxin	Homo sapiens	15-19
7929084-2	1994	Lipoprotein(a) (Lp(a)) is a lipoprotein formed by the disulfide linkage of apolipoprotein(a) (apo(a)) to the apoB100 of a low density lipoprotein particle.	Disulfides	54-63	lipoprotein(a)	Homo sapiens	0-14
7929084-2	1994	Lipoprotein(a) (Lp(a)) is a lipoprotein formed by the disulfide linkage of apolipoprotein(a) (apo(a)) to the apoB100 of a low density lipoprotein particle.	Disulfides	54-63	lipoprotein(a)	Homo sapiens	16-21
28875358-4	2017	Cell assay data revealed that the cys-64-cys74 disulfide bond in reduced GCSF imparts stabilization in absence of the cys-36-cys42 bond.	Disulfides	47-56	colony stimulating factor 3	Homo sapiens	73-77
23554500-6	2013	By introducing full-length and mutant GFP-tagged Navbeta4 into cultured neurons, we determined that the AIS and nodal localization of Navbeta4 depends on its direct interaction with Na(+) channel alpha subunits through an extracellular disulfide bond.	Disulfides	236-245	sodium voltage-gated channel alpha subunit 8	Rattus norvegicus	182-195
7929084-2	1994	Lipoprotein(a) (Lp(a)) is a lipoprotein formed by the disulfide linkage of apolipoprotein(a) (apo(a)) to the apoB100 of a low density lipoprotein particle.	Disulfides	54-63	lipoprotein(a)	Homo sapiens	75-92
8046222-2	1994	CD27 is a disulfide-linked 120-kDa transmembrane glycoprotein expressed on the majority of T cells, B cells, and NK cells; it has homology to a family of molecules that includes the receptors for nerve growth factor and TNF.	Disulfides	10-19	CD27 antigen	Mus musculus	0-4
23201556-9	2013	The data suggest that GLUT1 is acutely activated in L929 cells by modification of cysteine residues, possibly the formation of a disulfide bond within GLUT1 itself.	Disulfides	129-138	solute carrier family 2 (facilitated glucose transporter), member 1	Mus musculus	22-27
23201556-9	2013	The data suggest that GLUT1 is acutely activated in L929 cells by modification of cysteine residues, possibly the formation of a disulfide bond within GLUT1 itself.	Disulfides	129-138	solute carrier family 2 (facilitated glucose transporter), member 1	Mus musculus	151-156
28982367-1	2017	BACKGROUND: Human serum albumin (HSA)-one of the most demanded therapeutic proteins with immense biotechnological applications-is a large multidomain protein containing 17 disulfide bonds.	Disulfides	172-181	CD24 molecule	Rattus norvegicus	33-36
28982367-9	2017	Recovery of functional rHSA from inclusion bodies is not preferred because it is difficult to obtain a large multidomain disulfide bond rich protein like rHSA in its functional native form.	Disulfides	121-130	CD24 molecule	Rattus norvegicus	154-158
7981617-2	1994	HGF is a heterodimer of two glycosylated chains, alpha and beta, bound together by a disulfide bond.	Disulfides	85-94	hepatocyte growth factor	Homo sapiens	0-3
28894122-0	2017	Onset of disorder and protein aggregation due to oxidation-induced intermolecular disulfide bonds: case study of RRM2 domain from TDP-43.	Disulfides	82-91	ribonucleotide reductase regulatory subunit M2	Homo sapiens	113-117
28894122-3	2017	Under oxidizing conditions RRM2 forms disulfide-bonded dimers that experience unfolding and then assemble into aggregate particles (APs).	Disulfides	38-47	ribonucleotide reductase regulatory subunit M2	Homo sapiens	27-31
28894122-5	2017	They can recruit/release monomeric RRM2 through thiol-disulfide exchange reactions.	Disulfides	54-63	ribonucleotide reductase regulatory subunit M2	Homo sapiens	35-39
28894122-7	2017	The key to the observed aggregation behavior is the diminished ability of disulfide-bonded RRM2 dimers to refold and their increased propensity to misfold, which makes them vulnerable to large thermal fluctuations.	Disulfides	74-83	ribonucleotide reductase regulatory subunit M2	Homo sapiens	91-95
28165672-3	2017	We have recently indicated that a disulfide loop rather than a Zn-binding loop improves the anti-angiogenic and antitumor activities of the N-terminal fragment of endostatin.	Disulfides	34-43	collagen type XVIII alpha 1 chain	Homo sapiens	163-173
23356510-2	2013	New understanding of thiol-disulfide systems have occurred during the past decade as a consequence of the discoveries that thiol and disulfide systems are maintained in kinetically controlled steady states displaced from thermodynamic equilibrium, that a widely distributed family of NADPH oxidases produces oxidants that function in cell signaling and that a family of peroxiredoxins utilize thioredoxin as a reductant to complement the well-studied glutathione antioxidant system for peroxide elimination and redox regulation.	Disulfides	27-36	thioredoxin	Homo sapiens	393-404
23356510-2	2013	New understanding of thiol-disulfide systems have occurred during the past decade as a consequence of the discoveries that thiol and disulfide systems are maintained in kinetically controlled steady states displaced from thermodynamic equilibrium, that a widely distributed family of NADPH oxidases produces oxidants that function in cell signaling and that a family of peroxiredoxins utilize thioredoxin as a reductant to complement the well-studied glutathione antioxidant system for peroxide elimination and redox regulation.	Disulfides	133-142	thioredoxin	Homo sapiens	393-404
23197653-2	2013	Mouse homozygous (HM) and heterozygous (HT) mutant striatal cells with two or one allele encoding for a mutant huntingtin protein with 111 polyGln repeats showed a significant impairment of the mitochondrial disulfide relay system (MDRS).	Disulfides	208-217	huntingtin	Mus musculus	111-121
23333309-7	2013	We show that disulfide formation with transportin-1 is required for nuclear localization and the activation of FOXO4/DAF-16 induced by ROS, but not by the loss of insulin signaling.	Disulfides	13-22	Fork-head domain-containing protein;Forkhead box protein O	Caenorhabditis elegans	117-123
7516709-7	1994	In contrast, PDI did not catalyze the reaction of the reagent cystamine with the reduced peptide to form the mixed disulfide, nor the interchange of this mixed disulfide between cysteine residues, but did catalyze the subsequent intramolecular step of peptide disulfide bond formation to a similar extent as with the glutathione mixed disulfide.	Disulfides	160-169	prolyl 4-hydroxylase subunit beta	Homo sapiens	13-16
28400185-4	2017	Cc-Lec modeled 3D structure appeared as homodimer cross-linked by one disulfide bridge.	Disulfides	70-79	laryngotracheo esophageal cleft	Mus musculus	3-6
7516709-6	1994	In the presence of glutathione, PDI accelerated the formation of both single mixed disulfide species, plus their subsequent rearrangement to form the peptide disulfide bond, but not interchange of the mixed disulfide glutathione between the two cysteine residues.	Disulfides	83-92	prolyl 4-hydroxylase subunit beta	Homo sapiens	32-35
7516709-6	1994	In the presence of glutathione, PDI accelerated the formation of both single mixed disulfide species, plus their subsequent rearrangement to form the peptide disulfide bond, but not interchange of the mixed disulfide glutathione between the two cysteine residues.	Disulfides	158-167	prolyl 4-hydroxylase subunit beta	Homo sapiens	32-35
23223577-5	2013	The association is dependent on hTrx1-Cys-73 that bridges TF-Cys-209 via a disulfide bond.	Disulfides	75-84	thioredoxin	Homo sapiens	32-37
23223577-5	2013	The association is dependent on hTrx1-Cys-73 that bridges TF-Cys-209 via a disulfide bond.	Disulfides	75-84	coagulation factor III, tissue factor	Homo sapiens	58-60
7516709-6	1994	In the presence of glutathione, PDI accelerated the formation of both single mixed disulfide species, plus their subsequent rearrangement to form the peptide disulfide bond, but not interchange of the mixed disulfide glutathione between the two cysteine residues.	Disulfides	158-167	prolyl 4-hydroxylase subunit beta	Homo sapiens	32-35
23223577-10	2013	This reversible reduction-oxidation reaction occurs in the TF extracellular domain that contains partially opened Cys-49/-57 and Cys-186/-209 disulfide bonds.	Disulfides	142-151	coagulation factor III, tissue factor	Homo sapiens	59-61
28648616-6	2017	Engineered disulfide bridges, computationally predicted to interfere with IFNAR1 dynamics, were experimentally confirmed.	Disulfides	11-20	interferon alpha and beta receptor subunit 1	Homo sapiens	74-80
7516709-7	1994	In contrast, PDI did not catalyze the reaction of the reagent cystamine with the reduced peptide to form the mixed disulfide, nor the interchange of this mixed disulfide between cysteine residues, but did catalyze the subsequent intramolecular step of peptide disulfide bond formation to a similar extent as with the glutathione mixed disulfide.	Disulfides	115-124	prolyl 4-hydroxylase subunit beta	Homo sapiens	13-16
7516709-7	1994	In contrast, PDI did not catalyze the reaction of the reagent cystamine with the reduced peptide to form the mixed disulfide, nor the interchange of this mixed disulfide between cysteine residues, but did catalyze the subsequent intramolecular step of peptide disulfide bond formation to a similar extent as with the glutathione mixed disulfide.	Disulfides	160-169	prolyl 4-hydroxylase subunit beta	Homo sapiens	13-16
7516709-7	1994	In contrast, PDI did not catalyze the reaction of the reagent cystamine with the reduced peptide to form the mixed disulfide, nor the interchange of this mixed disulfide between cysteine residues, but did catalyze the subsequent intramolecular step of peptide disulfide bond formation to a similar extent as with the glutathione mixed disulfide.	Disulfides	160-169	prolyl 4-hydroxylase subunit beta	Homo sapiens	13-16
22949401-6	2013	Under reducing SDS-PAGE, a 24 kDa band corresponding to monomeric Spp24 was liberated, suggesting that Spp24 is bound to a complex linked by disulfide bonds.	Disulfides	141-150	secreted phosphoprotein 2	Mus musculus	66-71
28700690-5	2017	Particularly, ROS-related chemicals concomitantly induced intermolecular disulfide crosslinking of human DGAT2.	Disulfides	73-82	diacylglycerol O-acyltransferase 2	Homo sapiens	105-110
22949401-6	2013	Under reducing SDS-PAGE, a 24 kDa band corresponding to monomeric Spp24 was liberated, suggesting that Spp24 is bound to a complex linked by disulfide bonds.	Disulfides	141-150	secreted phosphoprotein 2	Mus musculus	103-108
7516709-8	1994	These effects on the two steps involving the mixed disulfides with glutathione or cystamine accounted for much of the overall catalytic effect of PDI on disulfide bond formation in the peptide, indicating that direct transfer of disulfide bonds from PDI to the peptide occurred less frequently.	Disulfides	51-61	prolyl 4-hydroxylase subunit beta	Homo sapiens	146-149
7516709-8	1994	These effects on the two steps involving the mixed disulfides with glutathione or cystamine accounted for much of the overall catalytic effect of PDI on disulfide bond formation in the peptide, indicating that direct transfer of disulfide bonds from PDI to the peptide occurred less frequently.	Disulfides	51-61	prolyl 4-hydroxylase subunit beta	Homo sapiens	250-253
7516709-8	1994	These effects on the two steps involving the mixed disulfides with glutathione or cystamine accounted for much of the overall catalytic effect of PDI on disulfide bond formation in the peptide, indicating that direct transfer of disulfide bonds from PDI to the peptide occurred less frequently.	Disulfides	51-60	prolyl 4-hydroxylase subunit beta	Homo sapiens	146-149
23188057-1	2013	A new bifunctional compound NCC, which undergoes thiol-mediated disulfide cleavage after cell entry, produces a red-shifted fluorescent emission in the cytosol and releases free active DNA alkylating agent CLB into the nucleus, and finally leads to DNA damage and cell death.	Disulfides	64-73	citramalyl-CoA lyase	Homo sapiens	206-209
23210856-7	2013	The method was applied for assigning the disulfide-bonding network of a recombinant monomer of the HIV envelope protein gp120.	Disulfides	41-50	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	120-125
28495929-1	2017	OBJECTIVE: Coagulation initiation by tissue factor (TF) is regulated by cellular inhibitors, cell surface availability of procoagulant phosphatidylserine, and thiol-disulfide exchange.	Disulfides	165-174	coagulation factor III, tissue factor	Homo sapiens	37-50
28495929-1	2017	OBJECTIVE: Coagulation initiation by tissue factor (TF) is regulated by cellular inhibitors, cell surface availability of procoagulant phosphatidylserine, and thiol-disulfide exchange.	Disulfides	165-174	coagulation factor III, tissue factor	Homo sapiens	52-54
29207620-1	2017	TXNDC5 (thioredoxin domain-containing protein 5) catalyzes disulfide bond formation, isomerization and reduction.	Disulfides	59-68	thioredoxin domain containing 5	Homo sapiens	0-6
29207620-1	2017	TXNDC5 (thioredoxin domain-containing protein 5) catalyzes disulfide bond formation, isomerization and reduction.	Disulfides	59-68	thioredoxin domain containing 5	Homo sapiens	8-47
7516709-8	1994	These effects on the two steps involving the mixed disulfides with glutathione or cystamine accounted for much of the overall catalytic effect of PDI on disulfide bond formation in the peptide, indicating that direct transfer of disulfide bonds from PDI to the peptide occurred less frequently.	Disulfides	51-60	prolyl 4-hydroxylase subunit beta	Homo sapiens	250-253
7516709-8	1994	These effects on the two steps involving the mixed disulfides with glutathione or cystamine accounted for much of the overall catalytic effect of PDI on disulfide bond formation in the peptide, indicating that direct transfer of disulfide bonds from PDI to the peptide occurred less frequently.	Disulfides	153-162	prolyl 4-hydroxylase subunit beta	Homo sapiens	146-149
24348563-2	2013	The main components of this disulfide relay machinery are the oxidoreductase Mia40 and the sulfhydryl oxidase Erv1/ALR.	Disulfides	28-37	growth factor, augmenter of liver regeneration	Homo sapiens	110-114
24348563-2	2013	The main components of this disulfide relay machinery are the oxidoreductase Mia40 and the sulfhydryl oxidase Erv1/ALR.	Disulfides	28-37	growth factor, augmenter of liver regeneration	Homo sapiens	115-118
7516709-8	1994	These effects on the two steps involving the mixed disulfides with glutathione or cystamine accounted for much of the overall catalytic effect of PDI on disulfide bond formation in the peptide, indicating that direct transfer of disulfide bonds from PDI to the peptide occurred less frequently.	Disulfides	153-162	prolyl 4-hydroxylase subunit beta	Homo sapiens	250-253
28316092-7	2017	Administration of cystamine (the disulfide form of cysteamine) in GPRC5A deficient cell lines inhibited gamma-GCS activity, leading to reduction of GSH level and increase of cell growth.	Disulfides	33-42	G protein-coupled receptor, family C, group 5, member A	Mus musculus	66-72
7923754-1	1994	Lipoprotein(a) [Lp(a)] is a plasma macromolecular complex that is assembled from low-density lipoproteins (LDL) and a large hydrophilic glycoprotein, named apolipoprotein(a) [apo(a)], linked by a disulfide bond to apolipoprotein B-100.	Disulfides	196-205	lipoprotein(a)	Homo sapiens	0-14
23326313-1	2013	Gamma-interferon-inducible lysosomal thiol reductase (GILT) is known to reduce disulfide bonds present in proteins internalized by antigen presenting cells, facilitating optimal processing and presentation of peptides on Major Histocompatibility Complex class II molecules, as well as the subsequent activation of CD4-positive T lymphocytes.	Disulfides	79-88	interferon gamma inducible protein 30	Mus musculus	0-52
23326313-1	2013	Gamma-interferon-inducible lysosomal thiol reductase (GILT) is known to reduce disulfide bonds present in proteins internalized by antigen presenting cells, facilitating optimal processing and presentation of peptides on Major Histocompatibility Complex class II molecules, as well as the subsequent activation of CD4-positive T lymphocytes.	Disulfides	79-88	interferon gamma inducible protein 30	Mus musculus	54-58
7923754-1	1994	Lipoprotein(a) [Lp(a)] is a plasma macromolecular complex that is assembled from low-density lipoproteins (LDL) and a large hydrophilic glycoprotein, named apolipoprotein(a) [apo(a)], linked by a disulfide bond to apolipoprotein B-100.	Disulfides	196-205	lipoprotein(a)	Homo sapiens	16-21
23949117-3	2013	Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides.	Disulfides	168-177	thioredoxin domain containing 5	Homo sapiens	121-126
28479060-5	2017	ERdj5 mutants with a fixed-cluster orientation compromised the ERAD enhancement activity, likely because of less-efficient reduction of aberrantly formed disulfide bonds and prevented substrate transfer in the ERdj5-mediated ERAD pathway.	Disulfides	154-163	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	0-5
28479060-6	2017	We propose a significant role of ERdj5 conformational dynamics in ERAD of disulfide-linked oligomers.	Disulfides	74-83	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	33-38
23949117-3	2013	Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides.	Disulfides	238-248	thioredoxin domain containing 5	Homo sapiens	121-126
7923754-1	1994	Lipoprotein(a) [Lp(a)] is a plasma macromolecular complex that is assembled from low-density lipoproteins (LDL) and a large hydrophilic glycoprotein, named apolipoprotein(a) [apo(a)], linked by a disulfide bond to apolipoprotein B-100.	Disulfides	196-205	lipoprotein(a)	Homo sapiens	156-173
23949117-4	2013	Remarkably, the Prx4-dependent formation of native disulfide bonds was accelerated when PDI was combined with ERp46 or P5, suggesting that PDIs work synergistically to increase the rate and fidelity of oxidative protein folding.	Disulfides	51-60	thioredoxin domain containing 5	Homo sapiens	110-115
8180220-1	1994	The disulfide bond location of a homodimeric peptide, prothoracicotropic hormone (PTTH) of the silkworm, Bombyx mori, was determined by a combination of partial reduction and sequence analysis of peptide fragments generated through a partial reduction of PTTH followed by alkylation and enzyme digestion.	Disulfides	4-13	prothoracicotropic hormone	Bombyx mori	255-259
8180220-4	1994	Sequence analysis of the fragments generated by lysyl endopeptidase digestion of this monomeric PTTH after complete reduction and S-alkylation by another S-alkylating reagent showed that only the Cys15 residue was reduced and S-alkylated by the foregoing partial reduction, indicating that this residue formed the interchain disulfide bond.	Disulfides	325-334	prothoracicotropic hormone	Bombyx mori	96-100
22985967-0	2012	Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50 and Arg146 for the reduction of yeast Tsa1 by thioredoxin.	Disulfides	0-9	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	106-110
28194735-6	2017	Since disulfide bond can be selectively cleaved and modified upon methoxy addition, subsequent MS2 CID of the methoxy addition product provides enhanced sequence coverage as demonstrated by the analysis of bovine insulin.	Disulfides	6-15	insulin	Bos taurus	213-220
28573185-3	2017	One approach to promote proper TCR chain pairing involves modifications of the introduced TCR genes: introducing a disulfide bridge, substituting murine for human constant regions, codon optimization, TCR chain leucine zipper fusions, and a single-chain TCR.	Disulfides	115-124	T cell receptor alpha variable 6-3	Mus musculus	31-34
28573185-3	2017	One approach to promote proper TCR chain pairing involves modifications of the introduced TCR genes: introducing a disulfide bridge, substituting murine for human constant regions, codon optimization, TCR chain leucine zipper fusions, and a single-chain TCR.	Disulfides	115-124	T cell receptor alpha variable 6-3	Mus musculus	90-93
28573185-3	2017	One approach to promote proper TCR chain pairing involves modifications of the introduced TCR genes: introducing a disulfide bridge, substituting murine for human constant regions, codon optimization, TCR chain leucine zipper fusions, and a single-chain TCR.	Disulfides	115-124	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	90-93
28573185-3	2017	One approach to promote proper TCR chain pairing involves modifications of the introduced TCR genes: introducing a disulfide bridge, substituting murine for human constant regions, codon optimization, TCR chain leucine zipper fusions, and a single-chain TCR.	Disulfides	115-124	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	90-93
23586953-7	2012	In addition, investigation of TDF by molecular modeling suggests that the Cys residues may form disulfide bridges between Cys17-Cys98 and Cys70-Cys17.	Disulfides	96-105	sex determining region Y	Homo sapiens	30-33
8180220-5	1994	The other disulfide bonds which formed intrachain bridgings were determined by sequence and mass analyses of the fragments generated by two successive enzyme digestions of the monomeric PTTH.	Disulfides	10-19	prothoracicotropic hormone	Bombyx mori	186-190
8180220-6	1994	In conclusion, the disulfide bond location of PTTH was assigned to Cys15-Cys15" as an interchain disulfide linkage and Cys17-Cys54, Cys40-Cys96, and Cys48-Cys98 as intrachain disulfide linkages.	Disulfides	19-28	prothoracicotropic hormone	Bombyx mori	46-50
22807031-4	2012	Here we show that transgenic mice overexpressing disulfide bond A oxidoreductase-like protein in fat (fDsbA-L) exhibited increased levels of total and the high-molecular-weight form of adiponectin compared with wild-type (WT) littermates.	Disulfides	49-58	adiponectin, C1Q and collagen domain containing	Mus musculus	185-196
8180220-6	1994	In conclusion, the disulfide bond location of PTTH was assigned to Cys15-Cys15" as an interchain disulfide linkage and Cys17-Cys54, Cys40-Cys96, and Cys48-Cys98 as intrachain disulfide linkages.	Disulfides	97-106	prothoracicotropic hormone	Bombyx mori	46-50
8180220-6	1994	In conclusion, the disulfide bond location of PTTH was assigned to Cys15-Cys15" as an interchain disulfide linkage and Cys17-Cys54, Cys40-Cys96, and Cys48-Cys98 as intrachain disulfide linkages.	Disulfides	97-106	prothoracicotropic hormone	Bombyx mori	46-50
8157676-0	1994	Disulfide mutants of the binding domain of the rat low affinity nerve growth factor receptor (p75NGFR).	Disulfides	0-9	nerve growth factor receptor	Rattus norvegicus	51-92
23006734-0	2012	cGMP-dependent activation of protein kinase G precludes disulfide activation: implications for blood pressure control.	Disulfides	56-65	protein kinase cGMP-dependent 1	Homo sapiens	29-45
22902630-3	2012	In response to peroxide, Prdx1 catalyzed oxidation of ASK1 to a disulfide-linked multimer, and this occurred via transient formation of a Prdx1-ASK1 mixed disulfide intermediate.	Disulfides	64-73	peroxiredoxin 1	Homo sapiens	25-30
8138569-8	1994	The larger loop connecting TMD3 and TMD4 of both UPIa and UPIb contains six highly conserved cysteine residues; at least one centrally located cysteine doublet in UPIa is involved in forming intramolecular disulfide bridges.	Disulfides	206-215	uroplakin 1B	Bos taurus	58-62
22918950-2	2012	The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins.	Disulfides	80-89	growth factor, augmenter of liver regeneration	Homo sapiens	127-131
22918950-8	2012	Thus Mia40 in cooperation with Erv1 promotes the formation of two disulfide bonds in the substrate protein, ensuring the efficiency of oxidative folding in the intermembrane space of mitochondria.	Disulfides	66-75	growth factor, augmenter of liver regeneration	Homo sapiens	31-35
8137941-0	1994	Localization of disulfide bridges and free sulfhydryl groups in human eosinophil granule major basic protein.	Disulfides	16-25	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	70-108
8131275-1	1994	Lipoprotein(a) [Lp(a)] is a low-density lipoprotein (LDL)-like particle in which apolipoprotein(a) [apo(a)] is disulfide-linked to apolipoprotein B (apoB).	Disulfides	111-120	lipoprotein(a)	Homo sapiens	0-14
22833674-1	2012	NADPH-dependent thioredoxin reductases (NTRs) contain a flavin cofactor and a disulfide as redox-active groups.	Disulfides	78-87	thioredoxin	Homo sapiens	16-27
8131275-1	1994	Lipoprotein(a) [Lp(a)] is a low-density lipoprotein (LDL)-like particle in which apolipoprotein(a) [apo(a)] is disulfide-linked to apolipoprotein B (apoB).	Disulfides	111-120	lipoprotein(a)	Homo sapiens	16-21
8131275-1	1994	Lipoprotein(a) [Lp(a)] is a low-density lipoprotein (LDL)-like particle in which apolipoprotein(a) [apo(a)] is disulfide-linked to apolipoprotein B (apoB).	Disulfides	111-120	lipoprotein(a)	Homo sapiens	81-98
8288048-1	1994	The insulin receptor is synthesized as a single chain of 190 kiloDaltons, which is processed to disulfide-linked mature alpha- and beta- subunits, containing N- and O-linked oligosaccharides and fatty acids.	Disulfides	96-105	insulin receptor	Homo sapiens	4-20
22684915-0	2012	Different inhibitory capacities of human and mouse KLRG1 are linked to distinct disulfide-mediated oligomerizations.	Disulfides	80-89	killer cell lectin-like receptor subfamily G, member 1	Mus musculus	51-56
22684915-4	2012	Biochemical analyses further showed that mKLRG1 formed monomers and disulfide-linked dimers, trimers, and tetramers whereas hKLRG1 was exclusively present as disulfide-linked dimer.	Disulfides	68-77	killer cell lectin-like receptor subfamily G, member 1	Mus musculus	41-47
8187234-1	1994	The protein moiety of Lp[a] is widely believed to consist of one molecule of apo B-100 and one molecule of apo[a] per particle, linked by at least one disulfide bond.	Disulfides	151-160	lipoprotein(a)	Homo sapiens	22-26
22684915-7	2012	Furthermore, mutated mKLRG1 molecules that were unable to form disulfide-linked dimers at all or at a decreased level lacked inhibitory activity.	Disulfides	63-72	killer cell lectin-like receptor subfamily G, member 1	Mus musculus	21-27
22704541-2	2012	We present evidence that disulfide bonds in FXI are reduced to free thiols by oxidoreductases thioredoxin-1 (TRX-1) and protein disulfide isomerase (PDI).	Disulfides	25-34	thioredoxin	Homo sapiens	94-107
22704541-2	2012	We present evidence that disulfide bonds in FXI are reduced to free thiols by oxidoreductases thioredoxin-1 (TRX-1) and protein disulfide isomerase (PDI).	Disulfides	25-34	thioredoxin	Homo sapiens	109-114
7903263-1	1993	Protein disulfide isomerase (PDI) catalyzes the formation of native disulfides of peptide chains from either the reduced form or randomly joined disulfides.	Disulfides	68-78	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
22704541-3	2012	We identified that Cys362-Cys482 and Cys118-Cys147 disulfide bonds are reduced by TRX-1.	Disulfides	51-60	thioredoxin	Homo sapiens	82-87
22760822-11	2012	A mutant with all but one cysteine changed to serine (Cys 247) also showed an enhanced capacity to form complexes with TRX demonstrating, in a pure molecular system, that this particular cysteine is likely responsible for the disulfide bridge between TRX-interacting protein and TRX.	Disulfides	226-235	thioredoxin	Homo sapiens	119-122
22760822-11	2012	A mutant with all but one cysteine changed to serine (Cys 247) also showed an enhanced capacity to form complexes with TRX demonstrating, in a pure molecular system, that this particular cysteine is likely responsible for the disulfide bridge between TRX-interacting protein and TRX.	Disulfides	226-235	thioredoxin	Homo sapiens	251-254
22760822-11	2012	A mutant with all but one cysteine changed to serine (Cys 247) also showed an enhanced capacity to form complexes with TRX demonstrating, in a pure molecular system, that this particular cysteine is likely responsible for the disulfide bridge between TRX-interacting protein and TRX.	Disulfides	226-235	thioredoxin	Homo sapiens	251-254
22761163-0	2012	Relative stabilities of IgG1 and IgG4 Fab domains: influence of the light-heavy interchain disulfide bond architecture.	Disulfides	91-100	FA complementation group B	Homo sapiens	38-41
22761163-6	2012	Introducing the IgG1 type L-H interchain disulfide bond (DSB) into the IgG4 Fab resulted in an increase in thermal stability to levels observed in the IgG1 Fab with the same variable region.	Disulfides	41-50	FA complementation group B	Homo sapiens	76-79
22761163-6	2012	Introducing the IgG1 type L-H interchain disulfide bond (DSB) into the IgG4 Fab resulted in an increase in thermal stability to levels observed in the IgG1 Fab with the same variable region.	Disulfides	41-50	FA complementation group B	Homo sapiens	156-159
7903263-1	1993	Protein disulfide isomerase (PDI) catalyzes the formation of native disulfides of peptide chains from either the reduced form or randomly joined disulfides.	Disulfides	68-78	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
7903263-1	1993	Protein disulfide isomerase (PDI) catalyzes the formation of native disulfides of peptide chains from either the reduced form or randomly joined disulfides.	Disulfides	145-155	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
22422582-8	2012	The native intramolecular disulfide bonds in the insoluble G-CSF aggregates were largely disrupted as shown by mass spectrometry.	Disulfides	26-35	colony stimulating factor 3	Homo sapiens	59-64
7903263-1	1993	Protein disulfide isomerase (PDI) catalyzes the formation of native disulfides of peptide chains from either the reduced form or randomly joined disulfides.	Disulfides	145-155	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
7903263-3	1993	It is suggested that PDI promotes folding of the chains as well as formation of the disulfides and plays a role similar to the chaperones in the folding process.	Disulfides	84-94	prolyl 4-hydroxylase subunit beta	Homo sapiens	21-24
22705624-0	2012	Importance of the disulfide bridges in the antibacterial activity of human hepcidin.	Disulfides	18-27	hepcidin antimicrobial peptide	Homo sapiens	75-83
8245130-6	1993	Recombinant fibulin-2 was produced and secreted by human cell clones as a disulfide-bonded trimer.	Disulfides	74-83	fibulin 2	Homo sapiens	12-21
22700979-5	2012	For the disulfide bond in cVIMP-Cys we determined the reduction potential to -200 mV, and showed it to be a good substrate of thioredoxin.	Disulfides	8-17	thioredoxin	Homo sapiens	126-137
8125062-0	1993	Disulfide linked dimers of apolipoprotein D in urine.	Disulfides	0-9	apolipoprotein D	Homo sapiens	27-43
22481271-8	2012	Under moderate stress, coexpression of WT and conformational variants in HEK-EBNA cells increased the intracellular retention of antithrombin and the formation of disulfide-linked polymers, which correlated with impaired secretion and reduction of anticoagulant activity in the medium.	Disulfides	163-172	serpin family C member 1	Homo sapiens	129-141
8125062-2	1993	This allows the formation of disulfide linked dimers of apoD, a phenomenon that could interfere with the study of the isoforms of apoD.	Disulfides	29-38	apolipoprotein D	Homo sapiens	56-60
22531851-2	2012	In solution, the EC1 protein has been shown to form a covalent dimer via a disulfide bond formation followed by physical aggregation and precipitation.	Disulfides	75-84	Susceptibility to lysis by alloreactive natural killer cells	Homo sapiens	17-20
8125062-2	1993	This allows the formation of disulfide linked dimers of apoD, a phenomenon that could interfere with the study of the isoforms of apoD.	Disulfides	29-38	apolipoprotein D	Homo sapiens	130-134
8125062-5	1993	Thus, we have studied the specificity of our polyclonal antibodies to apoD against the proteins present in normal urine, and at the same time, the existence of dimeric species of apoD linked by disulfide bonds in urine.	Disulfides	194-203	apolipoprotein D	Homo sapiens	179-183
8366073-1	1993	Protein disulfide isomerase (PDI) is a multifunctional protein resident in the lumen of the rough endoplasmic reticulum that facilitates protein folding via disulfide bond isomerization.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
22538198-3	2012	Here, we report the synthesis of a thermally responsive peptide polymer-based hydrogel composed of a recombinant elastin-like polypeptide (ELP) that rapidly forms a reversibly cross-linked hydrogel by the formation of intermolecular disulfide cross-links.	Disulfides	233-242	nuclear receptor subfamily 5 group A member 1	Homo sapiens	113-137
22538198-3	2012	Here, we report the synthesis of a thermally responsive peptide polymer-based hydrogel composed of a recombinant elastin-like polypeptide (ELP) that rapidly forms a reversibly cross-linked hydrogel by the formation of intermolecular disulfide cross-links.	Disulfides	233-242	nuclear receptor subfamily 5 group A member 1	Homo sapiens	139-142
8366073-3	1993	We have now investigated the relationship between the peptide binding site and the ability of PDI to catalyze disulfide bond isomerization.	Disulfides	110-119	prolyl 4-hydroxylase subunit beta	Homo sapiens	94-97
8366073-4	1993	PDI has two identical sequences, -WCGHCK-, that have been demonstrated to be important in PDI-catalyzed disulfide isomerization.	Disulfides	104-113	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-3
8366073-4	1993	PDI has two identical sequences, -WCGHCK-, that have been demonstrated to be important in PDI-catalyzed disulfide isomerization.	Disulfides	104-113	prolyl 4-hydroxylase subunit beta	Homo sapiens	90-93
8366073-6	1993	Moreover, although chemical modification of the 2 cysteines within the thioredoxin-like active site regions completely inhibits PDI-catalyzed disulfide isomerization, these modifications do not affect peptide binding by PDI.	Disulfides	142-151	prolyl 4-hydroxylase subunit beta	Homo sapiens	128-131
22764389-0	2004	(66)Ga-Labeled PEGylated nano-graphene oxide (GO) covalently linked to NOTA-conjugated anti-CD105 (endoglin) chimeric monoclonal antibody TRC105 The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked, homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	207-216	endoglin	Mus musculus	149-154
8366073-11	1993	Based on these findings we conclude that the peptide binding site is located in the COOH-terminal domain of the protein, and it is distinct from the two active sites for PDI-catalyzed disulfide isomerization and from the region of PDI that has estrogen receptor sequence similarity.	Disulfides	184-193	prolyl 4-hydroxylase subunit beta	Homo sapiens	170-173
8366073-11	1993	Based on these findings we conclude that the peptide binding site is located in the COOH-terminal domain of the protein, and it is distinct from the two active sites for PDI-catalyzed disulfide isomerization and from the region of PDI that has estrogen receptor sequence similarity.	Disulfides	184-193	prolyl 4-hydroxylase subunit beta	Homo sapiens	231-234
8366120-8	1993	Using site-directed mutagenesis, we demonstrated that Cys4057 in apo(a) is involved in disulfide linkage with apoB-100 in Lp(a) particles.	Disulfides	87-96	lipoprotein(a)	Homo sapiens	122-127
22741183-0	2004	(66)Ga-Labeled NOTA-conjugated anti-CD105 (endoglin) chimeric monoclonal antibody The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	144-153	endoglin	Mus musculus	36-41
22741183-0	2004	(66)Ga-Labeled NOTA-conjugated anti-CD105 (endoglin) chimeric monoclonal antibody The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	144-153	endoglin	Mus musculus	86-91
22741183-0	2004	(66)Ga-Labeled NOTA-conjugated anti-CD105 (endoglin) chimeric monoclonal antibody The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	144-153	endoglin	Mus musculus	101-109
22705788-4	2012	A trans-dimer homotypic disulfide bond involving Cys367 in K14"s stutter region occurs in the crystal and in skin keratinocytes, where it is concentrated in a keratin filament cage enveloping the nucleus.	Disulfides	24-33	keratin 14	Mus musculus	59-62
8338847-2	1993	Thereby, as is known from comparing the three-dimensional (3D) structures of thioredoxin and glutaredoxin in the reduced and oxidized state, reduction of the disulfide bond is accompanied by minimal perturbation of the backbone folding of the active sites.	Disulfides	158-167	glutaredoxin	Homo sapiens	93-105
22514274-5	2012	Initially, a CP12 conformation characterized by a circular structural motif including the C-terminal disulfide is selected by GAPDH.	Disulfides	101-110	cytochrome P450 family 1 subfamily A member 2	Homo sapiens	13-17
8329391-2	1993	Reduction of the two active-site disulfides in PDI by NADPH and bovine thioredoxin reductase was not reversible by addition of excess NADP+, consistent with a redox potential (E0") above -200 mV.	Disulfides	33-43	prolyl 4-hydroxylase subunit beta	Bos taurus	47-50
8329391-7	1993	Direct transfer of reducing equivalents from PDI to NADP+ via thioredoxin reductase during protein disulfide formation seems unlikely due to the unfavorable equilibrium.	Disulfides	99-108	prolyl 4-hydroxylase subunit beta	Bos taurus	45-48
8329391-7	1993	Direct transfer of reducing equivalents from PDI to NADP+ via thioredoxin reductase during protein disulfide formation seems unlikely due to the unfavorable equilibrium.	Disulfides	99-108	thioredoxin	Bos taurus	62-73
22582951-4	2012	Fusion of Ubc4" with the more stable glutathione-S-transferase domain demonstrates that QSOX can selectively introduce disulfides into the less stable domain of the fusion protein.	Disulfides	119-129	ubiquitin conjugating enzyme E2 D2	Homo sapiens	10-14
8324215-1	1993	Clusterin, a 70-Kd disulfide-linked two-chain plasma glycoprotein circulates in blood as a high-density lipoprotein particle and is highly induced after tissue injury and tissue remodeling.	Disulfides	19-28	clusterin	Homo sapiens	0-9
22326886-3	2012	We find that among the five members of the Grx family and two members of the thioredoxin (Trx) family (Trx1 and Trx2), Grx5 alone interacts with SPT10 via an intermolecular disulfide linkage between Cys60 of Grx5 and Cys385 of SPT10.	Disulfides	173-182	thioredoxin TRX1	Saccharomyces cerevisiae S288C	103-107
22326886-3	2012	We find that among the five members of the Grx family and two members of the thioredoxin (Trx) family (Trx1 and Trx2), Grx5 alone interacts with SPT10 via an intermolecular disulfide linkage between Cys60 of Grx5 and Cys385 of SPT10.	Disulfides	173-182	Spt10p	Saccharomyces cerevisiae S288C	145-150
22326886-6	2012	From this study, we suggest an interaction between Grx5 and SPT10 via intermolecular disulfide linkage and propose a model for a role of Grx5 in the regulation of protein expression under the control of SPT10.	Disulfides	85-94	Spt10p	Saccharomyces cerevisiae S288C	60-65
8324215-5	1993	Clusterin purified from human platelets had the same molecular weight as plasma clusterin under nonreducing conditions and was composed of two disulfide-linked nonidentical subunits of the same size.	Disulfides	143-152	clusterin	Homo sapiens	0-9
8324218-4	1993	Moreover, sequence analysis showed that guanosine-11499 coding for Cys 430 (TGC) in exon VIII was replaced by thymidine in half of the amplified DNAs, resulting in an amino acid change to Phe (TTC) and the destruction of a disulfide bond in the seventh Sushi domain.	Disulfides	223-232	cytochrome c oxidase subunit 8A	Homo sapiens	89-93
22296668-3	2012	The C-terminal FAD-binding domain of Erv1/ALR has an essential role in the import process by creating a transient  intermolecular disulfide bond with Mia40.	Disulfides	130-139	growth factor, augmenter of liver regeneration	Homo sapiens	37-41
22296668-3	2012	The C-terminal FAD-binding domain of Erv1/ALR has an essential role in the import process by creating a transient  intermolecular disulfide bond with Mia40.	Disulfides	130-139	growth factor, augmenter of liver regeneration	Homo sapiens	42-45
8100776-1	1993	CD69 is a disulfide-linked homo-dimer expressed on the surface of activated T cells, B cells, natural killer cells, neutrophils and platelets.	Disulfides	10-19	CD69 molecule	Homo sapiens	0-4
22296668-4	2012	The action of Mia40 is selective for the formation of both intra and intersubunit structural disulfide bonds of Erv1/ALR, but the complete maturation process requires additional binding of FAD.	Disulfides	93-102	growth factor, augmenter of liver regeneration	Homo sapiens	112-116
22296668-4	2012	The action of Mia40 is selective for the formation of both intra and intersubunit structural disulfide bonds of Erv1/ALR, but the complete maturation process requires additional binding of FAD.	Disulfides	93-102	growth factor, augmenter of liver regeneration	Homo sapiens	117-120
8101026-5	1993	Dog osteocalcin contains 49 amino acids, has a molecular mass of 5654 daltons, contains no Thr, Met, Hyp, or Trp, has a disulfide bond between Cys 23 and 29, and is fully gamma-carboxylated at residues 17, 21, and 24.	Disulfides	120-129	bone gamma-carboxyglutamate protein	Canis lupus familiaris	4-15
22124969-4	2012	Using 2D-PAGE and LC-MS/MS we identify a number of intracellular proteins (e.g., protein disulfide isomerise; elongation factor 2; calreticulin) that show a significant change in abundance relative to the general increase in HCP concentration observed with progression of culture.	Disulfides	89-98	calreticulin	Cricetulus griseus	131-143
8461300-9	1993	Thus, thioltransferase (glutaredoxin) appears to be specific for glutathione-containing mixed disulfides.	Disulfides	94-104	glutaredoxin	Homo sapiens	6-22
8461300-9	1993	Thus, thioltransferase (glutaredoxin) appears to be specific for glutathione-containing mixed disulfides.	Disulfides	94-104	glutaredoxin	Homo sapiens	24-36
8461300-10	1993	Apparent TTase catalysis of GSSG formation from the papain- and BSA-SScysteine mixed disulfides was observed by the spectrophotometric assay, but a lag phase occurred consistent with preenzymatic formation of GSScysteine which could serve as the actual TTase substrate.	Disulfides	85-95	glutaredoxin	Homo sapiens	9-14
22182490-3	2012	Evidence from studies in erythrocytes suggests that the activity of GLUT1 is enhanced by the formation of an internal disulfide bond.	Disulfides	118-127	solute carrier family 2 (facilitated glucose transporter), member 1	Mus musculus	68-73
8462142-2	1993	BACKGROUND: Lipoprotein(a) [Lp(a)] is an atherogenic particle that structurally resembles a low density lipoprotein (LDL) particle but contains a molecule of apolipoprotein(a) attached to apolipoprotein B-100 by a disulfide bond.	Disulfides	214-223	lipoprotein(a)	Homo sapiens	12-26
22182490-11	2012	These data suggest that GLUT1 is acutely activated in L929 cells by the formation of a disulfide bond, likely within GLUT1 itself.	Disulfides	87-96	solute carrier family 2 (facilitated glucose transporter), member 1	Mus musculus	24-29
22182490-11	2012	These data suggest that GLUT1 is acutely activated in L929 cells by the formation of a disulfide bond, likely within GLUT1 itself.	Disulfides	87-96	solute carrier family 2 (facilitated glucose transporter), member 1	Mus musculus	117-122
22230366-4	2012	Here, it was demonstrated that PDI and Trx1 have similar gp120 disulfide targets as determined by labeling after reduction, but with some pattern differences, including overall stronger labeling with Trx1 than with PDI.	Disulfides	63-72	thioredoxin	Homo sapiens	39-43
22230366-4	2012	Here, it was demonstrated that PDI and Trx1 have similar gp120 disulfide targets as determined by labeling after reduction, but with some pattern differences, including overall stronger labeling with Trx1 than with PDI.	Disulfides	63-72	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	57-62
22230366-7	2012	Carbohydrate binding agents (CBAs), previously shown to bind gp120 and inhibit HIV entry, were now demonstrated to inhibit gp120 disulfide reduction.	Disulfides	129-138	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	123-128
22265972-2	2012	Despite the overall similarity, we found an extra intermolecular disulfide bond in the lamin B1 coil 2B domain, which does not exist in lamin A/C.	Disulfides	65-74	lamin B1	Homo sapiens	87-95
8462142-2	1993	BACKGROUND: Lipoprotein(a) [Lp(a)] is an atherogenic particle that structurally resembles a low density lipoprotein (LDL) particle but contains a molecule of apolipoprotein(a) attached to apolipoprotein B-100 by a disulfide bond.	Disulfides	214-223	lipoprotein(a)	Homo sapiens	28-33
8440700-1	1993	The unoccupied insulin receptor is a structurally symmetric, disulfide-linked dimer, comprising two alpha beta halves, each with a potential insulin binding alpha subunit and a kinase active beta subunit.	Disulfides	61-70	insulin receptor	Homo sapiens	15-31
22223683-9	2012	Taken together, these findings are consistent with loop cysteines engaging in disulfide bonds that facilitate a Smo conformation that is silent in the absence of Hh, but can transition to a fully active state in response to ligand.	Disulfides	78-87	smoothened, frizzled class receptor	Homo sapiens	112-115
28315746-3	2017	The presence of two disulfide bridges makes difficult to produce functional recombinant PLAC1 in soluble form with high yield.	Disulfides	20-29	placenta enriched 1	Homo sapiens	88-93
7679103-2	1993	In this study, small assembly-competent oligomers of mouse and human keratin 1/keratin 10 keratin filaments were cross-linked by the formation of disulfide bonds catalyzed by the copper-phenanthroline reaction.	Disulfides	146-155	keratin 1	Homo sapiens	69-97
28422167-4	2017	For the biotin-transfer method, ASB is linked to a protein ligand through the sulfhydryl group in a two-step process that allows the introduction of a disulfide bond between the ligand and the crosslinker.	Disulfides	151-160	arylsulfatase B	Homo sapiens	32-35
22248238-1	2012	INTRODUCTION: Nowadays the "redox hypothesis" is based on the fact that thiol/disulfide couples such as glutathione (GSH/GSSG), cysteine (Cys/CySS) and thioredoxin ((Trx-(SH)2/Trx-SS)) are functionally organized in redox circuits controlled by glutathione pools, thioredoxins and other control nodes, and they are not in equilibrium relative to each other.	Disulfides	78-87	thioredoxin	Homo sapiens	152-163
22248238-1	2012	INTRODUCTION: Nowadays the "redox hypothesis" is based on the fact that thiol/disulfide couples such as glutathione (GSH/GSSG), cysteine (Cys/CySS) and thioredoxin ((Trx-(SH)2/Trx-SS)) are functionally organized in redox circuits controlled by glutathione pools, thioredoxins and other control nodes, and they are not in equilibrium relative to each other.	Disulfides	78-87	thioredoxin	Homo sapiens	166-169
22248238-1	2012	INTRODUCTION: Nowadays the "redox hypothesis" is based on the fact that thiol/disulfide couples such as glutathione (GSH/GSSG), cysteine (Cys/CySS) and thioredoxin ((Trx-(SH)2/Trx-SS)) are functionally organized in redox circuits controlled by glutathione pools, thioredoxins and other control nodes, and they are not in equilibrium relative to each other.	Disulfides	78-87	thioredoxin	Homo sapiens	176-179
7678252-8	1993	The amino-terminal region of VN and the thrombin moiety of the TAT complex were found to be responsible for their interaction, which was stabilized by disulfide bridges.	Disulfides	151-160	tyrosine aminotransferase	Homo sapiens	63-66
22015929-1	2012	The human epididymis 4 (HE4) gene product, also known as whey-acidic-protein four-disulfide core domain protein 2, was identified as the transcript expressed in the epididymis and respiratory tract.	Disulfides	82-91	WAP four-disulfide core domain 2	Homo sapiens	24-27
28422167-6	2017	Subsequent reduction of the disulfide bond results in biotin transfer from the ligand to the cell surface receptor.	Disulfides	28-37	CD177 molecule	Homo sapiens	93-114
8424686-2	1993	Mixed disulfide formation of GST-pi in cytosol was prevented by thioltransferase existing in cytosol with a low concentration of GSH.	Disulfides	6-15	glutaredoxin	Homo sapiens	64-80
28138741-3	2017	Hepcidin 1-25 is an interesting model system because this small protein contains four disulfide bridges with a particular connectivity that is difficult to reproduce and could induce a bias in quantification.	Disulfides	86-95	hepcidin antimicrobial peptide	Homo sapiens	0-8
22922528-7	2012	We observed rapid GPVI-dependent Syk-independent ROS generation and disulfide-dependent GPVI homodimerization, but not Syk-dependent ROS or ligand-induced shedding.	Disulfides	68-77	glycoprotein VI platelet	Homo sapiens	88-92
8274532-2	1993	The turbidimetric assay of thioredoxin with insulin as the disulfide substrate was optimized; by incorporation of the lag time (tau) into the calculations, linearity was maintained for a wider range of thioredoxin concentrations, and a distinction could be made between reduced and non-reduced forms.	Disulfides	59-68	thioredoxin	Bos taurus	27-38
21369940-2	2012	It is composed of a specific light chain, xCT, and a heavy chain, 4F2, linked by a disulfide bridge.	Disulfides	83-92	solute carrier family 3 member 2	Homo sapiens	66-69
22782563-5	2012	Removal of a noncritical Cys1-Cys16 disulfide bridge in GVIA or its selenopeptide analog had, as predicted, rather minimal effects on the inhibitory activity on calcium channels, as well as on in vivo activity following intracranial administration.	Disulfides	36-45	cystin 1	Homo sapiens	25-29
22484943-5	2012	Since GMCSF is of mammalian origin and it requires proper disulfide bond formation, we intended to use the baculovirus expression vector system (BEVS) for the expression of the recombinant fusion protein.	Disulfides	58-67	colony stimulating factor 2	Homo sapiens	6-11
22201972-5	2012	It has been suggested recently that protein disulfide isomerase regulates TF decryption through its oxidoreductase activity by targeting Cys186-Cys209 disulfide bond in TF extracellular domain or regulating the PS equilibrium at the plasma membrane.	Disulfides	44-53	coagulation factor III, tissue factor	Homo sapiens	74-76
22201972-5	2012	It has been suggested recently that protein disulfide isomerase regulates TF decryption through its oxidoreductase activity by targeting Cys186-Cys209 disulfide bond in TF extracellular domain or regulating the PS equilibrium at the plasma membrane.	Disulfides	44-53	coagulation factor III, tissue factor	Homo sapiens	169-171
22497150-1	2012	In this study, the tertiary, secondary structures and disulfide bond changes of bovine lactoferrin (bLF) under 6 differents physico-chemical treatments were investigated by fluorescence, circular dichroism(CD) and UV-Vis absorption.	Disulfides	54-63	lactotransferrin	Bos taurus	87-98
28216260-0	2017	Optimal expression of a Fab-effector fusion protein in Escherichia coli by removing the cysteine residues responsible for an interchain disulfide bond of a Fab molecule.	Disulfides	136-145	FA complementation group B	Homo sapiens	24-27
28216260-0	2017	Optimal expression of a Fab-effector fusion protein in Escherichia coli by removing the cysteine residues responsible for an interchain disulfide bond of a Fab molecule.	Disulfides	136-145	FA complementation group B	Homo sapiens	156-159
28216260-6	2017	Our results clearly demonstrated that the genetic linkage of an effector domain to the C-terminus of Fd (VH+CH1) and the removal of cysteine (Cys) residues responsible for an interchain disulfide bond (IDB) ina Fab molecule optimize the periplasmic expression of a Fab-effector fusion protein in E. coli.	Disulfides	186-195	FA complementation group B	Homo sapiens	211-214
28216260-6	2017	Our results clearly demonstrated that the genetic linkage of an effector domain to the C-terminus of Fd (VH+CH1) and the removal of cysteine (Cys) residues responsible for an interchain disulfide bond (IDB) ina Fab molecule optimize the periplasmic expression of a Fab-effector fusion protein in E. coli.	Disulfides	186-195	FA complementation group B	Homo sapiens	265-268
27993722-2	2017	We now describe the conjugation of poly(ethylene glycol)-co-poly(L-glutamic acid) (PEG-PGA) block-co-polymer to AGT via the formation of disulfide bonds between the polymer and solvent-exposed cysteine residues of the enzyme.	Disulfides	137-146	alanine--glyoxylate and serine--pyruvate aminotransferase	Homo sapiens	112-115
28106297-2	2017	Both human alpha defensin type 5 (HD5) and human beta defensin type 3 (hBD-3) have 6 cysteine residues which form 3 pairs of disulfide bonds in oxidizing condition.	Disulfides	125-134	defensin beta 103B	Homo sapiens	49-76
28106297-4	2017	In this project, microsecond long molecular dynamics simulations were performed to study the structure and dynamics of HD5 and hBD-3 wildtype and analogs which have all 3 disulfide bonds released in reducing condition.	Disulfides	171-180	defensin beta 103B	Homo sapiens	127-132
28106297-6	2017	The disulfide bridge breaking order of HD5 and hBD-3 in reducing condition was predicted by two kinds of methods, which gave consistent results.	Disulfides	4-13	defensin beta 103B	Homo sapiens	47-52
28106297-7	2017	It was found that the disulfide bonds breaking pathways for HD5 and hBD-3 are very different.	Disulfides	22-31	defensin beta 103B	Homo sapiens	68-73
28106297-11	2017	For hBD-3, the disulfide breaking is mainly entropy driven, while other factors such as the solvation effects may take the major role in controlling HD5 disulfide breaking pathway.	Disulfides	15-24	defensin beta 103B	Homo sapiens	4-9
28265627-0	2017	Synthesis, structural characterization and conversion of dinuclear iron-sulfur clusters containing the disulfide ligand: [Cp*Fe(mu-eta2:eta2-bdt)(cis-mu-eta1:eta1-S2)FeCp*], [Cp*Fe(mu-S(C6H4S2))(cis-mu-eta1:eta1-S2)FeCp*], and [{Cp*Fe(bdt)}2(trans-mu-eta1:eta1-S2)].	Disulfides	103-112	secreted phosphoprotein 1	Homo sapiens	153-157
28265627-0	2017	Synthesis, structural characterization and conversion of dinuclear iron-sulfur clusters containing the disulfide ligand: [Cp*Fe(mu-eta2:eta2-bdt)(cis-mu-eta1:eta1-S2)FeCp*], [Cp*Fe(mu-S(C6H4S2))(cis-mu-eta1:eta1-S2)FeCp*], and [{Cp*Fe(bdt)}2(trans-mu-eta1:eta1-S2)].	Disulfides	103-112	secreted phosphoprotein 1	Homo sapiens	158-162
28265627-0	2017	Synthesis, structural characterization and conversion of dinuclear iron-sulfur clusters containing the disulfide ligand: [Cp*Fe(mu-eta2:eta2-bdt)(cis-mu-eta1:eta1-S2)FeCp*], [Cp*Fe(mu-S(C6H4S2))(cis-mu-eta1:eta1-S2)FeCp*], and [{Cp*Fe(bdt)}2(trans-mu-eta1:eta1-S2)].	Disulfides	103-112	secreted phosphoprotein 1	Homo sapiens	158-162
28265627-0	2017	Synthesis, structural characterization and conversion of dinuclear iron-sulfur clusters containing the disulfide ligand: [Cp*Fe(mu-eta2:eta2-bdt)(cis-mu-eta1:eta1-S2)FeCp*], [Cp*Fe(mu-S(C6H4S2))(cis-mu-eta1:eta1-S2)FeCp*], and [{Cp*Fe(bdt)}2(trans-mu-eta1:eta1-S2)].	Disulfides	103-112	secreted phosphoprotein 1	Homo sapiens	158-162
28265627-0	2017	Synthesis, structural characterization and conversion of dinuclear iron-sulfur clusters containing the disulfide ligand: [Cp*Fe(mu-eta2:eta2-bdt)(cis-mu-eta1:eta1-S2)FeCp*], [Cp*Fe(mu-S(C6H4S2))(cis-mu-eta1:eta1-S2)FeCp*], and [{Cp*Fe(bdt)}2(trans-mu-eta1:eta1-S2)].	Disulfides	103-112	secreted phosphoprotein 1	Homo sapiens	158-162
28265627-0	2017	Synthesis, structural characterization and conversion of dinuclear iron-sulfur clusters containing the disulfide ligand: [Cp*Fe(mu-eta2:eta2-bdt)(cis-mu-eta1:eta1-S2)FeCp*], [Cp*Fe(mu-S(C6H4S2))(cis-mu-eta1:eta1-S2)FeCp*], and [{Cp*Fe(bdt)}2(trans-mu-eta1:eta1-S2)].	Disulfides	103-112	secreted phosphoprotein 1	Homo sapiens	158-162
28093500-4	2017	Here, we use a novel assay to demonstrate that the reduction in non-native disulfides requires NADPH as the ultimate electron donor, and a robust cytosolic thioredoxin system, driven by thioredoxin reductase 1 (TrxR1 or TXNRD1).	Disulfides	75-85	thioredoxin	Homo sapiens	156-167
28139457-1	2017	Thioredoxins are ubiquitous enzymes catalyzing reversible disulfide-bond formation to regulate structure and function of many proteins in diverse organisms.	Disulfides	58-67	thioredoxin	Homo sapiens	0-12
28011677-9	2017	Failure to improve clinical outcome occurred even though a reduction in VWF multimers was observed, demonstrating that NAC was efficient in reducing disulfide bonds in circulating VWF multimers.	Disulfides	149-158	Von Willebrand factor	Mus musculus	180-183
28003361-3	2017	Structural and biochemical analysis has led to the hypothesis that extracellular TG2 activation involves reduction of an allosteric disulfide bond by thioredoxin-1 (TRX), but cellular and in vivo evidence for this proposal is lacking.	Disulfides	132-141	transglutaminase 2, C polypeptide	Mus musculus	81-84
28003361-9	2017	Our findings support the potential pathophysiological relevance of TRX in celiac disease and establish the Cys370-Cys371 disulfide bond of TG2 as one of clearest examples of an allosteric disulfide bond in mammals.	Disulfides	121-130	transglutaminase 2, C polypeptide	Mus musculus	139-142
28003361-9	2017	Our findings support the potential pathophysiological relevance of TRX in celiac disease and establish the Cys370-Cys371 disulfide bond of TG2 as one of clearest examples of an allosteric disulfide bond in mammals.	Disulfides	188-197	transglutaminase 2, C polypeptide	Mus musculus	139-142
22044596-0	2012	Bioengineering of coagulation factor VIII for efficient  expression through elimination of a dispensable disulfide loop.	Disulfides	105-114	coagulation factor VIII, procoagulant component	Cricetulus griseus	18-41
22911720-6	2012	Our study clearly demonstrated that SAQ is a highly efficient oxidative engine, which shows high efficiency in the de novo disulfide formation and oxygen reduction and that this more efficient oxidative engine is necessary for the highly efficient catalysis of QSOXs compared to Erv1 and Erv2.	Disulfides	123-132	growth factor, augmenter of liver regeneration	Homo sapiens	279-283
22448222-10	2012	Thus, NE and PR3 possess proHNP1 convertase activity that requires the presence of the native HNP1 disulfide motif for high fidelity activation of the precursor in vitro.	Disulfides	99-108	HNP1	Homo sapiens	28-32
22292055-1	2012	Augmenter of Liver Regeneration (ALR) is a sulfhydryl oxidase carrying out fundamental functions facilitating protein disulfide bond formation.	Disulfides	118-127	growth factor, augmenter of liver regeneration (ERV1 homolog, S. cerevisiae)	Danio rerio	0-31
22292055-1	2012	Augmenter of Liver Regeneration (ALR) is a sulfhydryl oxidase carrying out fundamental functions facilitating protein disulfide bond formation.	Disulfides	118-127	growth factor, augmenter of liver regeneration (ERV1 homolog, S. cerevisiae)	Danio rerio	33-36
22107047-0	2011	Atomic force microscopy demonstrates that disulfide bridges are required for clustering of the yeast cell wall integrity sensor Wsc1.	Disulfides	42-51	Slg1p	Saccharomyces cerevisiae S288C	128-132
22107047-4	2011	Here, we used the combination of single-molecule atomic force microscopy (AFM) with genetic manipulations to demonstrate that Wsc1 clustering involves disulfide bridges of the CRD.	Disulfides	151-160	Slg1p	Saccharomyces cerevisiae S288C	126-130
22107047-6	2011	While Wsc1 formed nanoscale clusters on native cells, clustering was no longer observed after treatment with the reducing agent dithiothreitol (DTT), indicating that intra- or intermolecular disulfide bridges are required for clustering.	Disulfides	191-200	Slg1p	Saccharomyces cerevisiae S288C	6-10
27404998-7	2017	We also found that geldanamycin strongly synergises with PX-12, an inhibitor of thioredoxin, suggesting that the processes of L chain refolding and interchain disulfide reduction are strictly coupled.	Disulfides	159-168	thioredoxin	Homo sapiens	80-91
27960051-2	2017	Hence, eukaryotic cells contain protein disulfide bond formation pathways such as the protein disulfide isomerase (PDI)-ER oxidoreductin 1 (Ero1) system in the ER lumen.	Disulfides	40-49	protein disulfide-isomerase	Glycine max	86-113
27960051-2	2017	Hence, eukaryotic cells contain protein disulfide bond formation pathways such as the protein disulfide isomerase (PDI)-ER oxidoreductin 1 (Ero1) system in the ER lumen.	Disulfides	40-49	protein disulfide-isomerase	Glycine max	115-118
27923987-3	2017	Interaction with AtMIA40 is necessary for the phosphatase activity of AtSLP2 and is dependent on the formation of disulfide bridges on AtSLP2.	Disulfides	114-123	Cox19-like CHCH family protein	Arabidopsis thaliana	17-24
7680227-1	1993	The high-affinity receptor for IgE (Fc epsilon RI) has a tetrameric structure structure composed of one alpha, one beta, and two disulfide-linked gamma subunits, of which the alpha subunit binds IgE with high affinity.	Disulfides	129-138	Fc epsilon receptor Ia	Homo sapiens	36-49
27664222-0	2017	A Pap1-Oxs1 signaling pathway for disulfide stress in Schizosaccharomyces pombe.	Disulfides	34-43	phosphatidic acid phosphatase 1	Arabidopsis thaliana	2-6
27664222-1	2017	We describe a Pap1-Oxs1 pathway for diamide-induced disulfide stress in Schizosaccharomyces pombe, where the nucleocytoplasmic HMG protein Oxs1 acts cooperatively with Pap1 to regulate transcription.	Disulfides	52-61	phosphatidic acid phosphatase 1	Arabidopsis thaliana	14-18
27664222-1	2017	We describe a Pap1-Oxs1 pathway for diamide-induced disulfide stress in Schizosaccharomyces pombe, where the nucleocytoplasmic HMG protein Oxs1 acts cooperatively with Pap1 to regulate transcription.	Disulfides	52-61	phosphatidic acid phosphatase 1	Arabidopsis thaliana	168-172
22069028-1	2011	Quiescin sulfhydryl oxidases (QSOXs) catalyze the formation of disulfide bonds in peptides and proteins, and in vertebrates comprise two proteins: QSOX1 and QSOX2.	Disulfides	63-72	quiescin sulfhydryl oxidase 2	Homo sapiens	157-162
22209765-1	2011	Here, we identify Arabidopsis thaliana Lumen Thiol Oxidoreductase1 (LTO1) as a disulfide bond-forming enzyme in the thylakoid lumen.	Disulfides	79-88	NAD(P)H dehydrogenase (quinone)s	Arabidopsis thaliana	68-72
22209765-3	2011	LTO1 can partially substitute for the proteins catalyzing disulfide bond formation in the bacterial periplasm, which is topologically equivalent to the plastid lumen.	Disulfides	58-67	NAD(P)H dehydrogenase (quinone)s	Arabidopsis thaliana	0-4
22209765-7	2011	In a yeast two-hybrid assay, the thioredoxin-like domain of LTO1 interacts with PsbO, a lumenal PSII subunit known to be disulfide bonded, and a recombinant form of the molecule can introduce a disulfide bond in PsbO in vitro.	Disulfides	121-130	NAD(P)H dehydrogenase (quinone)s	Arabidopsis thaliana	60-64
22209765-7	2011	In a yeast two-hybrid assay, the thioredoxin-like domain of LTO1 interacts with PsbO, a lumenal PSII subunit known to be disulfide bonded, and a recombinant form of the molecule can introduce a disulfide bond in PsbO in vitro.	Disulfides	194-203	NAD(P)H dehydrogenase (quinone)s	Arabidopsis thaliana	60-64
29491510-5	2017	Use of our well-established insulin-like peptide synthesis protocol that entails separate solid phase assembly of each of the A- and B-chains with selective cysteine S-protection followed by sequential S-deprotection and simultaneous disulfide bond formation produced DILP2 in good overall yield and high purity.	Disulfides	234-243	Insulin-like peptide 2	Drosophila melanogaster	28-48
1280258-8	1992	The complex of apo(a) with LDL formed both in vivo and in vitro was resistant to boiling in the presence of detergents and denaturants, but was resolved upon disulfide reduction.	Disulfides	158-167	lipoprotein(a)	Homo sapiens	15-21
29491510-5	2017	Use of our well-established insulin-like peptide synthesis protocol that entails separate solid phase assembly of each of the A- and B-chains with selective cysteine S-protection followed by sequential S-deprotection and simultaneous disulfide bond formation produced DILP2 in good overall yield and high purity.	Disulfides	234-243	Insulin-like peptide 2	Drosophila melanogaster	268-273
29463951-2	2017	HLA-B*27 heavy chain (B27-HC) has an intrinsic propensity to fold slowly, leading to the accumulation of the misfolded B27-HC in the endoplasmic reticulum (ER) and formation of the HLA-B*27 HC homodimer, (B27-HC)2, by a disulfide linkage at Cys-67.	Disulfides	220-229	major histocompatibility complex, class I, B	Homo sapiens	0-8
21862690-5	2011	Protein sequence comparison among zebrafish GPR81s, mammalian GPR81s, GPR109a, and GPR109b identified a common structure (six Cys residues at the extracellular domains that potentially form three disulfide bonds) in this subfamily of receptors.	Disulfides	196-205	hydroxycarboxylic acid receptor 3	Homo sapiens	83-90
21704743-3	2011	With a disulfide bond formed between the two catalytic cysteines, Trx1 is not only inactive as a denitrosylase, but it may also be nitrosylated at Cys73 and serve as a transnitrosylating agent.	Disulfides	7-16	thioredoxin	Homo sapiens	66-70
29463951-2	2017	HLA-B*27 heavy chain (B27-HC) has an intrinsic propensity to fold slowly, leading to the accumulation of the misfolded B27-HC in the endoplasmic reticulum (ER) and formation of the HLA-B*27 HC homodimer, (B27-HC)2, by a disulfide linkage at Cys-67.	Disulfides	220-229	major histocompatibility complex, class I, B	Homo sapiens	0-5
1479288-0	1992	Characterization of disulfide-linked heterodimers containing apolipoprotein D in human plasma lipoproteins.	Disulfides	20-29	apolipoprotein D	Homo sapiens	61-77
21865601-3	2011	Its import into the IMS depends on the Mia40/Erv1 disulfide relay system, although Ccs1 is, in contrast to typical substrates, a multidomain protein and lacks twin Cx(n)C motifs.	Disulfides	50-59	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	45-49
21865601-8	2011	We conclude that the Mia40/Erv1 disulfide relay system introduces a structural disulfide bond in Ccs1 between the cysteine residues C27 and C64, thereby promoting mitochondrial import of this unconventional substrate.	Disulfides	32-41	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	27-31
21865601-8	2011	We conclude that the Mia40/Erv1 disulfide relay system introduces a structural disulfide bond in Ccs1 between the cysteine residues C27 and C64, thereby promoting mitochondrial import of this unconventional substrate.	Disulfides	79-88	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	27-31
21771788-2	2011	Here, ZPR9 was found to physically interact with apoptosis signal-regulating kinase 1 (ASK1) through a disulfide linkage involving Cys(1351) and Cys(1360) of ASK1 and Cys(305) and Cys(308) of ZPR9.	Disulfides	103-112	mitogen-activated protein kinase kinase kinase 5	Mus musculus	49-85
27770617-5	2016	Conjugate 18, containing a disulfide bond, exhibited the most potent anti-proliferative and DHFR inhibitory effects (IC50=4.1muM and 17.21nM, respectively).	Disulfides	27-36	dihydrofolate reductase	Homo sapiens	92-96
1479288-4	1992	Only the 29,000 M(r) band corresponding to apoD remained when the electrophoresis was conducted under reducing conditions, demonstrating that apoD is cross-linked to other proteins via disulfide bonds.	Disulfides	185-194	apolipoprotein D	Homo sapiens	43-47
27983990-0	2016	Selective disulfide reduction for labeling and enhancement of Fab antibody fragments.	Disulfides	10-19	FA complementation group B	Homo sapiens	62-65
27983990-5	2016	Here, a simple and efficient selective reduction of the single disulfide bond linking the partial heavy chain and the intact light chain which compose the Fab fragment is accomplished utilizing tris(2-carboxyethyl)phosphine (TCEP) immobilized on agarose beads.	Disulfides	63-72	FA complementation group B	Homo sapiens	155-158
21771788-2	2011	Here, ZPR9 was found to physically interact with apoptosis signal-regulating kinase 1 (ASK1) through a disulfide linkage involving Cys(1351) and Cys(1360) of ASK1 and Cys(305) and Cys(308) of ZPR9.	Disulfides	103-112	mitogen-activated protein kinase kinase kinase 5	Mus musculus	87-91
21771788-2	2011	Here, ZPR9 was found to physically interact with apoptosis signal-regulating kinase 1 (ASK1) through a disulfide linkage involving Cys(1351) and Cys(1360) of ASK1 and Cys(305) and Cys(308) of ZPR9.	Disulfides	103-112	mitogen-activated protein kinase kinase kinase 5	Mus musculus	158-162
21778880-3	2011	RECENT FINDINGS: TF contains a solvent-exposed allosteric disulfide bond that stabilizes the carboxyl-terminal domain involved in ligand interactions with coagulation factors VIIa and X.	Disulfides	58-67	coagulation factor III, tissue factor	Homo sapiens	17-19
21778880-4	2011	PDI is a prime candidate to modify the allosteric disulfide by reduction, S-nitrosylation and glutathionation, implicated as regulators of TF procoagulant activity.	Disulfides	50-59	coagulation factor III, tissue factor	Homo sapiens	139-141
1479288-4	1992	Only the 29,000 M(r) band corresponding to apoD remained when the electrophoresis was conducted under reducing conditions, demonstrating that apoD is cross-linked to other proteins via disulfide bonds.	Disulfides	185-194	apolipoprotein D	Homo sapiens	142-146
21593161-0	2011	Disulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation.	Disulfides	0-9	capsid portal protein	Human alphaherpesvirus 1	55-58
27869701-0	2016	The Role of Individual Disulfide Bonds of mu-Conotoxin GIIIA in the Inhibition of NaV1.4.	Disulfides	23-32	sodium voltage-gated channel alpha subunit 4	Homo sapiens	82-88
1479288-10	1992	Disulfide-linked heterodimers of apoD and apoB-100 were also found in low and very low density lipoproteins, and in whole plasma.	Disulfides	0-9	apolipoprotein D	Homo sapiens	33-37
1479288-11	1992	It is concluded that a fraction of human apoD, like other cysteine-containing apolipoproteins, exists as a disulfide-linked heterodimer with other apolipoproteins in all major human lipoprotein fractions.	Disulfides	107-116	apolipoprotein D	Homo sapiens	41-45
27739308-7	2016	The role of the secondary binding site in assembling the DUSP5-pERK pre-reactive complex was further demonstrated by molecular dynamics simulations that showed that the remote C197-C219 disulfide linkage controls the structure of the secondary binding pocket based on its redox state (i.e., disulfide/dithiol) and, in turn, the enzymatic activity of DUSP5.	Disulfides	186-195	eukaryotic translation initiation factor 2 alpha kinase 3	Homo sapiens	63-67
27739308-7	2016	The role of the secondary binding site in assembling the DUSP5-pERK pre-reactive complex was further demonstrated by molecular dynamics simulations that showed that the remote C197-C219 disulfide linkage controls the structure of the secondary binding pocket based on its redox state (i.e., disulfide/dithiol) and, in turn, the enzymatic activity of DUSP5.	Disulfides	291-300	eukaryotic translation initiation factor 2 alpha kinase 3	Homo sapiens	63-67
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	Disulfides	93-102	xanthine dehydrogenase	Homo sapiens	0-3
21594273-2	2011	Mechanisms associated with cysteine oxidation to form sulfenic acid and disulfides (i.e., cystine and glutathione adducts), and their reversibility through thioredoxin-dependent mechanisms, are broadly appreciated as important regulatory mechanisms that control the function of a range of different proteins.	Disulfides	72-82	thioredoxin	Homo sapiens	156-167
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	Disulfides	93-102	xanthine dehydrogenase	Homo sapiens	166-169
1328233-6	1992	XDH can be converted back to the XO form by the addition of three to four equivalents of the disulfide-forming reagent 4,4"-dithiodipyridine, suggesting that, in the XDH form of the enzyme, disulfide bonds are broken; this may cause a conformational change which creates a binding site for NAD and changes the protein structure near the flavin.	Disulfides	190-199	xanthine dehydrogenase	Homo sapiens	0-3
27717282-3	2016	Herein, a multi-responsive "turn-on" polyelectrolyte complex (DNA/OEI-SSx /HA-SS-COOH, DSS) delivery system is demonstrated with a sequential self-assembly of disulfide-conjugated oligoethylenimine (OEI-SSx ) and disulfide bond-modified hyaluronic acid envelope (HA-SS-COOH) that can combat multiple biological barriers collectively when administered intravenously.	Disulfides	159-168	SSX family member 2B	Homo sapiens	70-73
1400449-8	1992	Both cysteine-rich subdomains of this mucin have sequence similarity with von Willebrand factor, a serum protein that exists as a disulfide-linked polymer.	Disulfides	130-139	LOC100508689	Homo sapiens	38-43
27717282-3	2016	Herein, a multi-responsive "turn-on" polyelectrolyte complex (DNA/OEI-SSx /HA-SS-COOH, DSS) delivery system is demonstrated with a sequential self-assembly of disulfide-conjugated oligoethylenimine (OEI-SSx ) and disulfide bond-modified hyaluronic acid envelope (HA-SS-COOH) that can combat multiple biological barriers collectively when administered intravenously.	Disulfides	159-168	SSX family member 2B	Homo sapiens	203-206
27717282-3	2016	Herein, a multi-responsive "turn-on" polyelectrolyte complex (DNA/OEI-SSx /HA-SS-COOH, DSS) delivery system is demonstrated with a sequential self-assembly of disulfide-conjugated oligoethylenimine (OEI-SSx ) and disulfide bond-modified hyaluronic acid envelope (HA-SS-COOH) that can combat multiple biological barriers collectively when administered intravenously.	Disulfides	213-222	SSX family member 2B	Homo sapiens	70-73
21524995-6	2011	Remarkably, the engineered CD38 exhibited the ability to form the critical disulfide linkages required for its enzymatic activity.	Disulfides	75-84	CD38 molecule	Homo sapiens	27-31
21524995-9	2011	The engineered CD38 is thus a novel example challenging the general belief that cytosolic proteins do not possess disulfides.	Disulfides	114-124	CD38 molecule	Homo sapiens	15-19
21689404-4	2011	We have previously stabilized soluble trimeric mimics of Env by introducing a disulfide bond between gp120 and gp41 and adding a trimer stabilizing mutation in gp41 (SOSIP.R6 gp140).	Disulfides	78-87	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	101-106
1456954-0	1992	Reduction of nitrofuran compounds by heart lipoamide dehydrogenase: role of flavin and the reactive disulfide groups.	Disulfides	100-109	dihydrolipoamide dehydrogenase	Homo sapiens	43-66
21545152-1	2011	Phage panning led to the discovery of a disulfide-cyclized peptide CRYPEVEIC that inhibits Pin1 activity with a K(I) of 0.5 muM.	Disulfides	40-49	peptidylprolyl cis/trans isomerase, NIMA-interacting 1	Homo sapiens	91-95
21384150-2	2011	In a previous study, we showed that the cytokine-releasing activity of extracellular TCTP is generated only when TCTP dimerizes via the intermolecular disulfide bond of NH(2)-terminal truncated TCTP implying that the dimerized TCTP (dTCTP) promotes the inflammatory phenomena.	Disulfides	151-160	tumor protein, translationally-controlled 1	Homo sapiens	85-89
21384150-2	2011	In a previous study, we showed that the cytokine-releasing activity of extracellular TCTP is generated only when TCTP dimerizes via the intermolecular disulfide bond of NH(2)-terminal truncated TCTP implying that the dimerized TCTP (dTCTP) promotes the inflammatory phenomena.	Disulfides	151-160	tumor protein, translationally-controlled 1	Homo sapiens	113-117
21384150-2	2011	In a previous study, we showed that the cytokine-releasing activity of extracellular TCTP is generated only when TCTP dimerizes via the intermolecular disulfide bond of NH(2)-terminal truncated TCTP implying that the dimerized TCTP (dTCTP) promotes the inflammatory phenomena.	Disulfides	151-160	tumor protein, translationally-controlled 1	Homo sapiens	113-117
21384150-2	2011	In a previous study, we showed that the cytokine-releasing activity of extracellular TCTP is generated only when TCTP dimerizes via the intermolecular disulfide bond of NH(2)-terminal truncated TCTP implying that the dimerized TCTP (dTCTP) promotes the inflammatory phenomena.	Disulfides	151-160	tumor protein, translationally-controlled 1	Homo sapiens	113-117
27179418-9	2016	Cys104 and Cys243 form a redox-dependent disulfide bridge between the PGP catalytic core and cap domains, which may impair the open/close-dynamics of the catalytic cycle.	Disulfides	41-50	phosphoglycolate phosphatase	Homo sapiens	70-73
27273301-1	2016	Bovine alpha-lactalbumin (alpha-La) is a major food allergen found in milk and is characterized by high conformational stability because of its four disulfide bridges and being calcium bound.	Disulfides	149-158	lactalbumin alpha	Bos taurus	7-24
27273301-1	2016	Bovine alpha-lactalbumin (alpha-La) is a major food allergen found in milk and is characterized by high conformational stability because of its four disulfide bridges and being calcium bound.	Disulfides	149-158	lactalbumin alpha	Bos taurus	26-34
27346342-3	2016	Conversely, the nuclease activity of CPS-6 is enhanced, and its dimeric structure is stabilized by its interaction with the worm AIF homolog, WAH-1, which shifts to disulfide cross-linked dimers under high ROS levels.	Disulfides	165-174	Endonuclease G, mitochondrial	Caenorhabditis elegans	37-42
1390715-0	1992	Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14----S) and its mixed disulfide with glutathione.	Disulfides	112-121	glutaredoxin	Homo sapiens	74-86
27117233-0	2016	An intramolecular disulfide bond designed in myoglobin fine-tunes both protein structure and peroxidase activity.	Disulfides	18-27	myoglobin	Homo sapiens	45-54
21456627-1	2011	A new type of biodegradable micelles for glutathione-mediated intracellular drug delivery was developed on the basis of an amphiphilic hyperbranched multiarm copolymer (H40-star-PLA-SS-PEP) with disulfide linkages between the hydrophobic polyester core and hydrophilic polyphosphate arms.	Disulfides	195-204	progestagen associated endometrial protein	Homo sapiens	185-188
1390715-2	1992	In Escherichia coli glutaredoxin, the active site contains a redox-active disulfide/dithiol of the sequence Cys11-Pro12-Tyr13-Cys14.	Disulfides	74-83	glutaredoxin	Homo sapiens	20-32
1390715-3	1992	In this paper, we have prepared and characterized the Cys14----Ser mutant of E. coli glutaredoxin and its mixed disulfide with glutathione.	Disulfides	112-121	glutaredoxin	Homo sapiens	85-97
21377473-0	2011	Refined crystal structures of human Ca(2+)/Zn(2+)-binding S100A3 protein characterized by two disulfide bridges.	Disulfides	94-103	S100 calcium binding protein A3	Homo sapiens	58-64
21377473-4	2011	We identified two previously undocumented disulfide bridges in the crystal structure of properly folded S100A3: one disulfide bridge is between Cys30 in the N-terminal pseudo-EF-hand and Cys68 in the C-terminal EF-hand (SS1), and another disulfide bridge attaches Cys99 in the C-terminal coil structure to Cys81 in helix IV (SS2).	Disulfides	42-51	S100 calcium binding protein A3	Homo sapiens	104-110
25911959-2	2016	In vitro, thioredoxin reduces this disulfide and thioredoxin reductase (TrxR) is part of a cytosolic complex facilitating DTA-translocation.	Disulfides	35-44	thioredoxin	Homo sapiens	10-21
1390715-5	1992	The covalent structure of the mixed disulfide of glutaredoxin(C14S) with GSH prepared with 15N-labeling of the protein was confirmed with nuclear magnetic resonance (NMR) spectroscopy, establishing a basis for NMR structural studies of the glutathione binding site on glutaredoxin.	Disulfides	36-45	glutaredoxin	Homo sapiens	49-61
21377473-4	2011	We identified two previously undocumented disulfide bridges in the crystal structure of properly folded S100A3: one disulfide bridge is between Cys30 in the N-terminal pseudo-EF-hand and Cys68 in the C-terminal EF-hand (SS1), and another disulfide bridge attaches Cys99 in the C-terminal coil structure to Cys81 in helix IV (SS2).	Disulfides	116-125	S100 calcium binding protein A3	Homo sapiens	104-110
21521879-4	2011	Oxidized CRMP2 then formed a transient disulfide-linked complex with TRX, which stimulated CRMP2 phosphorylation by glycogen synthase kinase-3, leading to growth cone collapse.	Disulfides	39-48	thioredoxin	Homo sapiens	69-72
1390715-5	1992	The covalent structure of the mixed disulfide of glutaredoxin(C14S) with GSH prepared with 15N-labeling of the protein was confirmed with nuclear magnetic resonance (NMR) spectroscopy, establishing a basis for NMR structural studies of the glutathione binding site on glutaredoxin.	Disulfides	36-45	glutaredoxin	Homo sapiens	268-280
27107845-0	2016	ERAP1 reduces accumulation of aberrant and disulfide-linked forms of HLA-B27 on the cell surface.	Disulfides	43-52	endoplasmic reticulum aminopeptidase 1	Homo sapiens	0-5
1390644-1	1992	The Cys-71-Cys-81 disulfide bond of the cysteine proteinase inhibitor, chicken cystatin, was specifically reduced by thioredoxin or low concentrations of dithiothreitol.	Disulfides	18-27	thioredoxin	Gallus gallus	117-128
27107845-0	2016	ERAP1 reduces accumulation of aberrant and disulfide-linked forms of HLA-B27 on the cell surface.	Disulfides	43-52	major histocompatibility complex, class I, B	Homo sapiens	69-76
27107845-2	2016	The aim of this study was to determine whether reduced ERAP1 expression would alter the cell surface expression of HLA-B27 and the formation of aberrant disulfide-linked forms that have been implicated in the pathogenesis of spondyloarthritis.	Disulfides	153-162	endoplasmic reticulum aminopeptidase 1	Homo sapiens	55-60
1387699-1	1992	Lipoprotein(a) or Lp(a), is a member of the plasma lipoproteins with general properties of LDL but with a protein moiety represented by apoB100 disulfide linked to apolipoprotein(a) or apo(a).	Disulfides	144-153	lipoprotein(a)	Homo sapiens	18-23
27107845-5	2016	Cell surface expression of aberrant disulfide-linked HLA-B27 dimers was assessed by immunoprecipitation and electrophoresis on non-reducing polyacrylamide gels.	Disulfides	36-45	major histocompatibility complex, class I, B	Homo sapiens	53-60
27107845-6	2016	RESULTS: ERAP1 knockdown increased the accumulation of HLA-B27 on the cell surface including disulfide-linked dimers, but had no effect on levels of HLA-B18 or -B51.	Disulfides	93-102	endoplasmic reticulum aminopeptidase 1	Homo sapiens	9-14
27107845-6	2016	RESULTS: ERAP1 knockdown increased the accumulation of HLA-B27 on the cell surface including disulfide-linked dimers, but had no effect on levels of HLA-B18 or -B51.	Disulfides	93-102	major histocompatibility complex, class I, B	Homo sapiens	55-62
27107845-8	2016	IFN-gamma treatment resulted in striking increases in the expression of disulfide-linked HLA-B27 heavy chains, even in cells with normal ERAP1 expression.	Disulfides	72-81	major histocompatibility complex, class I, B	Homo sapiens	89-96
27107845-9	2016	CONCLUSIONS: Our results suggest that normal levels of ERAP1 reduce the accumulation of aberrant and disulfide-linked forms of HLA-B27 in monocytes, and thus help to maintain the integrity of cell surface HLA-B27 complexes.	Disulfides	101-110	endoplasmic reticulum aminopeptidase 1	Homo sapiens	55-60
27107845-9	2016	CONCLUSIONS: Our results suggest that normal levels of ERAP1 reduce the accumulation of aberrant and disulfide-linked forms of HLA-B27 in monocytes, and thus help to maintain the integrity of cell surface HLA-B27 complexes.	Disulfides	101-110	major histocompatibility complex, class I, B	Homo sapiens	127-134
27242425-2	2016	In the brain, activin A, which is formed by two disulfide-linked betaA subunits, is recognized as the predominant player in activin signaling.	Disulfides	48-57	inhibin subunit beta E	Homo sapiens	14-21
27242425-2	2016	In the brain, activin A, which is formed by two disulfide-linked betaA subunits, is recognized as the predominant player in activin signaling.	Disulfides	48-57	inhibin subunit beta E	Homo sapiens	124-131
21391620-7	2011	The two disulfide-linked conjugates, mAb-SPP-[(3)H]DM1 and mAb-SPDB-[(3)H]DM4, were also found to be catabolized to the analogous lysine-linked maytansinoid metabolites.	Disulfides	8-17	immunoglobulin heavy diversity 1-7	Homo sapiens	51-54
20969481-0	2011	Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase.	Disulfides	100-109	vitamin K epoxide reductase complex subunit 1	Homo sapiens	72-76
20969481-1	2011	We have presented evidence that a homologue of vertebrate membrane protein vitamin K epoxide reductase (VKOR) is an important component of the protein disulfide bond-forming pathway in many bacteria.	Disulfides	151-160	vitamin K epoxide reductase complex subunit 1	Homo sapiens	75-102
20969481-1	2011	We have presented evidence that a homologue of vertebrate membrane protein vitamin K epoxide reductase (VKOR) is an important component of the protein disulfide bond-forming pathway in many bacteria.	Disulfides	151-160	vitamin K epoxide reductase complex subunit 1	Homo sapiens	104-108
1412217-8	1992	The 40 kDa form is a heterodimer of TFPI in covalent disulfide linkage to human apolipoprotein AII.	Disulfides	53-62	tissue factor pathway inhibitor	Homo sapiens	36-40
21425467-5	2011	Using alkyne-azide click chemistry, PEG(Alk)/PMA multilayers are crosslinked with a bisazide linker that contains a disulfide bond, rendering these films and capsules redox-responsive.	Disulfides	116-125	progestagen associated endometrial protein	Homo sapiens	36-39
26945066-0	2016	Oxidant-induced Interprotein Disulfide Formation in Cardiac Protein DJ-1 Occurs via an Interaction with Peroxiredoxin 2.	Disulfides	29-38	Parkinsonism associated deglycase	Homo sapiens	60-72
26945066-2	2016	H2O2 induces a 50-kDa DJ-1 interprotein homodimer disulfide, known to form between Cys-53 on each subunit.	Disulfides	50-59	Parkinsonism associated deglycase	Homo sapiens	22-26
26945066-3	2016	A trimeric 75-kDa DJ-1 complex that mass spectrometry shows contained 2-Cys peroxiredoxin also formed and precedes the appearance of the disulfide dimer.	Disulfides	137-146	Parkinsonism associated deglycase	Homo sapiens	18-22
26945066-5	2016	The dimeric disulfide DJ-1 complex was stabilized by auranofin, suggesting that thioredoxin recycles it in cells.	Disulfides	12-21	Parkinsonism associated deglycase	Homo sapiens	22-26
26945066-5	2016	The dimeric disulfide DJ-1 complex was stabilized by auranofin, suggesting that thioredoxin recycles it in cells.	Disulfides	12-21	thioredoxin	Homo sapiens	80-91
1386254-1	1992	NMR experiments show that a stable complex can be formed between a 14-base-pair oligonucleotide and a disulfide-bonded dimer of a peptide containing 27 residues of the basic region of the yeast transcriptional activator GCN4; the complex is in slow exchange on the NMR time scale.	Disulfides	102-111	amino acid starvation-responsive transcription factor GCN4	Saccharomyces cerevisiae S288C	220-224
26945066-8	2016	DJ-1 also forms multiple disulfides with unknown target proteins during H2O2 treatment, the formation of which is also potentiated in cells expressing the C53A mutant.	Disulfides	25-35	Parkinsonism associated deglycase	Homo sapiens	0-4
26945066-11	2016	Nonetheless, expression of the DJ-1 C106A mutant, which fully prevents hyperoxidation, also showed exacerbated cell death responses to H2O2 A rational explanation for these findings is that DJ-1 Cys-106 forms disulfides with target proteins to limit oxidant-induced cell death.	Disulfides	209-219	Parkinsonism associated deglycase	Homo sapiens	31-35
26945066-11	2016	Nonetheless, expression of the DJ-1 C106A mutant, which fully prevents hyperoxidation, also showed exacerbated cell death responses to H2O2 A rational explanation for these findings is that DJ-1 Cys-106 forms disulfides with target proteins to limit oxidant-induced cell death.	Disulfides	209-219	Parkinsonism associated deglycase	Homo sapiens	190-194
26780347-6	2016	Moreover, we have reported that three kinds of oxidative stress, ultraviolet light-induced stress, osmotic stress and arsenic-induced stress, modulate kinase activity of RET-PTC1 without an extracellular domain as well as c-RET by conformational change of RET protein (dimerization) via disulfide bond formation.	Disulfides	287-296	ret proto-oncogene	Homo sapiens	170-173
21384867-1	2011	Relaxin-3 is a two-chain disulfide-rich peptide that is the ancestral member of the relaxin peptide family and, together with its G protein-coupled receptor RXFP3, is highly expressed in the brain.	Disulfides	25-34	relaxin 3	Rattus norvegicus	0-9
21439478-4	2011	A series of hepcidin mutants in which disulfide bonds were replaced with diselenide bonds showed no change in activity compared to native hepcidin.	Disulfides	38-47	hepcidin antimicrobial peptide	Homo sapiens	12-20
1353499-3	1992	During the first 15 min after biosynthesis, Tg is found in transient aggregates with and without interchain disulfide bonds, which precede the formation of free monomers (and ultimately dimers) within the ER.	Disulfides	108-117	thyroglobulin	Homo sapiens	44-46
20978134-8	2011	These results indicate a role for Cys-43 and Cys-51 in catalysis, suggesting a relay mechanism in which a redox protein transfers electrons to these loop residues, which in turn reduce the membrane-embedded Cys132-Cys135 disulfide bond to activate VKOR.	Disulfides	221-230	vitamin K epoxide reductase complex subunit 1	Homo sapiens	248-252
1353499-5	1992	Much of the Tg released from BiP by the addition of Mg-ATP was found in aggregates containing interchain disulfide bonds; other BiP-associated Tg represented non-covalent aggregates and unfolded free monomers.	Disulfides	105-114	thyroglobulin	Homo sapiens	12-14
27064346-3	2016	The activity of Rubisco is controlled in response to changes in irradiance by regulation of RCA activity, which is known to involve a redox-sensitive disulfide bond located in the carboxy-terminal extension of the RCAalpha subunit.	Disulfides	150-159	rubisco activase	Arabidopsis thaliana	92-95
1534588-2	1992	Lipoprotein(a) (Lp[a]) can be defined as a lipoprotein particle having as a protein moiety apolipoprotein B-100 (the protein associated with low-density lipoprotein) disulfide-linked to apolipoprotein(a), the distinctive glycoprotein of Lp(a) that is homologous to plasminogen.	Disulfides	166-175	lipoprotein(a)	Homo sapiens	0-14
26801181-6	2016	We expressed DLL1 proteins with mutations disrupting disulfide bridges in each individual EGF repeat from single-copy transgenes in the HPRT locus of embryonic stem cells.	Disulfides	53-62	delta like canonical Notch ligand 1	Mus musculus	13-17
26861293-2	2016	Both characteristic types of eukaryotic ferritin subunits are present in secreted ferritins from insects, but here dimers between Ferritin 1 Heavy Chain Homolog (Fer1HCH) and Ferritin 2 Light Chain Homolog (Fer2LCH) are further stabilized by disulfide-bridge in the 24-subunit complex.	Disulfides	242-251	Ferritin 2 light chain homologue	Drosophila melanogaster	175-197
26861293-2	2016	Both characteristic types of eukaryotic ferritin subunits are present in secreted ferritins from insects, but here dimers between Ferritin 1 Heavy Chain Homolog (Fer1HCH) and Ferritin 2 Light Chain Homolog (Fer2LCH) are further stabilized by disulfide-bridge in the 24-subunit complex.	Disulfides	242-251	Ferritin 2 light chain homologue	Drosophila melanogaster	207-214
26795153-4	2016	Thiol-disulfide redox regulation is dependent on the conserved redox proteins, glutathione/glutaredoxin (GRX) and thioredoxin (TRX) systems.	Disulfides	6-15	thioredoxin	Homo sapiens	114-125
26795153-4	2016	Thiol-disulfide redox regulation is dependent on the conserved redox proteins, glutathione/glutaredoxin (GRX) and thioredoxin (TRX) systems.	Disulfides	6-15	thioredoxin	Homo sapiens	127-130
20537978-4	2011	Mia40 is maintained in an oxidized, active conformation by the sulfhydryl oxidase Erv1, a homodimeric flavoenzyme, which can form disulfide bonds de novo.	Disulfides	130-139	growth factor, augmenter of liver regeneration	Homo sapiens	82-86
21215271-0	2011	Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation.	Disulfides	96-105	peptidyl arginine deiminase 1	Homo sapiens	26-29
20884319-0	2011	Disulfide bonds of phospholipase A2 from bee venom yield discrete contributions to its conformational stability.	Disulfides	0-9	LOC104974671	Bos taurus	19-35
21036950-8	2011	This study is the first in vitro observation indicating that glutaredoxin and thioredoxin in human liver are active in reducing the mixed disulfide formed between xenobiotics and glutathione.	Disulfides	138-147	thioredoxin	Homo sapiens	78-89
21117239-5	2011	These findings collectively support the hypothesis that the disulfide stitch shifts the conformational distribution of alpha1 to the unfolded state, meaning an unfolded alpha1 is not a strict requirement of the b12-bound conformational ensemble of gp120"s lacking the I109C/Q428C stitch.	Disulfides	60-69	adrenoceptor alpha 1D	Homo sapiens	119-125
26816344-2	2016	During entry, reduction of disulfide bridges in the viral envelope glycoprotein gp120 by cellular oxidoreductases is crucial.	Disulfides	27-36	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	80-85
1535625-1	1992	The high affinity IgE receptor (Fc epsilon RI) is a tetrameric hetero-oligomer composed of an alpha chain, a beta chain, and two disulfide-linked gamma chains.	Disulfides	129-138	Fc epsilon receptor Ia	Homo sapiens	32-45
21131979-0	2011	beta2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.	Disulfides	80-89	beta-2-microglobulin	Homo sapiens	0-19
1567868-3	1992	Available data indicate that the two thiol/disulfide centers of PDI can function independently in the isomerase reaction and that the cysteine residues in each active site are essential for catalysis.	Disulfides	43-52	prolyl 4-hydroxylase subunit beta	Homo sapiens	64-67
27766259-2	2016	However, high efficient expression of native hEGF in Escherichia coli has not been successful, since three disulfide bonds in monomer hEGF made it unable to fold into correct 3D structure using in vivo system.	Disulfides	107-116	epidermal growth factor	Homo sapiens	45-49
1577742-2	1992	Thioredoxin (Trx) from Escherichia coli was compared with bovine protein disulfide-isomerase (PDI) for its ability to catalyze native disulfide formation in either reduced or randomly oxidized (scrambled) ribonuclease A (RNase).	Disulfides	73-82	prolyl 4-hydroxylase subunit beta	Bos taurus	94-97
26458166-5	2015	Molecular docking of PTT onto gp120 argued that, with sufficient linker length, the peptide SH could approach and disrupt several alternative gp120 disulfides.	Disulfides	148-158	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	30-35
20719248-3	2011	It was observed that Cys27 was involved in the in vivo formation of intramolecular disulfide bonds when hCD83ext was expressed in Origami B(DE3).	Disulfides	83-92	CD83 molecule	Homo sapiens	104-109
1577742-3	1992	On a molar basis, a 100-fold higher concentration of Trx than of PDI was required to give the same rate of native disulfide formation measured as recovery of RNase activity.	Disulfides	114-123	thioredoxin	Bos taurus	53-56
1577742-3	1992	On a molar basis, a 100-fold higher concentration of Trx than of PDI was required to give the same rate of native disulfide formation measured as recovery of RNase activity.	Disulfides	114-123	prolyl 4-hydroxylase subunit beta	Bos taurus	65-68
20947114-1	2010	The orthopoxvirus protein A33 forms a disulfide-bonded high molecular weight species that could be either a homodimer or a heteromultimer.	Disulfides	38-47	glycoprotein A33	Homo sapiens	26-29
1577742-4	1992	A Pro-34 to His (P34H Trx) mutation in the active site of E. coli Trx (WCGPC), mimicking the two suggested active sites in PDI (WCGHC), increased the catalytic activity in disulfide formation about 10-fold.	Disulfides	172-181	thioredoxin	Bos taurus	22-25
20947114-2	2010	The protein is a major target for neutralizing antibodies and the majority of antibodies raised against A33 only recognize the disulfide-bonded form.	Disulfides	127-136	glycoprotein A33	Homo sapiens	104-107
20947114-3	2010	Here, we report that A33 is present as a disulfide-bonded homodimer during infection.	Disulfides	41-50	glycoprotein A33	Homo sapiens	21-24
20947114-4	2010	Additionally, we examined the function of intermolecular disulfide bonding in A33 homodimerization during infection.	Disulfides	57-66	glycoprotein A33	Homo sapiens	78-81
26449594-7	2015	Together with recent results obtained with BoNTs specific for SNAP25 and syntaxin, the present data demonstrate the essential role of the thioredoxin-thioredoxin reductase system in reducing the interchain disulfide during the nerve intoxication mechanism of all serotypes.	Disulfides	206-215	synaptosomal-associated protein 25	Mus musculus	62-68
1577742-4	1992	A Pro-34 to His (P34H Trx) mutation in the active site of E. coli Trx (WCGPC), mimicking the two suggested active sites in PDI (WCGHC), increased the catalytic activity in disulfide formation about 10-fold.	Disulfides	172-181	thioredoxin	Bos taurus	66-69
20947114-7	2010	The recombinant viruses had growth characteristics similar to their parental viruses, indicating that intermolecular disulfide-bonded homodimerization of A33 is not required for its function.	Disulfides	117-126	glycoprotein A33	Homo sapiens	154-157
1577742-4	1992	A Pro-34 to His (P34H Trx) mutation in the active site of E. coli Trx (WCGPC), mimicking the two suggested active sites in PDI (WCGHC), increased the catalytic activity in disulfide formation about 10-fold.	Disulfides	172-181	prolyl 4-hydroxylase subunit beta	Bos taurus	123-126
1428535-1	1992	The putative receptor-binding region of human transforming growth factor-alpha (TGF alpha) has been shown to be contributed by two fragments: an A-chain (residue 12-18) and a 17-residue carboxyl fragment (residue 34-50) that includes a disulfide-containing C-loop (residue 34-43).	Disulfides	236-245	transforming growth factor alpha	Homo sapiens	80-89
20853839-0	2010	Analysis of adenosine A2a receptor stability: effects of ligands and disulfide bonds.	Disulfides	69-78	adenosine A2a receptor	Homo sapiens	12-34
20956336-5	2010	In order to increase the yield and stability of the spike, we used an endodomain deleted and gp120-gp41 disulfide-linked variant.	Disulfides	104-113	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	93-98
26454085-11	2015	Further, analysis of serial tissue sections using X-ray absorption spectroscopy at the sulfur K-edge has revealed that CA1 pyramidal neurons have increased disulfide levels, a direct indicator of oxidative stress, at this time point.	Disulfides	156-165	carbonic anhydrase 1	Rattus norvegicus	119-122
26598606-4	2016	By analyzing the phenotypes of mutants with Opy2 cysteine-to-alanine mutations, we deduced that the CR domain forms four intramolecular disulfide bonds.	Disulfides	136-145	Opy2p	Saccharomyces cerevisiae S288C	44-48
26451472-0	2015	Thioredoxin Cross-Linking by Nitrogen Mustard in Lung Epithelial Cells: Formation of Multimeric Thioredoxin/Thioredoxin Reductase Complexes and Inhibition of Disulfide Reduction.	Disulfides	158-167	thioredoxin	Homo sapiens	0-11
26451472-1	2015	The thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (TrxR), is a major cellular disulfide reduction system important in antioxidant defense.	Disulfides	106-115	thioredoxin	Homo sapiens	4-15
26451472-1	2015	The thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (TrxR), is a major cellular disulfide reduction system important in antioxidant defense.	Disulfides	106-115	thioredoxin	Homo sapiens	17-20
26451472-1	2015	The thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (TrxR), is a major cellular disulfide reduction system important in antioxidant defense.	Disulfides	106-115	thioredoxin	Homo sapiens	48-51
26451472-1	2015	The thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (TrxR), is a major cellular disulfide reduction system important in antioxidant defense.	Disulfides	106-115	peroxiredoxin 5	Homo sapiens	56-77
26451472-1	2015	The thioredoxin (Trx) system, which consists of Trx and thioredoxin reductase (TrxR), is a major cellular disulfide reduction system important in antioxidant defense.	Disulfides	106-115	peroxiredoxin 5	Homo sapiens	79-83
26451472-11	2015	Inhibition of the Trx system by HN2 can disrupt cellular thiol-disulfide balance, contributing to vesicant-induced lung toxicity.	Disulfides	63-72	thioredoxin	Homo sapiens	18-21
20367259-4	2010	IMS import of SOD1 involves its copper chaperone, CCS, whose mitochondrial distribution is regulated by the Mia40/Erv1 disulfide relay system in a redox-dependent manner: CCS promotes SOD1 maturation and retention in the IMS.	Disulfides	119-128	growth factor, augmenter of liver regeneration	Homo sapiens	114-118
20367271-1	2010	Erv1 and Mia40 constitute the two important components of the disulfide relay system that mediates oxidative protein folding in the mitochondrial intermembrane space.	Disulfides	62-71	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	0-4
20688116-5	2010	After purification by immobilized metal ion affinity chromatography, refolding in vitro through disulfide reshuffling, and digestion by endoproteinase Asp-N, mature human relaxin-3 was obtained in high yield and at low cost.	Disulfides	96-105	relaxin 3	Homo sapiens	171-180
20688116-6	2010	Peptide mapping and circular dichroism spectroscopy studies suggested that the recombinant relaxin-3 adopted an insulin-like fold with the expected disulfide linkages.	Disulfides	148-157	relaxin 3	Homo sapiens	91-100
20886156-2	2010	In rhodopsin, ECL2 forms a rigid structure including a beta-sheet and interacts with the transmembrane region via a disulfide bond, hydrogen bonds, and hydrophobic interactions.	Disulfides	116-125	rhodopsin	Bos taurus	3-12
1639768-1	1992	Thioltransferase, an enzyme which catalyzes the thiol/disulfide exchange reaction in the presence of GSH, was purified to homogeneity on 15% SDS-PAGE from human (36,000-fold purification) and bovine (23,000-fold) erythrocyte hemolysates.	Disulfides	54-63	glutaredoxin	Homo sapiens	0-16
20801125-1	2010	AMH is a glycoprotein dimer composed of two 72kDa monomers linked by disulfide bridges.	Disulfides	69-78	anti-Mullerian hormone	Homo sapiens	0-3
25900303-7	2015	Furthermore, many of the plasma proteins of mass &lt;151 kDa were secreted as disulfide-bound complexes with members of the alpha2 -macroglobulin (A2M) family, which serve as intracellular and extracellular chaperones, not protease inhibitors.	Disulfides	78-87	alpha-2-macroglobulin	Homo sapiens	124-145
25900303-7	2015	Furthermore, many of the plasma proteins of mass &lt;151 kDa were secreted as disulfide-bound complexes with members of the alpha2 -macroglobulin (A2M) family, which serve as intracellular and extracellular chaperones, not protease inhibitors.	Disulfides	78-87	alpha-2-macroglobulin	Homo sapiens	147-150
1639768-4	1992	Phosphofructokinase and pyruvate kinase that had been inactivated by disulfides were reactivated effectively by the addition of thioltransferase with GSH.	Disulfides	69-79	glutaredoxin	Homo sapiens	128-144
1639768-5	1992	In addition, disulfides in membrane proteins of human erythrocytes that have been oxidatively damaged by diamide treatment were reduced to the SH-free form more effectively by incubation with thioltransferase.	Disulfides	13-23	glutaredoxin	Homo sapiens	192-208
1549912-4	1992	By comparison to reported properties of HIV-1 gp160 and SIVMAC gp160, it was possible to define antigenic domains in the loops of gp120 resulting from the reported interchain disulfide bonds defining putative antigenic domains specific for HIV-2.	Disulfides	175-184	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	46-51
26169129-1	2015	Hepcidin, a 25-amino-acid and highly disulfide bonded antimicrobial peptide, is the central regulator of iron homeostasis.	Disulfides	37-46	hepcidin antimicrobial peptide	Homo sapiens	0-8
20966255-4	2010	The oxidized form of ATM is a disulfide-cross-linked dimer, and mutation of a critical cysteine residue involved in disulfide bond formation specifically blocked activation through the oxidation pathway.	Disulfides	30-39	ATM serine/threonine kinase	Homo sapiens	21-24
20966255-4	2010	The oxidized form of ATM is a disulfide-cross-linked dimer, and mutation of a critical cysteine residue involved in disulfide bond formation specifically blocked activation through the oxidation pathway.	Disulfides	116-125	ATM serine/threonine kinase	Homo sapiens	21-24
1549912-4	1992	By comparison to reported properties of HIV-1 gp160 and SIVMAC gp160, it was possible to define antigenic domains in the loops of gp120 resulting from the reported interchain disulfide bonds defining putative antigenic domains specific for HIV-2.	Disulfides	175-184	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	63-68
26488649-8	2015	Furthermore, we found that oxidative stress induced by beta-AR stimulation caused the formation of disulfide bonds between two ryanodine receptor (RyR) subunits, referred to as intersubunit cross-linking.	Disulfides	99-108	LOC100009439	Oryctolagus cuniculus	127-145
1794612-6	1991	In the present study, we have examined the possibility that the disulfide bridges located in the NH2-terminal portion of the pro-region of POMC are essential for maintaining a determinant involved in the sorting of POMC to the regulated secretory pathway.	Disulfides	64-73	pro-opiomelanocortin-alpha	Mus musculus	139-143
26488649-8	2015	Furthermore, we found that oxidative stress induced by beta-AR stimulation caused the formation of disulfide bonds between two ryanodine receptor (RyR) subunits, referred to as intersubunit cross-linking.	Disulfides	99-108	LOC100009439	Oryctolagus cuniculus	147-150
20845358-9	2010	Interestingly, the native and reduced forms of LEAP-2 have similar membrane affinity and antimicrobial activities; this suggests that disulfide bonds are not essential for the bactericidal activity.	Disulfides	134-143	liver enriched antimicrobial peptide 2	Homo sapiens	47-53
20675861-0	2010	Isoform-specific intermolecular disulfide bond formation of heterochromatin protein 1 (HP1).	Disulfides	32-41	chromobox 5	Homo sapiens	60-85
20675861-0	2010	Isoform-specific intermolecular disulfide bond formation of heterochromatin protein 1 (HP1).	Disulfides	32-41	chromobox 5	Homo sapiens	87-90
20675861-3	2010	Here, we have identified intermolecular disulfide bond formation of HP1 cysteines in an isoform-specific manner.	Disulfides	40-49	chromobox 5	Homo sapiens	68-71
26302448-2	2015	RC-RNase 2, a cytotoxic ribonuclease isolated from oocytes of bullfrog Rana catesbeiana, consists of 105 residues linked with 4 disulfide bridges and belongs to the bovine pancreatic ribonuclease (RNase A) superfamily.	Disulfides	128-137	ribonuclease A family member 2	Rattus norvegicus	3-10
1794612-6	1991	In the present study, we have examined the possibility that the disulfide bridges located in the NH2-terminal portion of the pro-region of POMC are essential for maintaining a determinant involved in the sorting of POMC to the regulated secretory pathway.	Disulfides	64-73	pro-opiomelanocortin-alpha	Mus musculus	215-219
1794612-7	1991	Using site-directed and deletion mutagenesis of the porcine POMC cDNA, we created mutants in which one or both disulfide bridges were disrupted or in which the first 26 amino acid residues of the pro-region were deleted.	Disulfides	111-120	pro-opiomelanocortin-alpha	Mus musculus	60-64
26424450-4	2015	Likewise, ACHT4 reacted in planta with 2-Cys Prx, indicating that it is oxidized by a similar disulfide exchange reaction.	Disulfides	94-103	atypical CYS HIS rich thioredoxin 4	Arabidopsis thaliana	10-15
20561589-8	2010	The conserved disulfide bond-forming cysteine residues and the N-linked glycosylation sites that are preserved in CD83 are also found in SmCD83.	Disulfides	14-23	CD83 molecule	Homo sapiens	114-118
26424450-5	2015	ACHT4 further reacted uniquely with the small subunit (APS1) of ADP-glucose pyrophosphorylase (AGPase), the first committed enzyme of the starch synthesis pathway, suggesting that it transfers the disulfides it receives from 2-Cys Prx to APS1 and turns off AGPase.	Disulfides	197-207	atypical CYS HIS rich thioredoxin 4	Arabidopsis thaliana	0-5
1794612-14	1991	However, when both disulfide bridges were removed from the precursor from the precursor by deletion of the first 26 amino acid residues of POMC, the truncated precursor (POMC delta 1-26) behaved as the unmutated POMC.	Disulfides	19-28	pro-opiomelanocortin-alpha	Mus musculus	139-143
20584868-2	2010	Lp(a) is a subfraction of LDL, where apolipoprotein(a) [apo(a)] is disulfide bound to apolipoprotein B-100 (apoB).	Disulfides	67-76	apolipoprotein B	Mus musculus	108-112
1666024-2	1991	To modify the hormonal activity of hCG, hybrid molecules composed of hCG and other glycoproteins, either the A or B chain of lectin ricin (hCG-A and hCG-B) through disulfide bridges and horseradish peroxidase (hCG-HRP) through Schiff"s base, were synthesized.	Disulfides	164-173	chorionic gonadotropin subunit beta 5	Homo sapiens	35-38
20660346-5	2010	Here we used an optimized mass spectrometric method to demonstrate that Trx1 is itself nitrosylated by S-nitrosoglutathione at Cys(73) only after the formation of a Cys(32)-Cys(35) disulfide bond upon which the disulfide reductase and denitrosylase activities of Trx1 are attenuated.	Disulfides	181-190	thioredoxin	Homo sapiens	72-76
26690492-2	2015	The three-dimensional functional structure of gp120 contains intramolecular disulfide bonds, which are critical for the interaction with the CD4 receptor.	Disulfides	76-85	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	46-51
1666024-2	1991	To modify the hormonal activity of hCG, hybrid molecules composed of hCG and other glycoproteins, either the A or B chain of lectin ricin (hCG-A and hCG-B) through disulfide bridges and horseradish peroxidase (hCG-HRP) through Schiff"s base, were synthesized.	Disulfides	164-173	chorionic gonadotropin subunit beta 5	Homo sapiens	69-72
1666024-2	1991	To modify the hormonal activity of hCG, hybrid molecules composed of hCG and other glycoproteins, either the A or B chain of lectin ricin (hCG-A and hCG-B) through disulfide bridges and horseradish peroxidase (hCG-HRP) through Schiff"s base, were synthesized.	Disulfides	164-173	chorionic gonadotropin subunit beta 5	Homo sapiens	149-154
1666024-2	1991	To modify the hormonal activity of hCG, hybrid molecules composed of hCG and other glycoproteins, either the A or B chain of lectin ricin (hCG-A and hCG-B) through disulfide bridges and horseradish peroxidase (hCG-HRP) through Schiff"s base, were synthesized.	Disulfides	164-173	chorionic gonadotropin subunit beta 5	Homo sapiens	69-72
1833456-1	1991	The receptor for IgE (Fc epsilon RI) is a multimeric complex containing one alpha chain, one beta chain with four transmembrane domains and one homodimer of disulfide-linked gamma-chains.	Disulfides	157-166	Fc epsilon receptor Ia	Homo sapiens	22-35
26231588-3	2015	As an alternative to this issue, a linear analogue (named GmL) lacking the disulfide bonds was designed.	Disulfides	75-84	glycosylphosphatidylinositol anchored molecule like	Homo sapiens	58-61
19027991-3	2010	A random disulfide constrained heptapeptide phage display library was screened against A beta(42).	Disulfides	9-18	amyloid beta (A4) precursor protein	Mus musculus	87-93
20566323-1	2010	The formation of aberrant disulfide bonds is a structural consideration for the manufacturing of the extracellular domain of human CD83 (hCD83ext), a potential therapeutic protein.	Disulfides	26-35	CD83 molecule	Homo sapiens	131-135
20566323-1	2010	The formation of aberrant disulfide bonds is a structural consideration for the manufacturing of the extracellular domain of human CD83 (hCD83ext), a potential therapeutic protein.	Disulfides	26-35	CD83 molecule	Homo sapiens	137-142
20566323-2	2010	In certain instances, hCD83ext protein products, even when stored frozen, tended to dimerize or even multimerize through the formation of aberrant intermolecular disulfide bonds.	Disulfides	162-171	CD83 molecule	Homo sapiens	22-27
20566323-5	2010	The identification of this mutant variant as a more potent therapeutic protein than other hCD83ext species demonstrated that the structural variation associated with disulfide bond formation can be a critical issue for rigorous control of the quality and bioactivity of therapeutic proteins.	Disulfides	166-175	CD83 molecule	Homo sapiens	90-95
26396244-8	2015	Mass spectroscopy of the tandem repeat revealed that the PDI-induced interaction with heparin is characterized by ruptured disulfide bonds and that cysteine thiols remain reduced.	Disulfides	123-132	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	57-60
1833456-2	1991	The Fc epsilon RI gamma-chains form additional disulfide-linked dimers with the homologous zeta- and eta-chains, as part of the TCR complex.	Disulfides	47-56	Fc epsilon receptor Ig	Homo sapiens	4-23
1892828-3	1991	In addition, RP70 contained a disulfide bond between cysteine residues close to the ends of the molecule, forming a loop that is thought to constitute an important structural and immunological component of the intact glycoprotein.	Disulfides	30-39	pre-mRNA processing factor 4	Homo sapiens	13-17
26361352-1	2015	ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle.	Disulfides	51-60	protein disulfide isomerase associated 3	Mus musculus	0-5
20731416-0	2010	A novel disulfide pattern in laminin-type epidermal growth factor-like (LE) modules of laminin beta1 and gamma1 chains.	Disulfides	8-17	hemoglobin, beta adult major chain	Mus musculus	95-100
20731416-1	2010	In-depth mass spectrometric analysis of disulfide bond patterns in recombinant mouse laminin beta1 and gamma1 chain N-terminal fragments comprising the laminin N-terminal (LN) domain and the first four laminin epidermal growth factor-like (LE) domains revealed a novel disulfide pattern for LE domains.	Disulfides	40-49	hemoglobin, beta adult major chain	Mus musculus	93-98
26361352-1	2015	ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle.	Disulfides	51-60	protein disulfide isomerase associated 3	Mus musculus	21-26
26361352-1	2015	ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle.	Disulfides	51-60	protein disulfide isomerase associated 3	Mus musculus	31-36
26361352-1	2015	ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle.	Disulfides	51-60	calnexin	Mus musculus	144-152
25960419-3	2015	The LTBPs were first identified as forming latent complexes with TGFbeta by covalently binding the TGFbeta propeptide (LAP) via disulfide bonds in the endoplasmic reticulum.	Disulfides	128-137	LAP	Homo sapiens	119-122
20121341-6	2010	A steady-state flux analysis predicted an unequal distribution of the intracellular anti-oxidative burden between thioredoxin-dependent and glutathione-dependent antioxidant pathways, with the former contributing the majority of the cellular antioxidant defense due to peroxiredoxins and protein disulfides.	Disulfides	296-306	thioredoxin	Homo sapiens	114-125
23350160-2	2010	Several systems are able to control the activity, stability, and correct folding of enzymes through dithiol/disulfide isomerization reactions including the enzyme protein disulfide-isomerase, the glutathione-dependent glutaredoxin system, and the thioredoxin systems.	Disulfides	108-117	thioredoxin	Homo sapiens	247-258
20738721-3	2010	It has been proposed that disulfide bonds might be formed through two cysteine pairs in the extracellular LRR domains of CLV1 and CLV2 to stabilize the receptor complex.	Disulfides	26-35	Leucine-rich repeat (LRR) family protein	Arabidopsis thaliana	130-134
1888746-1	1991	Thioltransferase from human red blood cells (HRBC TTase), coupled to GSSG reductase, catalyzed glutathione (GSH)-dependent reduction of prototype substrates hydroxyethyl disulfide (HEDS) and sodium S-sulfocysteine as well as of other homo- and heterodisulfides, including the protein mixed disulfide albumin-S-S-cysteine.	Disulfides	170-179	glutaredoxin	Homo sapiens	0-16
20570702-6	2010	Using solid-phase peptide synthesis together with regioselective disulfide bond formation, two analogs of human INSL3 were prepared in which the intra-chain disulfide bond was replaced, one in which the corresponding Cys residues were substituted with the isosteric Ser and the other in which the Cys were removed altogether.	Disulfides	157-166	insulin like 3	Homo sapiens	112-117
20570702-7	2010	Both of these peptides retained nearly full RXFP2 receptor binding but were devoid of cAMP activity (receptor activation), indicating that the intra-A-chain disulfide bond makes a significant contribution to the ability of INSL3 to act as an RXFP2 agonist.	Disulfides	157-166	insulin like 3	Homo sapiens	223-228
29142703-0	2015	Mechanisms and energetics of free radical initiated disulfide bond cleavage in model peptides and insulin by mass spectrometry.	Disulfides	52-61	insulin	Bos taurus	98-105
29142703-3	2015	We show that even multiple disulfide bonds in intact bovine insulin are fragmented in the MS2 stage, releasing the A- and B-chains with a high yield, which has been challenging to achieve by other ion activation methods.	Disulfides	27-36	insulin	Bos taurus	60-67
20570702-8	2010	Replacement of the disulfide bond with a metabolically stable dicarba bond yielded two isomers of INSL3 that each exhibited bioactivity similar to native INSL3.	Disulfides	19-28	insulin like 3	Homo sapiens	98-103
1804554-1	1991	Saponin-permeabilized polymorphonuclear leukocytes (PMNs) released beta-glucuronidase, a lysosomal enzyme, dose-dependently in response to cupric phenanthroline (CuPh), a mild oxidant, which catalyzes the formation of disulfide bridges.	Disulfides	218-227	glucuronidase beta	Homo sapiens	67-85
20570702-9	2010	This study highlights the critical structural role played by the intra-A-chain disulfide bond of INSL3 in mediating agonist actions through the RXFP2 receptor.	Disulfides	79-88	insulin like 3	Homo sapiens	97-102
20570702-9	2010	This study highlights the critical structural role played by the intra-A-chain disulfide bond of INSL3 in mediating agonist actions through the RXFP2 receptor.	Disulfides	79-88	relaxin family peptide receptor 2	Homo sapiens	144-149
26132214-0	2015	Structures of cGMP-Dependent Protein Kinase (PKG) Ialpha Leucine Zippers Reveal an Interchain Disulfide Bond Important for Dimer Stability.	Disulfides	94-103	protein kinase cGMP-dependent 1	Homo sapiens	45-48
26132214-3	2015	The PKG Ialpha LZ contains C42 that is known to form a disulfide bond upon oxidation and to activate PKG Ialpha.	Disulfides	55-64	protein kinase cGMP-dependent 1	Homo sapiens	4-7
26132214-5	2015	Our data demonstrate that the C42-C42" disulfide bond dramatically stabilizes PKG Ialpha and that the C42L mutant mimics the oxidized WT LZ structurally.	Disulfides	39-48	protein kinase cGMP-dependent 1	Homo sapiens	78-81
1761367-1	1991	The receptor-recognition site human transforming growth factor-alpha (TGF alpha), a 50-residue tricyclic peptide with three disulfide bonds, was mapped by a set of 46 peptide analogs consisting of linear, monocyclic, bicyclic, and tricyclic structures representing individual and overlapping subdomains of human TGF alpha.	Disulfides	124-133	transforming growth factor alpha	Homo sapiens	70-79
20632359-2	2010	Through the use of MP2, QCI and CASPT2 molecular orbital (MO) methods, we elucidate, for the first time, the mechanisms that lead to unimolecular fragmentation of disulfide derivatives after electron attachment.	Disulfides	163-172	tryptase pseudogene 1	Homo sapiens	19-22
20538591-3	2010	In this study, we describe a novel recombinant CD4 protein designed to bind gp120 through a targeted disulfide-exchange mechanism.	Disulfides	101-110	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	76-81
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	186-195	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	169-174
26086621-7	2015	95% sequence coverage was obtained by reducing human granulocyte-colony stimulating factor (G-CSF) prior to MS/MS and MS(3) analysis to specifically target the residues between the disulfide bonds.	Disulfides	181-190	colony stimulating factor 3	Homo sapiens	53-90
26086621-7	2015	95% sequence coverage was obtained by reducing human granulocyte-colony stimulating factor (G-CSF) prior to MS/MS and MS(3) analysis to specifically target the residues between the disulfide bonds.	Disulfides	181-190	colony stimulating factor 3	Homo sapiens	92-97
1718344-0	1991	Peptides mimicking selected disulfide loops in HIV-1 gp120, other than V3, do not elicit virus-neutralizing antibodies.	Disulfides	28-37	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	53-58
25980911-0	2015	Enrichment of O-GlcNAc-modified peptides using novel thiol-alkyne and thiol-disulfide exchange.	Disulfides	76-85	O-linked N-acetylglucosamine (GlcNAc) transferase	Homo sapiens	14-22
20696394-2	2010	Here we show that the extracellular domains of murine and human Igbeta form an I-set immunoglobulin-like structure with an interchain disulfide between cysteines on their G strands.	Disulfides	134-143	CD79b molecule	Homo sapiens	64-70
20696394-4	2010	An Igalphabeta heterodimer model was generated based on the unique disulfide-bonded Igbeta dimer.	Disulfides	67-76	CD79b molecule	Homo sapiens	84-90
20979592-7	2010	RESULTS: We demonstrate that the Cys288-Cys326 disulfide in domain V of beta(2) GPI is the predominant disulfide reduced by thioredoxin-1.	Disulfides	47-56	apolipoprotein H	Homo sapiens	72-83
20979592-7	2010	RESULTS: We demonstrate that the Cys288-Cys326 disulfide in domain V of beta(2) GPI is the predominant disulfide reduced by thioredoxin-1.	Disulfides	103-112	apolipoprotein H	Homo sapiens	72-83
20979592-8	2010	Reduced beta(2) GPI in vitro displays increased binding to VWF that is dependent on disulfide bond formation.	Disulfides	84-93	apolipoprotein H	Homo sapiens	8-19
20473443-1	2010	Thiol-disulfide exchange reactions between thiol-disulfide oxidoreductases (e.g. thioredoxin or Trx) and client proteins can obtain a rate several orders faster than those between chemical reagents (e.g. dithiothreitol) and client proteins.	Disulfides	6-15	thioredoxin	Homo sapiens	81-92
25980911-1	2015	We have developed a selective method for the enrichment of O-linked beta-N-acetylglucosamine (O-GlcNAc)-modified peptides, which uses a newly synthesized thiol-alkyne and a thiol-disulfide exchange.	Disulfides	179-188	O-linked N-acetylglucosamine (GlcNAc) transferase	Homo sapiens	59-102
25990830-5	2015	The binding of PP to myosin suppressed disulfide bond formation in myosin subfragments 1 and 2 and partially inhibited oxidation-initiated cross-linking of heavy meromyosin during myosin gelation with a lesser effect on light meromyosin.	Disulfides	39-48	myosin heavy chain 14	Homo sapiens	21-27
25990830-5	2015	The binding of PP to myosin suppressed disulfide bond formation in myosin subfragments 1 and 2 and partially inhibited oxidation-initiated cross-linking of heavy meromyosin during myosin gelation with a lesser effect on light meromyosin.	Disulfides	39-48	myosin heavy chain 14	Homo sapiens	67-73
25990830-5	2015	The binding of PP to myosin suppressed disulfide bond formation in myosin subfragments 1 and 2 and partially inhibited oxidation-initiated cross-linking of heavy meromyosin during myosin gelation with a lesser effect on light meromyosin.	Disulfides	39-48	myosin heavy chain 14	Homo sapiens	67-73
20473443-1	2010	Thiol-disulfide exchange reactions between thiol-disulfide oxidoreductases (e.g. thioredoxin or Trx) and client proteins can obtain a rate several orders faster than those between chemical reagents (e.g. dithiothreitol) and client proteins.	Disulfides	6-15	thioredoxin	Homo sapiens	96-99
1718344-1	1991	The positions of all 9 intrachain disulfide bonds within the envelope glycoprotein gp120 of the human immunodeficiency virus (HIV-1) have been established recently.	Disulfides	34-43	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	83-88
1648963-1	1991	ATP synthesis by the membrane-bound chloroplast ATPase in the oxidized state of its gamma disulfide bridge was studied as a function of the ADP concentration, delta pH, and external pH values, under conditions where delta pH was clamped and delocalized.	Disulfides	90-99	dynein axonemal heavy chain 8	Homo sapiens	48-54
20527929-0	2010	Engineered disulfide bonds restore chaperone-like function of DJ-1 mutants linked to familial Parkinson"s disease.	Disulfides	11-20	Parkinsonism associated deglycase	Homo sapiens	62-66
20527929-5	2010	We found that the introduction of this disulfide linkage stabilized the mutants A104T and M26I against thermal denaturation, improved their ability to scavenge reactive oxygen species (ROS), and restored a chaperone-like function of blocking alpha-synuclein aggregation.	Disulfides	39-48	synuclein alpha	Homo sapiens	242-257
26020833-8	2015	Importantly, the caged-BK platform provided the first quantification of intracellular disulfide bond formation upon EGF stimulation.	Disulfides	86-95	epidermal growth factor	Homo sapiens	116-119
20609355-4	2010	We demonstrate that upon As(2)O(3) exposure, PML undergoes ROS-initiated intermolecular disulfide formation and binds arsenic directly.	Disulfides	88-97	PML nuclear body scaffold	Homo sapiens	45-48
1648964-1	1991	The disulfide bridges in porcine hydrophobic surfactant protein B (SP-B) were determined.	Disulfides	4-13	surfactant protein B	Homo sapiens	67-71
20609355-5	2010	Disulfide-linked PML or PML/RARA multimers form nuclear matrix-associated nuclear bodies (NBs), become sumoylated and are degraded.	Disulfides	0-9	PML nuclear body scaffold	Homo sapiens	17-20
26042044-8	2015	The pattern of conservation suggests a possible pairing of long loops in Domains I and III, which are bridged with core cysteines in NALCN, Cav, and Nav channels, and pairing of shorter loops in Domains II and IV in T-type channel through disulfide bonds involving T-type specific cysteines.	Disulfides	239-248	caveolin 2	Homo sapiens	140-143
1648964-6	1991	Notably, one of the three intrachain bonds common to all SP-B molecules is analogous to one of the disulfide linkages in the kringle structure of complex serine proteases.	Disulfides	99-108	surfactant protein B	Homo sapiens	57-61
1906465-2	1991	The nascent transferrin receptor containing core-glycosylated asparagine-linked oligosaccharides does not possess complete intersubunit disulfide bonds, sediments predominantly as a monomer in sucrose density gradients, and shows reduced binding to transferrin-agarose.	Disulfides	136-145	transferrin receptor	Homo sapiens	12-32
25880232-4	2015	Moreover, disulfide tethering of alpha1 to alpha2 or alpha6 blocks cytochrome c release, suggesting that alpha1 dissociation is required for further conformational changes during apoptosis.	Disulfides	10-19	adrenoceptor alpha 1D	Homo sapiens	33-39
25880232-4	2015	Moreover, disulfide tethering of alpha1 to alpha2 or alpha6 blocks cytochrome c release, suggesting that alpha1 dissociation is required for further conformational changes during apoptosis.	Disulfides	10-19	adrenoceptor alpha 1D	Homo sapiens	105-111
20189569-8	2010	Insoluble SAP accumulates in the lesions in covalent-bound forms conjugated to collagen/collagen-like substances via disulfide (-S-S-) bonds.	Disulfides	117-126	amyloid P component, serum	Homo sapiens	10-13
1710239-2	1991	CD69 is a phosphorylated disulfide-linked homodimer that appears on the surface of human T, B cells and thymocytes in the early steps of activation; its molecular mass is 28 to 34 kDa under reducing conditions.	Disulfides	25-34	CD69 molecule	Homo sapiens	0-4
20382731-6	2010	To date, single-molecule force spectroscopy has been applied to gain insight into the reduction of disulfide bonds by different enzymes of the thioredoxin family.	Disulfides	99-108	thioredoxin	Homo sapiens	143-154
1707541-5	1991	mIgD is not associated with MB-1 but is with IgD-alpha, which is also disulfide-linked to Ig-beta.	Disulfides	70-79	forkhead box C1	Homo sapiens	45-54
20525253-1	2010	BACKGROUND: The Protein Disulfide Isomerase (PDI) gene family encodes several PDI and PDI-like proteins containing thioredoxin domains and controlling diversified metabolic functions, including disulfide bond formation and isomerisation during protein folding.	Disulfides	194-203	protein disulfide-isomerase	Triticum aestivum	16-43
20525253-1	2010	BACKGROUND: The Protein Disulfide Isomerase (PDI) gene family encodes several PDI and PDI-like proteins containing thioredoxin domains and controlling diversified metabolic functions, including disulfide bond formation and isomerisation during protein folding.	Disulfides	194-203	protein disulfide-isomerase	Triticum aestivum	45-48
20525253-1	2010	BACKGROUND: The Protein Disulfide Isomerase (PDI) gene family encodes several PDI and PDI-like proteins containing thioredoxin domains and controlling diversified metabolic functions, including disulfide bond formation and isomerisation during protein folding.	Disulfides	194-203	protein disulfide-isomerase	Triticum aestivum	78-81
20525253-1	2010	BACKGROUND: The Protein Disulfide Isomerase (PDI) gene family encodes several PDI and PDI-like proteins containing thioredoxin domains and controlling diversified metabolic functions, including disulfide bond formation and isomerisation during protein folding.	Disulfides	194-203	protein disulfide-isomerase	Triticum aestivum	78-81
25869667-1	2015	We recently reported that a trans-dimer, homotypic disulfide bond involving Cys367 in keratin 14 (K14) occurs in an atomic-resolution structure of the interacting K5/K14 2B domains and in keratinocyte cell lines.	Disulfides	51-60	keratin 14	Mus musculus	86-96
25869667-1	2015	We recently reported that a trans-dimer, homotypic disulfide bond involving Cys367 in keratin 14 (K14) occurs in an atomic-resolution structure of the interacting K5/K14 2B domains and in keratinocyte cell lines.	Disulfides	51-60	keratin 14	Mus musculus	98-101
25869667-1	2015	We recently reported that a trans-dimer, homotypic disulfide bond involving Cys367 in keratin 14 (K14) occurs in an atomic-resolution structure of the interacting K5/K14 2B domains and in keratinocyte cell lines.	Disulfides	51-60	keratin 14	Mus musculus	166-169
25869667-2	2015	Here we show that a sizable fraction of the K14 and K5 protein pools participates in interkeratin disulfide bonding in primary cultures of mouse skin keratinocytes.	Disulfides	98-107	keratin 14	Mus musculus	44-47
25869667-3	2015	By comparing the properties of wild-type K14 with a completely cysteine-free variant thereof, we found that K14-dependent disulfide bonding limited filament elongation during polymerization in vitro but was necessary for the genesis of a perinuclear-concentrated network of keratin filaments, normal keratin cycling, and the sessile behavior of the nucleus and whole cell in keratinocytes studied by live imaging.	Disulfides	122-131	keratin 14	Mus musculus	41-44
25869667-3	2015	By comparing the properties of wild-type K14 with a completely cysteine-free variant thereof, we found that K14-dependent disulfide bonding limited filament elongation during polymerization in vitro but was necessary for the genesis of a perinuclear-concentrated network of keratin filaments, normal keratin cycling, and the sessile behavior of the nucleus and whole cell in keratinocytes studied by live imaging.	Disulfides	122-131	keratin 14	Mus musculus	108-111
25869667-5	2015	These findings establish disulfide bonding as a novel and important mechanism regulating the assembly, intracellular organization, and dynamics of K14-containing intermediate filaments in skin keratinocytes.	Disulfides	25-34	keratin 14	Mus musculus	147-150
25510931-8	2015	Insulin ions show dramatically reduced HDX levels and exchange rates, which can be attributed to decreased conformational flexibility resulting from the disulfide bonds.	Disulfides	153-162	insulin	Bos taurus	0-7
19967419-0	2010	Mimetics of the disulfide bridge between the N- and C-terminal cysteines of the KLK3-stimulating peptide B-2.	Disulfides	16-25	kallikrein related peptidase 3	Homo sapiens	80-84
20170694-4	2010	Furthermore, conjugation of siRNA to cholesterol with a cleavable disulfide linker appears to be beneficial for improving the potency of silencing of CNPase mRNA in oligodendrocytes in vivo.	Disulfides	66-75	2',3'-cyclic nucleotide 3' phosphodiesterase	Rattus norvegicus	150-156
2007114-4	1991	To assess the basis of host vs parasite enzyme recognition for their disulfide substrates, the interaction of bound glutathione with active-site residues in human red cell glutathione reductase as defined by prior X-ray analysis was used as the starting point for mutagenesis of three residues in trypanothione reductase from Trypanosoma congolense, a cattle parasite.	Disulfides	69-78	glutathione-disulfide reductase	Homo sapiens	172-193
20427771-5	2010	The introduction of a second disulfide bond between the TCR constant regions and/or creation of a chimeric protein in which the human constant regions were replaced by murine homologs resulted in enhanced TCR expression as demonstrated by tetramer staining and improved tumor reactivity that was comparable to PBL transduced with either anti-melanoma Ag recognized by T cells-1 or anti-gp100 TCR vectors currently used in clinical trials.	Disulfides	29-38	T cell receptor alpha variable 6-3	Mus musculus	56-59
20427771-5	2010	The introduction of a second disulfide bond between the TCR constant regions and/or creation of a chimeric protein in which the human constant regions were replaced by murine homologs resulted in enhanced TCR expression as demonstrated by tetramer staining and improved tumor reactivity that was comparable to PBL transduced with either anti-melanoma Ag recognized by T cells-1 or anti-gp100 TCR vectors currently used in clinical trials.	Disulfides	29-38	T cell receptor alpha variable 6-3	Mus musculus	205-208
20427771-5	2010	The introduction of a second disulfide bond between the TCR constant regions and/or creation of a chimeric protein in which the human constant regions were replaced by murine homologs resulted in enhanced TCR expression as demonstrated by tetramer staining and improved tumor reactivity that was comparable to PBL transduced with either anti-melanoma Ag recognized by T cells-1 or anti-gp100 TCR vectors currently used in clinical trials.	Disulfides	29-38	T cell receptor alpha variable 6-3	Mus musculus	205-208
25663701-6	2015	Exogenous expression of AMHRII, but not of type-II TGF-beta receptor (TbetaRII, also known as TGFR2), resulted in its disulfide-bond-mediated homo-oligomerization and intracellular retention, and in a decrease in its AMH-binding capacity.	Disulfides	118-127	anti-Mullerian hormone	Homo sapiens	24-27
25712564-3	2015	However, over-expression of HIV-1 gp120 in mammalian cells leads to the formation of aberrant disulfide-linked dimers that can bias the results of experiments aimed at measuring gp120 affinity with different ligands.	Disulfides	94-103	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	178-183
25712564-6	2015	Removal of these aberrant disulfide-linked gp120 dimers by standard size exclusion chromatography is sufficient to restore the overall affinity of gp120 preparations for these ligands.	Disulfides	26-35	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	43-48
1998667-0	1991	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.	Disulfides	16-25	coagulation factor XI	Homo sapiens	41-62
25712564-6	2015	Removal of these aberrant disulfide-linked gp120 dimers by standard size exclusion chromatography is sufficient to restore the overall affinity of gp120 preparations for these ligands.	Disulfides	26-35	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	147-152
25688043-5	2015	Previous kinetic analysis of the C55S mutant showed that in the oxidized inactive form of PRK, this residue formed a disulfide bridge with the Cys16 residue.	Disulfides	117-126	uncharacterized protein	Chlamydomonas reinhardtii	90-93
25688043-7	2015	Our data show for the first time that a disulfide bridge between Cys243 and Cys249 on PRK is required to form the PRK-GAPDH-CP12 complex.	Disulfides	40-49	uncharacterized protein	Chlamydomonas reinhardtii	114-117
25688043-7	2015	Our data show for the first time that a disulfide bridge between Cys243 and Cys249 on PRK is required to form the PRK-GAPDH-CP12 complex.	Disulfides	40-49	uncharacterized protein	Chlamydomonas reinhardtii	118-123
25688043-9	2015	Although Cys16 is the key residue involved in binding ATP and acting as a defense against oxidative damage, the formation of the algal ternary complex requires the formation of another disulfide bridge on PRK involving Cys243 and Cys249.	Disulfides	185-194	uncharacterized protein	Chlamydomonas reinhardtii	205-208
20235151-3	2010	Arsenic further activated RET-MEN2A kinase, which was already 3- to 10-fold augmented by genetic mutation compared with c-RET kinase activity, with promotion of disulfide bond-mediated dimerization of RET-MEN2A protein (superactivation).	Disulfides	161-170	ret proto-oncogene	Homo sapiens	205-210
20235151-4	2010	Arsenic also increased extracellular domain-deleted RET-PTC1 kinase activity with promotion of disulfide bond-mediated dimerization of RET-PTC1 protein.	Disulfides	95-104	ret proto-oncogene	Homo sapiens	135-138
19887450-4	2010	Using truncation mutagenesis we confirm that Lyve-1 in common with CD44 contains an extended HA-binding unit, comprising elements flanking the N and C termini of the consensus lectin-like Link module, bridged by a third conserved disulfide linkage that is critical for HA binding.	Disulfides	230-239	lymphatic vessel endothelial hyaluronan receptor 1	Homo sapiens	45-51
20145245-3	2010	Recently, peroxiredoxin (Prx)-induced relays of disulfide bond formation have been identified in budding yeast, namely the disulfide bond formation of Yap1, a crucial transcription factor for oxidative stress response, by a specific Prx Gpx3 and by a major Prx Tsa1.	Disulfides	48-57	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	237-241
20145245-3	2010	Recently, peroxiredoxin (Prx)-induced relays of disulfide bond formation have been identified in budding yeast, namely the disulfide bond formation of Yap1, a crucial transcription factor for oxidative stress response, by a specific Prx Gpx3 and by a major Prx Tsa1.	Disulfides	123-132	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	237-241
20196567-6	2010	These findings were demonstrated in 14 peptides containing disulfide bonds and further by bovine insulin, which has three disulfide bonds.	Disulfides	122-131	insulin	Bos taurus	97-104
25730439-6	2015	We speculated that in the more solvent-protected B isoform, the two Fab arms were brought into contact by the nonclassical disulfide bonds, resulting in a more compact global structure.	Disulfides	123-132	FA complementation group B	Homo sapiens	68-71
25638402-4	2015	The occurrence of thiol-dependent activities of plant GPX isoenzymes suggests that - besides detoxification of H2O2 and organic hydroperoxides - they may be involved in regulation of the cellular redox homeostasis by maintaining the thiol/disulfide or NADPH/NADP(+) balance.	Disulfides	239-248	glutathione peroxidase 2	Arabidopsis thaliana	54-57
1709050-10	1991	SDS-PAGE and isoelectric focusing analysis of immunoprecipitated mCD14 showed that mCD14 was a 53 kd disulfide-linked protein with a pI of 4.5-5.1.	Disulfides	101-110	CD14 antigen	Mus musculus	65-70
25666947-3	2015	Here, we report for the first time detailed structural modulation about the wild-type CP12 and its site-specific N-terminal and C-terminal disulfide bridge mutants upon interaction with GAPDH and PRK by Forster resonance energy transfer (FRET).	Disulfides	139-148	cytochrome P450 family 1 subfamily A member 2	Homo sapiens	86-90
25805991-2	2015	Glutathione-cysteine adducts may be removed from proteins by glutaredoxin, whereas disulfides may be reduced by thioredoxin.	Disulfides	83-93	thioredoxin	Homo sapiens	112-123
25805991-3	2015	Glutaredoxin is homologous to the disulfide-reducing thioredoxin and shares similar binding modes of the protein substrate.	Disulfides	34-43	thioredoxin	Homo sapiens	53-64
20332119-3	2010	Here, we show that a TCRalpha mutant lacking these intramembrane charged residues has a tendency to form homooligomers through an interchain disulfide bond that involves a specific pair of cysteine residues.	Disulfides	141-150	T cell receptor alpha joining 60 (pseudogene)	Homo sapiens	21-29
1709050-10	1991	SDS-PAGE and isoelectric focusing analysis of immunoprecipitated mCD14 showed that mCD14 was a 53 kd disulfide-linked protein with a pI of 4.5-5.1.	Disulfides	101-110	CD14 antigen	Mus musculus	83-88
1998728-4	1991	At pH 6.8, both the mammalian and the Escherichia coli thioredoxin systems inhibited microtubule assembly by 4-35% (19 +/- 9%) by reducing one intra-subunit disulfide bond in the tubulin dimer.	Disulfides	157-166	thioredoxin	Bos taurus	55-66
20089653-0	2010	Influence of disulfide-stabilized structure on the specificity of helper T-cell and antibody responses to HIV envelope glycoprotein gp120.	Disulfides	13-22	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	132-137
20089653-4	2010	In this work, three disulfide bonds in the outer domain of gp120 were individually deleted in order to destabilize the local three-dimensional structure and enhance the presentation of nearby weakly immunogenic epitopes.	Disulfides	20-29	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	59-64
25749683-3	2015	Among 30 disulfide-containing small molecules screened for efficient Tethering to ASH-bearing RNAs derived from pre-miR21, a benzotriazole-containing compound showed prominent adduct formation and selectivity for one of the RNAs tested.	Disulfides	9-18	microRNA 21	Homo sapiens	116-121
25849633-3	2015	In eukaryotes, the formation of most intramolecular disulfide bonds in the ER is thought to be catalyzed by protein disulfide isomerase (PDI) family proteins.	Disulfides	52-61	protein disulfide-isomerase	Triticum aestivum	108-135
1998728-5	1991	The thioredoxin-reducible disulfide of the tubulin dimer remains protected from thioredoxin in the assembled microtubules.	Disulfides	26-35	thioredoxin	Bos taurus	4-15
25849633-3	2015	In eukaryotes, the formation of most intramolecular disulfide bonds in the ER is thought to be catalyzed by protein disulfide isomerase (PDI) family proteins.	Disulfides	52-61	protein disulfide-isomerase	Triticum aestivum	137-140
25849633-13	2015	CONCLUSIONS: High expression of PDI family proteins during grain filling in the starchy endosperm suggest that these proteins play an important role in forming intramolecular disulfide bonds in seed storage proteins.	Disulfides	175-184	protein disulfide-isomerase	Triticum aestivum	32-35
20208521-2	2010	We report a chemical approach for monoubiquitylation and SUMOylation of PCNA through disulfide exchange and intein chemistry.	Disulfides	85-94	proliferating cell nuclear antigen	Homo sapiens	72-76
1998728-5	1991	The thioredoxin-reducible disulfide of the tubulin dimer remains protected from thioredoxin in the assembled microtubules.	Disulfides	26-35	thioredoxin	Bos taurus	80-91
1899030-9	1991	This includes the two cysteine residues that are known to be involved in an intramolecular disulfide bond in the sheep CA VI.	Disulfides	91-100	carbonic anhydrase 6	Ovis aries	119-124
20130111-6	2010	Moreover, treatment with sulfhydryl-modifying agents that oxidize SH-groups of cysteine residues to disulfide bonds abolished ATRA-mediated RARA nuclear localization, suggesting that the thiol oxidoreductase activity of GRp58 may be required for RARA nuclear import.	Disulfides	100-109	protein disulfide isomerase associated 3	Mus musculus	220-225
25617829-0	2015	N-glycosylation and disulfide bonding affects GPRC6A receptor expression, function, and dimerization.	Disulfides	20-29	G protein-coupled receptor class C group 6 member A	Homo sapiens	46-52
25617829-4	2015	GPRC6A has been speculated to form covalently linked dimers through cysteine disulfide linkage in the extracellular amino-terminal domain and here we show that GPRC6A indeed is a homodimer and that a disulfide bridge between the C131 residues is formed.	Disulfides	77-86	G protein-coupled receptor class C group 6 member A	Homo sapiens	0-6
25617829-4	2015	GPRC6A has been speculated to form covalently linked dimers through cysteine disulfide linkage in the extracellular amino-terminal domain and here we show that GPRC6A indeed is a homodimer and that a disulfide bridge between the C131 residues is formed.	Disulfides	77-86	G protein-coupled receptor class C group 6 member A	Homo sapiens	160-166
20384132-0	2010	[Effects of redox state of disulfide bonds on the intrinsic fluorescence and denaturation of Trx-fused gibberellin-induced cysteine-rich protein from Gymnadnia conopsea].	Disulfides	27-36	thioredoxin	Homo sapiens	93-96
1839706-2	1991	Its unique immunochemical properties are caused by the Lp(a) polypeptide chain which is attached to apolipoprotein B (apoB) by a disulfide bridge.	Disulfides	129-138	lipoprotein(a)	Homo sapiens	55-60
19950203-9	2010	Disulfide bond formation between Twist1 homodimers significantly reduced its ability to interact with two of its binding partners, Runx2 and HDAC4, indicating that disulfide dimerization in response to H(2)O(2) has functional significance.	Disulfides	0-9	histone deacetylase 4	Homo sapiens	141-146
19950203-9	2010	Disulfide bond formation between Twist1 homodimers significantly reduced its ability to interact with two of its binding partners, Runx2 and HDAC4, indicating that disulfide dimerization in response to H(2)O(2) has functional significance.	Disulfides	164-173	histone deacetylase 4	Homo sapiens	141-146
20225300-1	2010	Hepcidin is a four disulfide 25-residue peptide hormone which has a central role in the regulation of iron homeostasis.	Disulfides	19-28	hepcidin antimicrobial peptide	Homo sapiens	0-8
25710793-4	2015	Reduction of the disulfide bond located in the middle of LA stimulates HtrA activity in vivo suggesting that this S-S bond may play a regulatory role, although the mechanism of this stimulation is not known.	Disulfides	17-26	HtrA serine peptidase 1	Homo sapiens	71-75
25710793-8	2015	Thus, the lack of the disulfide within LA affected the stability and the overall structure of the HtrA molecule.	Disulfides	22-31	HtrA serine peptidase 1	Homo sapiens	98-102
19687800-4	2010	We showed that a large disulfide-bonded complex was present in the mouse cells that included ERp57, tapasin, and K(d).	Disulfides	23-32	protein disulfide isomerase associated 3	Mus musculus	93-98
1773019-0	1991	Crystallization and chemical modification of disulfide bond of calf chymosin.	Disulfides	45-54	chymosin	Bos taurus	68-76
19943337-1	2010	A 12-mer peptide nucleic acid (PNA) directed against the nociceptin/orphanin FQ receptor mRNA was disulfide bridged with various peptides without and with cell-penetrating features.	Disulfides	98-107	prepronociceptin	Rattus norvegicus	57-67
19902913-7	2010	Using this algorithm, we successfully identified about a dozen novel disulfide bonds in a hexa EF-hand calcium binding protein secretagogin and in a methionine sulfoxide reductase.	Disulfides	69-78	secretagogin, EF-hand calcium binding protein	Homo sapiens	127-139
25542804-6	2015	Here, a nano-DDS, GD16 peptide (H2N-GRCTNFHNFIYICFPD-CONH2, containing a disulfide bond between Cys3 and Cys13) conjugated nanoparticles loading paclitaxel (GD16-PTX-NP), which can specifically target the angiogenic marker Dll4, was fabricated for the investigation of antiangiogenic therapeutic efficacy in human head and neck cancer FaDu (Dll4-negative) xenograft in nude mice.	Disulfides	73-82	delta like canonical Notch ligand 4	Homo sapiens	223-227
25542804-6	2015	Here, a nano-DDS, GD16 peptide (H2N-GRCTNFHNFIYICFPD-CONH2, containing a disulfide bond between Cys3 and Cys13) conjugated nanoparticles loading paclitaxel (GD16-PTX-NP), which can specifically target the angiogenic marker Dll4, was fabricated for the investigation of antiangiogenic therapeutic efficacy in human head and neck cancer FaDu (Dll4-negative) xenograft in nude mice.	Disulfides	73-82	delta like canonical Notch ligand 4	Homo sapiens	341-345
1773019-4	1991	One disulfide bond located on the surface of chymosin molecule was reduced by 0.72 mM dithiothreitol (DTT) at pH 6.3.	Disulfides	4-13	chymosin	Bos taurus	45-53
25500122-3	2015	Activity is provided by a subfraction of h2, h2B, that is structurally constrained due its unique arrangement of hinge region disulfide bonds.	Disulfides	126-135	H2B clustered histone 21	Homo sapiens	45-48
1915695-2	1991	The spaceflight data suggest that formation of high molecular weight bioactive disulfide-linked aggregates of the 20 and 22K monomeric GH forms may be reduced in microgravity, thereby, reducing target tissue activity.	Disulfides	79-88	gonadotropin releasing hormone receptor	Rattus norvegicus	135-137
25514977-5	2015	The disulfide-bonded CTLA-2alpha/cathepsin L complex was isolated from mouse tissue.	Disulfides	4-13	cathepsin L	Mus musculus	33-44
18440095-0	2010	BRI2 homodimerizes with the involvement of intermolecular disulfide bonds.	Disulfides	58-67	integral membrane protein 2B	Homo sapiens	0-4
18440095-6	2010	We found that BRI2 dimerizes in cells and that dimers are held via non-covalent interactions and via disulfide bridges between the cysteines at position 89.	Disulfides	101-110	integral membrane protein 2B	Homo sapiens	14-18
1845824-5	1991	The formation of disulfide linkages and dimerization allow the transport of gp128 to the Golgi compartments where modification of N-linked carbohydrate structures and extension of O-linked oligosaccharide chains take place, cumulating in the appearance of the mature gp150.	Disulfides	17-26	alanyl aminopeptidase, membrane	Homo sapiens	267-272
19861413-5	2009	Based on a crystal structure of the nAChRalpha1 ECD, we generated a model of the human GlyRalpha1 where close proximity of the respective cysteines was consistent with the formation of both the Cys-loop and the GlyR-specific disulfide bonds.	Disulfides	225-234	glycine receptor alpha 1	Homo sapiens	87-97
19861413-6	2009	To identify native disulfide bonds, the GlyRalpha1 ECD was heterologously expressed and refolded under oxidative conditions.	Disulfides	19-28	glycine receptor alpha 1	Homo sapiens	40-50
25320327-0	2015	The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection.	Disulfides	69-78	DNA packaging protein UL32	Human alphaherpesvirus 1	54-58
25320327-8	2015	In addition, the disulfide bond profiles of the viral proteins UL6, UL25, and VP19C and the viral protease, VP24, were altered in the absence of UL32, suggesting that UL32 may act to modulate disulfide bond formation during procapsid assembly and maturation.	Disulfides	17-26	DNA packaging protein UL32	Human alphaherpesvirus 1	167-171
25320327-8	2015	In addition, the disulfide bond profiles of the viral proteins UL6, UL25, and VP19C and the viral protease, VP24, were altered in the absence of UL32, suggesting that UL32 may act to modulate disulfide bond formation during procapsid assembly and maturation.	Disulfides	192-201	DNA packaging protein UL32	Human alphaherpesvirus 1	167-171
25320327-10	2015	UL32 is a cysteine-rich viral protein that contains C-X-X-C motifs reminiscent of those in proteins that participate in the regulation of disulfide bond formation.	Disulfides	138-147	DNA packaging protein UL32	Human alphaherpesvirus 1	0-4
25320327-12	2015	In this report, we demonstrate that the disulfide bond profiles of the viral proteins UL6, UL25, and VP19C and the viral protease, VP24, are altered in cells infected with a newly isolated UL32-null mutant virus, suggesting that UL32 acts as a chaperone capable of modulating disulfide bond formation.	Disulfides	40-49	DNA packaging protein UL32	Human alphaherpesvirus 1	189-193
25320327-12	2015	In this report, we demonstrate that the disulfide bond profiles of the viral proteins UL6, UL25, and VP19C and the viral protease, VP24, are altered in cells infected with a newly isolated UL32-null mutant virus, suggesting that UL32 acts as a chaperone capable of modulating disulfide bond formation.	Disulfides	40-49	DNA packaging protein UL32	Human alphaherpesvirus 1	229-233
25320327-12	2015	In this report, we demonstrate that the disulfide bond profiles of the viral proteins UL6, UL25, and VP19C and the viral protease, VP24, are altered in cells infected with a newly isolated UL32-null mutant virus, suggesting that UL32 acts as a chaperone capable of modulating disulfide bond formation.	Disulfides	276-285	DNA packaging protein UL32	Human alphaherpesvirus 1	189-193
1845824-8	1991	However, the cleavage process is incomplete, resulting in the formation of multiple disulfide-linked complexes made up of different combinations of gp52, gp105, and gp150.	Disulfides	84-93	alanyl aminopeptidase, membrane	Homo sapiens	165-170
25320327-12	2015	In this report, we demonstrate that the disulfide bond profiles of the viral proteins UL6, UL25, and VP19C and the viral protease, VP24, are altered in cells infected with a newly isolated UL32-null mutant virus, suggesting that UL32 acts as a chaperone capable of modulating disulfide bond formation.	Disulfides	276-285	DNA packaging protein UL32	Human alphaherpesvirus 1	229-233
2289679-3	1990	The sea turtle PRL consists of 198 amino acid residues with three disulfide linkages formed between residues 4-11, 58-173, and 190-198 and possesses heterogeneity indicated by four replacements at positions 55, 145, 148, and 171.	Disulfides	66-75	prolactin	Chelonia mydas	15-18
25725525-11	2015	Thioredoxin reduces the disulfide bond more effectively than dithiothreitol, although the specificity mechanism has not been identified.	Disulfides	24-33	thioredoxin	Homo sapiens	0-11
26064419-7	2015	An increase in total antioxidant activity (82%, p &lt;= 0.01) and thiol-disulfide system response (thioredoxin increasing by 33%, p &lt;= 0.01; glutathione, 30%, p &lt;= 0.01 with stable reductases levels) maintains a balance of peroxidation-antioxidant processes, protecting cellular and subcellular structures from significant oxidative damage.	Disulfides	72-81	thioredoxin	Homo sapiens	99-110
19850922-6	2009	Val(A16) destabilizes the native state and so presumably perturbs a partial fold that directs initial disulfide pairing.	Disulfides	102-111	immunoglobulin kappa variable 3-31 (pseudogene)	Homo sapiens	0-7
19625007-2	2009	To solve such an efficiency-versus-cytotoxicity catch-22 problem, the disulfide bond has been previously used to link less toxic short PEI chains (2 kD), but previous literature results are controversial.	Disulfides	70-79	DiGeorge syndrome chromosome region	Homo sapiens	48-56
19703554-12	2009	In contrast, the oxidation of Trx1, Trx2, and Prx3 was reversible by disulfide reductants.	Disulfides	69-78	thioredoxin	Homo sapiens	30-34
19703554-12	2009	In contrast, the oxidation of Trx1, Trx2, and Prx3 was reversible by disulfide reductants.	Disulfides	69-78	thioredoxin 2	Homo sapiens	36-40
2258710-3	1990	Contrary to previous reports, we demonstrate here that the disulfide loop was required for the mitogenic activity of SEA and SEB.	Disulfides	59-68	SET binding protein 1	Homo sapiens	125-128
19679655-0	2009	Deciphering structural and functional roles of individual disulfide bonds of the mitochondrial sulfhydryl oxidase Erv1p.	Disulfides	58-67	growth factor, augmenter of liver regeneration	Homo sapiens	114-119
19679655-12	2009	Thus, we provided the first experimental evidence of electron transfer between the shuttle and active site disulfides of Erv1p, and we propose that both intersubunit and intermolecular electron transfer can occur.	Disulfides	107-117	growth factor, augmenter of liver regeneration	Homo sapiens	121-126
25551757-3	2014	Tetraspanin EC2 are all likely to have a conserved three helix sub-domain and a much less well-conserved or hypervariable sub-domain formed by short helices and interconnecting loops stabilised by two or more disulfide bridges.	Disulfides	209-218	transcription factor 15	Homo sapiens	12-15
25551757-6	2014	The cysteine residues involved in the formation of the disulfide bridges in CD9 EC2 were all essential for inhibitory activity but a conserved glycine residue in the tetraspanin-defining "CCG" motif was not.	Disulfides	55-64	transcription factor 15	Homo sapiens	80-83
2258710-6	1990	The disulfide linkage imparts considerable stability to these toxins as peptide cleavages within the loop of SEB were not associated with detectable loss of function, although cleavage in the conserved sequence outside the loop of SEA resulted in loss of mitogenic activity.	Disulfides	4-13	SET binding protein 1	Homo sapiens	109-112
19388826-4	2009	Here, we show that protein disulfide isomerase (PDI) catalyzes the disulfide bond formation of MHC class I molecules and thereby facilitates the assembly of MHC class I heavy chain with beta(2)-microglobulin (beta(2)m).	Disulfides	27-36	beta-2-microglobulin	Homo sapiens	186-207
2121540-4	1990	The overcome this, a short amino acid sequence from diphtheria toxin was engineered between the RTA and PA to produce a disulfide-linked loop containing a trypsin sensitive cleavage site.	Disulfides	120-129	RNA binding fox-1 homolog 2	Homo sapiens	96-99
19388826-4	2009	Here, we show that protein disulfide isomerase (PDI) catalyzes the disulfide bond formation of MHC class I molecules and thereby facilitates the assembly of MHC class I heavy chain with beta(2)-microglobulin (beta(2)m).	Disulfides	27-36	beta-2-microglobulin	Homo sapiens	209-217
19388826-7	2009	These observations suggest that PDI-catalyzed disulfide bond formation of MHC class I molecules is an event downstream of the interaction of class I molecules with calnexin and upstream of their interaction with beta(2)m.	Disulfides	46-55	beta-2-microglobulin	Homo sapiens	212-220
19422058-2	2009	The SPINK2 protein contains a typical Kazal domain composed by six cysteine residues forming three disulfide bridges.	Disulfides	99-108	serine peptidase inhibitor Kazal type 2	Homo sapiens	4-10
25362663-1	2014	Glutaredoxin 2 (Grx2) is an isozyme of glutaredoxin1 (thioltransferase) present in the mitochondria and nucleus with disulfide reductase and peroxidase activities, and it controls thiol/disulfide balance in cells.	Disulfides	117-126	glutaredoxin 2 (thioltransferase)	Mus musculus	0-14
25362663-1	2014	Glutaredoxin 2 (Grx2) is an isozyme of glutaredoxin1 (thioltransferase) present in the mitochondria and nucleus with disulfide reductase and peroxidase activities, and it controls thiol/disulfide balance in cells.	Disulfides	117-126	glutaredoxin 2 (thioltransferase)	Mus musculus	16-20
25400026-0	2014	Disulfide-mediated stabilization of the IkappaB kinase binding domain of NF-kappaB essential modulator (NEMO).	Disulfides	0-9	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	73-102
2121540-5	1990	Cleavage of this fusion protein with trypsin converted the RTA-DT-PA to the two chain form consisting of RTA linked by a disulfide bond to PA.	Disulfides	121-130	RNA binding fox-1 homolog 2	Homo sapiens	59-62
25400026-0	2014	Disulfide-mediated stabilization of the IkappaB kinase binding domain of NF-kappaB essential modulator (NEMO).	Disulfides	0-9	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	104-108
2221913-1	1990	Thioltransferase, catalyzing thiol-disulfide interchange between reduced glutathione and disulfides, was purified to homogeneity from Saccharomyces cerevisiae.	Disulfides	89-99	glutaredoxin	Homo sapiens	0-16
25400026-10	2014	The disulfide-linked constructs we describe herein may be useful for crystallization of NEMO"s IKKbeta binding domain in the absence of bound IKKbeta, thereby facilitating the structural characterization of small-molecule inhibitors.	Disulfides	4-13	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	88-92
25400026-10	2014	The disulfide-linked constructs we describe herein may be useful for crystallization of NEMO"s IKKbeta binding domain in the absence of bound IKKbeta, thereby facilitating the structural characterization of small-molecule inhibitors.	Disulfides	4-13	inhibitor of nuclear factor kappa B kinase subunit beta	Homo sapiens	95-102
19553669-1	2009	Hepcidin is a tightly folded 25-residue peptide hormone containing four disulfide bonds, which has been shown to act as the principal regulator of iron homeostasis in vertebrates.	Disulfides	72-81	hepcidin antimicrobial peptide	Homo sapiens	0-8
19553669-2	2009	We used multiple techniques to demonstrate a disulfide bonding pattern for hepcidin different from that previously published.	Disulfides	45-54	hepcidin antimicrobial peptide	Homo sapiens	75-83
2119582-2	1990	The mature TGF beta molecule is a 25 kDa protein composed of two 12.5 kDa monomers linked by disulfide bonds.	Disulfides	93-102	transforming growth factor alpha	Homo sapiens	11-19
19549785-0	2009	Identification of a disulfide bridge essential for transport function of the human proton-coupled amino acid transporter hPAT1.	Disulfides	20-29	solute carrier family 36 member 1	Homo sapiens	121-126
19549785-10	2009	Biotinylation of free sulfhydryl groups using maleimide-PEG(11)-biotin and SDS-PAGE analysis under reducing and nonreducing conditions provided direct evidence for the existence of an essential disulfide bond between Cys-180 and Cys-329.	Disulfides	194-203	retrotransposon Gag like 1	Homo sapiens	56-63
25526565-1	2014	Thioredoxin domain-containing 5 (TXNDC5) is a member of the protein disulfide isomerase family, acting as a chaperone of endoplasmic reticulum under not fully characterized conditions As a result, TXNDC5 interacts with many cell proteins, contributing to their proper folding and correct formation of disulfide bonds through its thioredoxin domains.	Disulfides	68-77	thioredoxin domain containing 5	Homo sapiens	0-31
25526565-1	2014	Thioredoxin domain-containing 5 (TXNDC5) is a member of the protein disulfide isomerase family, acting as a chaperone of endoplasmic reticulum under not fully characterized conditions As a result, TXNDC5 interacts with many cell proteins, contributing to their proper folding and correct formation of disulfide bonds through its thioredoxin domains.	Disulfides	68-77	thioredoxin domain containing 5	Homo sapiens	33-39
25526565-1	2014	Thioredoxin domain-containing 5 (TXNDC5) is a member of the protein disulfide isomerase family, acting as a chaperone of endoplasmic reticulum under not fully characterized conditions As a result, TXNDC5 interacts with many cell proteins, contributing to their proper folding and correct formation of disulfide bonds through its thioredoxin domains.	Disulfides	68-77	thioredoxin domain containing 5	Homo sapiens	197-203
25448389-7	2014	Unlike other venomous animals, a number of ant venoms also contain a range of homodimeric and heterodimeric peptides with one or two interchain disulfide bonds possessing pore-forming, allergenic and paralytic actions.	Disulfides	144-153	solute carrier family 25 member 6	Homo sapiens	43-46
25448389-8	2014	However, ant venoms seem to have only a small number of monomeric disulfide-linked peptides.	Disulfides	66-75	solute carrier family 25 member 6	Homo sapiens	9-12
19477928-1	2009	Mia40 and Erv1 execute a disulfide relay to import the small Tim proteins into the mitochondrial intermembrane space.	Disulfides	25-34	growth factor, augmenter of liver regeneration	Homo sapiens	10-14
19477928-8	2009	Last, mutating C133 of the catalytic C130-C133 pair or C30 of the shuttle C30-C33 pair in Erv1 abolished oxidation of Tim13, whereas mutating the cysteines in the redox-active CPC motif, but not the structural disulfide linkages of the CX(9)C motif of Mia40, prevented Tim13 oxidation.	Disulfides	210-219	growth factor, augmenter of liver regeneration	Homo sapiens	90-94
19597482-1	2009	Thioredoxins (Trxs) are oxidoreductase enzymes, present in all organisms, that catalyze the reduction of disulfide bonds in proteins.	Disulfides	105-114	thioredoxin	Homo sapiens	0-12
2376594-2	1990	ApoJ is a glycoprotein consisting of disulfide-linked subunits of 34-36 and 36-39 kDa.	Disulfides	37-46	clusterin	Homo sapiens	0-4
19597482-2	2009	By applying a calibrated force to a substrate disulfide, the chemical mechanisms of Trx catalysis can be examined in detail at the single-molecule level.	Disulfides	46-55	thioredoxin	Homo sapiens	84-87
19675666-0	2009	How thioredoxin dissociates its mixed disulfide.	Disulfides	38-47	thioredoxin	Homo sapiens	4-15
19675666-1	2009	The dissociation mechanism of the thioredoxin (Trx) mixed disulfide complexes is unknown and has been debated for more than twenty years.	Disulfides	58-67	thioredoxin	Homo sapiens	34-45
19675666-1	2009	The dissociation mechanism of the thioredoxin (Trx) mixed disulfide complexes is unknown and has been debated for more than twenty years.	Disulfides	58-67	thioredoxin	Homo sapiens	47-50
25332193-7	2014	Formation of the disulfide bond causes compaction of AS69-GS3, increases its thermostability, and is a prerequisite for high-affinity binding to alpha-syn.	Disulfides	17-26	synuclein alpha	Homo sapiens	145-154
25332193-8	2014	Comparison of AS69-GS3 and AS69 demonstrates that head-to-tail linkage promotes alpha-syn binding by affording accelerated disulfide bond formation.	Disulfides	123-132	synuclein alpha	Homo sapiens	80-89
19675666-5	2009	With theoretical reactivity analysis, molecular dynamics simulations, and biochemical complex formation experiments with Cys-mutants, Trx mixed disulfide dissociation was studied.	Disulfides	144-153	thioredoxin	Homo sapiens	134-137
2272751-7	1990	Disulfide bridging across antiparallel extended strands is observed in alpha-lytic protease, crambin, and beta-trypsin and this structure is shown to be very similar to those obtained in small cystine peptides.	Disulfides	0-9	serine protease 1	Homo sapiens	106-118
19675666-9	2009	This multidisciplinary approach provides fresh insights into a universal thiol/disulfide exchange reaction mechanism that results in reduced substrate and oxidized Trx.	Disulfides	79-88	thioredoxin	Homo sapiens	164-167
25253686-4	2014	Assessment of phagosomal disulfide reduction upon internalization of IgG-opsonized experimental particles confirmed a major role for GILT in phagosomal disulfide reduction in both resting and interferon-gamma-activated macrophages.	Disulfides	152-161	interferon gamma inducible protein 30	Mus musculus	133-137
2142832-4	1990	Lp(a) is essentially an LDL-like lipoprotein particle to which the glycoprotein apo(a) is attached through a disulfide bridge with apo B-100.	Disulfides	109-118	lipoprotein(a)	Homo sapiens	80-86
24898092-0	2014	Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1.	Disulfides	10-19	heat shock protein family B (small) member 1	Homo sapiens	118-123
24898092-1	2014	Temperature-induced conformational changes of reduced and oxidized HspB1 crosslinked by disulfide bond between single Cys137 of neighboring monomers were analyzed by means of different techniques.	Disulfides	88-97	heat shock protein family B (small) member 1	Homo sapiens	67-72
24898092-7	2014	It is concluded that oxidative stress, inducing formation of disulfide bond, can affect stability and conformational mobility of human HspB1.	Disulfides	61-70	heat shock protein family B (small) member 1	Homo sapiens	135-140
24094148-0	2014	Disulfide-containing high mobility group box-1 promotes N-methyl-D-aspartate receptor function and excitotoxicity by activating Toll-like receptor 4-dependent signaling in hippocampal neurons.	Disulfides	0-9	glutamate receptor, ionotropic, NMDA1 (zeta 1)	Mus musculus	56-85
19469538-4	2009	Fab fragments were generated by reduction of the disulfide bond of F(ab)(2) fragments obtained by bromelain digestion of CDC5 antibody.	Disulfides	49-58	FA complementation group B	Homo sapiens	0-3
19374945-5	2009	WFDC1 is a small secretory protein containing a WAP-type four disulfide core domain.	Disulfides	62-71	WAP four-disulfide core domain 1	Bos taurus	0-5
2138452-1	1990	Lipoprotein(a) (Lp[a]) is a complex plasma lipoprotein in which apolipoprotein (apo) B-100 is covalently linked by a disulfide bridge to a unique apolipoprotein, apo(a).	Disulfides	117-126	lipoprotein(a)	Homo sapiens	0-14
19369327-0	2009	Disulfide bond formation at the C termini of vaccinia virus A26 and A27 proteins does not require viral redox enzymes and suppresses glycosaminoglycan-mediated cell fusion.	Disulfides	0-9	immunoglobulin kappa variable 6-21 (non-functional)	Homo sapiens	60-63
19369327-5	2009	A26 protein contains six cysteine residues, and in vitro mutagenesis showed that Cys441 and Cys442 mediated intermolecular disulfide bonds with Cys71 and Cys72 of viral A27 protein, whereas Cys43 and Cys342 mediated intramolecular disulfide bonds.	Disulfides	123-132	immunoglobulin kappa variable 6-21 (non-functional)	Homo sapiens	0-3
19369327-5	2009	A26 protein contains six cysteine residues, and in vitro mutagenesis showed that Cys441 and Cys442 mediated intermolecular disulfide bonds with Cys71 and Cys72 of viral A27 protein, whereas Cys43 and Cys342 mediated intramolecular disulfide bonds.	Disulfides	231-240	immunoglobulin kappa variable 6-21 (non-functional)	Homo sapiens	0-3
19369327-6	2009	A26 and A27 proteins formed disulfide-linked complexes in transfected 293T cells, showing that the intermolecular disulfide bond formation did not depend on viral redox pathways.	Disulfides	28-37	immunoglobulin kappa variable 6-21 (non-functional)	Homo sapiens	0-3
19369327-6	2009	A26 and A27 proteins formed disulfide-linked complexes in transfected 293T cells, showing that the intermolecular disulfide bond formation did not depend on viral redox pathways.	Disulfides	114-123	immunoglobulin kappa variable 6-21 (non-functional)	Homo sapiens	0-3
19397338-1	2009	Augmenter of liver regeneration (ALR) is both a growth factor and a sulfhydryl oxidase that binds FAD in an unusual helix-rich domain containing a redox-active CxxC disulfide proximal to the flavin ring.	Disulfides	165-174	growth factor, augmenter of liver regeneration	Homo sapiens	0-31
19397338-1	2009	Augmenter of liver regeneration (ALR) is both a growth factor and a sulfhydryl oxidase that binds FAD in an unusual helix-rich domain containing a redox-active CxxC disulfide proximal to the flavin ring.	Disulfides	165-174	growth factor, augmenter of liver regeneration	Homo sapiens	33-36
26461388-6	2014	Here we examine the design requirements for the Peroxiredoxin/Thioredoxin/Thioredoxin-Reductase/Protein-Dithiol System (PTTRDS) to effectively integrate H2O2 signaling and anticipatory blocking of protein dithiols as disulfides, and we compared them to the designs found in cells.	Disulfides	217-227	thioredoxin	Homo sapiens	62-73
26461388-6	2014	Here we examine the design requirements for the Peroxiredoxin/Thioredoxin/Thioredoxin-Reductase/Protein-Dithiol System (PTTRDS) to effectively integrate H2O2 signaling and anticipatory blocking of protein dithiols as disulfides, and we compared them to the designs found in cells.	Disulfides	217-227	peroxiredoxin 5	Homo sapiens	74-95
25220457-3	2014	Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction.	Disulfides	201-210	thioredoxin	Homo sapiens	23-34
25220457-3	2014	Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction.	Disulfides	201-210	peroxiredoxin 5	Homo sapiens	281-302
25220457-3	2014	Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction.	Disulfides	201-210	thioredoxin	Homo sapiens	45-56
28470603-0	2017	A Generic Protocol for Purifying Disulfide-Bonded Domains and Random Protein Fragments Using Fusion Proteins with SUMO3 and Cleavage by SenP2 Protease.	Disulfides	33-42	SUMO specific peptidase 2	Homo sapiens	136-141
25135935-3	2014	The lumenally oriented active site CVVC motif in MagT1 is required for glycosylation of STT3B-dependent acceptor sites including those that are closely bracketed by disulfides or contain cysteine as the internal residue (NCT/S).	Disulfides	165-175	STT3 oligosaccharyltransferase complex catalytic subunit B	Homo sapiens	88-93
25135935-5	2014	The predominant form of MagT1 in vivo is oxidized, which is consistent with transient formation of mixed disulfides between MagT1 and a glycoprotein substrate to facilitate access of STT3B to unmodified acceptor sites.	Disulfides	105-115	STT3 oligosaccharyltransferase complex catalytic subunit B	Homo sapiens	183-188
25135935-6	2014	Cotranslational N-glycosylation by the STT3A isoform of the OST, which lacks MagT1, allows efficient modification of acceptor sites in cysteine-rich protein domains before disulfide bond formation.	Disulfides	172-181	STT3 oligosaccharyltransferase complex catalytic subunit A	Homo sapiens	39-44
18951281-5	2009	The TLXI structure model, generated with the crystal structure of thaumatin as template, shows the occurrence of five disulfide bridges and three beta-sheets.	Disulfides	118-127	tlxi	Triticum aestivum	4-8
18951281-8	2009	All ten cysteine residues in TLXI are involved in disulfide bridges.	Disulfides	50-59	tlxi	Triticum aestivum	29-33
19250966-6	2009	The pathway is redox-sensitive and oxidation of Tf thiols to disulfides induces release from Tf of highly reactive ferrous iron, which contributes to free radical production.	Disulfides	61-71	coagulation factor III, tissue factor	Homo sapiens	48-50
19250966-6	2009	The pathway is redox-sensitive and oxidation of Tf thiols to disulfides induces release from Tf of highly reactive ferrous iron, which contributes to free radical production.	Disulfides	61-71	coagulation factor III, tissue factor	Homo sapiens	93-95
25880503-8	2015	While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding.	Disulfides	85-95	glutaredoxin	Homo sapiens	22-34
19034494-0	2009	Probing S4 and S5 segment proximity in mammalian hyperpolarization-activated HCN channels by disulfide bridging and Cd2+ coordination.	Disulfides	93-102	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	77-80
24988145-5	2014	Application of the new methodology to the top-down HDX MS characterization of a small (99 residue long) disulfide-containing protein beta2-microglobulin allowed the backbone amide protection to be probed with nearly a single-residue resolution across the entire sequence.	Disulfides	104-113	beta-2-microglobulin	Homo sapiens	133-152
25880503-8	2015	While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding.	Disulfides	85-95	prolyl 4-hydroxylase subunit beta	Homo sapiens	181-184
25109988-7	2014	The consequences of the regulation of the FOXO4 (forkhead box O4) transcription factor by formation of intermolecular disulfides with both TNPO1 (transportin 1) and p300/CBP [CREB (cAMP-response-element-binding protein)-binding protein] are discussed in more detail.	Disulfides	118-128	forkhead box O4	Homo sapiens	42-47
25880503-8	2015	While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding.	Disulfides	85-94	glutaredoxin	Homo sapiens	22-34
25109988-7	2014	The consequences of the regulation of the FOXO4 (forkhead box O4) transcription factor by formation of intermolecular disulfides with both TNPO1 (transportin 1) and p300/CBP [CREB (cAMP-response-element-binding protein)-binding protein] are discussed in more detail.	Disulfides	118-128	forkhead box O4	Homo sapiens	49-64
25109988-7	2014	The consequences of the regulation of the FOXO4 (forkhead box O4) transcription factor by formation of intermolecular disulfides with both TNPO1 (transportin 1) and p300/CBP [CREB (cAMP-response-element-binding protein)-binding protein] are discussed in more detail.	Disulfides	118-128	transportin 1	Homo sapiens	139-144
25109988-7	2014	The consequences of the regulation of the FOXO4 (forkhead box O4) transcription factor by formation of intermolecular disulfides with both TNPO1 (transportin 1) and p300/CBP [CREB (cAMP-response-element-binding protein)-binding protein] are discussed in more detail.	Disulfides	118-128	transportin 1	Homo sapiens	146-159
24863694-2	2014	The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress.	Disulfides	147-157	thioredoxin	Homo sapiens	4-15
24863694-2	2014	The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress.	Disulfides	147-157	thioredoxin	Homo sapiens	17-20
19375587-11	2009	A synthetic cyclized Cys(1)-to-Cys(19) disulfide-bonded peptide (BMP binding peptide) corresponding to the transforming growth factor-beta receptor II homology 1 domain of spp24 and spp18.5 binds BMP-2 and increases the rate and magnitude of BMP-2-mediated ectopic bone formation.	Disulfides	39-48	bone morphogenetic protein 1	Homo sapiens	65-68
19375587-11	2009	A synthetic cyclized Cys(1)-to-Cys(19) disulfide-bonded peptide (BMP binding peptide) corresponding to the transforming growth factor-beta receptor II homology 1 domain of spp24 and spp18.5 binds BMP-2 and increases the rate and magnitude of BMP-2-mediated ectopic bone formation.	Disulfides	39-48	secreted phosphoprotein 2	Homo sapiens	172-177
19170994-8	2009	RESULTS: Using disulfide-reducing compounds to chemically modify anti-D significantly increases the efficacy of the anti-D to induce an FcgammaR blockade and decrease phagocytosis in vitro of opsonized D+ or D- RBCs.	Disulfides	15-24	Fc gamma receptor Ia	Homo sapiens	136-144
19170994-11	2009	CONCLUSION: Our results demonstrate that irreversible reduction of interchain disulfide bonds within the immunoglobulin anti-D results in a significantly increased efficacy to inhibit FcgammaR-mediated phagocytosis regardless of opsonized target cell.	Disulfides	78-87	Fc gamma receptor Ia	Homo sapiens	184-192
25880503-8	2015	While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding.	Disulfides	85-94	prolyl 4-hydroxylase subunit beta	Homo sapiens	181-184
24971648-0	2014	Mass spectrometric determination of disulfide bonds in the biologically active recombinant HBx protein of hepatitis B virus.	Disulfides	36-45	X protein	Hepatitis B virus	91-94
25880503-8	2015	While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding.	Disulfides	106-115	glutaredoxin	Homo sapiens	22-34
24971648-6	2014	Now we have determined the disulfide linkages in soluble and biologically active recombinant maltose binding protein-HBx fusion protein using matrix-assisted laser desorption ionization time-of-flight mass spectrometry.	Disulfides	27-36	X protein	Hepatitis B virus	117-120
25880503-8	2015	While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding.	Disulfides	106-115	prolyl 4-hydroxylase subunit beta	Homo sapiens	152-179
24971648-7	2014	We report four disulfide linkages in HBx protein, viz., between Cys(7) and Cys(69), Cys(61) and Cys(115), Cys(78) and Cys(137), and Cys(17) and Cys(143), based on the differential mobility of corresponding disulfide-linked peptide ions under reducing and nonreducing conditions.	Disulfides	15-24	X protein	Hepatitis B virus	37-40
24971648-7	2014	We report four disulfide linkages in HBx protein, viz., between Cys(7) and Cys(69), Cys(61) and Cys(115), Cys(78) and Cys(137), and Cys(17) and Cys(143), based on the differential mobility of corresponding disulfide-linked peptide ions under reducing and nonreducing conditions.	Disulfides	206-215	X protein	Hepatitis B virus	37-40
19245794-11	2009	The SWn sequence also harbored one cysteine residue that could form a disulfide bridge between two Fab-SWn-PE38 monomers.	Disulfides	70-79	FA complementation group B	Homo sapiens	99-102
25880503-8	2015	While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding.	Disulfides	106-115	prolyl 4-hydroxylase subunit beta	Homo sapiens	181-184
15050695-4	2004	Both AmGluRA and AmGluRB form homodimers independently on disulfide bonds, and bind [3H]glutamate with K(D) values of 156.7 and 80.7 nM, respectively.	Disulfides	58-67	metabotropic glutamate receptor B	Apis mellifera	17-24
19343240-2	2009	We describe the replacement of the A-chain intramolecular disulfide bond of human relaxin-3 (H3 relaxin, INSL7), an insulin-like peptide that has potential applications in the treatment of stress and obesity, with the physiologically stable dicarba bond.	Disulfides	58-67	relaxin 3	Homo sapiens	82-103
19343240-2	2009	We describe the replacement of the A-chain intramolecular disulfide bond of human relaxin-3 (H3 relaxin, INSL7), an insulin-like peptide that has potential applications in the treatment of stress and obesity, with the physiologically stable dicarba bond.	Disulfides	58-67	relaxin 3	Homo sapiens	105-110
24483600-1	2014	SIGNIFICANCE: The thioredoxin (Trx) superfamily proteins, including protein disulfide isomerases (PDI) and Dsb protein family, are major players in oxidative protein folding, which involves native disulfide bond formation.	Disulfides	76-85	thioredoxin	Homo sapiens	18-29
24483600-1	2014	SIGNIFICANCE: The thioredoxin (Trx) superfamily proteins, including protein disulfide isomerases (PDI) and Dsb protein family, are major players in oxidative protein folding, which involves native disulfide bond formation.	Disulfides	76-85	thioredoxin	Homo sapiens	31-34
34931753-6	2022	The expressions of HMGB1 (fully reduced and disulfide (ds)HMGB1), MD-2, and NLRP3 in SAE mice were determined.	Disulfides	55-57	high mobility group box 1	Mus musculus	58-63
24483600-1	2014	SIGNIFICANCE: The thioredoxin (Trx) superfamily proteins, including protein disulfide isomerases (PDI) and Dsb protein family, are major players in oxidative protein folding, which involves native disulfide bond formation.	Disulfides	76-85	peptidyl arginine deiminase 1	Homo sapiens	98-101
24483600-4	2014	Atomic force microscopy revealed that PDI works as a placeholder to prevent early non-native disulfide bond formation and further misfolding.	Disulfides	93-102	peptidyl arginine deiminase 1	Homo sapiens	38-41
24483600-6	2014	CRITICAL ISSUES: Electron transfer pathways of the oxidative protein folding show conserved Trx-like thiol-disulfide chemistry.	Disulfides	107-116	thioredoxin	Homo sapiens	92-95
19351836-8	2009	Analysis of the redox status of the OGG1 protein in the cells confirms that the lower activity of OGG1-Cys326 is associated with the oxidation of Cys326 to form a disulfide bond.	Disulfides	163-172	8-oxoguanine DNA glycosylase	Homo sapiens	36-40
19351836-8	2009	Analysis of the redox status of the OGG1 protein in the cells confirms that the lower activity of OGG1-Cys326 is associated with the oxidation of Cys326 to form a disulfide bond.	Disulfides	163-172	8-oxoguanine DNA glycosylase	Homo sapiens	98-102
19181668-1	2009	The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties.	Disulfides	75-84	thioredoxin	Homo sapiens	15-26
19238172-0	2009	Oxidative modification of caspase-9 facilitates its activation via disulfide-mediated interaction with Apaf-1.	Disulfides	67-76	caspase 9	Homo sapiens	26-35
19238172-5	2009	Hydrogen peroxide treatment causes the activation of caspase-9 and apoptosis, and promotes an interaction between caspase-9 and apoptotic protease-activating factor 1 (Apaf-1) via disulfide formation.	Disulfides	180-189	caspase 9	Homo sapiens	114-123
19238172-6	2009	In addition, in an in vitro mitochondria-free system, the thiol-oxidant diamide promotes auto-cleavage of caspase-9 and the caspase-9/Apaf-1 interaction by facilitating the formation of disulfide-linked complexes.	Disulfides	186-195	caspase 9	Homo sapiens	106-115
19238172-6	2009	In addition, in an in vitro mitochondria-free system, the thiol-oxidant diamide promotes auto-cleavage of caspase-9 and the caspase-9/Apaf-1 interaction by facilitating the formation of disulfide-linked complexes.	Disulfides	186-195	caspase 9	Homo sapiens	124-133
19238172-7	2009	Finally, a point mutation at C403 of caspase-9 impairs both H(2)O(2)-promoted caspase-9 activation and interaction with Apaf-1 through the abolition of disulfide formation.	Disulfides	152-161	caspase 9	Homo sapiens	37-46
19238172-7	2009	Finally, a point mutation at C403 of caspase-9 impairs both H(2)O(2)-promoted caspase-9 activation and interaction with Apaf-1 through the abolition of disulfide formation.	Disulfides	152-161	caspase 9	Homo sapiens	78-87
24959670-4	2014	Post-translational modifications including monoubiquitination and disulfide crosslinking regulate the stability and cellular localization of NT-UCH-L1, as confirmed by mutational and proteomic studies.	Disulfides	66-75	ubiquitin C-terminal hydrolase L1	Homo sapiens	144-150
34519602-1	2021	A novel tumor-targeted glutathione responsive Glycosylated-Camptothecin nanosupramolecular prodrug (CPT-GL NSp) was designed and fabricated via a disulfide bond.	Disulfides	146-155	serine peptidase inhibitor Kazal type 5	Homo sapiens	107-110
24698993-1	2014	Interferon-gamma-inducible lysosomal thiol reductase (GILT) plays a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction, thus unfolding native protein Ag and facilitating subsequent cleavage by proteases.	Disulfides	166-175	interferon gamma inducible protein 30	Mus musculus	54-58
19192250-2	2009	Initially made as an inactive glycosylated disulfide-linked dimer, cystatin F is converted to an active monomer by proteolytic cleavage following transport to the endosomal/lysosomal system.	Disulfides	43-52	cystatin F	Homo sapiens	67-77
19718808-2	2009	The OPG was chemically conjugated to a "bone seeking" thiol-bisphosphonate (thiolBP) via a disulfide linkage.	Disulfides	91-100	TNF receptor superfamily member 11B	Rattus norvegicus	4-7
34943830-0	2021	Post-Translational Modification of HMGB1 Disulfide Bonds in Stimulating and Inhibiting Inflammation.	Disulfides	41-50	high mobility group box 1	Homo sapiens	35-40
18848566-0	2009	Homodimeric chicken galectin CG-1B (C-14): Crystal structure and detection of unique redox-dependent shape changes involving inter- and intrasubunit disulfide bridges by gel filtration, ultracentrifugation, site-directed mutagenesis, and peptide mass fingerprinting.	Disulfides	149-158	galectin 1A	Gallus gallus	20-34
18848566-0	2009	Homodimeric chicken galectin CG-1B (C-14): Crystal structure and detection of unique redox-dependent shape changes involving inter- and intrasubunit disulfide bridges by gel filtration, ultracentrifugation, site-directed mutagenesis, and peptide mass fingerprinting.	Disulfides	149-158	galectin 1A	Gallus gallus	36-40
24661219-12	2014	In addition to disulfide reduction, TrxR is also known to mediate chemical redox cycling.	Disulfides	15-24	peroxiredoxin 5	Homo sapiens	36-40
24661219-13	2014	We found that menadione redox cycling by TrxR was markedly less sensitive to NAPQI than disulfide reduction, suggesting that TrxR mediates these reactions via distinct mechanisms.	Disulfides	88-97	peroxiredoxin 5	Homo sapiens	125-129
24150425-9	2014	The significance of the dehydroascorbate reductase activity of protein disulfide isomerase was debated because protein disulfide isomerase as a dehydroascorbate reductase was found to be too slow to be the major route for the reduction of dehydroascorbate (and formation of disulfides) in the endoplasmic reticulum lumen.	Disulfides	274-284	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	63-90
34411303-7	2021	PIGR/FCAMR/FCMR are members of a larger superfamily including TREM, CD300, and NKp44, which we name the "double-disulfide Ig superfamily" (ddIgSF).	Disulfides	112-121	Fc mu receptor	Homo sapiens	11-15
24150425-9	2014	The significance of the dehydroascorbate reductase activity of protein disulfide isomerase was debated because protein disulfide isomerase as a dehydroascorbate reductase was found to be too slow to be the major route for the reduction of dehydroascorbate (and formation of disulfides) in the endoplasmic reticulum lumen.	Disulfides	274-284	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	111-138
34565182-7	2021	In contrast, the blockade of disulfide bonds formation using a peptide decreased both CaSR and hypoxia-induced mitogenic factor expression as well as other hypoxic-related genes in vitro and in vivo and attenuated pulmonary hypertension development in rats.	Disulfides	29-38	resistin like alpha	Rattus norvegicus	95-127
24759145-2	2014	For the conversion of encrypted into decrypted tissue factor with sufficient procoagulant activity, four distinct models have been proposed: 1; dimer formation, 2; lipid rafts, 3; disulfide bonds, and 4; phosphatidylserine exposure.	Disulfides	180-189	coagulation factor III, tissue factor	Homo sapiens	47-60
19159616-0	2009	Prostate specific antigen: one out of five disulfide bridges determines inactivation by reduction.	Disulfides	43-52	kallikrein related peptidase 3	Homo sapiens	0-25
19159616-7	2009	This indicated that it is the accessabilty of the Cys 191-Cys 220 disulfide near the catalytic serine 195 that decides on the ability of reductants to inactivate the proteolytic activity of PSA.	Disulfides	66-75	kallikrein related peptidase 3	Homo sapiens	190-193
34558135-2	2021	The interaction between the SARS-CoV-2 spike protein and the human receptor angiotensin-converting enzyme 2, both of which contain several cysteine residues, is impacted by the disulfide-thiol balance in the host cell.	Disulfides	177-186	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	39-44
19170525-2	2009	The TRX redox mechanism is based on reversible oxidation of two cysteine thiol groups to a disulfide, accompanied by the transfer of two protons.	Disulfides	91-100	thioredoxin	Homo sapiens	4-7
19106090-5	2009	In the present study, we show that Tsa1 can interact with Yap1 via disulfide linkages and induce the formation of intramolecular disulfide bonds in Yap1 in ybp1-1 cells.	Disulfides	129-138	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	35-39
19106090-5	2009	In the present study, we show that Tsa1 can interact with Yap1 via disulfide linkages and induce the formation of intramolecular disulfide bonds in Yap1 in ybp1-1 cells.	Disulfides	129-138	Ybp1p	Saccharomyces cerevisiae S288C	156-162
24623670-4	2014	A disulfide-linked drug conjugate with the maytansinoid DM1 as the cytotoxic payload and a derivative of acetazolamide as the targeting ligand exhibited a potent antitumor effect in SKRC52 renal cell carcinoma in vivo.	Disulfides	2-11	immunoglobulin heavy diversity 1-7	Homo sapiens	56-59
24452853-5	2014	This article will review some of the still controversial mechanisms implicated in cellular TF activation or decryption with particular focus on the coordinated effects of outer leaflet phosphatidylserine exposure and thiol-disulfide exchange pathways involving protein disulfide isomerase (PDI).	Disulfides	223-232	coagulation factor III, tissue factor	Homo sapiens	91-93
24374250-0	2014	Activity assays of mammalian thioredoxin and thioredoxin reductase: fluorescent disulfide substrates, mechanisms, and use with tissue samples.	Disulfides	80-89	thioredoxin	Homo sapiens	29-40
24374250-0	2014	Activity assays of mammalian thioredoxin and thioredoxin reductase: fluorescent disulfide substrates, mechanisms, and use with tissue samples.	Disulfides	80-89	peroxiredoxin 5	Homo sapiens	45-66
24374250-2	2014	Human cytosolic Trx1 has Cys32 and Cys35 as the active site and three additional cysteine residues (Cys62, Cys69, and Cys73), which by oxidation generates inactive Cys62 to Cys69 two-disulfide Trx.	Disulfides	183-192	thioredoxin	Homo sapiens	16-20
24374250-2	2014	Human cytosolic Trx1 has Cys32 and Cys35 as the active site and three additional cysteine residues (Cys62, Cys69, and Cys73), which by oxidation generates inactive Cys62 to Cys69 two-disulfide Trx.	Disulfides	183-192	thioredoxin	Homo sapiens	16-19
19036822-6	2009	A distinct disulfide bond isomerization and cleavage pattern of the major capsid protein VP1 was observed, which was also influenced by alterations in pH and disruption of trafficking to the ER.	Disulfides	11-20	VP1	Human polyomavirus 1	89-92
19033278-2	2009	Moreover, selection was characterized by enrichment for V(H)s with (i) an even number of disulfide forming Cys residues in complementarity-determining region (CDR) 1 and CDR3 and (ii) acidic isoelectric points.	Disulfides	89-98	cerebellar degeneration related protein 1	Homo sapiens	123-165
19177574-5	2009	We show that ecE and ecK are highly unstable by themselves but form very stable parallel helical tetramers when mixed, as judged by circular dichroism, analytical ultracentrifugation, and disulfide crosslinking studies.	Disulfides	188-197	endothelin converting enzyme 1	Homo sapiens	13-16
34558135-2	2021	The interaction between the SARS-CoV-2 spike protein and the human receptor angiotensin-converting enzyme 2, both of which contain several cysteine residues, is impacted by the disulfide-thiol balance in the host cell.	Disulfides	177-186	angiotensin converting enzyme 2	Homo sapiens	76-107
19177574-5	2009	We show that ecE and ecK are highly unstable by themselves but form very stable parallel helical tetramers when mixed, as judged by circular dichroism, analytical ultracentrifugation, and disulfide crosslinking studies.	Disulfides	188-197	CTPP	Homo sapiens	21-24
34169459-1	2021	Human protein disulfide isomerase (PDI), a protein containing 4 domains a, b, b", a", disordered x linker and C-terminus, plays critical roles in disulfide bond reactions and proper protein folding in the endoplasmic reticulum.	Disulfides	146-155	prolyl 4-hydroxylase subunit beta	Homo sapiens	6-33
19010334-7	2009	The IMS of mitochondria harbors a disulfide relay system consisting of the import receptor Mia40 and the thiol oxidase Erv1, which drives the import of substrates with conserved cysteine residues arranged in typical twin Cx(3)C and twin Cx(9)C motifs.	Disulfides	34-43	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	119-123
24604812-0	2014	Total synthesis of human hepcidin through regioselective disulfide-bond formation by using the safety-catch cysteine protecting group 4,4"-dimethylsulfinylbenzhydryl.	Disulfides	57-66	hepcidin antimicrobial peptide	Homo sapiens	25-33
24604812-2	2014	The directed regioselective synthesis of human hepcidin, which contains four disulfide bonds, was undertaken and led to a high-resolution NMR structure under more physiologically relevant conditions than previously.	Disulfides	77-86	hepcidin antimicrobial peptide	Homo sapiens	47-55
24462249-0	2014	Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.	Disulfides	74-83	thioredoxin	Homo sapiens	20-31
24462249-0	2014	Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family.	Disulfides	74-83	thioredoxin domain containing 5	Homo sapiens	54-59
19071118-0	2009	Disulfide cross-links in the interaction of a cataract-linked alphaA-crystallin mutant with betaB1-crystallin.	Disulfides	0-9	crystallin beta B1	Homo sapiens	92-109
34169459-1	2021	Human protein disulfide isomerase (PDI), a protein containing 4 domains a, b, b", a", disordered x linker and C-terminus, plays critical roles in disulfide bond reactions and proper protein folding in the endoplasmic reticulum.	Disulfides	146-155	prolyl 4-hydroxylase subunit beta	Homo sapiens	35-38
19071118-2	2009	We report the formation of affinity-driven disulfide bonds in the interaction of alphaA-R49C with betaB1-crystallin.	Disulfides	43-52	crystallin beta B1	Homo sapiens	98-115
24462249-1	2014	The mammalian endoplasmic reticulum (ER) contains a diverse oxidative protein folding network in which ERp46, a member of the protein disulfide isomerase (PDI) family, serves as an efficient disulfide bond introducer together with Peroxiredoxin-4 (Prx4).	Disulfides	134-143	thioredoxin domain containing 5	Homo sapiens	103-108
19071118-3	2009	To mimic cysteine thiolation in the lens, betaB1-crystallin was modified by a bimane probe through a disulfide linkage.	Disulfides	101-110	crystallin beta B1	Homo sapiens	42-59
34381568-0	2021	Glucose starvation induces NADPH collapse and disulfide stress in SLC7A11high cancer cells.	Disulfides	46-55	solute carrier family 7 (cationic amino acid transporter, y+ system), member 11	Mus musculus	66-73
19071118-4	2009	Our data suggest a mechanism whereby a transient disulfide bond occurs between alphaA- and betaB1-crystallin followed by a disulfide exchange with cysteine 49 of a neighboring alphaA-crystallin subunit.	Disulfides	49-58	crystallin beta B1	Homo sapiens	91-108
19071118-4	2009	Our data suggest a mechanism whereby a transient disulfide bond occurs between alphaA- and betaB1-crystallin followed by a disulfide exchange with cysteine 49 of a neighboring alphaA-crystallin subunit.	Disulfides	123-132	crystallin beta B1	Homo sapiens	91-108
24357333-1	2014	Urotensin II (U-II) is a disulfide bridged peptide hormone identified as the ligand of a G protein-coupled receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	0-12
34544533-3	2021	Developed based on peptide BP10 with affinity to PROCR as a targeting element, constructing a peptide drug conjugate of BP10 covalently coupling doxorubicin with disulfide bonds.	Disulfides	162-171	protein C receptor	Homo sapiens	49-54
18761382-5	2009	Substrates are imported via a disulfide exchange relay with two components Mia40 and Erv1.	Disulfides	30-39	growth factor, augmenter of liver regeneration	Homo sapiens	85-89
34505054-5	2021	We also report that the ectodomain of syndecan-4, corresponding to a natural isoform, is able to dimerize via a disulfide bond.	Disulfides	112-121	syndecan 4	Homo sapiens	38-48
23045011-2	2009	Examination of thiol/disulfide redox changes in thioredoxin (Trx) family members including Trx1 in cytoplasm and nucleus and Trx2 in mitochondria should aid in the understanding of compartmentalized redox signaling mechanisms.	Disulfides	21-30	thioredoxin	Homo sapiens	48-59
23045011-2	2009	Examination of thiol/disulfide redox changes in thioredoxin (Trx) family members including Trx1 in cytoplasm and nucleus and Trx2 in mitochondria should aid in the understanding of compartmentalized redox signaling mechanisms.	Disulfides	21-30	thioredoxin	Homo sapiens	61-64
18783346-11	2008	CTRP3, CTRP5, CTRP6 and CTRP10 trimers are further assembled into higher-order oligomeric complexes via disulfide bonding mediated by their N-terminal cysteine residues.	Disulfides	104-113	C1q and tumor necrosis factor related protein 6	Mus musculus	14-19
24361609-2	2014	Two forms of TF were described: an oxidized functional form and a reduced nonfunctional form that is converted to the active form through the formation of an allosteric disulfide.	Disulfides	169-178	coagulation factor III, tissue factor	Homo sapiens	13-15
24506865-6	2014	Thioredoxin1 (Trx1), an important reducing enzyme that cleaves disulfides in proteins, prevents AMPK oxidation, serving as an essential cofactor for AMPK activation.	Disulfides	63-73	thioredoxin	Homo sapiens	0-12
24506865-6	2014	Thioredoxin1 (Trx1), an important reducing enzyme that cleaves disulfides in proteins, prevents AMPK oxidation, serving as an essential cofactor for AMPK activation.	Disulfides	63-73	thioredoxin	Homo sapiens	14-18
19011089-0	2008	A disulfide-bond A oxidoreductase-like protein (DsbA-L) regulates adiponectin multimerization.	Disulfides	2-11	glutathione S-transferase kappa 1	Mus musculus	48-54
34155214-5	2021	Additional disulfide mutations caused the fixing of a closed ACE2 conformation to avoid off-target effects of protease activity, and also improved structural stability.	Disulfides	11-20	angiotensin converting enzyme 2	Homo sapiens	61-65
34150335-3	2021	While groups such as disulfides in ACE2"s zinc metallopeptidase, and also in COVID-19"s spikes, facilitate such binding, it is worth exploring how similar complementary sites on materials such as polymers, metals, ceramics, fabrics, and biomaterials promote binding of viruses and bacteria and how they could be further engineered to prevent bioactivity, or to act as agents to collect viral payloads in filters or similar devices.	Disulfides	21-31	angiotensin converting enzyme 2	Homo sapiens	35-39
34400955-6	2021	Due to the cytoplasmic expression of DsbC and the ability to the correct formation of disulfide bonds, the Shuffle  T7 strain can be a suitable host for the soluble production of recombinant proteins.	Disulfides	86-95	putative protein DsbC	Escherichia coli	37-41
35413120-1	2022	Phosphoribulokinase (PRK), one of the enzymes in the Calvin-Benson cycle, is a well-known target of thioredoxin (Trx), which regulates various enzyme activities by the reduction of disulfide bonds in a light-dependent manner.	Disulfides	181-190	phosphoribulokinase	Arabidopsis thaliana	0-19
35413120-1	2022	Phosphoribulokinase (PRK), one of the enzymes in the Calvin-Benson cycle, is a well-known target of thioredoxin (Trx), which regulates various enzyme activities by the reduction of disulfide bonds in a light-dependent manner.	Disulfides	181-190	phosphoribulokinase	Arabidopsis thaliana	21-24
35413120-1	2022	Phosphoribulokinase (PRK), one of the enzymes in the Calvin-Benson cycle, is a well-known target of thioredoxin (Trx), which regulates various enzyme activities by the reduction of disulfide bonds in a light-dependent manner.	Disulfides	181-190	thioredoxin H-type 1	Arabidopsis thaliana	100-111
35413120-1	2022	Phosphoribulokinase (PRK), one of the enzymes in the Calvin-Benson cycle, is a well-known target of thioredoxin (Trx), which regulates various enzyme activities by the reduction of disulfide bonds in a light-dependent manner.	Disulfides	181-190	thioredoxin H-type 1	Arabidopsis thaliana	113-116
35413120-10	2022	Furthermore, in vivo analysis of the redox states of PRK showed that only one disulfide bond is reduced in response to light.	Disulfides	78-87	phosphoribulokinase	Arabidopsis thaliana	53-56
35504352-7	2022	This stimulatory effect of TMPRSS2 on ENaC was partially preserved when inhibiting its proteolytic activity at the cell surface using aprotinin, but was abolished when the gamma-inhibitory tract remained attached to its binding site following introduction of two cysteine residues (S155C - Q426C) to form a disulfide bridge.	Disulfides	307-316	transmembrane serine protease 2 L homeolog	Xenopus laevis	27-34
35410347-4	2022	Notably, crystallographic analyses reveal that the unusual dimerization mode of JMJD7, which involves interactions between both the N- and C-terminal regions of both dmJMJD7 monomers and disulfide formation, is conserved in human JMJD7 (hsJMJD7).	Disulfides	187-196	jumonji domain containing 7	Homo sapiens	80-85
35410347-4	2022	Notably, crystallographic analyses reveal that the unusual dimerization mode of JMJD7, which involves interactions between both the N- and C-terminal regions of both dmJMJD7 monomers and disulfide formation, is conserved in human JMJD7 (hsJMJD7).	Disulfides	187-196	jumonji domain containing 7	Homo sapiens	230-235
35077997-1	2022	Protein disulfide isomerase (PDI), an oxidoreductase, possesses two vicinal cysteines in the -Cys-Gly-His-Cys-motif that either form a disulfide bridge (S-S) or exist in a sulfhydryl form (-SH), forming oxidized or reduced PDI, respectively.	Disulfides	135-144	prolyl 4-hydroxylase subunit beta	Homo sapiens	0-27
35077997-1	2022	Protein disulfide isomerase (PDI), an oxidoreductase, possesses two vicinal cysteines in the -Cys-Gly-His-Cys-motif that either form a disulfide bridge (S-S) or exist in a sulfhydryl form (-SH), forming oxidized or reduced PDI, respectively.	Disulfides	135-144	prolyl 4-hydroxylase subunit beta	Homo sapiens	29-32
35077997-1	2022	Protein disulfide isomerase (PDI), an oxidoreductase, possesses two vicinal cysteines in the -Cys-Gly-His-Cys-motif that either form a disulfide bridge (S-S) or exist in a sulfhydryl form (-SH), forming oxidized or reduced PDI, respectively.	Disulfides	135-144	prolyl 4-hydroxylase subunit beta	Homo sapiens	223-226
35341795-3	2022	We previously showed that mouse hepatic Cyp2a5 is induced during reductive ER stress caused by the intramolecular disulfide form of dithiothreitol, trans-4,5-dihydroxy-1,2-dithiane (DTTox), and that overexpression of Cyp2a5 provides partial protection against apoptosis due to bilirubin (BR), a compound known to cause ER stress.	Disulfides	114-123	cytochrome P450, family 2, subfamily a, polypeptide 5	Mus musculus	40-46
35341795-3	2022	We previously showed that mouse hepatic Cyp2a5 is induced during reductive ER stress caused by the intramolecular disulfide form of dithiothreitol, trans-4,5-dihydroxy-1,2-dithiane (DTTox), and that overexpression of Cyp2a5 provides partial protection against apoptosis due to bilirubin (BR), a compound known to cause ER stress.	Disulfides	114-123	cytochrome P450, family 2, subfamily a, polypeptide 5	Mus musculus	217-223
35157849-4	2022	Using this system, approximately 41% of the ORF8 expressed in 293T cells was secreted extracellularly as a glycoprotein homodimer with inter/intramolecular disulfide bonds.	Disulfides	156-165	ORF8 protein	Severe acute respiratory syndrome coronavirus 2	44-48
35130281-0	2022	A proximity-based in silico approach to identify redox-labile disulfide bonds: The example of FVIII.	Disulfides	62-71	coagulation factor VIII	Homo sapiens	94-99
35130281-3	2022	FVIII has eight disulfide bonds and is known to be redox labile, but it is not known how reduction/oxidation affects the structure-function relationship, or its immunogenicity-a serious complication for 30% severe HA patients.	Disulfides	16-25	coagulation factor VIII	Homo sapiens	0-5
35130281-5	2022	FVIII is a challenging molecule to work with owing to its poor expression and instability so, in a proof-of-concept study, we used molecular dynamics (MD) to identify which disulfide bonds were most likely to be reduced and how this would affect structure/function; results were then experimentally verified.	Disulfides	173-182	coagulation factor VIII	Homo sapiens	0-5
35014648-0	2022	Improved myocardial performance in infarcted rat heart by injection of disulfide-cross-linked chitosan hydrogels loaded with basic fibroblast growth factor.	Disulfides	71-80	fibroblast growth factor 2	Rattus norvegicus	125-155
2692565-6	1989	Mucins in HMFG membrane and breast tumor cells may be associated therefore to disulfide-linked linker proteins similar to those described for intestinal and gastric mucins, that would co-purify with the mucin under non-reducing conditions.	Disulfides	78-87	milk fat globule EGF and factor V/VIII domain containing	Homo sapiens	10-14
18942855-0	2008	Disulfide bond shuffling in bovine alpha-lactalbumin: MD simulation confirms experiment.	Disulfides	0-9	lactalbumin alpha	Bos taurus	35-52
18590794-0	2008	Effects of removing a conserved disulfide bond on the biological characteristics of rat lipocalin-type prostaglandin D synthase.	Disulfides	32-41	prostaglandin D2 synthase	Rattus norvegicus	88-127
18590794-1	2008	Three cysteine residues, Cys(65), Cys(89), and Cys(186) in lipocalin-type prostaglandin D synthase (L-PGDS), are conserved among all species and the disulfide bond between Cys(89) and Cys(186) is highly conserved among most, but not all, lipocalins.	Disulfides	149-158	prostaglandin D2 synthase	Rattus norvegicus	59-98
18590794-1	2008	Three cysteine residues, Cys(65), Cys(89), and Cys(186) in lipocalin-type prostaglandin D synthase (L-PGDS), are conserved among all species and the disulfide bond between Cys(89) and Cys(186) is highly conserved among most, but not all, lipocalins.	Disulfides	149-158	prostaglandin D2 synthase	Rattus norvegicus	100-106
18590794-2	2008	In this study, four rat L-PGDS variants were constructed by site-directed mutagenesis, and the conserved disulfide bond in several variants was removed by substituting cysteine with alanine.	Disulfides	105-114	prostaglandin D2 synthase	Rattus norvegicus	24-30
18725456-4	2008	The RAMP1 structure is a three-helix bundle that is stabilized by three disulfide bonds.	Disulfides	72-81	receptor activity modifying protein 1	Homo sapiens	4-9
18552403-6	2008	We propose thus a four-step disulfide cascade mechanism involving the transient glutathionylation of Cys(4) to convert this atypical thioredoxin h back to its active reduced form.	Disulfides	28-37	thioredoxin	Homo sapiens	133-144
18695247-6	2008	Our bioinformatic and experimental results suggest that many bacteria may not generally oxidatively fold proteins, and implicate the bacterial homolog of the enzyme vitamin K epoxide reductase, a protein required for blood clotting in humans, as part of a disulfide bond formation pathway present in several major bacterial phyla.	Disulfides	256-265	vitamin K epoxide reductase complex subunit 1	Homo sapiens	165-192
18660822-2	2008	Ligands contain a disulfide-rich Delta/Serrate/LAG-2 (DSL) domain required for Notch trans-activation or cis-inhibition.	Disulfides	18-27	serrate, RNA effector molecule	Homo sapiens	33-46
18653895-4	2008	Here, we found that an ER-resident protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins, and accelerated ERAD through its physical and functional associations with EDEM (ER degradation-enhancing alpha-mannosidase-like protein) and an ER-resident chaperone BiP.	Disulfides	87-96	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	43-48
18514182-4	2008	Loss of Palisade or the microvillar protein Cad99C results in abnormal uptake into the oocyte of sV17, a major vitelline membrane protein, and defects in non-disulfide cross-linking of sV17 and sV23, while loss of Palisade has additional effects on processing and disulfide cross-linking of these proteins.	Disulfides	158-167	Cadherin 99C	Drosophila melanogaster	44-50
18514182-4	2008	Loss of Palisade or the microvillar protein Cad99C results in abnormal uptake into the oocyte of sV17, a major vitelline membrane protein, and defects in non-disulfide cross-linking of sV17 and sV23, while loss of Palisade has additional effects on processing and disulfide cross-linking of these proteins.	Disulfides	264-273	Cadherin 99C	Drosophila melanogaster	44-50
18529069-1	2008	An efficient solid-phase synthesis protocol has been developed which, together with regioselective sequential formation of the three disulfide bonds, enabled the preparation of specifically monolanthanide (europium)-labeled human insulin-like peptide 3 (INSL3) for the study of its interaction with its G-protein-coupled receptor, RXFP2, via time-resolved fluorometry.	Disulfides	133-142	insulin like 3	Homo sapiens	230-252
18479973-5	2008	Interestingly, LvTRX contains aside of the canonical active site CXXC disulfide motif, one Cys (C73) residue in the interface of a putative dimer previously reported for human TRX.	Disulfides	70-79	thioredoxin	Homo sapiens	17-20
18507380-2	2008	The structure was obtained by irradiation and flash-freezing of a disulfide-cross-linked (DXLed) complex of hOgg1 bound to DNA containing a novel photocaged derivative of oxoG.	Disulfides	66-75	8-oxoguanine DNA glycosylase	Homo sapiens	108-113
18555775-1	2008	Thioredoxin 1 (Trx1) facilitates the reduction of signaling molecules and transcription factors by cysteine thiol-disulfide exchange, thereby regulating cell growth and death.	Disulfides	114-123	thioredoxin	Homo sapiens	0-13
18555775-1	2008	Thioredoxin 1 (Trx1) facilitates the reduction of signaling molecules and transcription factors by cysteine thiol-disulfide exchange, thereby regulating cell growth and death.	Disulfides	114-123	thioredoxin	Homo sapiens	15-19
18555775-4	2008	Both Cys-274/Cys-276 in DnaJb5 and Cys-667/Cys-669 in HDAC4 are oxidized and form intramolecular disulfide bonds in response to reactive oxygen species (ROS)-generating hypertrophic stimuli, such as phenylephrine, whereas they are reduced by Trx1.	Disulfides	97-106	DnaJ heat shock protein family (Hsp40) member B5	Homo sapiens	24-30
18555775-4	2008	Both Cys-274/Cys-276 in DnaJb5 and Cys-667/Cys-669 in HDAC4 are oxidized and form intramolecular disulfide bonds in response to reactive oxygen species (ROS)-generating hypertrophic stimuli, such as phenylephrine, whereas they are reduced by Trx1.	Disulfides	97-106	histone deacetylase 4	Homo sapiens	54-59
18555775-4	2008	Both Cys-274/Cys-276 in DnaJb5 and Cys-667/Cys-669 in HDAC4 are oxidized and form intramolecular disulfide bonds in response to reactive oxygen species (ROS)-generating hypertrophic stimuli, such as phenylephrine, whereas they are reduced by Trx1.	Disulfides	97-106	thioredoxin	Homo sapiens	242-246
18519672-5	2008	The conformation of TIP30 was altered with the formation of an intermolecular disulfide bridge under oxidative stress.	Disulfides	78-87	HIV-1 Tat interactive protein 2	Homo sapiens	20-25
18593333-5	2008	Functional IL-12 is a heterodimer consisting of two disulfide-linked subunits, p35 and p40.	Disulfides	52-61	interleukin 12a	Mus musculus	79-82
17914732-8	2008	It rules out the supposition that there is one disulfide bond in rh-IL-1ra crystals based on X-ray diffraction.	Disulfides	47-56	interleukin 1 receptor antagonist	Homo sapiens	68-74
18537713-1	2008	An intermolecular disulfide bond serves as a thioredoxin-dependent redox-sensing switch for the regulation of the enzymatic activity of 3-mercaptopyruvate sulfurtransferase (MST, EC.2.8.1.2).	Disulfides	18-27	thioredoxin	Homo sapiens	45-56
18537713-2	2008	A cysteine residue on the surface of each subunit was oxidized to form an intersubunit disulfide bond so as to decrease MST activity, and thioredoxin-specific conversion of a dimer to a monomer increased MST activity.	Disulfides	87-96	thioredoxin	Homo sapiens	138-149
18310660-2	2008	Hepcidin homologs of very similar structures are found in lower vertebrates, all comprise approximately 20-25 amino acids with 8 highly conserved cysteines forming 4 intramolecular disulfide bonds, giving hepcidin a hairpin structure.	Disulfides	181-190	hepcidin antimicrobial peptide	Homo sapiens	0-8
18396871-0	2008	PEG-detachable polyplex micelles based on disulfide-linked block catiomers as bioresponsive nonviral gene vectors.	Disulfides	42-51	progestagen associated endometrial protein	Homo sapiens	0-3
18396871-2	2008	A novel block catiomer, PEG-SS-P[Asp(DET)], was designed as follows: (i) insertion of biocleavable disulfide linkage between PEG and polycation segment to trigger PEG detachment and (ii) a cationic segment based on poly(aspartamide) with a flanking N-(2-aminoethyl)-2-aminoethyl group, P[Asp(DET)], in which the Asp(DET) unit acts as a buffering moiety inducing endosomal escape with minimal cytotoxicity.	Disulfides	99-108	progestagen associated endometrial protein	Homo sapiens	24-27
18396871-2	2008	A novel block catiomer, PEG-SS-P[Asp(DET)], was designed as follows: (i) insertion of biocleavable disulfide linkage between PEG and polycation segment to trigger PEG detachment and (ii) a cationic segment based on poly(aspartamide) with a flanking N-(2-aminoethyl)-2-aminoethyl group, P[Asp(DET)], in which the Asp(DET) unit acts as a buffering moiety inducing endosomal escape with minimal cytotoxicity.	Disulfides	99-108	progestagen associated endometrial protein	Homo sapiens	125-128
18396871-2	2008	A novel block catiomer, PEG-SS-P[Asp(DET)], was designed as follows: (i) insertion of biocleavable disulfide linkage between PEG and polycation segment to trigger PEG detachment and (ii) a cationic segment based on poly(aspartamide) with a flanking N-(2-aminoethyl)-2-aminoethyl group, P[Asp(DET)], in which the Asp(DET) unit acts as a buffering moiety inducing endosomal escape with minimal cytotoxicity.	Disulfides	99-108	progestagen associated endometrial protein	Homo sapiens	125-128
18448684-6	2008	We show here that the C-terminal recombinant half of fibrillin-1 assembles into disulfide-bonded multimeric globular structures with peripheral arms and a dense core.	Disulfides	80-89	fibrillin 1	Homo sapiens	53-64
18065762-0	2008	Identification of disulfide-linked dimers of the receptor tyrosine kinase DDR1.	Disulfides	18-27	discoidin domain receptor tyrosine kinase 1	Homo sapiens	74-78
18065762-4	2008	Here we show that DDR1 exists as a disulfide-linked dimer in transfected as well as endogenously expressing cells.	Disulfides	35-44	discoidin domain receptor tyrosine kinase 1	Homo sapiens	18-22
18321861-6	2008	Mass spectra analysis demonstrated binding of 2.5 mol of Hg(2+) and 5 mol of MeHg(+)/mol of Trx1 with the very strong Hg(2+) complexes involving active site and structural disulfides.	Disulfides	172-182	thioredoxin	Homo sapiens	92-96
18451518-3	2008	Some bis[2-(acylamino)phenyl] disulfides might have the ability to form a disulfide bond with the cysteine residues of beta-catenin, leading to inhibition of the growth of human colon cells.	Disulfides	30-39	catenin beta 1	Homo sapiens	119-131
18331844-3	2008	The active site dithiol/disulfide of thioredoxin fold proteins is CXXC where variations of the residues inside the disulfide ring are known to increase the redox potential like in protein disulfide isomerases.	Disulfides	24-33	thioredoxin	Homo sapiens	37-48
18331844-3	2008	The active site dithiol/disulfide of thioredoxin fold proteins is CXXC where variations of the residues inside the disulfide ring are known to increase the redox potential like in protein disulfide isomerases.	Disulfides	115-124	thioredoxin	Homo sapiens	37-48
18331844-4	2008	In the catalytic mechanism thioredoxin fold proteins bind to target proteins through conserved backbone-backbone hydrogen bonds and induce conformational changes of the target disulfide followed by nucleophilic attack by the N-terminally located low pK(a) Cys residue.	Disulfides	176-185	thioredoxin	Homo sapiens	27-38
18186468-0	2008	The crystal structure of human chloride intracellular channel protein 2: a disulfide bond with functional implications.	Disulfides	75-84	chloride intracellular channel 2	Homo sapiens	31-71
18349143-1	2008	Thioredoxins (Trxs) are ubiquitous small proteins with a redox-active disulfide bridge.	Disulfides	70-79	thioredoxin	Homo sapiens	0-12
18164270-4	2008	Increased H2O2 triggers peroxiredoxin overoxidation to a sulphinic acid; however during apoptosis peroxiredoxin 3 was captured as a disulfide, suggesting impairment of the thioredoxin system responsible for maintaining peroxiredoxin 3 in its reduced form.	Disulfides	132-141	thioredoxin	Homo sapiens	172-183
18180295-3	2008	However, here we show that HBD3 (human beta-defensin 3) alkylated with iodoactemide and devoid of any disulfide bonds is still a potent chemoattractant.	Disulfides	102-111	defensin beta 103B	Homo sapiens	27-31
18180295-3	2008	However, here we show that HBD3 (human beta-defensin 3) alkylated with iodoactemide and devoid of any disulfide bonds is still a potent chemoattractant.	Disulfides	102-111	defensin beta 103B	Homo sapiens	39-54
18297547-1	2008	Multimerin 1 is a massive, soluble, disulfide-linked homopolymeric protein that is expressed in megakaryocytes, platelets and endothelial cells.	Disulfides	36-45	multimerin 1	Homo sapiens	0-12
18297547-3	2008	Recently, multimerin 1 was designated as a member of the EMILIN protein family, a group of structurally similar, disulfide-linked multimeric proteins.	Disulfides	113-122	multimerin 1	Homo sapiens	10-22
18297547-3	2008	Recently, multimerin 1 was designated as a member of the EMILIN protein family, a group of structurally similar, disulfide-linked multimeric proteins.	Disulfides	113-122	elastin microfibril interfacer 1	Homo sapiens	57-63
18164680-0	2008	Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347.	Disulfides	15-24	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	47-51
18164680-2	2008	Herein, we show that NEMO exists as a disulfide-bonded dimer when isolated from several cell types and analyzed by SDS-polyacrylamide gel electrophoresis under non-reducing conditions.	Disulfides	38-47	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	21-25
18164680-4	2008	Disulfide bond-mediated formation of NEMO dimers requires Cys54 and Cys347.	Disulfides	0-9	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	37-41
18164680-5	2008	The ability of these residues to form disulfide bonds is consistent with their location in a NEMO dimer structure that we generated by molecular modeling.	Disulfides	38-47	inhibitor of nuclear factor kappa B kinase regulatory subunit gamma	Homo sapiens	93-97
18220349-6	2008	It is furthermore demonstrated that the PEG coating of the siRNA-PEG complexes can be rendered biodegradable through the use of a pH-sensitive hydrazone or a reducible disulfide bond linker between the K14 and the PEG blocks.	Disulfides	168-177	keratin 14	Homo sapiens	202-205
17947231-3	2008	CP12-2 is monomeric in solution and contains four cysteines, which can form two intramolecular disulfides with midpoint redox potentials of -326 and -352 mV, respectively, at pH 7.9.	Disulfides	95-105	CP12 domain-containing protein 2	Arabidopsis thaliana	0-4
17947231-4	2008	Site-specific mutants indicate that the C-terminal disulfide is involved in the interaction between CP12-2 and GAPDH (isoform A(4)), whereas the N-terminal disulfide is involved in the interaction between this binary complex and PRK.	Disulfides	51-60	CP12 domain-containing protein 2	Arabidopsis thaliana	100-106
18575274-1	2008	Thioredoxin (TRX) is a small multifunctional protein with a redox-active dithiol/disulfide in the conserved active site.	Disulfides	81-90	thioredoxin	Homo sapiens	0-11
18575274-1	2008	Thioredoxin (TRX) is a small multifunctional protein with a redox-active dithiol/disulfide in the conserved active site.	Disulfides	81-90	thioredoxin	Homo sapiens	13-16
18236022-1	2008	Relaxin-3 (R3) is the most recently identified member of the insulin superfamily, which is composed of peptides with diverse sequences held together by characteristic disulfide links connecting A and B peptide chains.	Disulfides	167-176	relaxin 3	Rattus norvegicus	0-13
18217133-7	2008	This inactivation is mostly due to decreased stability of FVIIIa since a disulfide bond that prevents A2 subunit dissociation from FVIIIa prevents any loss of activity due to cathepsin G proteolysis.	Disulfides	73-82	cathepsin G	Homo sapiens	175-186
17963731-4	2007	The third domain of RAP can be significantly truncated, with material retention of monovalent CR pair-binding affinity, provided that the minimized sequence is stabilized with an intramolecular disulfide bond.	Disulfides	194-203	LDL receptor related protein associated protein 1	Homo sapiens	20-23
17963731-5	2007	We demonstrate that the avidity of full-length RAP for LRP1 in vitro can be partially reconstituted by assembly of truncated, disulfide-linked RAP peptides on tetravalent streptavidin or bivalent immunoglobulin scaffolds.	Disulfides	126-135	LDL receptor related protein associated protein 1	Homo sapiens	47-50
17963731-5	2007	We demonstrate that the avidity of full-length RAP for LRP1 in vitro can be partially reconstituted by assembly of truncated, disulfide-linked RAP peptides on tetravalent streptavidin or bivalent immunoglobulin scaffolds.	Disulfides	126-135	LDL receptor related protein associated protein 1	Homo sapiens	143-146
17964539-0	2007	Association of chicken zona pellucida glycoprotein (ZP) B1 with ZPC induces formation of ZPB1-ZPC fibrous aggregates containing disulfide-bridged ZPB1 dimer.	Disulfides	128-137	zona pellucida sperm-binding protein 3	Gallus gallus	64-67
17964539-0	2007	Association of chicken zona pellucida glycoprotein (ZP) B1 with ZPC induces formation of ZPB1-ZPC fibrous aggregates containing disulfide-bridged ZPB1 dimer.	Disulfides	128-137	zona pellucida sperm-binding protein 3	Gallus gallus	94-97
19086590-4	2007	According to this computational analysis 6 good disulfide binding states in Iranian gp120 were predicted.	Disulfides	48-57	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	84-89
17945253-4	2007	Site-directed mutagenesis studies show that removal of the intramolecular disulfide or introduction of cysteine residues in CLIC2, equivalent to those that form the intramolecular disulfide in CLIC1, does not cause dimer formation under oxidizing conditions.	Disulfides	180-189	chloride intracellular channel 2	Homo sapiens	124-129
17711389-5	2007	Here the authors demonstrate that PDI-1, PDI-2, and PDI-3 show comparable kinetic properties in catalyzing thiol:disulfide exchange reactions in two simple peptide-based assays.	Disulfides	113-122	Protein disulfide-isomerase 1	Caenorhabditis elegans	34-39
17922544-0	2007	Insulin receptor substrate 1 knockdown in human MCF7 ER+ breast cancer cells by nuclease-resistant IRS1 siRNA conjugated to a disulfide-bridged D-peptide analogue of insulin-like growth factor 1.	Disulfides	126-135	insulin receptor substrate 1	Homo sapiens	0-28
17922544-0	2007	Insulin receptor substrate 1 knockdown in human MCF7 ER+ breast cancer cells by nuclease-resistant IRS1 siRNA conjugated to a disulfide-bridged D-peptide analogue of insulin-like growth factor 1.	Disulfides	126-135	insulin receptor substrate 1	Homo sapiens	99-103
17893039-6	2007	As exemplified for thioredoxin 1, the Tnk-1 kinase SH3 domain, and the hSH3(N) domain of the T cell protein ADAP, the conformational changes associated with disulfide bond formation can be followed directly upon titration with different ratios of reduced to oxidized glutathione.	Disulfides	157-166	FYN binding protein 1	Homo sapiens	108-112
17960122-10	2007	The 346T&gt;G mutation was predicted to result in a substitution of the highly conserved Cys116 to Gly and disruption of the disulfide bridge essential for the normal structure and function of the OA1 protein.	Disulfides	125-134	OA1	Homo sapiens	197-200
17621593-0	2007	Differential structure and activity between human and mouse intelectin-1: human intelectin-1 is a disulfide-linked trimer, whereas mouse homologue is a monomer.	Disulfides	98-107	intelectin 1	Homo sapiens	60-72
17621593-0	2007	Differential structure and activity between human and mouse intelectin-1: human intelectin-1 is a disulfide-linked trimer, whereas mouse homologue is a monomer.	Disulfides	98-107	intelectin 1	Homo sapiens	80-92
17621593-4	2007	Recombinant hITLN-1 is a trimer, disulfide-linked through Cys-31 and Cys-48, and N-glycosylated at Asn-163.	Disulfides	33-42	intelectin 1	Homo sapiens	12-19
17673175-7	2007	All these tested Trx-independent MsrB enzymes lack an additional cysteine (resolving cysteine) that is capable of forming a disulfide bond on the enzyme during the catalytic reaction.	Disulfides	124-133	thioredoxin	Homo sapiens	17-20
17644519-3	2007	We have produced a covalent dimer of the CC chemokine macrophage inflammatory protein-1beta (MIP-1beta) by placing a disulfide bond at the center of its dimer interface through a single amino acid substitution (MIP-1beta-A10C).	Disulfides	117-126	C-C motif chemokine ligand 4	Homo sapiens	93-102
17644519-3	2007	We have produced a covalent dimer of the CC chemokine macrophage inflammatory protein-1beta (MIP-1beta) by placing a disulfide bond at the center of its dimer interface through a single amino acid substitution (MIP-1beta-A10C).	Disulfides	117-126	C-C motif chemokine ligand 4	Homo sapiens	211-220
17548047-2	2007	C93S-Trx2 was detected as a disulfide with mitochondrial peroxiredoxin-3 (Prx3) but not peroxiredoxin-5 (Prx5).	Disulfides	28-37	thioredoxin 2	Homo sapiens	5-9
17555533-1	2007	Gamma interferon-induced lysosomal thiolreductase (GILT) is expressed constitutively in antigen-presenting cells, where it reduces disulfide bonds to facilitate antigen presentation.	Disulfides	131-140	interferon gamma inducible protein 30	Mus musculus	0-49
17555533-1	2007	Gamma interferon-induced lysosomal thiolreductase (GILT) is expressed constitutively in antigen-presenting cells, where it reduces disulfide bonds to facilitate antigen presentation.	Disulfides	131-140	interferon gamma inducible protein 30	Mus musculus	51-55
17675462-2	2007	We recently identified a patient with a homozygous amino acid substitution in Igbeta, a glycine to serine at codon 137, adjacent to the cysteine required for the disulfide bond between Igalpha and Igbeta.	Disulfides	162-171	CD79b molecule	Homo sapiens	78-84
17675462-2	2007	We recently identified a patient with a homozygous amino acid substitution in Igbeta, a glycine to serine at codon 137, adjacent to the cysteine required for the disulfide bond between Igalpha and Igbeta.	Disulfides	162-171	CD79b molecule	Homo sapiens	197-203
17675462-4	2007	Using expression vectors in 293T cells or Jurkat T cells, we show that the mutant Igbeta can form disulfide-linked complexes and bring the mu H chain to the cell surface as part of the BCR but is inefficient at both tasks.	Disulfides	98-107	CD79b molecule	Homo sapiens	82-88
17553782-2	2007	Biogenesis of IMS proteins involves a disulfide relay between precursor proteins, the cysteine-rich IMS protein Mia40 and the sulfhydryl oxidase Erv1.	Disulfides	38-47	growth factor, augmenter of liver regeneration	Homo sapiens	145-149
17635130-3	2007	The secretin receptor includes the typical signature sequences for this receptor family within its predicted transmembrane segments and the highly conserved six cysteine residues contributing to three intradomain disulfide bonds within its long N-terminus.	Disulfides	213-222	secretin receptor	Homo sapiens	4-21
17766407-3	2007	Mass spectrometry identified two disulfide bonds (Cys186-Cys406 and Cys349-Cys364) in GCL.	Disulfides	33-42	glutamate-cysteine ligase	Arabidopsis thaliana	86-89
17640393-9	2007	The HIV envelope glycoprotein gp120, for example, is regulated by thiol/disulfide exchange and contains allosteric -RHStaple bonds that can exist in the -LHStaple configuration.	Disulfides	72-81	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	30-35
17472958-13	2007	Moreover, we identified one crucial disulfide bond located in the C-terminal helical domain of CHLI1 protein, which may regulate the binding of the nucleotide to the N-terminal catalytic domain.	Disulfides	36-45	P-loop containing nucleoside triphosphate hydrolases superfamily protein	Arabidopsis thaliana	95-100
17525470-7	2007	We suggest that the mutations have altered the interaction between gp120 C5 and the gp41 disulfide loop, resulting in decreased accessibility of the furin recognition site and implying that the interaction between the gp120 C5 and gp41 loop is a conformational requirement for gp160 processing.	Disulfides	89-98	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	67-72
17525470-7	2007	We suggest that the mutations have altered the interaction between gp120 C5 and the gp41 disulfide loop, resulting in decreased accessibility of the furin recognition site and implying that the interaction between the gp120 C5 and gp41 loop is a conformational requirement for gp160 processing.	Disulfides	89-98	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	218-223
17307004-5	2007	The cDNA for zLIF encoded a predicted 215-amino acid protein with a putative 32-amino acid signal peptide, two disulfide bonds, and two N-linked glycosylation sites.	Disulfides	111-120	IL-6 subfamily cytokine M17	Danio rerio	13-17
17440104-3	2007	We here show that it is possible to improve TCR gene transfer by adding a single cysteine on each receptor chain to promote the formation of an additional interchain disulfide bond.	Disulfides	166-175	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	44-47
17316609-9	2007	Our study confirms the redox regulation of PTEN through disulfide bond formation with the hTrx-1 in Drosophila and suggests conserved mechanisms for thioredoxins and their interactions with the phosphatidylinositol-3-kinase signaling pathway in humans and fruit flies.	Disulfides	56-65	lysine methyltransferase 2A	Homo sapiens	90-96
17336303-1	2007	The thiol oxidase Erv1 and the redox-regulated receptor Mia40/Tim40 are components of a disulfide relay system which mediates import of proteins into the intermembrane space (IMS) of mitochondria.	Disulfides	88-97	growth factor, augmenter of liver regeneration	Homo sapiens	18-22
17336303-3	2007	After passage across the translocase of the mitochondrial outer membrane Erv1 interacts via disulfide bonds with Mia40.	Disulfides	92-101	growth factor, augmenter of liver regeneration	Homo sapiens	73-77
17110014-3	2007	Recently we have shown that native bovine plasma fetuin-A partially exists as a disulfide-bridged two-chain protein with a heavy N-terminal and a lighter C-terminal chain similar to the structure of human fetuin-A homologue (alpha2HS glycoprotein), and also is partially phosphorylated at residues Ser120, Ser302, Ser305 and Ser306 (Wind et al., Anal.	Disulfides	80-89	alpha 2-HS glycoprotein	Bos taurus	49-57
17110014-7	2007	In this study we show that authentic bovine fetuin-A disulfide-bridged two-chain forms, which include the original C-terminus, were liberated from the single-chain precursor by metalloproteinases MMP-3 (stromelysin-1) and MMP-7 (matrilysin), but not by elastase, cathepsin E and cathepsin G.	Disulfides	53-62	alpha 2-HS glycoprotein	Bos taurus	44-52
17444035-4	2007	The research in thioltransferase (TTase) and thioredoxin (Trx) system show TTase can specifically dithiolate protein-S-S-glutathione and restore protein free SH groups for proper enzymatic or protein functions; Trx system can dithiolate protein disulfides and thus is an extremely important regulator for redox homeostasis in the cells.	Disulfides	245-255	thioredoxin	Homo sapiens	45-56
17444035-4	2007	The research in thioltransferase (TTase) and thioredoxin (Trx) system show TTase can specifically dithiolate protein-S-S-glutathione and restore protein free SH groups for proper enzymatic or protein functions; Trx system can dithiolate protein disulfides and thus is an extremely important regulator for redox homeostasis in the cells.	Disulfides	245-255	thioredoxin	Homo sapiens	58-61
17444035-4	2007	The research in thioltransferase (TTase) and thioredoxin (Trx) system show TTase can specifically dithiolate protein-S-S-glutathione and restore protein free SH groups for proper enzymatic or protein functions; Trx system can dithiolate protein disulfides and thus is an extremely important regulator for redox homeostasis in the cells.	Disulfides	245-255	thioredoxin	Homo sapiens	211-214
17287520-5	2007	Here we used a disulfide cross-linking approach to identify pairs of residues that are in close proximity within the ATP binding site of the P2X1 homotrimer.	Disulfides	15-24	purinergic receptor P2X, ligand gated ion channel, 1 L homeolog	Xenopus laevis	141-145
17120268-5	2007	In order to further define the structure-activity relationships of cyclic analogues of the INSL3 B-chain, we used a structure-based approach to design a series of cyclic, disulfide-constrained INSL3 B-chain mimetics.	Disulfides	171-180	insulin like 3	Homo sapiens	91-96
17120268-5	2007	In order to further define the structure-activity relationships of cyclic analogues of the INSL3 B-chain, we used a structure-based approach to design a series of cyclic, disulfide-constrained INSL3 B-chain mimetics.	Disulfides	171-180	insulin like 3	Homo sapiens	193-198
17120268-7	2007	This model of INSL3 was then used as a template to design a series of disulfide-constrained mimetics of the INSL3 B-chain.	Disulfides	70-79	insulin like 3	Homo sapiens	14-19
17120268-7	2007	This model of INSL3 was then used as a template to design a series of disulfide-constrained mimetics of the INSL3 B-chain.	Disulfides	70-79	insulin like 3	Homo sapiens	108-113
16624411-2	2007	C8 is an oligomeric protein composed of a disulfide-linked C8alpha-gamma heterodimer and a noncovalently associated C8beta chain.	Disulfides	42-51	complement C8 alpha chain	Homo sapiens	59-66
17061249-3	2007	In the research presented, we examined how macromolecular crowding agents, such as albumin, ovalbumin, and polysaccharides, influenced the kinetics and thermodynamics of forming disulfide bonds in four model peptides of varying molecular size from 13 residues (1.4 kDa) to 58-residues (6.5 kDa): conotoxins: GI, PVIIA, r11a, and bovine pancreatic trypsin inhibitor.	Disulfides	178-187	albumin	Bos taurus	83-90
17135761-19	2007	The dimers of Can f 1 and of Can f 2 were not built with a disulfide bridge but by non-covalent association.	Disulfides	59-68	major allergen Can f 1	Canis lupus familiaris	14-21
18045229-5	2007	Western blotting based on non-reducing Tricine-SDS-PAGE indicated that IGF-II expression coupled with IGFBP-6 might significantly avoid the mispairing of disulfide bonds compared with the IGF-II expressed alone.	Disulfides	154-163	insulin like growth factor 2	Homo sapiens	71-77
17659658-0	2007	Redox-dependent formation of disulfide bonds in human replication protein A.	Disulfides	29-38	replication protein A1	Homo sapiens	54-75
17659658-7	2007	The results demonstrated that the formation of disulfide bonds at the zinc-finger site was responsible for the redox regulation of the DNA-binding activity of RPA.	Disulfides	47-56	replication protein A1	Homo sapiens	159-162
18084890-2	2007	Though details of reductive recycling after cysteine sulfenic acid formation at the active site vary among members of different Prx classes, local unfolding around the active site cysteine is likely generally required in these proteins for disulfide bond formation with a second resolving cysteine and/or for access of the reductant to the oxidized active site.	Disulfides	240-249	periaxin	Homo sapiens	128-131
17142755-2	2006	gamma-IFN-inducible lysosomal thiol reductase (GILT) is present in the MHC class II loading compartment and has been shown to facilitate class II Ag processing and recall responses to Ags containing disulfide bonds such as hen egg lysozyme (HEL).	Disulfides	199-208	interferon gamma inducible protein 30	Mus musculus	0-45
17142755-2	2006	gamma-IFN-inducible lysosomal thiol reductase (GILT) is present in the MHC class II loading compartment and has been shown to facilitate class II Ag processing and recall responses to Ags containing disulfide bonds such as hen egg lysozyme (HEL).	Disulfides	199-208	interferon gamma inducible protein 30	Mus musculus	47-51
17011580-5	2006	In addition to the canonical internal disulfide bridge, Ig1 contains a second, solvent-exposed disulfide bridge, which our biochemical data indicate is critical for proper folding of Ig1 and processing of MuSK.	Disulfides	95-104	muscle associated receptor tyrosine kinase	Homo sapiens	205-209
17087494-6	2006	Last, we measured an E(m) value of -255 mV for the Cys36-Cys82 disulfide bond at pH 6.0 in the glutathione peroxidase-like enzyme, oxidant receptor protein (Orp1).	Disulfides	63-72	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	157-161
17087494-7	2006	We were unable to obtain satisfactory redox titration data for Orp1 at pH 7.0, but if the redox-active disulfide of Orp1 exhibits the -59 mV per pH unit dependence for E(m) typical of protein disulfides in this pH region, an E(m) value of -315 mV can be estimated for Orp1 at pH 7.0 by extrapolation.	Disulfides	103-112	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	116-120
17087494-7	2006	We were unable to obtain satisfactory redox titration data for Orp1 at pH 7.0, but if the redox-active disulfide of Orp1 exhibits the -59 mV per pH unit dependence for E(m) typical of protein disulfides in this pH region, an E(m) value of -315 mV can be estimated for Orp1 at pH 7.0 by extrapolation.	Disulfides	103-112	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	116-120
17087494-7	2006	We were unable to obtain satisfactory redox titration data for Orp1 at pH 7.0, but if the redox-active disulfide of Orp1 exhibits the -59 mV per pH unit dependence for E(m) typical of protein disulfides in this pH region, an E(m) value of -315 mV can be estimated for Orp1 at pH 7.0 by extrapolation.	Disulfides	192-202	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	116-120
17087494-7	2006	We were unable to obtain satisfactory redox titration data for Orp1 at pH 7.0, but if the redox-active disulfide of Orp1 exhibits the -59 mV per pH unit dependence for E(m) typical of protein disulfides in this pH region, an E(m) value of -315 mV can be estimated for Orp1 at pH 7.0 by extrapolation.	Disulfides	192-202	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	116-120
17087494-8	2006	Together, these data suggest that, at physiological ratios of Trx(ox)/Trx(red), the reduction of both the E(m) = -315 mV disulfide of Orp1 and the E(m) = -330 mV disulfide of Yap1 by either Trx1 or Trx2 would be thermodynamically possible.	Disulfides	121-130	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	134-138
17087494-8	2006	Together, these data suggest that, at physiological ratios of Trx(ox)/Trx(red), the reduction of both the E(m) = -315 mV disulfide of Orp1 and the E(m) = -330 mV disulfide of Yap1 by either Trx1 or Trx2 would be thermodynamically possible.	Disulfides	162-171	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	134-138
17034341-4	2006	The thioredoxin system also makes a significant contribution to the redox environment by reducing inter- and intrachain protein disulfide bonds as well as maintaining the activity of important antioxidant enzymes such as peroxiredoxins and methionine sulfoxide reductases.	Disulfides	128-137	thioredoxin	Homo sapiens	4-15
16962095-6	2006	The disulfide bond between Cys23 and Cys45 is a target of glutathione-dependent reduction by glutaredoxin.	Disulfides	4-13	glutaredoxin-1	Cricetulus griseus	93-105
17002301-0	2006	Evidence for activation of tissue factor by an allosteric disulfide bond.	Disulfides	58-67	coagulation factor III, tissue factor	Homo sapiens	27-40
16787389-2	2006	We expressed the C-terminal cysteine-rich part of the human MUC5AC mucin in CHO-K1 cells (Chinese-hamster ovary K1 cells) where it formed disulfide-linked dimers in the ER (endoplasmic reticulum).	Disulfides	138-147	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	60-66
16877534-5	2006	Ig-betaC65 and Ig-betaC120 form the canonical Ig fold disulfide bond.	Disulfides	54-63	chemokine (C-X-C motif) ligand 9	Mus musculus	15-17
16877534-5	2006	Ig-betaC65 and Ig-betaC120 form the canonical Ig fold disulfide bond.	Disulfides	54-63	chemokine (C-X-C motif) ligand 9	Mus musculus	15-17
17089213-3	2006	The most studied redox system in photosynthetic organisms is the thioredoxin (TRX) system, involved in the regulation of a growing number of target proteins via thiol/disulfide exchanges.	Disulfides	167-176	thioredoxin	Homo sapiens	65-76
17089213-3	2006	The most studied redox system in photosynthetic organisms is the thioredoxin (TRX) system, involved in the regulation of a growing number of target proteins via thiol/disulfide exchanges.	Disulfides	167-176	thioredoxin	Homo sapiens	78-81
16507315-6	2006	We found that the ability of thioredoxin to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 Env gp120 and that thioredoxin also reduces disulfide bonds in gp120 directly in the absence of CD4.	Disulfides	158-167	thioredoxin	Homo sapiens	133-144
16098567-4	2006	Interestingly, the proteins that are responsible for maintenance of the reduced state belong to the same superfamily as those responsible for the formation of disulfide bridges: all are members of the thioredoxin superfamily.	Disulfides	159-168	thioredoxin	Homo sapiens	201-212
16547350-9	2006	Consequently, intramolecularly disulfide-linked analogs of the B-chain showed a potentiation of INSL3 antagonistic activity, as well as exhibiting increased proteolytic stability, as assessed in rat serum in vitro.	Disulfides	31-40	insulin like 3	Homo sapiens	96-101
16674666-7	2006	The three-dimensional model revealed that porcine SPARC contains a single N-linked glycosylation at N113, seven intramolecular disulfide bridges, and assembles into dimers.	Disulfides	127-136	secreted protein acidic and cysteine rich	Homo sapiens	50-55
16618105-1	2006	Thioredoxin reductase and thioredoxin constitute the cellular thioredoxin system, which provides reducing equivalents to numerous intracellular target disulfides.	Disulfides	151-161	peroxiredoxin 5	Homo sapiens	0-21
16618105-1	2006	Thioredoxin reductase and thioredoxin constitute the cellular thioredoxin system, which provides reducing equivalents to numerous intracellular target disulfides.	Disulfides	151-161	thioredoxin	Homo sapiens	26-37
16618105-1	2006	Thioredoxin reductase and thioredoxin constitute the cellular thioredoxin system, which provides reducing equivalents to numerous intracellular target disulfides.	Disulfides	151-161	thioredoxin	Homo sapiens	62-73
16519899-5	2006	One class corresponded to the unfolding of rhodopsin with the highly conserved Cys110-Cys187 disulfide bond remaining intact and the other class corresponded to the unfolding of the entire rhodopsin polypeptide chain.	Disulfides	93-102	rhodopsin	Bos taurus	43-52
16455647-0	2006	Efficient leukocyte Ig-like receptor signaling and crystal structure of disulfide-linked HLA-G dimer.	Disulfides	72-81	leukocyte immunoglobulin like receptor A6	Homo sapiens	10-36
16463284-7	2006	Among these, a beta3 substitution, p.Cys39Gly (Cys13Gly) was found to cause intracellular degradation of the beta3 subunit, in contrast to previous findings that mutations at Cys435, the partner of Cys13 in a disulfide bond, cause constitutive activation of alphaIIbbeta3.	Disulfides	209-218	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	15-20
16463284-7	2006	Among these, a beta3 substitution, p.Cys39Gly (Cys13Gly) was found to cause intracellular degradation of the beta3 subunit, in contrast to previous findings that mutations at Cys435, the partner of Cys13 in a disulfide bond, cause constitutive activation of alphaIIbbeta3.	Disulfides	209-218	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	109-114
16537584-3	2006	We show that the purified protein contains bound flavin adenine dinucleotide and is capable of catalyzing the formation of disulfide bonds both in a protein substrate and in the small molecule dithiothreitol, the catalytic activity being comparable to that of the Erv1p protein.	Disulfides	123-132	growth factor, augmenter of liver regeneration	Homo sapiens	264-269
16451355-2	2006	The objective of this study was to compare stability of gonadotropin-releasing hormone (GnRH)-toxin conjugates made with disulfide linkers to those using a maleimidodibutyryl (mb) linkage.	Disulfides	121-130	Progonadoliberin-1	Ovis aries	88-92
16677075-3	2006	A precise molecular explanation for the association between HLA-B27 and AS is still lacking, although it is known that inappropriately disulfide bonded HLA-B27 heavy chains can be found at both the cell surface and in the endoplasmic reticulum (ER) of HLA-B27 expressing cells.	Disulfides	135-144	major histocompatibility complex, class I, B	Homo sapiens	152-159
16677075-3	2006	A precise molecular explanation for the association between HLA-B27 and AS is still lacking, although it is known that inappropriately disulfide bonded HLA-B27 heavy chains can be found at both the cell surface and in the endoplasmic reticulum (ER) of HLA-B27 expressing cells.	Disulfides	135-144	major histocompatibility complex, class I, B	Homo sapiens	152-159
16677075-5	2006	Also shown is that major differences exist in the disulfide-dependent conformations of two HLA-B27 subtypes, HLA-B2704 and HLA-B2705.	Disulfides	50-59	major histocompatibility complex, class I, B	Homo sapiens	91-98
16677079-2	2006	The structure of fibrillin-1 is dominated by two types of disulfide-rich motifs, the calcium- binding epidermal growth factor-like (cbEGF) and transforming growth factor beta binding protein-like (TB) domains.	Disulfides	58-67	fibrillin 1	Homo sapiens	17-28
16677079-7	2006	Patients with HC often exhibit ocular and skeletal defects resembling the MFS phenotype, suggesting that elevated homocysteine levels may lead to chemical reduction of disulfide bonds within fibrillin-1 domains resulting in the loss of native structure.	Disulfides	168-177	fibrillin 1	Homo sapiens	191-202
16415107-5	2006	Moreover, p21ras S-glutathiolation and activation can be reversed by dithiothreitol, confirming the importance of a disulfide bond.	Disulfides	116-125	H3 histone pseudogene 16	Homo sapiens	10-13
16497933-3	2006	Here we report the use of disulfide cross-linking (DXL) technology to obtain structures of a bacterial DNA glycosylase, MutM, interrogating undamaged DNA.	Disulfides	26-35	8-oxoguanine DNA glycosylase	Homo sapiens	120-124
16375859-4	2006	Reduction of microtubule-associated protein disulfides by ascorbic acid following peroxynitrite treatment restores microtubule polymerization kinetics to control levels.	Disulfides	44-54	regulator of microtubule dynamics 1	Homo sapiens	13-43
16455490-5	2006	This is due to direct and reversible inhibition of SUMO conjugating enzymes through the formation of (a) disulfide bond(s) involving the catalytic cysteines of the SUMO E1 subunit Uba2 and the E2-conjugating enzyme Ubc9.	Disulfides	105-114	ubiquitin like modifier activating enzyme 2	Homo sapiens	180-184
16411781-3	2006	A regioselective disulfide-bond synthesis protocol was developed and used for the chemical synthesis of human (H3) relaxin-3.	Disulfides	17-26	relaxin 3	Homo sapiens	115-124
16401067-14	2006	We conclude that reactivation of oxidized 1-Cys Prx by GST pi occurs by heterodimerization of 1-Cys Prx and GST pi harboring bound GSH, followed by glutathionylation of 1-Cys Prx and then formation of an intersubunit disulfide.	Disulfides	217-226	periaxin	Homo sapiens	48-51
16257968-8	2006	Phage display of a C214A mutation of FGF-BP1 reduced binding to FGF-2, indicating the functional significance of this disulfide bond.	Disulfides	118-127	fibroblast growth factor binding protein 1	Homo sapiens	37-44
17130669-0	2006	Reduction of disulfide bridges in the lumenal domain of ATF6 in response to glucose starvation.	Disulfides	13-22	activating transcription factor 6	Homo sapiens	56-60
17130669-4	2006	We recently found that, owing to the presence of intra- and intermolecular disulfide bridges, ATF6 occurs in unstressed ER in monomer, dimer and oligomer forms.	Disulfides	75-84	activating transcription factor 6	Homo sapiens	94-98
17130669-5	2006	Disulfide-bonded ATF6 is reduced on treatment of cells with various chemical ER stress inducers, and only the reduced monomer ATF6 reaches the Golgi apparatus.	Disulfides	0-9	activating transcription factor 6	Homo sapiens	17-21
17192673-4	2006	ColQ characterizes the collagen-tailed forms (Aforms) of AChE and butyrylcholinesterase (BChE), which are localized in the basal lamina at neuromuscular junctions (NMJs) of vertebrates (Krejci et al., 1999); in these molecules (A4, A8, A12), one, two, or three tetramers of catalytic subunits are disulfide-linked to the strands of a triple helix of ColQ collagen.	Disulfides	297-306	butyrylcholinesterase	Homo sapiens	66-87
17192673-4	2006	ColQ characterizes the collagen-tailed forms (Aforms) of AChE and butyrylcholinesterase (BChE), which are localized in the basal lamina at neuromuscular junctions (NMJs) of vertebrates (Krejci et al., 1999); in these molecules (A4, A8, A12), one, two, or three tetramers of catalytic subunits are disulfide-linked to the strands of a triple helix of ColQ collagen.	Disulfides	297-306	butyrylcholinesterase	Homo sapiens	89-93
24616921-2	2014	We report an analysis of 3D-DS in bovine seminal ribonuclease, a homodimeric protein whose subunits are linked by two disulfide bridges, based on NMR and biochemical studies.	Disulfides	118-127	seminal ribonuclease	Bos taurus	41-61
24465767-0	2014	Soluble expression of disulfide bond containing proteins FGF15 and FGF19 in the cytoplasm of Escherichia coli.	Disulfides	22-31	fibroblast growth factor 15	Mus musculus	57-62
24465767-0	2014	Soluble expression of disulfide bond containing proteins FGF15 and FGF19 in the cytoplasm of Escherichia coli.	Disulfides	22-31	fibroblast growth factor 15	Mus musculus	67-72
24465767-2	2014	FGF15/FGF19 protein contains two disulfide bonds.	Disulfides	33-42	fibroblast growth factor 15	Mus musculus	0-5
24465767-2	2014	FGF15/FGF19 protein contains two disulfide bonds.	Disulfides	33-42	fibroblast growth factor 15	Mus musculus	6-11
24465767-12	2014	In summary, we have successfully developed a method to express functional FGF19 protein in prokaryotic cells, and this strategy may be adapted for the expression of other disulfide-containing proteins.	Disulfides	171-180	fibroblast growth factor 15	Mus musculus	74-79
24328262-4	2014	The small, cellular peptide, glutathione, was used to degrade the particles through the reductive cleavage of disulfide bonds that stabilize the individual PRX polymers.	Disulfides	110-119	periaxin	Homo sapiens	156-159
24409188-2	2014	Thioredoxin1 (Trx1) and Thioredoxin2 (Trx2), mainly located in the cytoplasm and mitochondria, respectively, are ubiquitously expressed in variety of cells and control cellular reactive oxygen species by reducing the disulfides into thiol groups.	Disulfides	217-227	thioredoxin	Homo sapiens	14-18
24409188-2	2014	Thioredoxin1 (Trx1) and Thioredoxin2 (Trx2), mainly located in the cytoplasm and mitochondria, respectively, are ubiquitously expressed in variety of cells and control cellular reactive oxygen species by reducing the disulfides into thiol groups.	Disulfides	217-227	thioredoxin 2	Homo sapiens	24-36
24409188-2	2014	Thioredoxin1 (Trx1) and Thioredoxin2 (Trx2), mainly located in the cytoplasm and mitochondria, respectively, are ubiquitously expressed in variety of cells and control cellular reactive oxygen species by reducing the disulfides into thiol groups.	Disulfides	217-227	thioredoxin 2	Homo sapiens	38-42
24409188-3	2014	Thioredoxin interacting protein (Txnip/thioredoxin binding protein-2/vitamin D3 upregulated protein) directly binds to Trx1 and Trx2 (Trx) and inhibit the reducing activity of Trx through their disulfide exchange.	Disulfides	194-203	thioredoxin	Homo sapiens	0-11
24409188-3	2014	Thioredoxin interacting protein (Txnip/thioredoxin binding protein-2/vitamin D3 upregulated protein) directly binds to Trx1 and Trx2 (Trx) and inhibit the reducing activity of Trx through their disulfide exchange.	Disulfides	194-203	thioredoxin	Homo sapiens	119-123
24409188-3	2014	Thioredoxin interacting protein (Txnip/thioredoxin binding protein-2/vitamin D3 upregulated protein) directly binds to Trx1 and Trx2 (Trx) and inhibit the reducing activity of Trx through their disulfide exchange.	Disulfides	194-203	thioredoxin 2	Homo sapiens	128-132
24409188-3	2014	Thioredoxin interacting protein (Txnip/thioredoxin binding protein-2/vitamin D3 upregulated protein) directly binds to Trx1 and Trx2 (Trx) and inhibit the reducing activity of Trx through their disulfide exchange.	Disulfides	194-203	thioredoxin 2	Homo sapiens	119-122
24409188-3	2014	Thioredoxin interacting protein (Txnip/thioredoxin binding protein-2/vitamin D3 upregulated protein) directly binds to Trx1 and Trx2 (Trx) and inhibit the reducing activity of Trx through their disulfide exchange.	Disulfides	194-203	thioredoxin 2	Homo sapiens	128-131
24300993-1	2014	The thylakoid protein LTO1/AtVKOR-DsbA is recently found to be an oxidoreductase involved in disulfide bond formation and the assembly of photosystem II (PSII) in Arabidopsis thaliana.	Disulfides	93-102	NAD(P)H dehydrogenase (quinone)s	Arabidopsis thaliana	22-26
24254994-7	2014	No differences in the abundance of any protein were observed; however, FABP9 in Adcy10-null cauda epididymal spermatozoa contained fewer disulfide bonds than wild-type sperm cells.	Disulfides	137-146	adenylate cyclase 10	Mus musculus	80-86
32481977-5	2013	The disulfide bonds in protein bovine alpha-lactalbumin (BLA) can be ruptured by controlled UV illumination, which triggers the formation of nano-sized protein aggregates and releases free thiol groups for the modification of the active targeting ligand of circular RGD peptide.	Disulfides	4-13	lactalbumin alpha	Bos taurus	38-55
24391652-3	2013	Through a dithiol-disulfide exchange reaction, the reduced form of thioredoxin preferentially interacts with the oxidized forms of targets, which are immediately released after this reaction is complete.	Disulfides	18-27	thioredoxin	Homo sapiens	67-78
24391652-7	2013	These results explain the reason for selective association of thioredoxin with oxidized targets for reduction, whereas immediate dissociation from a reduced target when the dithiol-disulfide exchange reaction is complete.	Disulfides	181-190	thioredoxin	Homo sapiens	62-73
24900791-0	2014	Replacement of the Disulfide Bridge in a KLK3-Stimulating Peptide Using Orthogonally Protected Building Blocks.	Disulfides	19-28	kallikrein related peptidase 3	Homo sapiens	41-45
24900791-1	2014	Peptide "B-2", which is one of the most potent kallikrein-related peptidase 3 (KLK3)-stimulating compounds, consists of 12 amino acids and is cyclized by a disulfide bridge between the N- and C-terminal cysteines.	Disulfides	156-165	kallikrein related peptidase 3	Homo sapiens	47-77
24900791-1	2014	Peptide "B-2", which is one of the most potent kallikrein-related peptidase 3 (KLK3)-stimulating compounds, consists of 12 amino acids and is cyclized by a disulfide bridge between the N- and C-terminal cysteines.	Disulfides	156-165	kallikrein related peptidase 3	Homo sapiens	79-83
24056075-2	2013	To establish an ultrasensitive receptor-binding assay for INSL3-RXFP2 interaction studies, in the present work we labeled a recombinant INSL3 peptide with a newly developed nanoluciferase (NanoLuc) reporter through a convenient chemical conjugation approach, including the introduction of an active disulfide bond to INSL3 by chemical modification and engineering of a 6x His-Cys-NanoLuc carrying a unique exposed cysteine at the N-terminus.	Disulfides	299-308	insulin like 3	Homo sapiens	136-141
24056075-2	2013	To establish an ultrasensitive receptor-binding assay for INSL3-RXFP2 interaction studies, in the present work we labeled a recombinant INSL3 peptide with a newly developed nanoluciferase (NanoLuc) reporter through a convenient chemical conjugation approach, including the introduction of an active disulfide bond to INSL3 by chemical modification and engineering of a 6x His-Cys-NanoLuc carrying a unique exposed cysteine at the N-terminus.	Disulfides	299-308	insulin like 3	Homo sapiens	136-141
24076538-5	2013	The unique gene structure, the conservation of both cysteines that form the single disulfide bridge in leptin, and stable clustering in phylogenetic analyses substantiate the unambiguous orthology of mammalian and fish leptins, despite low amino acid identity.	Disulfides	83-92	leptin	Homo sapiens	103-109
24142694-5	2013	The disulfide bond has a standard redox potential of -301 mV and is stoichiometrically reduced by the inflammatory mediator, thioredoxin, with a rate constant of 350 m(-1) s(-1).	Disulfides	4-13	thioredoxin	Homo sapiens	125-136
24062305-3	2013	A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase.	Disulfides	6-15	thioredoxin	Homo sapiens	24-28
24062305-3	2013	A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase.	Disulfides	6-15	thioredoxin	Homo sapiens	24-27
24062305-3	2013	A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase.	Disulfides	56-65	thioredoxin	Homo sapiens	24-28
24062305-3	2013	A two-disulfide form of Trx1, containing an active site disulfide between Cys-32 and Cys-35 and a non-active site disulfide between Cys-62 and Cys-69, is inactive either as a disulfide reductase or as a substrate for Trx reductase.	Disulfides	56-65	thioredoxin	Homo sapiens	24-27
24003229-2	2013	Ricin holotoxin does not inhibit translation unless the disulfide bond between the A (RTA) and B (RTB) subunits is reduced.	Disulfides	56-65	MAS related GPR family member F	Homo sapiens	86-89
24146829-6	2013	We found that a single disulfide bond strategically inserted between the highly conserved layers 1 and 2 (C65-C115) is able to "lock" gp120 in a CD4 receptor bound conformation (in the absence of CD4), as indicated by the lower dissociation constant (Kd) for the CD4-induced (CD4i) epitope binding 17b antibody.	Disulfides	23-32	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	134-139
24146829-7	2013	When disulfide-stabilized monomeric (gp120) and trimeric (gp140) Envs were used to immunize rabbits, they were found to elicit a higher proportion of antibodies directed against both CD4i and CD4 binding site epitopes than the wild-type proteins.	Disulfides	5-14	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	37-42
23748428-2	2013	To get insights into possible causes of this heterogeneity of UAKD, we describe the new mutant mouse line Umod(C93F), leading to disruption of a putative disulfide bond which is also absent in a known human UMOD mutation, and compare the phenotype of this new mouse line with the recently published mouse line Umod(A227T).	Disulfides	154-163	uromodulin	Mus musculus	106-110
23748428-2	2013	To get insights into possible causes of this heterogeneity of UAKD, we describe the new mutant mouse line Umod(C93F), leading to disruption of a putative disulfide bond which is also absent in a known human UMOD mutation, and compare the phenotype of this new mouse line with the recently published mouse line Umod(A227T).	Disulfides	154-163	uromodulin	Mus musculus	310-314
23713588-6	2013	The complex involved a stable non-covalent interaction that was disassociated by the reduction of intramolecular disulfides in ERp46, or by disruption of the decameric structure of hyperoxidized Prx2.	Disulfides	113-123	thioredoxin domain containing 5	Homo sapiens	127-132
23403036-2	2013	Thioredoxin is an important regulator of cellular redox homeostasis, which catalyzes the reduction of disulfide bonds.	Disulfides	102-111	thioredoxin	Homo sapiens	0-11
23289792-7	2013	The thylakoid-located Lumen thiol oxidoreductase 1 (LTO1, At4g35760) can catalyze the formation of the disulfide bond of the extrinsic PsbO protein of PSII.	Disulfides	103-112	NAD(P)H dehydrogenase (quinone)s	Arabidopsis thaliana	22-50
22846892-3	2013	The C-terminal coiled domain is cross-linked to the presumed docking surface of the dimeric S100A3 via a disulfide bridge.	Disulfides	105-114	S100 calcium binding protein A3	Homo sapiens	92-98
23368764-7	2013	The degradation of the PRX capsules was demonstrated through the disassembly of the PE PRXs using glutathione, which cleaves the disulfide bonds linking the end-capping groups of the PE PRXs.	Disulfides	129-138	periaxin	Homo sapiens	23-26
23296632-1	2013	Upon controlled UV illumination, disulfide bonds in bovine alpha-lactalbumin (BLA) are selectively broken, leading to self-assembly of the BLA and doxorubicin (DOX) molecules into nanoparticles via hydrophobic interactions and intermolecular disulfide bonds.	Disulfides	33-42	lactalbumin alpha	Bos taurus	59-76
23296632-1	2013	Upon controlled UV illumination, disulfide bonds in bovine alpha-lactalbumin (BLA) are selectively broken, leading to self-assembly of the BLA and doxorubicin (DOX) molecules into nanoparticles via hydrophobic interactions and intermolecular disulfide bonds.	Disulfides	242-251	lactalbumin alpha	Bos taurus	59-76
23482568-9	2013	The protective activity of DEFB114 on RAW264.7, human sperm, and the d-galactosamine-sensitized mice was disulfide bond-dependent because alkylated DEFB114 lost its activity.	Disulfides	105-114	defensin beta 114	Homo sapiens	27-34
23482568-9	2013	The protective activity of DEFB114 on RAW264.7, human sperm, and the d-galactosamine-sensitized mice was disulfide bond-dependent because alkylated DEFB114 lost its activity.	Disulfides	105-114	defensin beta 114	Homo sapiens	148-155
23597483-1	2013	The mitochondrial disulfide relay system of Mia40 and Erv1/ALR facilitates import of the small translocase of the inner membrane (Tim) proteins and cysteine-rich proteins.	Disulfides	18-27	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	54-58
23597483-1	2013	The mitochondrial disulfide relay system of Mia40 and Erv1/ALR facilitates import of the small translocase of the inner membrane (Tim) proteins and cysteine-rich proteins.	Disulfides	18-27	growth factor, augmenter of liver regeneration	Homo sapiens	59-62
23597483-2	2013	A chemical screen identified small molecules that inhibit Erv1 oxidase activity, thereby facilitating dissection of the disulfide relay system in yeast and vertebrate mitochondria.	Disulfides	120-129	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	58-62
23593125-5	2013	A higher abundance of PDI and PDI-like proteins was observed which possess a known function of assisting disulfide bond formation.	Disulfides	105-114	protein disulfide-isomerase	Triticum aestivum	22-25
23593125-5	2013	A higher abundance of PDI and PDI-like proteins was observed which possess a known function of assisting disulfide bond formation.	Disulfides	105-114	protein disulfide-isomerase	Triticum aestivum	30-33
23413836-1	2013	Hepcidin is a liver-secreted small disulfide-rich peptide that plays a key role in iron homeostasis by binding and mediating the internalization and degradation of the only iron efflux transporter so far known, ferroportin (Fpn).	Disulfides	35-44	hepcidin antimicrobial peptide	Homo sapiens	0-8
23440420-2	2013	B27 can be expressed at the cell surface of APC as both classical beta2-microglobulin-associated B27 and B27 free H chain forms (FHC), including disulfide-bonded H chain homodimers (termed B27(2)).	Disulfides	145-154	major histocompatibility complex, class I, B	Homo sapiens	0-3
24621840-0	2013	The WAP four-disulfide core domain protein HE4: a novel biomarker for heart failure.	Disulfides	13-22	WAP four-disulfide core domain 2	Homo sapiens	43-46
23414292-1	2013	Thioredoxin protects cells against oxidative damage by reducing disulfide bonds in improperly oxidized proteins.	Disulfides	64-73	thioredoxin	Homo sapiens	0-11
23416356-0	2013	Mixed disulfide formation in vitro between a glycoprotein substrate and yeast oligosaccharyltransferase subunits Ost3p and Ost6p.	Disulfides	6-15	dolichyl-diphosphooligosaccharide--protein glycotransferase OST3	Saccharomyces cerevisiae S288C	113-118
23416356-0	2013	Mixed disulfide formation in vitro between a glycoprotein substrate and yeast oligosaccharyltransferase subunits Ost3p and Ost6p.	Disulfides	6-15	dolichyl-diphosphooligosaccharide--protein glycotransferase	Saccharomyces cerevisiae S288C	123-128
23416356-3	2013	A model of Ost3p and Ost6p function has been proposed in which their thioredoxin-like active site cysteines form transient mixed disulfide bonds with cysteines in substrate proteins to enhance the glycosylation of nearby asparagine residues.	Disulfides	129-138	dolichyl-diphosphooligosaccharide--protein glycotransferase OST3	Saccharomyces cerevisiae S288C	11-16
23416356-3	2013	A model of Ost3p and Ost6p function has been proposed in which their thioredoxin-like active site cysteines form transient mixed disulfide bonds with cysteines in substrate proteins to enhance the glycosylation of nearby asparagine residues.	Disulfides	129-138	dolichyl-diphosphooligosaccharide--protein glycotransferase	Saccharomyces cerevisiae S288C	21-26
23327656-0	2013	Selective inhibition of extracellular thioredoxin by asymmetric disulfides.	Disulfides	64-74	thioredoxin	Homo sapiens	38-49
23327656-2	2013	Only few extracellular targets of Trx-mediated thiol-disulfide exchange are known.	Disulfides	53-62	thioredoxin	Homo sapiens	34-37
23327656-3	2013	For example, Trx activates extracellular transglutaminase 2 (TG2) via reduction of an intramolecular disulfide bond.	Disulfides	101-110	thioredoxin	Homo sapiens	13-16
23327656-5	2013	Starting from a clinical-stage asymmetric disulfide lead, we have identified analogs with &gt;100-fold specificity for Trx.	Disulfides	42-51	thioredoxin	Homo sapiens	119-122
24273480-5	2013	The covalent attachment of siRNAs to PP75 using disulfide linkages generates conjugates that effectively traffic siRNAs to the cytoplasm of target cells both in vitro and in vivo.	Disulfides	48-57	RAB11 family interacting protein 5	Homo sapiens	37-41
23009931-9	2013	These data support a model for the acute activation of GLUT1 that suggests that the activity of GLUT1 is enhanced by the formation of an internal disulfide bond within GLUT1 itself.	Disulfides	146-155	solute carrier family 2 (facilitated glucose transporter), member 1	Mus musculus	55-60
23009931-9	2013	These data support a model for the acute activation of GLUT1 that suggests that the activity of GLUT1 is enhanced by the formation of an internal disulfide bond within GLUT1 itself.	Disulfides	146-155	solute carrier family 2 (facilitated glucose transporter), member 1	Mus musculus	96-101
23009931-9	2013	These data support a model for the acute activation of GLUT1 that suggests that the activity of GLUT1 is enhanced by the formation of an internal disulfide bond within GLUT1 itself.	Disulfides	146-155	solute carrier family 2 (facilitated glucose transporter), member 1	Mus musculus	96-101
23390666-0	2004	(89)Zr-Labeled anti-CD105 (endoglin) chimeric monoclonal antibody TRC105 linked to IRDye 800CW The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked, homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	157-166	endoglin	Mus musculus	20-25
23390666-0	2004	(89)Zr-Labeled anti-CD105 (endoglin) chimeric monoclonal antibody TRC105 linked to IRDye 800CW The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked, homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	157-166	endoglin	Mus musculus	27-35
23390666-0	2004	(89)Zr-Labeled anti-CD105 (endoglin) chimeric monoclonal antibody TRC105 linked to IRDye 800CW The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked, homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	157-166	endoglin	Mus musculus	99-104
23390666-0	2004	(89)Zr-Labeled anti-CD105 (endoglin) chimeric monoclonal antibody TRC105 linked to IRDye 800CW The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked, homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	157-166	endoglin	Mus musculus	114-122
22702224-4	2013	RECENT ADVANCES: Human cytosolic/nuclear Trx1 in the disulfide form can be nitrosylated at Cys73 and transnitrosylate target proteins, including caspase 3.	Disulfides	53-62	thioredoxin	Homo sapiens	41-45
23220234-4	2013	Herein we show that AGR2 homo-dimerizes through an intermolecular disulfide bond.	Disulfides	66-75	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	20-24
23250361-0	2012	A Promising Vector for TCR Gene Therapy: Differential Effect of siRNA, 2A Peptide, and Disulfide Bond on the Introduced TCR Expression.	Disulfides	87-96	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	120-123
22949627-0	2012	Reversible disulfide formation of the glutamate carboxypeptidase II inhibitor E2072 results in prolonged systemic exposures in vivo.	Disulfides	11-20	folate hydrolase 1	Rattus norvegicus	38-67
23070980-1	2012	EPPIN (epididymal protease inhibitor; SPINLW1), an antimicrobial cysteine-rich protein containing both Kunitz and whey acidic protein (WAP)-type four disulfide core protease inhibitor consensus sequences, is a target for male contraception because of its critical role in sperm motility.	Disulfides	150-159	epididymal peptidase inhibitor	Rattus norvegicus	0-5
23070980-1	2012	EPPIN (epididymal protease inhibitor; SPINLW1), an antimicrobial cysteine-rich protein containing both Kunitz and whey acidic protein (WAP)-type four disulfide core protease inhibitor consensus sequences, is a target for male contraception because of its critical role in sperm motility.	Disulfides	150-159	epididymal peptidase inhibitor	Rattus norvegicus	7-36
23070980-1	2012	EPPIN (epididymal protease inhibitor; SPINLW1), an antimicrobial cysteine-rich protein containing both Kunitz and whey acidic protein (WAP)-type four disulfide core protease inhibitor consensus sequences, is a target for male contraception because of its critical role in sperm motility.	Disulfides	150-159	epididymal peptidase inhibitor	Rattus norvegicus	38-45
23006734-1	2012	Protein kinase G (PKG) is activated by nitric oxide (NO)-induced cGMP binding or alternatively by oxidant-induced interprotein disulfide formation.	Disulfides	127-136	protein kinase cGMP-dependent 1	Homo sapiens	0-16
23006734-1	2012	Protein kinase G (PKG) is activated by nitric oxide (NO)-induced cGMP binding or alternatively by oxidant-induced interprotein disulfide formation.	Disulfides	127-136	protein kinase cGMP-dependent 1	Homo sapiens	18-21
23006734-3	2012	1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one (ODQ) blockade of cGMP production increased disulfide PKG to 13 +- 2% and 29+-4% of total in aorta and mesenteries, respectively.	Disulfides	88-97	protein kinase cGMP-dependent 1	Homo sapiens	98-101
23006734-6	2012	Thus, mesenteries, but not aorta, can compensate for loss of NO-cGMP by recruiting disulfide activation of PKG.	Disulfides	83-92	protein kinase cGMP-dependent 1	Homo sapiens	107-110
23006734-12	2012	In summary, cGMP binding to PKG induces a state that is resistant to disulfide formation.	Disulfides	69-78	protein kinase cGMP-dependent 1	Homo sapiens	28-31
22959994-4	2012	We have visualized the cytoskeletons formed by actin and tubulin, the chaperone PDI that catalyses native disulfide bond formation of proteins in the endoplasmic reticulum (ER) and the calcium sensor STIM1 that is integrated in ER membranes, using established cell lines.	Disulfides	106-115	peptidyl arginine deiminase 1	Homo sapiens	80-83
22902630-3	2012	In response to peroxide, Prdx1 catalyzed oxidation of ASK1 to a disulfide-linked multimer, and this occurred via transient formation of a Prdx1-ASK1 mixed disulfide intermediate.	Disulfides	64-73	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	54-58
22902630-3	2012	In response to peroxide, Prdx1 catalyzed oxidation of ASK1 to a disulfide-linked multimer, and this occurred via transient formation of a Prdx1-ASK1 mixed disulfide intermediate.	Disulfides	64-73	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	144-148
22902630-3	2012	In response to peroxide, Prdx1 catalyzed oxidation of ASK1 to a disulfide-linked multimer, and this occurred via transient formation of a Prdx1-ASK1 mixed disulfide intermediate.	Disulfides	155-164	peroxiredoxin 1	Homo sapiens	25-30
22902630-3	2012	In response to peroxide, Prdx1 catalyzed oxidation of ASK1 to a disulfide-linked multimer, and this occurred via transient formation of a Prdx1-ASK1 mixed disulfide intermediate.	Disulfides	155-164	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	54-58
22902630-3	2012	In response to peroxide, Prdx1 catalyzed oxidation of ASK1 to a disulfide-linked multimer, and this occurred via transient formation of a Prdx1-ASK1 mixed disulfide intermediate.	Disulfides	155-164	peroxiredoxin 1	Homo sapiens	138-143
22902630-3	2012	In response to peroxide, Prdx1 catalyzed oxidation of ASK1 to a disulfide-linked multimer, and this occurred via transient formation of a Prdx1-ASK1 mixed disulfide intermediate.	Disulfides	155-164	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	144-148
22902630-6	2012	These data imply that Prdx1 can function as a peroxide receptor in response to extracellular H(2)O(2), receiving the peroxide signal and transducing it into a disulfide bond that is subsequently transmitted to the substrate, ASK1, resulting in p38 phosphorylation.	Disulfides	159-168	peroxiredoxin 1	Homo sapiens	22-27
22902630-6	2012	These data imply that Prdx1 can function as a peroxide receptor in response to extracellular H(2)O(2), receiving the peroxide signal and transducing it into a disulfide bond that is subsequently transmitted to the substrate, ASK1, resulting in p38 phosphorylation.	Disulfides	159-168	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	225-229
22902630-7	2012	Interestingly, in response to peroxide, Prdx1 and Prdx3 transiently formed reducible higher molecular weight complexes, suggesting that multiple proteins are targets for Prdx-mediated oxidation via a disulfide-exchange mechanism.	Disulfides	200-209	peroxiredoxin 1	Homo sapiens	40-45
22842048-6	2012	These results suggest a model where the molecular interactions guiding the protein recognition between Mia40 and the disulfide-reduced CHCHD5 and CHCHD7 substrates occurs in vivo when the latter proteins are partially embedded in the protein import pore of the outer membrane of mitochondria.	Disulfides	117-126	coiled-coil-helix-coiled-coil-helix domain containing 5	Homo sapiens	135-141
22918950-2	2012	The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins.	Disulfides	4-13	growth factor, augmenter of liver regeneration	Homo sapiens	127-131
22897429-5	2012	In this study, we synthetically linked two DV1 peptides with the formation of a disulfide bond between the two cysteine residues present in the peptide sequence to generate a dimeric molecule potentially capable of interacting with two CXCR4 receptors.	Disulfides	80-89	intraflagellar transport 81	Homo sapiens	43-46
22760822-0	2012	Mutagenic analysis in a pure molecular system shows that thioredoxin-interacting protein residue Cys247 is necessary and sufficient for a mixed disulfide formation with thioredoxin.	Disulfides	144-153	thioredoxin	Homo sapiens	57-68
22665445-7	2012	Additionally, coimmunoprecipitation of XXT2YFP and XXT5HA proteins from Arabidopsis protoplasts indicated that while the formation of the XXT2-XXT2 homocomplex involves disulfide bonds, the formation of the XXT2-XXT5 heterocomplex does not involve covalent interactions.	Disulfides	169-178	UDP-xylosyltransferase 2	Arabidopsis thaliana	39-43
22665445-7	2012	Additionally, coimmunoprecipitation of XXT2YFP and XXT5HA proteins from Arabidopsis protoplasts indicated that while the formation of the XXT2-XXT2 homocomplex involves disulfide bonds, the formation of the XXT2-XXT5 heterocomplex does not involve covalent interactions.	Disulfides	169-178	UDP-xylosyltransferase 2	Arabidopsis thaliana	138-142
22665445-7	2012	Additionally, coimmunoprecipitation of XXT2YFP and XXT5HA proteins from Arabidopsis protoplasts indicated that while the formation of the XXT2-XXT2 homocomplex involves disulfide bonds, the formation of the XXT2-XXT5 heterocomplex does not involve covalent interactions.	Disulfides	169-178	UDP-xylosyltransferase 2	Arabidopsis thaliana	138-142
22764390-0	2004	(64)Cu-Labeled PEGylated nano-graphene oxide (GO) covalently linked to NOTA-conjugated anti-CD105 (endoglin) chimeric monoclonal antibody TRC105 The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked, homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	207-216	endoglin	Mus musculus	99-107
22764390-0	2004	(64)Cu-Labeled PEGylated nano-graphene oxide (GO) covalently linked to NOTA-conjugated anti-CD105 (endoglin) chimeric monoclonal antibody TRC105 The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked, homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	207-216	endoglin	Mus musculus	149-154
22514274-2	2012	The redox switch CP12 is an intrinsically disordered protein that can form two disulfide bridges.	Disulfides	79-88	cytochrome P450 family 1 subfamily A member 2	Homo sapiens	17-21
22586035-2	2012	GILT(-/-) mice are phenotypically normal, but their T cells exhibit reduced proliferation to several exogenously administered Ags that include cysteine residues and disulfide bonds.	Disulfides	165-174	interferon gamma inducible protein 30	Mus musculus	0-4
22586035-3	2012	We undertook the present studies to determine if GILT(-/-) mice would process exogenously administered myelin oligodendrocyte glycoprotein (MOG), which contains disulfide bonds, to generate experimental autoimmune encephalomyelitis (EAE) to the endogenous protein.	Disulfides	161-170	myelin oligodendrocyte glycoprotein	Mus musculus	103-138
22586035-3	2012	We undertook the present studies to determine if GILT(-/-) mice would process exogenously administered myelin oligodendrocyte glycoprotein (MOG), which contains disulfide bonds, to generate experimental autoimmune encephalomyelitis (EAE) to the endogenous protein.	Disulfides	161-170	myelin oligodendrocyte glycoprotein	Mus musculus	140-143
22593621-11	2012	Disulfide-dependent B27 H chain dimers and multimers are stronger ligands for LILRB2 than HLA class I heterotrimers and H chains.	Disulfides	0-9	major histocompatibility complex, class I, B	Homo sapiens	20-23
22229892-8	2012	FUTURE DIRECTIONS: The importance of disulfide bond reduction in misfolded proteins for retrotranslocation through the dislocon channel will be discussed by comparing the function of ERdj5 with that of other oxidoreductases in the ER.	Disulfides	37-46	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	183-188
22503978-12	2012	The molecule resides in the lumen of the endoplasmic reticulum and participates in disulfide bond formation during protein folding by interacting with calnexin and calreticulin.	Disulfides	83-92	calnexin	Bos taurus	151-159
21545288-1	2012	Pyroglutamate helix B surface peptide (pHBSP) is an 11 amino acid peptide, designed to interact with a novel cell surface receptor, composed of the classical erythropoietin (EPO) receptor disulfide linked to the beta common receptor.	Disulfides	188-197	erythropoietin	Rattus norvegicus	158-172
21545288-1	2012	Pyroglutamate helix B surface peptide (pHBSP) is an 11 amino acid peptide, designed to interact with a novel cell surface receptor, composed of the classical erythropoietin (EPO) receptor disulfide linked to the beta common receptor.	Disulfides	188-197	erythropoietin	Rattus norvegicus	174-177
22334695-7	2012	Despite the absence of the globular C1q domain, immunoprecipitation and Western blot analyses demonstrated that EMILIN-3 forms disulfide-bonded homotrimers and higher order oligomers.	Disulfides	127-136	elastin microfibril interfacer 3	Mus musculus	112-120
22354149-0	2012	A disulfide bound-molecular beacon as a fluorescent probe for the detection of reduced glutathione and its application in cells.	Disulfides	2-11	ubiquitin like 5	Homo sapiens	28-34
22354149-1	2012	A disulfide-bound molecular beacon (MB) is reported to respond sensitively to changing levels of glutathione in vitro.	Disulfides	2-11	ubiquitin like 5	Homo sapiens	28-34
22412017-1	2012	The endoplasmic reticulum (ER) provides an environment optimized for oxidative protein folding through the action of Ero1p, which generates disulfide bonds, and Pdi1p, which receives disulfide bonds from Ero1p and transfers them to substrate proteins.	Disulfides	183-192	peptidyl arginine deiminase 1	Homo sapiens	161-166
22412017-6	2012	Pdi1p responded to the availability of free thiols and the relative levels of reduced and oxidized glutathione in the ER to control Ero1p activity and ensure that cells generate the minimum number of disulfide bonds needed for efficient oxidative protein folding.	Disulfides	200-209	peptidyl arginine deiminase 1	Homo sapiens	0-5
22002549-2	2012	Wild-type HspB1 and Cys mutants of HspB5, HspB6 and HspB8 containing a single Cys residue in position homologous to that of Cys137 of human HspB1 were able to generate heterodimers cross-linked by disulfide bond.	Disulfides	197-206	heat shock protein family B (small) member 1	Homo sapiens	10-15
22002549-2	2012	Wild-type HspB1 and Cys mutants of HspB5, HspB6 and HspB8 containing a single Cys residue in position homologous to that of Cys137 of human HspB1 were able to generate heterodimers cross-linked by disulfide bond.	Disulfides	197-206	heat shock protein family B (small) member 1	Homo sapiens	140-145
22245752-9	2012	The developed "pCold-PDI" vector has potential for overproduction of other scFvs and disulfide-containing proteins in the Origami strains.	Disulfides	85-94	protein-disulfide isomerase	Escherichia coli	21-24
22379637-5	2004	CD105 (endoglin, EDG) is a homodimeric transmembrane glycoprotein (180 kDa) with disulfide-linked subunits of 95,000.	Disulfides	81-90	endoglin	Mus musculus	0-5
22249117-6	2012	Moreover, further NO treatment induced the formation of SDS-stable insoluble tau mega-aggregates that were composed of dephosphorylated full-length tau molecules and other proteins, and were stabilized through disulfide bonds.	Disulfides	210-219	microtubule associated protein tau	Homo sapiens	77-80
22129136-2	2012	Mature AgRP(83-132), produced by endoproteolytic processing, contains a central region that folds as an inhibitor cystine knot (ICK) stabilized by a network of disulfide bonds; this domain alone carries the molecular features for high affinity McR binding and inverse agonism.	Disulfides	160-169	agouti related neuropeptide	Rattus norvegicus	7-11
22207737-1	2012	A close homologue to protein disulfide isomerase (PDI) called ERp57 forms disulfide bonds in glycoproteins in the endoplasmic reticulum and is expressed on the platelet surface.	Disulfides	29-38	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	50-53
22207737-1	2012	A close homologue to protein disulfide isomerase (PDI) called ERp57 forms disulfide bonds in glycoproteins in the endoplasmic reticulum and is expressed on the platelet surface.	Disulfides	29-38	protein disulfide isomerase associated 3	Mus musculus	62-67
22036880-2	2012	Then, a biodegradable polyethylenimine containing multiple disulfide bonds (SS-PEI) was successfully applied as a potent non-viral carrier for intracellular delivery of the hTERT siRNA in vitro and in vivo.	Disulfides	59-68	telomerase reverse transcriptase	Homo sapiens	173-178
22224850-0	2012	An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR.	Disulfides	46-55	growth factor, augmenter of liver regeneration	Homo sapiens	100-103
22224850-1	2012	The oxidative folding mechanism in the intermembrane space of human mitochondria underpins a disulfide relay system consisting of the import receptor Mia40 and the homodimeric FAD-dependent thiol oxidase ALR.	Disulfides	93-102	growth factor, augmenter of liver regeneration	Homo sapiens	204-207
22259814-5	2004	CD105 (endoglin, EDG) is a homodimeric transmembrane glycoprotein (180 kDa) with disulfide-linked subunits of 95 kDa.	Disulfides	81-90	endoglin	Mus musculus	0-5
22259815-5	2004	CD105 (endoglin, EDG) is a homodimeric transmembrane glycoprotein (180 kDa) with disulfide-linked subunits of 95 kDa.	Disulfides	81-90	endoglin	Mus musculus	0-5
22126836-6	2012	We also demonstrate how this methodology is used with experimental NMR data for peptides with complex disulfide topologies, including hepcidin, Kalata-B1, and mu-Conotoxin KIIIA.	Disulfides	102-111	hepcidin antimicrobial peptide	Homo sapiens	134-142
21833020-1	2012	Gamma-IFN-inducible lysosomal thiol reductase (GILT) facilitates major histocompatibility complex class II-restricted processing through endocytic reduction of protein disulfide bonds and is necessary for efficient class II-restricted processing of melanocyte differentiation antigen, tyrosinase-related protein 1 (TRP1).	Disulfides	168-177	interferon gamma inducible protein 30	Mus musculus	0-45
21833020-1	2012	Gamma-IFN-inducible lysosomal thiol reductase (GILT) facilitates major histocompatibility complex class II-restricted processing through endocytic reduction of protein disulfide bonds and is necessary for efficient class II-restricted processing of melanocyte differentiation antigen, tyrosinase-related protein 1 (TRP1).	Disulfides	168-177	interferon gamma inducible protein 30	Mus musculus	47-51
22723105-6	2012	Hence, protocols for mono-PEGylation of Fab via free cysteine in the hinge region and di-PEGylation of Fab via interchain disulfide bridge are provided in this chapter.	Disulfides	122-131	FA complementation group B	Homo sapiens	40-43
22723105-6	2012	Hence, protocols for mono-PEGylation of Fab via free cysteine in the hinge region and di-PEGylation of Fab via interchain disulfide bridge are provided in this chapter.	Disulfides	122-131	FA complementation group B	Homo sapiens	103-106
23029461-11	2012	The long distance between TrxR C153 and disulfide bond of Trx C387-C390 has been observed in AtNTRA-(Trx-D) because of following reasons: i) unstable and unfavorable interaction of the linker region, ii) shifted Trx domain, and iii) different or weak interface interaction of Trx domains.	Disulfides	40-49	NADPH-dependent thioredoxin reductase A	Arabidopsis thaliana	93-99
22347366-1	2012	Endoglin, a type I membrane glycoprotein expressed as a disulfide-linked homodimer on human vascular endothelial cells, is a component of the transforming growth factor (TGF)-beta receptor complex and is implicated in a dominant vascular dysplasia known as hereditary hemorrhagic telangiectasia as well as in preeclampsia.	Disulfides	56-65	endoglin	Homo sapiens	0-8
22125416-0	2011	Cleavage of Multiple Disulfide Bonds in Insulin via Gold Cationization and Collision-induced Dissociation.	Disulfides	21-30	insulin	Bos taurus	40-47
22125416-5	2011	However, the incorporation of two gold cations, regardless of oxidation state, resulted in efficient cleavage of the disulfide bonds connecting the two chains of insulin.	Disulfides	117-126	insulin	Bos taurus	162-169
20955713-1	2011	Thioredoxin 1 (Trx1) is a small molecule with reactive cysteines that reduces proteins with disulfide bonds through a thiol disulfide exchange reaction.	Disulfides	92-101	thioredoxin	Homo sapiens	0-13
20955713-1	2011	Thioredoxin 1 (Trx1) is a small molecule with reactive cysteines that reduces proteins with disulfide bonds through a thiol disulfide exchange reaction.	Disulfides	92-101	thioredoxin	Homo sapiens	15-19
21576020-3	2011	Irreversible inhibition required a glycosylated K(+) channel subunit and was completely reversible with mild reductant when the tether connecting the toxin to the maleimide contained a disulfide bond.	Disulfides	185-194	potassium voltage-gated channel subfamily C member 4	Homo sapiens	48-68
21576020-4	2011	Cleavage of the disulfide bond not only restored function, but delivered a biotin moiety to the modified K(+) channel subunit, providing a novel approach for preferentially labeling wild type K(+) channel complexes functioning in cells.	Disulfides	16-25	potassium voltage-gated channel subfamily C member 4	Homo sapiens	105-125
21947919-3	2011	Here, we present a novel, disulfide-linked nitroxide spin label, R1p, as an alternative to these flexible labels for PRE studies.	Disulfides	26-35	CD1b molecule	Homo sapiens	65-68
21788476-9	2011	Next, we created disulfide-linked NK1 homodimers through introduction of an N-terminal cysteine residue.	Disulfides	17-26	tachykinin receptor 1	Homo sapiens	34-37
21674661-4	2011	This version of caspase-7 is allosterically inactivated when two of the substrate-binding loops are locked together via an engineered disulfide.	Disulfides	134-143	caspase 7	Homo sapiens	16-25
21812504-6	2011	The overall cellular redox state is regulated by three systems that modulate cellular redox status by counteracting free radicals and ROS, or by reversing the formation of disulfides; two of these are dependent on glutathione and the third on thioredoxin.	Disulfides	172-182	thioredoxin	Homo sapiens	243-254
21540283-3	2011	Here we find that PDX1 is a direct transcriptional regulator of ER oxidoreductin-1-like beta (Ero1lbeta), which maintains the oxidative environment of the ER to facilitate disulfide bond formation.	Disulfides	172-181	endoplasmic reticulum oxidoreductase 1 beta	Mus musculus	94-103
21744417-0	2011	Application of MALDI TOF/TOF mass spectrometry and collision-induced dissociation for the identification of disulfide-bonded peptides.	Disulfides	108-117	FEZ family zinc finger 2	Homo sapiens	15-28
20177947-3	2011	The redox-sensing cysteine residues and the disulfide bond formed between these cysteine residues serve as redox-sensing molecular switches; these switches sense cellular oxidizing factors such as oxygen, reactive oxygen species, and cellular reducing factors such as thioredoxin (Trx), glutathione (GSH), and their family molecules.	Disulfides	44-53	thioredoxin	Homo sapiens	268-279
20177947-3	2011	The redox-sensing cysteine residues and the disulfide bond formed between these cysteine residues serve as redox-sensing molecular switches; these switches sense cellular oxidizing factors such as oxygen, reactive oxygen species, and cellular reducing factors such as thioredoxin (Trx), glutathione (GSH), and their family molecules.	Disulfides	44-53	thioredoxin	Homo sapiens	281-284
21454581-4	2011	Here we describe the production, crystallization, and structure of the LILRB4 ectodomain to 1.7 A using an expression strategy involving engineering of an additional disulfide bond in the D2 domain to enhance protein stability.	Disulfides	166-175	leukocyte immunoglobulin like receptor B4	Homo sapiens	71-77
21295137-6	2011	We used in situ mechanism-based kinetic trapping to identify disulfide-exchange interactions of Trx2 within functional mitochondria of intact cells.	Disulfides	61-70	thioredoxin 2	Homo sapiens	96-100
21377473-4	2011	We identified two previously undocumented disulfide bridges in the crystal structure of properly folded S100A3: one disulfide bridge is between Cys30 in the N-terminal pseudo-EF-hand and Cys68 in the C-terminal EF-hand (SS1), and another disulfide bridge attaches Cys99 in the C-terminal coil structure to Cys81 in helix IV (SS2).	Disulfides	116-125	S100 calcium binding protein A3	Homo sapiens	104-110
21357685-9	2011	PDI catalyzes the reduction of the PABP disulfide bond resulting in specific binding of PABP to the insulin 5" UTR.	Disulfides	40-49	poly(A) binding protein cytoplasmic 1	Homo sapiens	35-39
21357685-9	2011	PDI catalyzes the reduction of the PABP disulfide bond resulting in specific binding of PABP to the insulin 5" UTR.	Disulfides	40-49	poly(A) binding protein cytoplasmic 1	Homo sapiens	88-92
21329361-9	2011	Analysis of the cysteine reactivity of the compound shows that compound binding to Cys(107) in RGS8 inhibits Galpha binding in a manner that can be reversed by cleavage of the compound-RGS disulfide bond.	Disulfides	189-198	regulator of G protein signaling 8	Homo sapiens	95-99
21329361-9	2011	Analysis of the cysteine reactivity of the compound shows that compound binding to Cys(107) in RGS8 inhibits Galpha binding in a manner that can be reversed by cleavage of the compound-RGS disulfide bond.	Disulfides	189-198	succinate-CoA ligase GDP/ADP-forming subunit alpha	Homo sapiens	109-115
21467296-3	2011	However, a landmark discovery reveals an unexpected intersection of ROS and kinase signaling: ATM can be directly activated by oxidation to form a disulfide-linked dimer in a mechanism distinct from DNA damage activation.	Disulfides	147-156	ATM serine/threonine kinase	Homo sapiens	94-97
21256110-2	2011	The membrane topology of PCFT has been defined using the substituted cysteine accessibility method; an intramolecular disulfide bond between the Cys 66 and 298 residues, in the first and fourth extracellular loops, respectively, is present but not essential for function.	Disulfides	118-127	solute carrier family 46 member 1	Homo sapiens	25-29
21384830-5	2011	We compare these results with those obtained on the monomeric and dimeric forms of rat IAPP (rIAPP) with a disulfide bridge which differ from the hIAPP by 6 amino acids in the C-terminal region, but it is unable to form fibrils.	Disulfides	107-116	islet amyloid polypeptide	Rattus norvegicus	87-91
21384830-5	2011	We compare these results with those obtained on the monomeric and dimeric forms of rat IAPP (rIAPP) with a disulfide bridge which differ from the hIAPP by 6 amino acids in the C-terminal region, but it is unable to form fibrils.	Disulfides	107-116	islet amyloid polypeptide	Rattus norvegicus	93-98
21383138-3	2011	Here we present the mechanistic basis of ALR-MIA40 interaction at atomic resolution by biochemical and structural analyses of the mitochondrial ALR isoform and its covalent mixed disulfide intermediate with MIA40.	Disulfides	179-188	growth factor, augmenter of liver regeneration	Homo sapiens	41-44
21329881-2	2011	ERdj5 was recently discovered to be a key ER-resident PDI family member protein that accelerates ERAD by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1.	Disulfides	124-133	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	0-5
21237164-0	2011	The role of the C-terminus of human alpha-synuclein: intra-disulfide bonds between the C-terminus and other regions stabilize non-fibrillar monomeric isomers.	Disulfides	59-68	synuclein alpha	Homo sapiens	36-51
21237164-4	2011	Five X-isomers of oxidative-folded mutation of alpha-synuclein with three disulfides were isolated and their secondary structures and aggregating features were analyzed.	Disulfides	74-84	synuclein alpha	Homo sapiens	47-62
22312332-7	2011	Fixation of the C-terminus by introducing a disulfide bridge between the N- and C-termini of the peptide significantly enhanced the affinity to gp120.	Disulfides	44-53	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	144-149
20971184-2	2011	H(2)O(2) activates Yap1 through the Gpx3-mediated formation of a Yap1 Cys303-Cys598 intramolecular disulfide bond.	Disulfides	99-108	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	36-40
21099205-7	2011	We further addressed a role of the conserved disulfide bonds of Crp4 by analyzing reduced Crp4 (r-Crp4).	Disulfides	45-54	defensin, alpha, 20	Mus musculus	64-68
21888769-2	2011	The Cys124 and Cys71 residues of PTEN were critical for the formation of a disulfide bond and the intermediate glutathionylation in the process of reduction of the disulfide bond.	Disulfides	75-84	phosphatase and tensin homolog	Homo sapiens	33-37
21888769-2	2011	The Cys124 and Cys71 residues of PTEN were critical for the formation of a disulfide bond and the intermediate glutathionylation in the process of reduction of the disulfide bond.	Disulfides	164-173	phosphatase and tensin homolog	Homo sapiens	33-37
20929858-5	2010	The reduction of the catalytic disulfide of the atypical 2-Cys Prx5 is limited to the Trx system.	Disulfides	31-40	thioredoxin	Homo sapiens	86-89
20943653-0	2010	Disulfide bond that constrains the HIV-1 gp120 V3 domain is cleaved by thioredoxin.	Disulfides	0-9	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	41-46
20943653-0	2010	Disulfide bond that constrains the HIV-1 gp120 V3 domain is cleaved by thioredoxin.	Disulfides	0-9	thioredoxin	Homo sapiens	71-82
20943653-1	2010	A functional disulfide bond in both the HIV envelope glycoprotein, gp120, and its immune cell receptor, CD4, is involved in viral entry, and compounds that block cleavage of the disulfide bond in these proteins inhibit HIV entry and infection.	Disulfides	13-22	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	67-72
20943653-1	2010	A functional disulfide bond in both the HIV envelope glycoprotein, gp120, and its immune cell receptor, CD4, is involved in viral entry, and compounds that block cleavage of the disulfide bond in these proteins inhibit HIV entry and infection.	Disulfides	178-187	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	67-72
20943653-2	2010	The disulfide bonds in both proteins are cleaved at the cell surface by the small redox protein, thioredoxin.	Disulfides	4-13	thioredoxin	Homo sapiens	97-108
20943653-3	2010	The target gp120 disulfide and its mechanism of cleavage were determined using a thioredoxin kinetic trapping mutant and mass spectrometry.	Disulfides	17-26	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	11-16
20943653-3	2010	The target gp120 disulfide and its mechanism of cleavage were determined using a thioredoxin kinetic trapping mutant and mass spectrometry.	Disulfides	17-26	thioredoxin	Homo sapiens	81-92
20943653-4	2010	A single disulfide bond was cleaved in isolated and cell surface gp120, but not the gp160 precursor, and the extent of the reaction was enhanced when gp120 was bound to CD4.	Disulfides	9-18	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	65-70
20943653-4	2010	A single disulfide bond was cleaved in isolated and cell surface gp120, but not the gp160 precursor, and the extent of the reaction was enhanced when gp120 was bound to CD4.	Disulfides	9-18	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	150-155
20943653-5	2010	The Cys(32) sulfur ion of thioredoxin attacks the Cys(296) sulfur ion of the gp120 V3 domain Cys(296)-Cys(331) disulfide bond, cleaving the bond.	Disulfides	111-120	thioredoxin	Homo sapiens	26-37
20943653-5	2010	The Cys(32) sulfur ion of thioredoxin attacks the Cys(296) sulfur ion of the gp120 V3 domain Cys(296)-Cys(331) disulfide bond, cleaving the bond.	Disulfides	111-120	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	77-82
21150274-4	2010	The active ATM in this case is a disulfide-crosslinked dimer containing 2 or more disulfide bonds.	Disulfides	33-42	ATM serine/threonine kinase	Homo sapiens	11-14
21150274-4	2010	The active ATM in this case is a disulfide-crosslinked dimer containing 2 or more disulfide bonds.	Disulfides	82-91	ATM serine/threonine kinase	Homo sapiens	11-14
21150274-5	2010	Mutation of a critical cysteine residue in the FATC domain involved in disulfide bond formation specifically blocks ATM activation by oxidative stress.	Disulfides	71-80	ATM serine/threonine kinase	Homo sapiens	116-119
21151939-1	2010	The CD94 transmembrane-anchored glycoprotein forms disulfide-bonded heterodimers with the NKG2A subunit to form an inhibitory receptor or with the NKG2C or NKG2E subunits to assemble a receptor complex with activating DAP12 signaling proteins.	Disulfides	51-60	killer cell lectin like receptor C1	Homo sapiens	90-95
20857335-8	2010	Mutation screening of FOLR1 revealed a new homozygous missense mutation (p.Cys105Arg) that is predicted to abolish a disulfide bond, probably necessary for the correct folding of the protein.	Disulfides	117-126	folate receptor alpha	Homo sapiens	22-27
2532601-1	1989	The T cell receptor (TcR) for antigen, on the majority of T cells, is a disulfide-linked heterodimer composed of the alpha and beta chains, noncovalently associated with the CD3 complex of polypeptides (gamma, delta, epsilon and zeta).	Disulfides	72-81	T cell receptor alpha variable 6-3	Mus musculus	4-19
20835491-0	2010	The application of negative ion electrospray mass spectrometry for the sequencing of underivatized disulfide-containing proteins: insulin and lysozyme.	Disulfides	99-108	insulin	Bos taurus	130-137
21073997-3	2010	Hepcidin contains eight cysteine residues that form four disulfide bridges, which stabilize a hairpin-shaped structure with two beta sheets.	Disulfides	57-66	hepcidin antimicrobial peptide	Homo sapiens	0-8
20729124-7	2010	Because the position 1307 serves as part of the Cys1307-Cys1320 disulfide bond of the fibrillin-1, the p.C1307Y substitution results in loss of the intramolecular disulfide bond.	Disulfides	64-73	fibrillin 1	Homo sapiens	86-97
20729124-7	2010	Because the position 1307 serves as part of the Cys1307-Cys1320 disulfide bond of the fibrillin-1, the p.C1307Y substitution results in loss of the intramolecular disulfide bond.	Disulfides	163-172	fibrillin 1	Homo sapiens	86-97
2532601-1	1989	The T cell receptor (TcR) for antigen, on the majority of T cells, is a disulfide-linked heterodimer composed of the alpha and beta chains, noncovalently associated with the CD3 complex of polypeptides (gamma, delta, epsilon and zeta).	Disulfides	72-81	T cell receptor alpha variable 6-3	Mus musculus	21-24
20724473-4	2010	Using the purified HA I-domain locked by disulfide bonds for immunization, we developed an mAb, 2E8, that specifically binds to cells expressing the HA LFA-1.	Disulfides	41-50	integrin alpha L	Mus musculus	152-157
2600138-4	1989	Like FN itself, the cDNA-encoded polypeptides (deminectins [DNs]) containing the V120 or V95 segment are efficiently secreted as disulfide-bonded homodimers.	Disulfides	129-138	fibronectin 1	Rattus norvegicus	5-7
20214493-5	2010	Proteins destined to the intermembrane space are trapped by a disulfide relay mechanism that involves an electron cascade from the incoming substrate to Mia40, then on to Erv1, and finally to molecular oxygen via cytochrome c.	Disulfides	62-71	growth factor, augmenter of liver regeneration	Homo sapiens	171-175
2690076-1	1989	Epidermal growth factor (EGF) is a small protein containing 53 amino acids and three disulfide bonds.	Disulfides	85-94	epidermal growth factor	Mus musculus	25-28
2605244-1	1989	Thiol-disulfide exchange reactions between myosin and 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB) lead to the formation of 5-thio-2-nitrobenzoic acid (TNB)-mixed disulfides as well as to protein disulfide bonds.	Disulfides	6-15	myosin heavy chain 14	Homo sapiens	43-49
20435060-3	2010	The anti-oxidative effect of Trx 1 is mediated by the dithiol-disulfide exchange in the active site.	Disulfides	62-71	thioredoxin	Homo sapiens	29-34
2605244-1	1989	Thiol-disulfide exchange reactions between myosin and 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB) lead to the formation of 5-thio-2-nitrobenzoic acid (TNB)-mixed disulfides as well as to protein disulfide bonds.	Disulfides	161-171	myosin heavy chain 14	Homo sapiens	43-49
2605244-1	1989	Thiol-disulfide exchange reactions between myosin and 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB) lead to the formation of 5-thio-2-nitrobenzoic acid (TNB)-mixed disulfides as well as to protein disulfide bonds.	Disulfides	161-170	myosin heavy chain 14	Homo sapiens	43-49
2553722-7	1989	The 46-kDa and larger forms of unreduced plasma LACI are associated with apolipoprotein A-II (apoA-II) in mixed disulfide linkages.	Disulfides	112-121	apolipoprotein A2	Homo sapiens	73-92
20635096-7	2010	Unlike all other matrix metalloproteinases investigated so far, NtMMP1 contains a disulfide bond within its propeptide thus rendering the proenzyme catalytically active.	Disulfides	82-91	metalloendoproteinase 2-MMP-like	Nicotiana tabacum	64-70
2553722-7	1989	The 46-kDa and larger forms of unreduced plasma LACI are associated with apolipoprotein A-II (apoA-II) in mixed disulfide linkages.	Disulfides	112-121	apolipoprotein A2	Homo sapiens	94-101
2692595-3	1989	Peptide mapping demonstrated that the two disulfide pairs in bovine somatotropin dimer were identical to those in monomer.	Disulfides	42-51	somatotropin	Bos taurus	68-80
20572021-5	2010	The disulfide pairing in the chemically synthesized SD1 was forced into predetermined topologies: SD1A (Cys20-Cys26, Cys32-Cys38) or SD1B (Cys20-Cys32, Cys26-Cys38).	Disulfides	4-13	CUP2Q35	Homo sapiens	52-55
2692595-6	1989	Since the single cleaved peptide bond is present in the large disulfide loop of bovine somatotropin, these data demonstrate that the dimeric molecule exists as a novel concatenated structure through the interlocking of the disulfide loops of this protein.	Disulfides	62-71	somatotropin	Bos taurus	87-99
2692595-6	1989	Since the single cleaved peptide bond is present in the large disulfide loop of bovine somatotropin, these data demonstrate that the dimeric molecule exists as a novel concatenated structure through the interlocking of the disulfide loops of this protein.	Disulfides	223-232	somatotropin	Bos taurus	87-99
2783142-0	1989	Calcium regulates folding and disulfide-bond formation in alpha-lactalbumin.	Disulfides	30-39	lactalbumin alpha	Bos taurus	58-75
20616115-5	2010	Bi- and tribodies were made using the disulfide-stabilized Fab fragment as a heterodimerization scaffold with PH1 single-chain variable fragments fused to either one or both Fab-chain C-termini.	Disulfides	38-47	FA complementation group B	Homo sapiens	59-62
20616115-5	2010	Bi- and tribodies were made using the disulfide-stabilized Fab fragment as a heterodimerization scaffold with PH1 single-chain variable fragments fused to either one or both Fab-chain C-termini.	Disulfides	38-47	alanine--glyoxylate and serine--pyruvate aminotransferase	Homo sapiens	110-113
2783142-1	1989	Refolding and disulfide bond formation in reduced denatured bovine alpha-lactalbumin is shown to be Ca2+-dependent.	Disulfides	14-23	lactalbumin alpha	Bos taurus	67-84
2670497-8	1989	In all cases mentioned, IL-5 was found to be glycosylated, and its biological activity was dependent on a 40- to 50-kD homodimer configuration, linked together by disulfide bridges.	Disulfides	163-172	interleukin 5	Mus musculus	24-28
20735812-8	2010	All molecules were initially poorly secreted from eukaryotic cells, but replacement of unfavourable amino acids in the V regions improved secretion, as did the introduction of a disulfide bridge between the TCR C domains and the removal of an unpaired cysteine.	Disulfides	178-187	T cell receptor alpha variable 6-3	Mus musculus	207-210
20735812-10	2010	Molecules that included the complete heterodimeric TCR, with a stabilizing disulfide bridge, were correctly folded as they bound TCR-specific antibodies (Abs) and detected pMHC on cells after specific peptide loading.	Disulfides	75-84	T cell receptor alpha variable 6-3	Mus musculus	51-54
20735812-10	2010	Molecules that included the complete heterodimeric TCR, with a stabilizing disulfide bridge, were correctly folded as they bound TCR-specific antibodies (Abs) and detected pMHC on cells after specific peptide loading.	Disulfides	75-84	T cell receptor alpha variable 6-3	Mus musculus	129-132
2668279-2	1989	PDI catalyzes the reduction of protein disulfide bonds in the presence of excess reduced glutathione and has been implicated in the reductive degradation of insulin; E. coli thioredoxin is homologous to two regions in PDI and can also degrade insulin.	Disulfides	39-48	protein-disulfide isomerase	Escherichia coli	218-221
20696932-4	2010	Our results suggest that, during the redox reaction, Cys43 in a luminal loop of human VKOR forms a transient disulfide bond with a thioredoxin (Trx)-like protein located in the lumen of the endoplasmic reticulum (ER).	Disulfides	109-118	vitamin K epoxide reductase complex subunit 1	Homo sapiens	86-90
20696932-4	2010	Our results suggest that, during the redox reaction, Cys43 in a luminal loop of human VKOR forms a transient disulfide bond with a thioredoxin (Trx)-like protein located in the lumen of the endoplasmic reticulum (ER).	Disulfides	109-118	thioredoxin	Homo sapiens	144-147
20696932-5	2010	We screened for redox partners of VKOR among the large number of mammalian Trx-like ER proteins by testing a panel of these candidates for their ability to form this specific disulfide bond with human VKOR.	Disulfides	175-184	vitamin K epoxide reductase complex subunit 1	Homo sapiens	34-38
20696932-5	2010	We screened for redox partners of VKOR among the large number of mammalian Trx-like ER proteins by testing a panel of these candidates for their ability to form this specific disulfide bond with human VKOR.	Disulfides	175-184	thioredoxin	Homo sapiens	75-78
20696932-5	2010	We screened for redox partners of VKOR among the large number of mammalian Trx-like ER proteins by testing a panel of these candidates for their ability to form this specific disulfide bond with human VKOR.	Disulfides	175-184	vitamin K epoxide reductase complex subunit 1	Homo sapiens	201-205
20538586-5	2010	During reperfusion, AR-SOH was converted to a mixed disulfide (AR-SSG).	Disulfides	52-61	aldo-keto reductase family 1, member B3 (aldose reductase)	Mus musculus	20-22
20399532-6	2010	Redox titrations demonstrated that the four conserved cysteines of each CP12 isoform could form two internal disulfide bridges with different midpoint redox potentials (E(m,7.9) -326 mV and -350 mV in both CP12-1 and CP12-2; E(m,7.9) -332 mV and -373 mV in CP12-3).	Disulfides	109-118	CP12 domain-containing protein 2	Arabidopsis thaliana	72-76
2528460-2	1989	After reduction of the interchange disulfide bonds of these fragments by dithiothreitol, a thiol-disulfide interchain reagent, 5,5"-dithiobis-2-nitrobenzoic acid, was added to convert the free SH groups of one of the Fab" fragments to mixed disulfide derivatives.	Disulfides	97-106	FA complementation group B	Homo sapiens	217-220
20399532-6	2010	Redox titrations demonstrated that the four conserved cysteines of each CP12 isoform could form two internal disulfide bridges with different midpoint redox potentials (E(m,7.9) -326 mV and -350 mV in both CP12-1 and CP12-2; E(m,7.9) -332 mV and -373 mV in CP12-3).	Disulfides	109-118	CP12 domain-containing protein 2	Arabidopsis thaliana	206-210
20399532-6	2010	Redox titrations demonstrated that the four conserved cysteines of each CP12 isoform could form two internal disulfide bridges with different midpoint redox potentials (E(m,7.9) -326 mV and -350 mV in both CP12-1 and CP12-2; E(m,7.9) -332 mV and -373 mV in CP12-3).	Disulfides	109-118	CP12 domain-containing protein 2	Arabidopsis thaliana	206-210
20538591-4	2010	According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond.	Disulfides	377-386	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	169-174
2528460-2	1989	After reduction of the interchange disulfide bonds of these fragments by dithiothreitol, a thiol-disulfide interchain reagent, 5,5"-dithiobis-2-nitrobenzoic acid, was added to convert the free SH groups of one of the Fab" fragments to mixed disulfide derivatives.	Disulfides	97-106	FA complementation group B	Homo sapiens	217-220
2519114-1	1989	Evidence for an interchain disulfide bond in nitrate reductase.	Disulfides	27-36	nitrate reductase [NADH] 1	Zea mays	45-62
20593814-2	2010	Head-to-tail interchain disulfide bonds link subunits within the homodimer of both the short, cytokine-like, form of ALR (sfALR), and a longer form (lfALR) which resides in the mitochondrial intermembrane space (IMS).	Disulfides	24-33	growth factor, augmenter of liver regeneration	Homo sapiens	117-120
20593814-14	2010	However, the mutation adversely affects the stability of both ALR forms: e.g., by decreasing the melting temperature by about 10 degrees C, by increasing the rate of dissociation of FAD from the holoenzyme by about 45-fold, and by strongly enhancing the susceptibility of sfALR to partial proteolysis and to reduction of its intersubunit disulfide bridges by glutathione.	Disulfides	338-347	growth factor, augmenter of liver regeneration	Homo sapiens	62-65
20507993-5	2010	Upon oxidative folding of equimolar amounts of the alpha1, alpha2, and alpha3 chains of NC2, a stable heterotrimer with a disulfide bridge between alpha1 and alpha3 chains is formed.	Disulfides	122-131	adrenoceptor alpha 1D	Homo sapiens	147-164
2473918-2	1989	Thus localization of disulfide and thiol groups is a key to understanding the conformation and orientation of myelin proteolipid protein (PLP) in the myelin membrane.	Disulfides	21-30	proteolipid protein 1	Bos taurus	110-136
20615204-2	2010	This novel in vivo cleavable disulfide linker, based on a dithiocyclopeptide containing a thrombin-sensitive sequence and an intramolecular disulfide bond, was inserted between transferrin and granulocyte colony-stimulating factor (G-CSF) recombinant fusion protein domains.	Disulfides	29-38	colony stimulating factor 3	Homo sapiens	193-230
20615204-2	2010	This novel in vivo cleavable disulfide linker, based on a dithiocyclopeptide containing a thrombin-sensitive sequence and an intramolecular disulfide bond, was inserted between transferrin and granulocyte colony-stimulating factor (G-CSF) recombinant fusion protein domains.	Disulfides	29-38	colony stimulating factor 3	Homo sapiens	232-237
20615204-2	2010	This novel in vivo cleavable disulfide linker, based on a dithiocyclopeptide containing a thrombin-sensitive sequence and an intramolecular disulfide bond, was inserted between transferrin and granulocyte colony-stimulating factor (G-CSF) recombinant fusion protein domains.	Disulfides	140-149	colony stimulating factor 3	Homo sapiens	193-230
2473918-2	1989	Thus localization of disulfide and thiol groups is a key to understanding the conformation and orientation of myelin proteolipid protein (PLP) in the myelin membrane.	Disulfides	21-30	proteolipid protein 1	Bos taurus	138-141
2544589-0	1989	Heparin binding domain of human antithrombin III inferred from the sequential reduction of its three disulfide linkages.	Disulfides	101-110	serpin family C member 1	Homo sapiens	32-48
2472117-0	1989	Disulfide structures of human interleukin-6 are similar to those of human granulocyte colony stimulating factor.	Disulfides	0-9	colony stimulating factor 3	Homo sapiens	74-111
2669972-1	1989	Thioredoxin contains a single disulfide bond that can be reduced without perturbing significantly the structure of the enzyme.	Disulfides	30-39	thioredoxin	Homo sapiens	0-11
20347046-9	2010	In another example the protein disulfide isomerase ERdj5 binds specifically to EDEM (which is probably a mannosidase) and a lectin OS9, and reduces the disulfide bonds of bound glycoproteins destined for ERAD.	Disulfides	31-40	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	51-56
2669972-3	1989	We have experimentally tested the expected linkage relationship between disulfide bond formation and protein stability for thioredoxin.	Disulfides	72-81	thioredoxin	Homo sapiens	123-134
2669972-5	1989	Using glutathione as a reference species, we have measured the equilibrium constant for forming the disulfide bond (effective concentration) in thioredoxin as a function of urea concentration.	Disulfides	100-109	thioredoxin	Homo sapiens	144-155
20491447-13	2010	The intra chain disulfide bonds in the Fab region of IgG1kappa were also less susceptible than disulfide bonds in the Fab region of IgG1lambda.	Disulfides	16-25	FA complementation group B	Homo sapiens	39-42
2669972-7	1989	Comparison of the values obtained for disulfide bond formation in the folded and unfolded states with the free energies for unfolding oxidized and reduced thioredoxin using circular dichroism confirms the expected linkage relationship.	Disulfides	38-47	thioredoxin	Homo sapiens	155-166
20491447-13	2010	The intra chain disulfide bonds in the Fab region of IgG1kappa were also less susceptible than disulfide bonds in the Fab region of IgG1lambda.	Disulfides	95-104	FA complementation group B	Homo sapiens	39-42
20491447-13	2010	The intra chain disulfide bonds in the Fab region of IgG1kappa were also less susceptible than disulfide bonds in the Fab region of IgG1lambda.	Disulfides	95-104	FA complementation group B	Homo sapiens	118-121
20534461-8	2010	We demonstrate that inclusion of an extra disulfide bond between the constant domains of the introduced TCR markedly reduced neoreactivity, whereas enhanced effectiveness of the introduced TCR was observed.	Disulfides	42-51	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	104-107
2722836-0	1989	Structure and activity dependence of recombinant human insulin-like growth factor II on disulfide bond pairing.	Disulfides	88-97	insulin like growth factor 2	Homo sapiens	55-84
20534461-8	2010	We demonstrate that inclusion of an extra disulfide bond between the constant domains of the introduced TCR markedly reduced neoreactivity, whereas enhanced effectiveness of the introduced TCR was observed.	Disulfides	42-51	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	189-192
20354169-1	2010	The von Willebrand factor (VWF) A2 crystal structure has revealed the presence of a rare vicinal disulfide bond between C1669 and C1670, predicted to influence domain unfolding required for proteolysis by ADAMTS13.	Disulfides	97-106	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	205-213
19967419-6	2010	To increase the in vivo stability of the KLK3-stimulating peptide B-2, we made differently cyclized analogues by replacing both terminal cysteines and the disulfide bridge between them.	Disulfides	155-164	kallikrein related peptidase 3	Homo sapiens	41-45
20361855-7	2010	Reversible oxidation of thiols in serine threonine protein phosphatase PP2A and in protein tyrosin phosphatases SHP1, SHP2 and CD45 leads to their inactivation generally by formation of intramolecular disulfides.	Disulfides	201-211	protein phosphatase 2 phosphatase activator	Homo sapiens	71-75
20479109-4	2010	Using cysteine cross-linking, we biochemically screened over 300 cysteine pairs in the KCNQ1-KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain.	Disulfides	184-193	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	87-92
20479109-4	2010	Using cysteine cross-linking, we biochemically screened over 300 cysteine pairs in the KCNQ1-KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain.	Disulfides	184-193	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	140-145
20458450-3	2010	In the present study, a kinetic trapping approach was used to capture the disulfide cross-linking intermediate between gp120 and PDI.	Disulfides	74-83	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	119-132
20458450-5	2010	The active site mutant PDIs were able to covalently cross-link with gp120 through a mixed disulfide bond in vitro.	Disulfides	90-99	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	68-73
20225272-4	2010	Both proteins were multi-subunit oligomers, but subunits of Hsp27(WT) were disulfide-linked unlike those of Hsp27(C137A), which were monomeric.	Disulfides	75-84	heat shock protein family B (small) member 1	Homo sapiens	60-65
20459719-9	2010	Additionally, the disulfide bond formation protein A (DsbA) was firstly identified as a selenoprotein in the ancient chordates of Ciona intestinalis, Ciona savignyi and Branchiostoma floridae, while selenoprotein DsbAs had only been found in bacteria and green algae before.	Disulfides	18-27	disulfide bond formation protein A	Ciona intestinalis	54-58
20385746-2	2010	From the extents of disulfide cross-linking in channels on the cell surface between cysteine (Cys) substituted for residues in the first turns in the membrane of the S0 transmembrane (TM) helix, unique to BK alpha, and of the voltage-sensing domain TM helices S1-S4, we infer that S0 is next to S3 and S4, but not to S1 and S2.	Disulfides	20-29	FCF1 rRNA-processing protein	Homo sapiens	205-213
20156289-4	2010	To identify peptides that specifically interact with DR5, a disulfide-constrained phage display peptide library was screened for binders towards this receptor.	Disulfides	60-69	TNF receptor superfamily member 10b	Homo sapiens	53-56
2722836-1	1989	The complete peptide map of purified folded recombinant human insulin-like growth factor II (rhIGF-II) was determined to verify its sequence and disulfide bonding scheme.	Disulfides	145-154	insulin like growth factor 2	Homo sapiens	62-91
2673306-0	1989	Structure of the pig pancreatic GP-2: role of intramolecular disulfides in the resistance to proteolysis.	Disulfides	61-71	glycoprotein 2	Sus scrofa	32-36
2673306-7	1989	It was also shown that GP-2 only becomes sensitive to proteolytic digestion when its disulfide bonds are reduced, and that DTT does not activate the protease.	Disulfides	85-94	glycoprotein 2	Sus scrofa	23-27
2673306-8	1989	Seven intramolecular disulfide bonds were identified on GP-2.	Disulfides	21-30	glycoprotein 2	Sus scrofa	56-60
2540173-6	1989	These findings are most consistent with a model for glucose-6-phosphatase of a single polypeptide or a disulfide-linked dimer which spans the endoplasmic reticulum with the various activities of this multifunctional enzyme residing in distinct protein domains.	Disulfides	103-112	glucose-6-phosphatase catalytic subunit 1	Rattus norvegicus	52-73
2539974-10	1989	This study demonstrates that 1) pancreatic acinar cells rapidly internalize [125I]secretin; 2) internalization of secretin does not enhance cAMP production; and 3) disulfide linkages are important for secretin receptor activity.	Disulfides	164-173	secretin receptor	Homo sapiens	201-218
2495940-1	1989	Isolated uncoupling protein (UCP) can be cross-linked, by various disulfide-forming reagents, to dimers.	Disulfides	66-75	uncoupling protein 1	Homo sapiens	29-32
2495940-5	1989	In mitochondria, cross-linking of UCP with disulfide-forming agents is even more efficient than in isolated state.	Disulfides	43-52	uncoupling protein 1	Homo sapiens	34-37
2467292-14	1989	The proposed model of cytotactin specifies the orientation of the polypeptides, the localization of interchain disulfide bonds, the structural elements constituting the thin and thick segments (EGFL repeats and type III repeats, respectively), the terminal fibrinogen-like nodular region, and the relative location of the cell-binding region.	Disulfides	111-120	tenascin C	Gallus gallus	22-32
2784209-6	1989	Thus, the disulfide-linked form of TcR-1 (BB3+ clones) was associated with the expression of J segments upstream to the C gamma 1 gene segment, whereas the nondisulfide-linked form (delta-TCS1+ clones) was associated with the expression of J segments upstream to C gamma 2. delta-TCS1+ clones, in most instances, exhibited a growth pattern different from that of BB3+ or conventional TcR alpha/beta+ clones as they adhered promptly to surfaces, spread, and emitted long filopodia ending with adhesion plaques.	Disulfides	10-19	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	35-38
2469470-6	1989	The interchain disulfide bond present in the human alpha 2M carboxyl-terminal 20-kDa fragment was conserved in bovine alpha 2M and rat alpha 1I3, but not in rat alpha 1M.	Disulfides	15-24	alpha-2-macroglobulin	Homo sapiens	51-59
2521487-9	1989	Evidence was obtained that neuromodulin isolated from cytosolic extract exists as a mixture of molecular forms and that the Ca2+-binding S100 protein-beta discriminates among the different neuromodulin isoforms in forming covalent complexes via disulfide bridges; this discrimination may be explained by analogous differences observed between the NH2-terminal amino acid sequences of p57 and F1.	Disulfides	245-254	growth associated protein 43	Bos taurus	27-39
2463792-0	1989	Disulfide and secondary structures of recombinant human granulocyte colony stimulating factor.	Disulfides	0-9	colony stimulating factor 3	Homo sapiens	56-93
2558637-5	1989	Altogether the results indicated that Cys402, probably by participating in a disulfide bridge, is essential for (i) the CD4-binding ability of env gene products and for (ii) the physical stability of gp 120.	Disulfides	77-86	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	200-206
2497743-0	1989	Role of disulfides in biological activity and conformational stability of pig kidney diamine oxidase: evidence for two disulfide states.	Disulfides	8-18	amine oxidase copper containing 1	Sus scrofa	85-100
2497743-0	1989	Role of disulfides in biological activity and conformational stability of pig kidney diamine oxidase: evidence for two disulfide states.	Disulfides	8-17	amine oxidase copper containing 1	Sus scrofa	85-100
2497743-1	1989	Six disulfides are found to be present in pig kidney diamine oxidase and all of these are available to reducing agents under nondenaturating conditions.	Disulfides	4-14	amine oxidase copper containing 1	Sus scrofa	53-68
2521314-9	1989	The BB3-reactive TCR molecules were represented by C gamma 1-encoded disulfide-linked heterodimers, whereas delta-TCS-1 reacted with C gamma 2-encoded nondisulfide-linked molecules.	Disulfides	69-78	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	17-20
2784109-7	1989	G1 mAb reacted with 5 clones, that were also stained by the previously described BB3 mAb (recognizing the disulfide-linked form of TcR gamma/delta).	Disulfides	106-115	T cell receptor alpha variable 6-3	Mus musculus	131-134
20375792-5	2010	RESULTS: The LAT1 was significantly up-regulated in various human epithelial ovarian cancers that was localized predominantly on their plasma membrane and in the plasma membrane of the ovarian cancer cell line in conjunction with 4F2hc via disulfide bonds.	Disulfides	240-249	solute carrier family 7 member 5	Homo sapiens	13-17
20375792-5	2010	RESULTS: The LAT1 was significantly up-regulated in various human epithelial ovarian cancers that was localized predominantly on their plasma membrane and in the plasma membrane of the ovarian cancer cell line in conjunction with 4F2hc via disulfide bonds.	Disulfides	240-249	solute carrier family 3 member 2	Homo sapiens	230-235
3144280-2	1988	Fast atom bombardment mass spectrometric analysis of the untreated molecule produced an ion consistent with a structure involving an intramolecular disulfide bond between Cys(1) and Cys(3).	Disulfides	148-157	cystin 1	Homo sapiens	171-177
20108326-4	2010	Extraction of Spetex-1 from spermatozoa by SDS or urea required dithiothreitol, suggesting crosslinking by disulfide bond is involved in the assembly of satellite fibrils containing Spetex-1.	Disulfides	107-116	spermatogenesis associated 18	Homo sapiens	14-22
2901412-6	1988	Three previously mapped transport-deficient alleles of the LDL receptor were traced to the cysteine-rich repeats of the protein, suggesting that the generation of non-disulfide-bonded (free) cysteines might cause the block in transport.	Disulfides	167-176	low density lipoprotein receptor	Homo sapiens	59-71
20089850-2	2010	Structural integrity of individual ectodomain modules in these receptors depends on calcium, and we showed before that the LDL receptor folds its modules late after synthesis via intermediates with abundant non-native disulfide bonds and structure.	Disulfides	218-227	low density lipoprotein receptor	Homo sapiens	123-135
20152808-0	2010	An antiviral disulfide compound blocks interaction between arenavirus Z protein and cellular promyelocytic leukemia protein.	Disulfides	13-22	transmembrane BAX inhibitor motif containing 4	Homo sapiens	70-79
20152808-0	2010	An antiviral disulfide compound blocks interaction between arenavirus Z protein and cellular promyelocytic leukemia protein.	Disulfides	13-22	PML nuclear body scaffold	Homo sapiens	93-123
3409984-3	1988	The present paper reports the conformational destabilization by the mixed disulfide formation in calf alpha- and gamma-II crystallin.	Disulfides	74-83	G protein subunit gamma 7	Bos taurus	102-121
20152808-3	2010	In a previous report, we have shown that the disulfide compound NSC20625 has antiviral and virucidal properties against arenaviruses, inducing unfolding and oligomerization of Z without affecting cellular RING-containing proteins such as the PML.	Disulfides	45-54	PML nuclear body scaffold	Homo sapiens	242-245
20152808-4	2010	Here, we further studied the effect of the zinc-finger-reactive disulfide NSC20625 on PML-Z interaction.	Disulfides	64-73	PML nuclear body scaffold	Homo sapiens	86-89
3166978-7	1988	Deacylation of TF with hydroxylamine resulted in the spontaneous generation of disulfide-linked TF dimers.	Disulfides	79-88	coagulation factor III, tissue factor	Homo sapiens	96-98
3166978-8	1988	This result suggests that the disulfide-linked TF dimer, a minor component of most TF preparations, and the recently described heterodimeric form of TF are artifacts produced by deacylation of Cys245 and subsequent interchain disulfide bond formation.	Disulfides	30-39	coagulation factor III, tissue factor	Homo sapiens	47-49
19882737-5	2010	Although transiently silencing PDI in NS0/2N2 cells suggests that PDI is involved in disulfide bond formation of this subclass of antibody, our results show that PDI does not control the overall IgG4 productivity.	Disulfides	85-94	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	66-69
19882737-5	2010	Although transiently silencing PDI in NS0/2N2 cells suggests that PDI is involved in disulfide bond formation of this subclass of antibody, our results show that PDI does not control the overall IgG4 productivity.	Disulfides	85-94	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	66-69
3166978-8	1988	This result suggests that the disulfide-linked TF dimer, a minor component of most TF preparations, and the recently described heterodimeric form of TF are artifacts produced by deacylation of Cys245 and subsequent interchain disulfide bond formation.	Disulfides	30-39	coagulation factor III, tissue factor	Homo sapiens	83-85
3166978-8	1988	This result suggests that the disulfide-linked TF dimer, a minor component of most TF preparations, and the recently described heterodimeric form of TF are artifacts produced by deacylation of Cys245 and subsequent interchain disulfide bond formation.	Disulfides	30-39	coagulation factor III, tissue factor	Homo sapiens	83-85
3166978-8	1988	This result suggests that the disulfide-linked TF dimer, a minor component of most TF preparations, and the recently described heterodimeric form of TF are artifacts produced by deacylation of Cys245 and subsequent interchain disulfide bond formation.	Disulfides	226-235	coagulation factor III, tissue factor	Homo sapiens	47-49
2454080-5	1988	Reduction of hEGF with dithiothreitol decreased its reactivity with these MAbs, suggesting that they recognized the conformation of the hEGF molecule maintained by the three disulfide bonds.	Disulfides	174-183	epidermal growth factor	Homo sapiens	13-17
20188670-0	2010	Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione.	Disulfides	14-23	growth factor, augmenter of liver regeneration	Homo sapiens	86-90
20022943-0	2010	Enhanced formation of disulfide-bridged dimer (Fab-PE38)2 utilizing repeats of the Fab binding domain of protein G. Fab-PE38 used in this study is B3(Fab)-ext-PE38, and it is an antibody toxin that is made by fusing the Pseudomonas exotoxin to the Fab domain of B3 antibody.	Disulfides	22-31	FA complementation group B	Homo sapiens	47-50
2454080-5	1988	Reduction of hEGF with dithiothreitol decreased its reactivity with these MAbs, suggesting that they recognized the conformation of the hEGF molecule maintained by the three disulfide bonds.	Disulfides	174-183	epidermal growth factor	Homo sapiens	136-140
20022943-0	2010	Enhanced formation of disulfide-bridged dimer (Fab-PE38)2 utilizing repeats of the Fab binding domain of protein G. Fab-PE38 used in this study is B3(Fab)-ext-PE38, and it is an antibody toxin that is made by fusing the Pseudomonas exotoxin to the Fab domain of B3 antibody.	Disulfides	22-31	FA complementation group B	Homo sapiens	83-86
20022943-0	2010	Enhanced formation of disulfide-bridged dimer (Fab-PE38)2 utilizing repeats of the Fab binding domain of protein G. Fab-PE38 used in this study is B3(Fab)-ext-PE38, and it is an antibody toxin that is made by fusing the Pseudomonas exotoxin to the Fab domain of B3 antibody.	Disulfides	22-31	FA complementation group B	Homo sapiens	83-86
20022943-0	2010	Enhanced formation of disulfide-bridged dimer (Fab-PE38)2 utilizing repeats of the Fab binding domain of protein G. Fab-PE38 used in this study is B3(Fab)-ext-PE38, and it is an antibody toxin that is made by fusing the Pseudomonas exotoxin to the Fab domain of B3 antibody.	Disulfides	22-31	FA complementation group B	Homo sapiens	83-86
20022943-0	2010	Enhanced formation of disulfide-bridged dimer (Fab-PE38)2 utilizing repeats of the Fab binding domain of protein G. Fab-PE38 used in this study is B3(Fab)-ext-PE38, and it is an antibody toxin that is made by fusing the Pseudomonas exotoxin to the Fab domain of B3 antibody.	Disulfides	22-31	FA complementation group B	Homo sapiens	83-86
20022943-2	2010	B3(Fab)-ext-PE38 has a cysteine residue on the ext sequence, and (B3(Fab)-ext-PE38)(2) is the disulfide-bridged dimer of the B3(Fab)-ext-PE38 monomer.	Disulfides	94-103	FA complementation group B	Homo sapiens	69-72
20022943-2	2010	B3(Fab)-ext-PE38 has a cysteine residue on the ext sequence, and (B3(Fab)-ext-PE38)(2) is the disulfide-bridged dimer of the B3(Fab)-ext-PE38 monomer.	Disulfides	94-103	FA complementation group B	Homo sapiens	69-72
3355556-1	1988	Porcine C5a anaphylatoxin, the primary structure of which was first determined by Gerard and Hugli in 1980 as a 74-amino acid peptide having three intramolecular disulfide bonds, was synthesized by the solution procedure applying our maximum protection strategy.	Disulfides	162-171	complement C5	Homo sapiens	8-25
20027620-3	2010	The experimental results show that there are two anodic peaks for the oxidative damage of bovine insulin, which arise from the oxidation of the exposed disulfide bond S--S(CYS7A,CYS7B), forming sulfenic acid RSOH (1.20 V, vs. SCE), sulfinic acid RSO(2)H and sulfonic acid RSO(3)H (1.35 V, vs. SCE).	Disulfides	152-161	insulin	Bos taurus	97-104
19902913-6	2010	To determine disulfide linked sites, DBond takes into account fragmentation patterns of disulfide linked peptides in nucleoside diphosphate kinase (NDPK) as a model protein, considering fragment ions including cysteine, cysteine thioaldehyde (-2 Da, C(T)), cysteine persulfide (+32 Da, C(S)) and dehydroalanine (-34 Da, C(Delta)).	Disulfides	13-22	cytidine/uridine monophosphate kinase 2	Homo sapiens	148-152
2971791-9	1988	In affinity-labeling studies, [125I]MSA/rIGF-I labeled a complex of Mr greater than 300,000 (unreduced) and of Mr 140,000 (reduced), consistent with a type I somatomedin receptor composed of disulfide-linked subunits.	Disulfides	191-200	insulin-like growth factor 1	Rattus norvegicus	40-46
20419425-2	2010	The newly synthesised precursors are trapped in the IMS by a disulfide relay mechanism that involves introduction of disulfides from the sulfhydryl oxidase Erv1 to the redox-regulated import receptor Mia40 and then on to the substrate.	Disulfides	61-70	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	156-160
20419425-2	2010	The newly synthesised precursors are trapped in the IMS by a disulfide relay mechanism that involves introduction of disulfides from the sulfhydryl oxidase Erv1 to the redox-regulated import receptor Mia40 and then on to the substrate.	Disulfides	117-127	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	156-160
2971791-9	1988	In affinity-labeling studies, [125I]MSA/rIGF-I labeled a complex of Mr greater than 300,000 (unreduced) and of Mr 140,000 (reduced), consistent with a type I somatomedin receptor composed of disulfide-linked subunits.	Disulfides	191-200	insulin-like growth factor 1	Rattus norvegicus	158-169
19878651-3	2009	IL-4 disulfides were in vitro reduced by thioredoxin 1 (Trx1) and protein disulfide isomerase (PDI).	Disulfides	5-15	thioredoxin	Homo sapiens	41-54
19878651-3	2009	IL-4 disulfides were in vitro reduced by thioredoxin 1 (Trx1) and protein disulfide isomerase (PDI).	Disulfides	5-15	thioredoxin	Homo sapiens	56-60
3426230-10	1987	HCII differs from antithrombin III, which contains an essential disulfide bond for heparin-dependent thrombin inhibition (Longas, M. O., et al.	Disulfides	64-73	serpin family C member 1	Homo sapiens	18-34
19878651-4	2009	Reduction of IL-4 disulfides by the cell surface of HeLa cells was inhibited by auranofin, an inhibitor of thioredoxin reductase that is an electron donor to both Trx1 and PDI.	Disulfides	18-28	thioredoxin	Homo sapiens	163-167
19878651-5	2009	Both Trx1 and PDI have been shown to be located at the cell surface and our data suggests that these enzymes are involved in catalyzing reduction of IL-4 disulfides.	Disulfides	154-164	thioredoxin	Homo sapiens	5-9
2961572-4	1987	At the cell surface, the T-ALL cells of patient DD expressed a CD3-associated disulfide-linked dimer, which contained the TcR gamma protein.	Disulfides	78-87	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	122-125
19908864-3	2009	FTR reduces an intramolecular disulfide bridge of Trx, and Trx reduction involves a transient cross-link with FTR.	Disulfides	30-39	thioredoxin	Homo sapiens	50-53
3427041-10	1987	Therefore, a plausible disulfide bond pattern can now be proposed for both the asialoglycoprotein receptors and the C-terminal domain of the proteoglycan core protein.	Disulfides	23-32	decorin	Homo sapiens	141-166
19801666-5	2009	The results show that an oxidized sulfiredoxin under disulfide state is formed between the catalytic Cys(84) and Cys(48).	Disulfides	53-62	sulfiredoxin	Saccharomyces cerevisiae S288C	34-46
2892525-1	1987	A new family of asymmetric thiol-disulfide exchange reagents, the dinitrophenyl alkyl disulfides (DNPSSR), was used to modify rat liver phenylalanine hydroxylase.	Disulfides	33-42	phenylalanine hydroxylase	Rattus norvegicus	136-161
3654616-0	1987	Formation of a covalent disulfide-linked antithrombin-albumin complex by an antithrombin variant, antithrombin "Northwick Park".	Disulfides	24-33	serpin family C member 1	Homo sapiens	41-53
19919128-3	2009	This restriction of myofibril swelling, caused largely by disulfide cross-linkages formed between oxidized myosin tails, was positioned on the transversely expansible thick filaments, reflecting a significant role and susceptibility of intra- as well as intermyofilamental structures.	Disulfides	58-67	myosin heavy chain 14	Homo sapiens	107-113
19463935-4	2009	We show that 1) cysteinylated beta-CN formed mainly dimers bridged by disulfide bonds; 2) the process of dimerization adds to the micellization process with temperature and is poorly reversible; 3) covalent disulfide linkage forms at the air-water interface at a lower temperature than in bulk.	Disulfides	70-79	casein beta	Homo sapiens	30-37
3654616-0	1987	Formation of a covalent disulfide-linked antithrombin-albumin complex by an antithrombin variant, antithrombin "Northwick Park".	Disulfides	24-33	serpin family C member 1	Homo sapiens	76-88
19463935-4	2009	We show that 1) cysteinylated beta-CN formed mainly dimers bridged by disulfide bonds; 2) the process of dimerization adds to the micellization process with temperature and is poorly reversible; 3) covalent disulfide linkage forms at the air-water interface at a lower temperature than in bulk.	Disulfides	207-216	casein beta	Homo sapiens	30-37
3654616-0	1987	Formation of a covalent disulfide-linked antithrombin-albumin complex by an antithrombin variant, antithrombin "Northwick Park".	Disulfides	24-33	serpin family C member 1	Homo sapiens	76-88
19875047-7	2009	The utility of this class of ligands was further demonstrated by the radiolabelling of a cyclic peptide that is known to target the serine protease receptor uPAR; essentially quantitative incorporation of (99m)Tc occurred exclusively at the SAAC site, despite the presence of a His residue, and without disruption of the disulfide bond.	Disulfides	321-330	plasminogen activator, urokinase receptor	Homo sapiens	157-161
3654616-6	1987	In this communication, we present evidence that this Mr approximately 120,000 variant component is comprised of an antithrombin-albumin covalent disulfide-linked complex.	Disulfides	145-154	serpin family C member 1	Homo sapiens	115-127
3115973-0	1987	Location of disulfide bonds within the sequence of human serum cholinesterase.	Disulfides	12-21	butyrylcholinesterase	Homo sapiens	63-77
19649253-4	2009	Interestingly, only NH(2)-terminal truncated TCTP, unlike full-length TCTP, forms dimers through intermolecular disulfide bonds.	Disulfides	112-121	tumor protein, translationally-controlled 1	Homo sapiens	45-49
3115973-1	1987	Human serum cholinesterase was digested with pepsin under conditions which left disulfide bonds intact.	Disulfides	80-89	butyrylcholinesterase	Homo sapiens	12-26
3115973-9	1987	A peptide containing the interchain disulfide is readily cleaved from cholinesterase by trypsin (Lockridge, O., and La Du, B. N. (1982) J. Biol.	Disulfides	36-45	butyrylcholinesterase	Homo sapiens	70-84
3115973-12	1987	The disulfide bridges in human cholinesterase have exactly the same location as in Torpedo californica acetylcholinesterase.	Disulfides	4-13	butyrylcholinesterase	Homo sapiens	31-45
3312247-8	1987	By promoting the formation of disulfide bonds, hydrogen peroxide also stabilizes the glucocorticoid receptor-hsp90 complex and prevents receptor transformation.	Disulfides	30-39	heat shock protein 90 alpha family class A member 1	Homo sapiens	109-114
19584915-8	2009	All the newly discovered PRL2 sequences possess three conserved disulfide linkages with the exception of the shark PRL2 which has only two.	Disulfides	64-73	protein tyrosine phosphatase 4A2	Homo sapiens	25-29
19308325-1	2009	Periostin, also called osteoblast-specific factor 2 (OSF-2), is a member of the fasciclin family and a disulfide-linked cell adhesion protein that has been shown to be expressed preferentially in the periosteum and periodontal ligaments, where it acts as a critical regulator of bone and tooth formation and maintenance.	Disulfides	103-112	periostin	Homo sapiens	0-9
19308325-1	2009	Periostin, also called osteoblast-specific factor 2 (OSF-2), is a member of the fasciclin family and a disulfide-linked cell adhesion protein that has been shown to be expressed preferentially in the periosteum and periodontal ligaments, where it acts as a critical regulator of bone and tooth formation and maintenance.	Disulfides	103-112	periostin	Homo sapiens	23-51
2442250-5	1987	Immunoprecipitation studies indicate that the target antigen of CD27 antibodies is a polypeptide of 55 kDa, which appears in the form of a disulfide-linked homodimer on the T lymphocyte membrane (Tp55).	Disulfides	139-148	CD27 molecule	Homo sapiens	64-68
19308325-1	2009	Periostin, also called osteoblast-specific factor 2 (OSF-2), is a member of the fasciclin family and a disulfide-linked cell adhesion protein that has been shown to be expressed preferentially in the periosteum and periodontal ligaments, where it acts as a critical regulator of bone and tooth formation and maintenance.	Disulfides	103-112	periostin	Homo sapiens	53-58
19420245-9	2009	Deletion of disulfide loop Cys(309)-Cys(336) of NgR1 selectively increases its affinity for Nogo-66 and OMgp.	Disulfides	12-21	oligodendrocyte myelin glycoprotein	Homo sapiens	104-108
2956146-1	1987	Antigen-specific, major histocompatibility complex-restricted recognition by classical T cells is mediated by a T cell receptor (TCR) consisting of a disulfide-linked alpha beta heterodimer.	Disulfides	150-159	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	112-127
19409522-0	2009	The mitochondrial disulfide relay system protein GFER is mutated in autosomal-recessive myopathy with cataract and combined respiratory-chain deficiency.	Disulfides	18-27	growth factor, augmenter of liver regeneration	Homo sapiens	49-53
2956146-1	1987	Antigen-specific, major histocompatibility complex-restricted recognition by classical T cells is mediated by a T cell receptor (TCR) consisting of a disulfide-linked alpha beta heterodimer.	Disulfides	150-159	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	129-132
3110143-11	1987	Identification of this critical lysine for heparin binding strongly supports previous data which indicate that the heparin-binding domain of antithrombin is located at the NH2 terminus within one of the disulfide cross-linked loops of the protein.	Disulfides	203-212	serpin family C member 1	Homo sapiens	141-153
19204006-6	2009	Although SEL1L-C is in monomeric form, SEL1L-B is engaged in intramolecular/intermolecular disulfide bonds.	Disulfides	91-100	SEL1L adaptor subunit of ERAD E3 ubiquitin ligase	Homo sapiens	39-44
2438695-13	1987	This gamma-chain TCR is disulfide linked and has a molecular mass of 80 kDa under nonreducing conditions.	Disulfides	24-33	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	17-20
19383476-0	2009	Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils.	Disulfides	45-54	insulin	Bos taurus	7-14
19383476-2	2009	Insulin is a 51-residue polypeptide hormone, with its two polypeptide chains linked by one intrachain and two interchain disulfide bonds, and has long been known to self-assemble in vitro into amyloid fibrils.	Disulfides	121-130	insulin	Bos taurus	0-7
19285555-1	2009	Fibronectin (FN) matrix fibrils have long been thought to be formed by disulfide-bonded FN multimers, although there is no direct evidence that they are covalently linked with each other.	Disulfides	71-80	fibronectin 1	Mus musculus	0-11
3593416-9	1987	However, incubation of the microsomal fraction from menadione-treated hepatocytes with purified glutathione reductase in the presence of NADPH also resulted in the reduction of a significant portion of the glutathione-protein mixed disulfides present in this fraction.	Disulfides	232-242	glutathione-disulfide reductase	Rattus norvegicus	96-117
19285555-1	2009	Fibronectin (FN) matrix fibrils have long been thought to be formed by disulfide-bonded FN multimers, although there is no direct evidence that they are covalently linked with each other.	Disulfides	71-80	fibronectin 1	Mus musculus	13-15
19285555-1	2009	Fibronectin (FN) matrix fibrils have long been thought to be formed by disulfide-bonded FN multimers, although there is no direct evidence that they are covalently linked with each other.	Disulfides	71-80	fibronectin 1	Mus musculus	88-90
3593416-10	1987	Our results suggest that the formation of glutathione-protein mixed disulfides occurs as a result of increased GSSG formation and inhibition of glutathione reductase activity during menadione metabolism in hepatocytes.	Disulfides	68-78	glutathione-disulfide reductase	Rattus norvegicus	144-165
3612817-1	1987	The unidirectional crosslinking agent N-succinimidyl 3-(2-pyridyldithio)propionate (SPDP) was used to covalently couple fibrin-specific antibody Fab" to low-molecular-weight urokinase by means of the sulfhydryl groups of the inter-heavy-chain disulfide bonds.	Disulfides	243-252	FA complementation group B	Homo sapiens	145-148
18427801-3	2009	We have previously shown that replacement of two conserved residues, K68 and F291, by cysteine residues leads to disulfide cross-linking between neighbouring P2X(1) subunits.	Disulfides	113-122	purinergic receptor P2X, ligand gated ion channel, 1 L homeolog	Xenopus laevis	158-164
19435051-6	2009	Afterwards, 5"-thiolated oligodeoxynucleotide-probes were immobilized onto these thiol-terminated poly(NIPA) layers on the surface by disulfide bond formation.	Disulfides	134-143	zinc finger C3HC-type containing 1	Homo sapiens	103-107
3327411-1	1987	Ricin A chain, a potent ribosomal poison, was disulfide linked either to the iron transport protein, transferrin, or to anti-transferrin receptor antibodies to produce highly specific derivative toxins, Tf-A and TfR-A, respectively.	Disulfides	46-55	coagulation factor III, tissue factor	Homo sapiens	203-207
3759951-0	1986	Thiol/disulfide redox equilibrium and kinetic behavior of chicken liver fatty acid synthase.	Disulfides	6-15	fatty acid synthase	Gallus gallus	72-91
19170536-5	2009	Its structure is quite similar to that of mu-KIIIA, indicating that the Cys1-Cys9 disulfide bond could be removed without any significant distortion of the alpha-helix bearing the key residues.	Disulfides	82-91	cystin 1	Homo sapiens	72-76
3759951-1	1986	Chicken liver fatty acid synthase is rapidly inactivated and cross-linked at pH 7.2 and 8.0 by incubation with low concentrations of common biological disulfides including glutathione disulfide, coenzyme A disulfide, and glutathione-coenzyme A-mixed disulfide.	Disulfides	151-161	fatty acid synthase	Gallus gallus	14-33
3759951-1	1986	Chicken liver fatty acid synthase is rapidly inactivated and cross-linked at pH 7.2 and 8.0 by incubation with low concentrations of common biological disulfides including glutathione disulfide, coenzyme A disulfide, and glutathione-coenzyme A-mixed disulfide.	Disulfides	151-160	fatty acid synthase	Gallus gallus	14-33
19048311-0	2009	A disulfide linked model of the complement protein C8gamma complexed with C8alpha indel peptide.	Disulfides	2-11	complement C8 alpha chain	Homo sapiens	74-81
3759951-1	1986	Chicken liver fatty acid synthase is rapidly inactivated and cross-linked at pH 7.2 and 8.0 by incubation with low concentrations of common biological disulfides including glutathione disulfide, coenzyme A disulfide, and glutathione-coenzyme A-mixed disulfide.	Disulfides	184-193	fatty acid synthase	Gallus gallus	14-33
19048311-2	2009	Computer modeling and molecular dynamics simulations were performed in order to check the hypothesis that the residues Ala164 of C8alpha and Ala40 of C8gamma occupied the right position if cysteine residues were in their place for disulfide bonding.	Disulfides	231-240	complement C8 alpha chain	Homo sapiens	129-136
3463991-0	1986	Thioredoxin-catalyzed refolding of disulfide-containing proteins.	Disulfides	35-44	thioredoxin	Homo sapiens	0-11
3463991-1	1986	Thioredoxin, a known catalyst for reducing protein disulfides, was shown to catalyze efficiently the refolding of pancreatic RNase either from the reduced, denatured form or from the scrambled form containing oxidized but incorrectly paired disulfides.	Disulfides	51-61	thioredoxin	Homo sapiens	0-11
3463991-1	1986	Thioredoxin, a known catalyst for reducing protein disulfides, was shown to catalyze efficiently the refolding of pancreatic RNase either from the reduced, denatured form or from the scrambled form containing oxidized but incorrectly paired disulfides.	Disulfides	241-251	thioredoxin	Homo sapiens	0-11
19212810-1	2009	Under stressed conditions such as prolonged exposure to high pH, the C-terminal disulfide bridge in bovine somatotropin (bST) is susceptible to a base catalyzed beta-elimination reaction.	Disulfides	80-89	somatotropin	Bos taurus	107-119
3463991-2	1986	Thioredoxin was 1000-fold more efficient on a molar basis than the model dithiol, dithiothreitol, in reactivating reduced, denatured RNase, suggesting that thioredoxin acts as an efficient catalyst for disulfide interchange.	Disulfides	202-211	thioredoxin	Homo sapiens	0-11
3463991-2	1986	Thioredoxin was 1000-fold more efficient on a molar basis than the model dithiol, dithiothreitol, in reactivating reduced, denatured RNase, suggesting that thioredoxin acts as an efficient catalyst for disulfide interchange.	Disulfides	202-211	thioredoxin	Homo sapiens	156-167
3463991-5	1986	Thioredoxin was most effective in reactivating inactive scrambled RNase, which contained mispaired disulfides, showing a t1/2 of 2 hr.	Disulfides	99-109	thioredoxin	Homo sapiens	0-11
18555370-1	1986	Purified rat liver phenylalanine hydroxylase [L-phenylalanine:tetrahydropteridine:oxygen oxidoreductase (4-hydroxylating), EC 1.14.16.1] was immobilized with activated thiol-Sepharose 4B via disulfide bond formation, which is expected to immobilize the enzyme in its activated form through the SH modification.	Disulfides	191-200	phenylalanine hydroxylase	Rattus norvegicus	19-44
19131515-0	2009	Location of KCNE1 relative to KCNQ1 in the I(KS) potassium channel by disulfide cross-linking of substituted cysteines.	Disulfides	70-79	potassium voltage-gated channel subfamily E member 1	Cricetulus griseus	12-17
3081579-3	1986	The immunotoxins studied were T cell-specific monoclonal anti-T11 antibodies conjugated by disulfide linkage to ribosome-inactivating toxins.	Disulfides	91-100	CD2 molecule	Homo sapiens	62-65
19028676-9	2009	In contrast, when cysteine residues involved in disulfide bond formation were mutated to serines, ANGPTL4 retained its activity.	Disulfides	48-57	angiopoietin like 4	Homo sapiens	98-105
19121228-9	2009	WhiB1 has a C37XXC40 motif thus a C40S mutation renders C37 to exist as a free thiol to form a hetero-disulfide bond with the cysteine residue of substrate protein.	Disulfides	102-111	transcriptional regulator WhiB1	Mycobacterium tuberculosis H37Rv	0-5
19121228-14	2009	WhiB1, a thioredoxin like protein interacts with GlgB and transfers its electrons to the disulfide thus reduces the intra-molecular disulfide bond of GlgB.	Disulfides	89-98	transcriptional regulator WhiB1	Mycobacterium tuberculosis H37Rv	0-5
19121228-14	2009	WhiB1, a thioredoxin like protein interacts with GlgB and transfers its electrons to the disulfide thus reduces the intra-molecular disulfide bond of GlgB.	Disulfides	132-141	transcriptional regulator WhiB1	Mycobacterium tuberculosis H37Rv	0-5
3944096-15	1986	Preincubation of the enzyme with disulfide compounds prevented the enzyme from inactivation by iodoacetamide but inhibited the thioltransferase activity in the absence of iodoacetamide.	Disulfides	33-42	glutaredoxin-1	Bos taurus	127-143
19225211-1	2009	Disulfide-bond-A oxidoreductase-like protein (DsbA-L) has been suggested to take part in the disulfide bond formation progress of proteins, including insulin and adiponectin.	Disulfides	93-102	glutathione S-transferase kappa 1	Mus musculus	46-52
3944096-16	1986	The results suggest that the active center of thioltransferase is cysteine dependent and that substrates may form mixed disulfides with the enzyme.	Disulfides	120-130	glutaredoxin-1	Bos taurus	46-62
3944096-17	1986	Based on the iodoacetamide inactivation and disulfide protection of thioltransferase activity, a model for the catalytic mechanism of the thiol-disulfide oxidoreduction is proposed.	Disulfides	44-53	glutaredoxin-1	Bos taurus	68-84
19120451-4	2009	Antibody recognition of NTPDase3 is greatly attenuated by denaturation with SDS, and abolished by reducing agents, indicating the significance of the native conformation and the disulfide bonds for epitope recognition.	Disulfides	178-187	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	24-32
3944096-17	1986	Based on the iodoacetamide inactivation and disulfide protection of thioltransferase activity, a model for the catalytic mechanism of the thiol-disulfide oxidoreduction is proposed.	Disulfides	144-153	glutaredoxin-1	Bos taurus	68-84
3554822-5	1986	Two other highly conserved structures, the disulfide bridges of the C-1 and C-2 domains, appear by this methodology to function in both intracellular processing and immune recognition.	Disulfides	43-52	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	68-71
18980249-0	2008	Cell size increased in tissues from transgenic mice overexpressing a cell surface growth-related and cancer-specific hydroquinone oxidase, tNOX, with protein disulfide-thiol interchange activity.	Disulfides	158-167	ecto-NOX disulfide-thiol exchanger 2	Mus musculus	139-143
18980249-1	2008	tNOX (ENOX2), a cancer-specific and growth-related cell surface protein with protein disulfide-thiol interchange and hydroquinone (NADH) oxidase activities was overexpressed in a transgenic mouse model.	Disulfides	85-94	ecto-NOX disulfide-thiol exchanger 2	Mus musculus	0-4
18980249-1	2008	tNOX (ENOX2), a cancer-specific and growth-related cell surface protein with protein disulfide-thiol interchange and hydroquinone (NADH) oxidase activities was overexpressed in a transgenic mouse model.	Disulfides	85-94	ecto-NOX disulfide-thiol exchanger 2	Mus musculus	6-11
3899711-0	1985	Nonspecific reaction of a thiol: protein disulfide oxidoreductase with the disulfide bonds of insulin.	Disulfides	41-50	insulin	Bos taurus	94-101
19018669-8	2008	This shows that the Cys228-Cys239 disulfide bond of gp120 is required for high-affinity binding to CD4.	Disulfides	34-43	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	52-57
18842719-6	2008	Here, we provide evidence that A26 forms a disulfide-bonded complex with A27 that is anchored to the MV through a noncovalent interaction with the A17 transmembrane protein.	Disulfides	43-52	immunoglobulin kappa variable 6-21 (non-functional)	Homo sapiens	31-34
2997060-1	1985	Human insulin-like growth factor II (IGF-II) with 67 amino acids and three disulfide bridges has been synthesized by the solid-phase method.	Disulfides	75-84	insulin like growth factor 2	Homo sapiens	6-43
18975914-2	2008	We had shown earlier that recombinant human resistin has a tendency to form aggregates by formation of inter/intramolecular disulfide linkages and that it undergoes a concentration-dependent conformational change in secondary structure from alpha-helical to beta-sheet form.	Disulfides	124-133	resistin	Homo sapiens	44-52
2992476-6	1985	These results indicate that the ANF receptor, having a Mr of 130,000 - 140,000, is composed of disulfide-linked subunits and the ANF-binding site is located on the 70-kDa component.	Disulfides	95-104	natriuretic peptide A	Bos taurus	32-35
18725202-3	2008	HB-EGF immunoreactive proteins with M(r) of 6.5, 21 and 24 kDa were observed from lysates of HB-EGF and each HB-EGF disulfide analogue.	Disulfides	116-125	heparin-binding EGF-like growth factor	Mus musculus	0-6
18725202-6	2008	Each HB-EGF disulfide analogue lacked the ability to stimulate tyrosine phosphorylation of the 170 kDa EGFR.	Disulfides	12-21	heparin-binding EGF-like growth factor	Mus musculus	5-11
18852299-6	2008	The ternary complex represents a transient and intermediate step in the oxidation of intermembrane space precursors, where the oxidase Erv1 promotes disulfide transfer to the precursor while both oxidase and precursor are associated with the disulfide carrier Mia40.	Disulfides	149-158	growth factor, augmenter of liver regeneration	Homo sapiens	135-139
3928592-2	1985	The conjugate was prepared by a novel and convenient procedure devised to couple an amino group of CL to thiol groups of bovine serum albumin (BSA) introduced by thiol exchange reduction of its disulfide bonds with dithiothreitol, using N-(m-maleimidobenzoyloxy)succinimide (MBS) as a cross-linker.	Disulfides	194-203	LOC100136344	Oncorhynchus mykiss	128-141
18852299-6	2008	The ternary complex represents a transient and intermediate step in the oxidation of intermembrane space precursors, where the oxidase Erv1 promotes disulfide transfer to the precursor while both oxidase and precursor are associated with the disulfide carrier Mia40.	Disulfides	242-251	growth factor, augmenter of liver regeneration	Homo sapiens	135-139
18693759-0	2008	A second disulfide bridge from the N-terminal domain to extracellular loop 2 dampens receptor activity in GPR39.	Disulfides	9-18	G protein-coupled receptor 39	Homo sapiens	106-111
18693759-7	2008	We conclude that the second disulfide bridge, which according to the beta2-adrenergic structure will form a covalent link across the entrance to the main ligand binding pocket, serves to dampen GPR39 activation.	Disulfides	28-37	G protein-coupled receptor 39	Homo sapiens	194-199
3884009-1	1985	Human insulin-like growth factor II with 67 amino acid residues and three disulfide bridges has been synthesized by the solid-phase method.	Disulfides	74-83	insulin like growth factor 2	Homo sapiens	6-35
18489898-0	2008	The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins.	Disulfides	89-98	peroxiredoxin 5	Homo sapiens	50-65
4096891-1	1985	The molecular basis of the high reactivity toward reducing agents of intersubunit disulfides at positions 31 and 32 of dimeric bovine seminal ribonuclease was investigated by studying in the monomeric enzyme the fast reaction kinetics with disulfides of the adjacent cysteine-31 and -32, exposed by selective reduction of the intersubunit disulfides.	Disulfides	82-92	seminal ribonuclease	Bos taurus	134-154
18544535-5	2008	Similar findings were obtained when the TNFR1- and TNFR2-transfected cells were pretreated with a cell-impermeable oxidase, DsbA, that catalyzes disulfide bond formation between thiol groups on cysteine residues.	Disulfides	145-154	TNF receptor superfamily member 1A	Homo sapiens	40-45
4096891-1	1985	The molecular basis of the high reactivity toward reducing agents of intersubunit disulfides at positions 31 and 32 of dimeric bovine seminal ribonuclease was investigated by studying in the monomeric enzyme the fast reaction kinetics with disulfides of the adjacent cysteine-31 and -32, exposed by selective reduction of the intersubunit disulfides.	Disulfides	240-250	seminal ribonuclease	Bos taurus	134-154
4096891-1	1985	The molecular basis of the high reactivity toward reducing agents of intersubunit disulfides at positions 31 and 32 of dimeric bovine seminal ribonuclease was investigated by studying in the monomeric enzyme the fast reaction kinetics with disulfides of the adjacent cysteine-31 and -32, exposed by selective reduction of the intersubunit disulfides.	Disulfides	240-250	seminal ribonuclease	Bos taurus	134-154
4096891-5	1985	The data indicate that the superreactivity of intersubunit disulfides of seminal ribonuclease is matched by the high reactivity at neutral pH of adjacent cysteine residues 31 and 32, as compared to all small thiol compounds tested.	Disulfides	59-69	seminal ribonuclease	Bos taurus	73-93
18557934-7	2008	The corresponding peptides, purified after cleavage from thioredoxin, were properly folded and contained the expected four-disulfide bridges without the need of any renaturation or oxidation steps.	Disulfides	123-132	thioredoxin	Homo sapiens	57-68
6094938-12	1984	Reduction of the disulfide bridge of ANF inactivates the peptide.	Disulfides	17-26	natriuretic peptide A	Bos taurus	37-40
18624400-4	2008	This review examines the usefulness of a disulfide proteome technique for the analysis of thioredoxin-dependent redox regulation as well as for use in allergen studies.	Disulfides	41-50	thioredoxin	Homo sapiens	90-101
18550799-4	2008	In vitro experiments with OOC-5, a torsinA homolog from Caenorhabditis elegans, demonstrate that redox changes that reduce this disulfide bond affect the binding of ATP and ADP and cause an attendant local conformational change detected by limited proteolysis.	Disulfides	128-137	torsin family 1 member A	Homo sapiens	35-42
6437445-6	1984	The complex was thus unlike those of thrombin and alpha 2-macroglobulin or antithrombin III, but it had characteristics of a disulfide-linked complex.	Disulfides	125-134	alpha-2-macroglobulin	Homo sapiens	50-71
6438823-2	1984	Limited reduction of disulfide bonds in this complex by NADPH, thioredoxin reductase and thioredoxin leads to partial disaggregation of the multimeric VIII:vWF with concomitant loss of its platelet agglutinating activity in the presence of ristocetin, and with dissociation of factor VIII:C from the complex.	Disulfides	21-30	peroxiredoxin 5	Homo sapiens	63-84
18452709-4	2008	We further identified MsrB2- or MsrB3-Trx complexes formed through intermolecular disulfide bonds involving catalytic residue of Trx.	Disulfides	82-91	thioredoxin	Homo sapiens	38-41
18452709-4	2008	We further identified MsrB2- or MsrB3-Trx complexes formed through intermolecular disulfide bonds involving catalytic residue of Trx.	Disulfides	82-91	thioredoxin	Homo sapiens	129-132
6438823-2	1984	Limited reduction of disulfide bonds in this complex by NADPH, thioredoxin reductase and thioredoxin leads to partial disaggregation of the multimeric VIII:vWF with concomitant loss of its platelet agglutinating activity in the presence of ristocetin, and with dissociation of factor VIII:C from the complex.	Disulfides	21-30	thioredoxin	Homo sapiens	63-74
18502910-7	2008	Hydrogen peroxide induced an array of changes in the myocardium, including formation of disulfide bonds that were intermolecular for Prdx1, Prdx2, and Prdx3 but intramolecular within Prdx5.	Disulfides	88-97	peroxiredoxin 1	Rattus norvegicus	133-138
16663773-3	1984	The activation induced by dithiothreitol was reversed by diamide, an oxidant of vicinal dithiols, suggesting that the redox state of disulfide bonds of the enzyme may be important in the expression of the maximal catalytic activity.Titration of thiol groups before and after activation of maize phosphoenolpyruvate carboxylase by dithiothreitol shows an increase of the accessible groups from 8 to 12 suggesting that the reduction of two disulfide bonds accompanied the activation.	Disulfides	133-142	MLO-like protein 4	Zea mays	295-326
18502910-7	2008	Hydrogen peroxide induced an array of changes in the myocardium, including formation of disulfide bonds that were intermolecular for Prdx1, Prdx2, and Prdx3 but intramolecular within Prdx5.	Disulfides	88-97	peroxiredoxin 2	Rattus norvegicus	140-145
18502910-7	2008	Hydrogen peroxide induced an array of changes in the myocardium, including formation of disulfide bonds that were intermolecular for Prdx1, Prdx2, and Prdx3 but intramolecular within Prdx5.	Disulfides	88-97	peroxiredoxin 3	Rattus norvegicus	151-156
18502910-8	2008	For Prdx1, Prdx2, and Prdx5, disulfide bond formation can be approximated to an EC(50) of 10-100, 1-10, and 100-1,000 microM peroxide, respectively.	Disulfides	29-38	peroxiredoxin 1	Rattus norvegicus	4-9
18502910-8	2008	For Prdx1, Prdx2, and Prdx5, disulfide bond formation can be approximated to an EC(50) of 10-100, 1-10, and 100-1,000 microM peroxide, respectively.	Disulfides	29-38	peroxiredoxin 2	Rattus norvegicus	11-16
16663773-3	1984	The activation induced by dithiothreitol was reversed by diamide, an oxidant of vicinal dithiols, suggesting that the redox state of disulfide bonds of the enzyme may be important in the expression of the maximal catalytic activity.Titration of thiol groups before and after activation of maize phosphoenolpyruvate carboxylase by dithiothreitol shows an increase of the accessible groups from 8 to 12 suggesting that the reduction of two disulfide bonds accompanied the activation.	Disulfides	438-447	MLO-like protein 4	Zea mays	295-326
18445134-4	2008	Here we identified constitutively active mutation sites at the cytoplasmic borders of helices II and IV of mGluR8 and successfully inhibited the G protein activation ability by engineering disulfide cross-linking between these cytoplasmic regions.	Disulfides	189-198	glutamate receptor, metabotropic 8	Mus musculus	107-113
16663773-5	1984	It is concluded that the mechanism of phosphoenolpyruvate carboxylase activation by dithiothreitol involves the net reduction of two disulfide bonds in the enzyme.	Disulfides	133-142	MLO-like protein 4	Zea mays	38-69
6089874-1	1984	Human alpha (leukocyte) interferons contain two disulfide bonds between Cys-1 and Cys-98 and between Cys-29 and Cys-138.	Disulfides	48-57	cystin 1	Homo sapiens	72-77
6207102-4	1984	The shared determinants appear to be associated with the disulphide-bonded cysteines in the first and third constant domains of the IgG molecule and the 9-112 disulfide bond of Thy 1.	Disulfides	159-168	Thy-1 cell surface antigen	Homo sapiens	177-182
18587263-1	2008	CD98, a disulfide-linked 125-kDa heterodimeric type II transmembrane glycoprotein, regulates beta1 integrin- mediated cell adhesion.	Disulfides	8-17	solute carrier family 3 member 2	Homo sapiens	0-4
18514596-7	2008	Under reduced circumstances (induced by mercaptoethanol, a component of the denaturating solution) the disulfide bonds connecting IgA heavy and light chains are broken up and chains can be detected as separate peaks during electrophoresis.	Disulfides	103-112	immunoglobulin heavy variable 4-38-2-like	Homo sapiens	130-133
6232337-0	1984	The Fab fragment of a directly activating monoclonal antibody that precipitates a disulfide-linked heterodimer from a helper T cell clone blocks activation by either allogeneic Ia or antigen and self-Ia.	Disulfides	82-91	FA complementation group B	Homo sapiens	4-7
6370035-9	1984	The principles of the method are illustrated by applying the graphical analysis to the two site protein, thioredoxin reductase, which contains an oxidation-reduction active site disulfide in addition to FAD.	Disulfides	178-187	peroxiredoxin 5	Homo sapiens	105-126
18447393-6	2008	Our data suggest that the alkylation of the essential thiol(s) of Trx2 has profound impact on the mitochondrial redox circuitry and that such effects are distinct from the responses to agents causing reversible disulfide bond formation between the vicinal dithiols in the active center.	Disulfides	211-220	thioredoxin 2	Homo sapiens	66-70
18440555-2	2008	C8 contains three genetically distinct subunits (C8 alpha, C8 beta, C8 gamma) arranged as a disulfide-linked C8 alpha-gamma dimer that is noncovalently associated with C8 beta.	Disulfides	92-101	complement C8 alpha chain	Homo sapiens	109-117
18440555-8	2008	In the present study, we determined the crystal structure of the human C8 alpha MACPF domain disulfide-linked to C8 gamma (alphaMACPF-gamma) at 2.15 A resolution.	Disulfides	93-102	complement C8 alpha chain	Homo sapiens	71-79
6361025-7	1983	Two specific insulin-binding species are observed after velocity sedimentation in linear sucrose density gradients: peak II whose protein molecular weight (Mp) is 180,000 +/- 45,000 and its disulfide-linked dimer, peak I (Mp, 355,000 +/- 65,000).	Disulfides	190-199	insulin	Meleagris gallopavo	13-20
18343813-1	2008	The ligand binding module five (LA5) of the low density lipoprotein receptor is a small, single-domain protein of 40 residues and three disulfide bonds with a calcium binding motif that is essential for its structure and function.	Disulfides	136-145	low density lipoprotein receptor	Homo sapiens	44-76
6310598-1	1983	The conformationally restricted, cyclic, disulfide-containing, enkephalin analogs [2-D-penicillamine, 5-L-penicillamine]enkephalin [(D-Pen2,L-Pen5]enkephalin) and [2-D-penicillamine, 5-D-penicillamine]enkephalin [(D-Pen2,D-Pen5]enkephalin) were synthesized by solid-phase methods.	Disulfides	41-50	proenkephalin	Rattus norvegicus	63-73
18396871-4	2008	The PEG-SS-P[Asp(DET)] micelles showed both a 1-3 orders of magnitude higher gene transfection efficiency and a more rapid onset of gene expression than PEG-P[Asp(DET)] micelles without disulfide linkages, due to much more effective endosomal escape based on the PEG detachment in endosome.	Disulfides	186-195	progestagen associated endometrial protein	Homo sapiens	4-7
6310598-1	1983	The conformationally restricted, cyclic, disulfide-containing, enkephalin analogs [2-D-penicillamine, 5-L-penicillamine]enkephalin [(D-Pen2,L-Pen5]enkephalin) and [2-D-penicillamine, 5-D-penicillamine]enkephalin [(D-Pen2,D-Pen5]enkephalin) were synthesized by solid-phase methods.	Disulfides	41-50	proenkephalin	Rattus norvegicus	120-130
18294274-6	2008	These mAb immunoprecipitated 35- and 90-kDa proteins under reducing conditions in extracts prepared from human HeLa tumor cells, indicating the existence of intermolecular disulfide bonds between cysteine residues in the 90-kDa hc and 35-kDa lc (LAT1).	Disulfides	172-181	solute carrier family 7 member 5	Homo sapiens	246-250
6310598-1	1983	The conformationally restricted, cyclic, disulfide-containing, enkephalin analogs [2-D-penicillamine, 5-L-penicillamine]enkephalin [(D-Pen2,L-Pen5]enkephalin) and [2-D-penicillamine, 5-D-penicillamine]enkephalin [(D-Pen2,D-Pen5]enkephalin) were synthesized by solid-phase methods.	Disulfides	41-50	proenkephalin	Rattus norvegicus	120-130
18508598-3	2008	These domains belong to the Ly-6/uPAR (LU) protein domain family, which is defined by a consensus sequence predominantly based on disulfide connectivities, and they adopt a characteristic three-finger fold.	Disulfides	130-139	plasminogen activator, urokinase receptor	Homo sapiens	33-37
6310598-1	1983	The conformationally restricted, cyclic, disulfide-containing, enkephalin analogs [2-D-penicillamine, 5-L-penicillamine]enkephalin [(D-Pen2,L-Pen5]enkephalin) and [2-D-penicillamine, 5-D-penicillamine]enkephalin [(D-Pen2,D-Pen5]enkephalin) were synthesized by solid-phase methods.	Disulfides	41-50	proenkephalin	Rattus norvegicus	120-130
6310598-1	1983	The conformationally restricted, cyclic, disulfide-containing, enkephalin analogs [2-D-penicillamine, 5-L-penicillamine]enkephalin [(D-Pen2,L-Pen5]enkephalin) and [2-D-penicillamine, 5-D-penicillamine]enkephalin [(D-Pen2,D-Pen5]enkephalin) were synthesized by solid-phase methods.	Disulfides	41-50	proenkephalin	Rattus norvegicus	120-130
6824689-7	1983	On the basis of present results it is suggested that ornithine decarboxylase may be reversibly inactivated through microsome-catalyzed formation of mixed or enzyme-enzyme disulfides and that NADPH plays a crucial role in ornithine decarboxylase reactivation, probably by cytosolic reductase(s).	Disulfides	171-181	ornithine decarboxylase 1	Rattus norvegicus	53-76
18382651-6	2008	The redox active disulfide/dithiol motif in the N-terminal domain of TrxR had to be maintained for manifestation of SecTRAP cytotoxicity.	Disulfides	17-26	peroxiredoxin 5	Homo sapiens	69-73
18331844-2	2008	Oxidoreductases of the thioredoxin fold superfamily catalyze steps in oxidative protein folding via protein-protein interactions and covalent catalysis to act as chaperones and isomerases of disulfides to generate a native fold.	Disulfides	191-201	thioredoxin	Homo sapiens	23-34
6761143-2	1982	Recycling of the disulfide of thioredoxin subunit to its dithiol form was made by thioredoxin reductase.	Disulfides	17-26	thioredoxin	Homo sapiens	30-41
18055186-4	2008	Fab" fragments were then immobilized onto these surfaces via a thiol-disulfide interchange reaction and the reactivity of antibodies with antigens was investigated.	Disulfides	69-78	FA complementation group B	Homo sapiens	0-3
18274674-10	2008	We propose that reduced PDI activates TF by isomerization of a mixed disulfide and a free thiol to an intramolecular disulfide.	Disulfides	69-78	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	24-27
6761143-2	1982	Recycling of the disulfide of thioredoxin subunit to its dithiol form was made by thioredoxin reductase.	Disulfides	17-26	peroxiredoxin 5	Homo sapiens	82-103
18274674-10	2008	We propose that reduced PDI activates TF by isomerization of a mixed disulfide and a free thiol to an intramolecular disulfide.	Disulfides	117-126	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	24-27
6282878-2	1982	The binding of thiol, thiolate, thioether, and disulfide sulfur donor ligands to ferric cytochrome P-450-CAM and myoglobin has been investigated by UV-visible absorption, magnetic circular dichroism (MCD), and EPR spectroscopy.	Disulfides	47-56	myoglobin	Homo sapiens	88-122
18589824-1	2008	We study the techniques of synthesis of disulfide bond-bearing cyclopeptides FIK.	Disulfides	40-49	ZFP90 zinc finger protein	Homo sapiens	77-80
6284211-11	1982	These results indicate that the glucagon receptor is an oligomer probably composed of at least two different subunits that are linked together or greatly stabilized by disulfide bonds.	Disulfides	168-177	glucagon receptor	Rattus norvegicus	32-49
18174165-3	2008	Treatment of mouse brain synaptosomes with H2O2, diamide, and sodium nitroprusside caused aggregation of CaMKII through formation of disulfide and non-disulfide linkages, and partial inhibition of the kinase activity.	Disulfides	133-142	calcium/calmodulin-dependent protein kinase II gamma	Mus musculus	105-111
18174165-3	2008	Treatment of mouse brain synaptosomes with H2O2, diamide, and sodium nitroprusside caused aggregation of CaMKII through formation of disulfide and non-disulfide linkages, and partial inhibition of the kinase activity.	Disulfides	151-160	calcium/calmodulin-dependent protein kinase II gamma	Mus musculus	105-111
6802116-2	1982	Apo A-II contains two identical polypeptide chains linked by a disulfide bond.	Disulfides	63-72	apolipoprotein A2	Homo sapiens	0-8
18237164-0	2008	Mechanism of thioredoxin-catalyzed disulfide reduction.	Disulfides	35-44	thioredoxin	Homo sapiens	13-24
6950391-1	1981	Thioredoxin and glutaredoxin may be important in regulating cell metabolism by mediating interchanges between sulfhydryl and disulfide groups.	Disulfides	125-134	thioredoxin	Homo sapiens	0-11
17692377-2	2008	It contains three genetically distinct subunits; C8alpha and C8gamma form a disulfide-linked C8alpha-gamma heterodimer that is noncovalently associated with C8beta.	Disulfides	76-85	complement C8 alpha chain	Homo sapiens	49-56
17692377-2	2008	It contains three genetically distinct subunits; C8alpha and C8gamma form a disulfide-linked C8alpha-gamma heterodimer that is noncovalently associated with C8beta.	Disulfides	76-85	complement C8 alpha chain	Homo sapiens	93-100
17692377-11	2008	The validity of the structure is supported by the spatial arrangement of C8alpha Ala 164 in the peptide and C8gamma Ala 40, which are within disulfide-bonding distance of each other.	Disulfides	141-150	complement C8 alpha chain	Homo sapiens	73-80
6950391-8	1981	The HeLa enzyme has low species and substrate specificity and can reduce HeLa PI and PIII, E. coli thioredoxin and glutaredoxin, and the disulfide bond in 5,5"-dithiobis(2-nitrobenzoic acid).	Disulfides	137-146	thioredoxin	Homo sapiens	99-110
6950410-2	1981	The functionally C3b-like glycoprotein of cobra venom was linked to a murine monoclonal Ab directed to a human melanoma-associated antigen by a disulfide bond, by using a heterobifunctional crosslinking reagent.	Disulfides	144-153	ankyrin repeat domain 36B	Homo sapiens	111-138
6947213-2	1981	Shortly after synthesis and glycosylation, Pr80env is cleaved into two species, gp70 and Pr15E, that are found associated, perhaps through disulfide bonds, in infected cells.	Disulfides	139-148	embigin	Mus musculus	80-84
18070921-8	2008	Iron affects the sulfhydryl status of Yap5, which is indicative of the generation of intramolecular disulfide bonds.	Disulfides	100-109	Yap5p	Saccharomyces cerevisiae S288C	38-42
7250117-5	1981	In the presence of gamma-glutamyltransferase inhibitor, the synthesis of intracellular GSH was accompanied by an accumulation of extracellular cysteine-glutathione mixed disulfide whereas only minor amounts of GSH and glutathione disulfide could be detected.	Disulfides	170-179	gamma-glutamyltransferase 1	Rattus norvegicus	19-44
17974571-10	2008	In contrast to human Prx I, which was recently reported to exist predominantly as the decamer with Cys(83)-Cys(83) disulfide bonds at all dimer-dimer interfaces, rat HBP23/Prx I has a Cys(83)-Cys(83) disulfide bond at only one dimer-dimer interface (S-S separation of approximately 2.1A), whereas the interactions at the other interfaces (mean S-S separation of 3.6A) appear to involve hydrophobic and van der Waals forces.	Disulfides	115-124	peroxiredoxin 1	Homo sapiens	21-26
17974571-10	2008	In contrast to human Prx I, which was recently reported to exist predominantly as the decamer with Cys(83)-Cys(83) disulfide bonds at all dimer-dimer interfaces, rat HBP23/Prx I has a Cys(83)-Cys(83) disulfide bond at only one dimer-dimer interface (S-S separation of approximately 2.1A), whereas the interactions at the other interfaces (mean S-S separation of 3.6A) appear to involve hydrophobic and van der Waals forces.	Disulfides	200-209	peroxiredoxin 1	Rattus norvegicus	166-171
17956189-2	2008	A large number of thiol-disulfide oxidoreductases, belonging to the thioredoxin superfamily, catalyze protein disulfide bond formation in all living cells, from bacteria to humans.	Disulfides	24-33	thioredoxin	Homo sapiens	68-79
7426659-13	1980	The inactivating cleavage occurred within a disulfide loop of the antithrombin III molecule, since the lower molecular weight species was detected only under reducing conditions.	Disulfides	44-53	serpin family C member 1	Homo sapiens	66-82
18638502-6	2008	TSR domains of the three trout properdin isoforms seem to adopt the folding pattern of human thrombospondin 1 TSP-1 domains, where each TSP-1 domain forms an antiparallel three-stranded structure that consists of alternative stacked layers of Trp and Arg residues from respective strands capped by disulfide bonds on each end.	Disulfides	298-307	complement factor properdin L homeolog	Xenopus laevis	31-40
6772227-0	1980	Kinetics of thymidylate synthase inhibition by disulfides.	Disulfides	47-57	thymidylate synthetase	Homo sapiens	12-32
17978092-4	2008	Import of the precursors requires the essential intermembrane space proteins Mia40 and Erv1 that were proposed to form a relay for disulfide formation in the precursor proteins.	Disulfides	131-140	growth factor, augmenter of liver regeneration	Homo sapiens	87-91
18691492-0	2008	Role of tissue factor disulfides and lipid rafts in signaling.	Disulfides	22-32	coagulation factor III, tissue factor	Homo sapiens	8-21
18691492-2	2008	This brief review summarizes recent controversial data on the importance of protein disulfide isomerase-mediated disulfide bond switching in extracellular domain of TF in regulating its coagulant and cell-signaling activities.	Disulfides	84-93	coagulation factor III, tissue factor	Homo sapiens	165-167
18691493-5	2008	It has been proposed that PDI activates TF by changing the disulfide status of the membrane-proximal Cys186-Cys209 pair of TF.	Disulfides	59-68	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	26-29
18691493-6	2008	Indeed, PDI was shown to cleave mixed disulfide bonds of TF with glutathione.	Disulfides	38-47	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	8-11
6772227-1	1980	The inactivation of thymidylate synthase (5,10-methylene-tetrahydrofolate: dUMP C-methyltransferase, EC 2.1.1.45) by a number of disulfides has been examined and found to be a second-order process.	Disulfides	129-139	thymidylate synthetase	Homo sapiens	20-40
6445748-0	1980	Reaction of 5,5"-dithiobis(2-nitrobenzoic acid) with myosin subfragment one: evidence for formation of a single protein disulfide with trapping of metal nucleotide at the active site.	Disulfides	120-129	myosin heavy chain 14	Homo sapiens	53-59
17994770-0	2007	Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: a disulfide mapping study.	Disulfides	85-94	hepcidin antimicrobial peptide	Homo sapiens	27-31
17994770-5	2007	This study uses cysteine and disulfide chemistry to test this archeal HAMP model in the full-length, membrane-bound aspartate receptor of bacterial chemotaxis.	Disulfides	29-38	hepcidin antimicrobial peptide	Homo sapiens	70-74
518865-9	1979	There is a significant homology between the second disulfide loop region of the chain (residues 182-271) and immunoglobulin (Ig) constant domains and beta 2-microglobulin [Orr, H. T., Lancet, D., Robb, R. J., Lopez de Castro, J.	Disulfides	51-60	beta-2-microglobulin	Homo sapiens	150-170
17994770-8	2007	Moreover, disulfide mapping reveals that the four helices of the aspartate receptor HAMP domain are arranged in the same parallel, four-helix bundle architecture observed in the archeal HAMP structure.	Disulfides	10-19	hepcidin antimicrobial peptide	Homo sapiens	84-88
17994770-8	2007	Moreover, disulfide mapping reveals that the four helices of the aspartate receptor HAMP domain are arranged in the same parallel, four-helix bundle architecture observed in the archeal HAMP structure.	Disulfides	10-19	hepcidin antimicrobial peptide	Homo sapiens	186-190
17726162-0	2007	Tissue factor activation: is disulfide bond switching a regulatory mechanism?	Disulfides	29-38	coagulation factor III, tissue factor	Homo sapiens	0-13
403960-2	1977	Quaternary structure of IgA dimer is formed when joining subunits with disulfide bonds and is stabilized by non-covalent interactions between them.	Disulfides	71-80	immunoglobulin heavy variable 4-38-2-like	Homo sapiens	24-27
17724034-5	2007	Human 4F2hc expressed in several cell types resulted in cell surface and Cys(109) disulfide bridge-linked homodimers with major architectural features of the crystal dimer, as demonstrated by cross-linking experiments.	Disulfides	82-91	solute carrier family 3 member 2	Homo sapiens	6-11
17724034-9	2007	This location of the N terminus and the Cys(109)-intervening disulfide bridge imposes space restrictions sufficient to support a model for electrostatic interaction of the 4F2hc ectodomain with membrane phospholipids.	Disulfides	61-70	solute carrier family 3 member 2	Homo sapiens	172-177
12950-0	1976	Enzyme reduction of disulfide bonds by thioredoxin.	Disulfides	20-29	thioredoxin	Homo sapiens	39-50
17699160-7	2007	This mechanism is in line with an unpaired Cys residue in the same surface region that can form a disulfide cross-link with apolipoprotein A-II.	Disulfides	98-107	apolipoprotein A2	Homo sapiens	124-143
12950-2	1976	The NADPH-dependent enzymic reduction of disulfide bonds in human choriogonadotropin and its two subunits, alpha and beta, was examined with thioredoxin and thioredoxin reductase from Escherichia coli.	Disulfides	41-50	thioredoxin	Homo sapiens	141-152
12950-2	1976	The NADPH-dependent enzymic reduction of disulfide bonds in human choriogonadotropin and its two subunits, alpha and beta, was examined with thioredoxin and thioredoxin reductase from Escherichia coli.	Disulfides	41-50	peroxiredoxin 5	Homo sapiens	157-178
12950-3	1976	With 12 muM thioredoxin and 0.1 muM thioredoxin reductase at pH 7 all disulfide bonds in the alpha subunit could be reduced in 15 min.	Disulfides	70-79	thioredoxin	Homo sapiens	12-23
12950-3	1976	With 12 muM thioredoxin and 0.1 muM thioredoxin reductase at pH 7 all disulfide bonds in the alpha subunit could be reduced in 15 min.	Disulfides	70-79	peroxiredoxin 5	Homo sapiens	36-57
17421043-1	2007	Protein disulfide isomerase (PDI), one of the ER-resident molecular chaperones, forms and isomerizes disulfide bonds.	Disulfides	8-17	protein disulfide-isomerase	Cricetulus griseus	29-32
12950-6	1976	The usefulness of thioredoxin reduction of disulfide bonds as a chemical probe of protein structure was shown by the much slower reaction of disulfide bonds in the intact hormone as compared to its two biologically inactive subunits.	Disulfides	43-52	thioredoxin	Homo sapiens	18-29
12950-6	1976	The usefulness of thioredoxin reduction of disulfide bonds as a chemical probe of protein structure was shown by the much slower reaction of disulfide bonds in the intact hormone as compared to its two biologically inactive subunits.	Disulfides	141-150	thioredoxin	Homo sapiens	18-29
127613-2	1975	A purine disulfide analog of ATP, 6,6"-dithiobis(inosinyl imidodiphosphate), forms mixed disulfide bonds between the 6 thiol group on the purine ring and certain key cysteines on myosin, heavy meromyosin, and subfragment one.	Disulfides	9-18	myosin heavy chain 14	Homo sapiens	179-185
17727880-0	2007	Design of disulfide-linked thioredoxin dimers and multimers through analysis of crystal contacts.	Disulfides	10-19	thioredoxin	Homo sapiens	27-38
17714875-1	2007	The selenoenzyme sperm nuclei glutathione peroxidase (snGPx), also called the nuclear form of phospholipid hydroperoxide glutathione peroxidase (n-PHGPx), was found to be involved in the stabilization of condensed sperm chromatin, most likely by thiol to disulfide oxidation of the cysteine residues of the mammalian protamines, small nuclear basic proteins in the nuclei of sperm cells.	Disulfides	255-264	glutathione peroxidase 4	Homo sapiens	17-52
127613-2	1975	A purine disulfide analog of ATP, 6,6"-dithiobis(inosinyl imidodiphosphate), forms mixed disulfide bonds between the 6 thiol group on the purine ring and certain key cysteines on myosin, heavy meromyosin, and subfragment one.	Disulfides	89-98	myosin heavy chain 14	Homo sapiens	179-185
17714875-1	2007	The selenoenzyme sperm nuclei glutathione peroxidase (snGPx), also called the nuclear form of phospholipid hydroperoxide glutathione peroxidase (n-PHGPx), was found to be involved in the stabilization of condensed sperm chromatin, most likely by thiol to disulfide oxidation of the cysteine residues of the mammalian protamines, small nuclear basic proteins in the nuclei of sperm cells.	Disulfides	255-264	glutathione peroxidase 4	Homo sapiens	54-59
17714875-1	2007	The selenoenzyme sperm nuclei glutathione peroxidase (snGPx), also called the nuclear form of phospholipid hydroperoxide glutathione peroxidase (n-PHGPx), was found to be involved in the stabilization of condensed sperm chromatin, most likely by thiol to disulfide oxidation of the cysteine residues of the mammalian protamines, small nuclear basic proteins in the nuclei of sperm cells.	Disulfides	255-264	glutathione peroxidase 4	Homo sapiens	147-152
123760-1	1975	A site-specific analog of ATP, 6,6"-dithiobis (inosinyl imidodiphosphate (S2P-PNP), inactivates the ATPase activities of myosin"s proteolytic fragments, heavy meromyosin (HMM) and subfragment one (SF1), by formation of mixed disulfides between the 6 position of the purine ring and certain key cysteines.	Disulfides	225-235	myosin heavy chain 14	Homo sapiens	121-127
17675287-4	2007	It is surprising that nearly all of our thioredoxin mutants had increased activity in disulfide isomerization in vitro and in vivo.	Disulfides	86-95	thioredoxin	Homo sapiens	40-51
123761-1	1975	A purine disulfide analog of ATP, 6,6"-dithiobis(inosinyl imidodiphosphate), forms mixed disulfides with cysteine residues at what are believed to be ATP regulatory sites of myosin.	Disulfides	89-99	myosin heavy chain 14	Homo sapiens	174-180
47633-6	1975	We suggest a model for the folding of beta-2-microglobulin (and immunoglobulin domains) in which one of the early folding events results in disulfide bond formation, the latter being an obligatory step for continued folding to the native state.	Disulfides	140-149	beta-2-microglobulin	Homo sapiens	38-58
17627468-1	2007	Human thioredoxin-1 (hTrx) exhibits a disulfide reducing activity and was originally identified as a soluble cytokine-like factor secreted from cells of a human T-cell leukemia virus type I (HTLV-I)-transformed cell line.	Disulfides	38-47	thioredoxin	Homo sapiens	21-25
4424566-1	1974	The fourth component of human complement (C4) was shown to be composed of three distinct polypeptide chains linked by disulfide bonds and noncovalent forces.	Disulfides	118-127	complement C4A (Rodgers blood group)	Homo sapiens	30-44
17673310-4	2007	Oxidation reversibly inhibited the phosphatase activity of PRL-1 due to the formation of an intramolecular disulfide bridge between Cys104 within the active site and another conserved Cys, Cys49.	Disulfides	107-116	protein tyrosine phosphatase 4A1	Homo sapiens	59-64
4269559-8	1973	Reduction of the alpha(2)-macroglobulin-enzyme mixture was required for the identification of the derivative subunit chains establishing that these cleavage products were covalently linked to the parent molecule by disulfide bridges.	Disulfides	215-224	alpha-2-macroglobulin	Homo sapiens	17-39
17591774-3	2007	We developed a homology model based on the crystal structure of bovine rhodopsin and predicted novel cysteine substitutions that should dramatically reduce E2 loop flexibility via disulfide bond formation and significantly inhibit the binding of both types of ligands.	Disulfides	180-189	rhodopsin	Bos taurus	71-80
4558655-3	1972	beta(2)-Microglobulin contains an intrachain disulfide loop of 57 amino-acid residues that is similar in size to disulfide loops found in the constant regions of immunoglobulin G. These findings suggest that beta(2)-microglobulin is a free immunoglobulin domain, possibly serving an effector function similar to that of the C(H)3 domain of gamma1 chains of immunoglobulin G.	Disulfides	45-54	beta-2-microglobulin	Homo sapiens	0-21
17555889-3	2007	However, the internal disulfide bond (CD7-D5) of human neuroglobin can be reduced by thioredoxin reductase.	Disulfides	22-31	peroxiredoxin 5	Homo sapiens	85-106
17697175-7	2007	We suggest that PrdxI induction could be considered a crucial part of the cellular adaptive response to the B-cell differentiation process to cope with the additional H(2)O(2) associated with massive disulfide bond formation during immunoglobulin folding in the endoplasmic reticulum of plasma cells.	Disulfides	200-209	peroxiredoxin 1	Mus musculus	16-21
4558655-3	1972	beta(2)-Microglobulin contains an intrachain disulfide loop of 57 amino-acid residues that is similar in size to disulfide loops found in the constant regions of immunoglobulin G. These findings suggest that beta(2)-microglobulin is a free immunoglobulin domain, possibly serving an effector function similar to that of the C(H)3 domain of gamma1 chains of immunoglobulin G.	Disulfides	45-54	beta-2-microglobulin	Homo sapiens	208-229
4558655-3	1972	beta(2)-Microglobulin contains an intrachain disulfide loop of 57 amino-acid residues that is similar in size to disulfide loops found in the constant regions of immunoglobulin G. These findings suggest that beta(2)-microglobulin is a free immunoglobulin domain, possibly serving an effector function similar to that of the C(H)3 domain of gamma1 chains of immunoglobulin G.	Disulfides	113-122	beta-2-microglobulin	Homo sapiens	0-21
14192907-0	1964	MODIFICATION OF L-MYOSIN BY DISULFIDE-SULFHYDRYL INTERCHANGE REACTION.	Disulfides	28-37	myosin heavy chain 14	Homo sapiens	18-24
17561102-4	2007	Yap1 activation involved oxidation to the intramolecular disulfide bond, a signature of activation by peroxide, and was dependent on the Yap1 peroxide sensor Orp1/Gpx3.	Disulfides	57-66	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	158-162
17561102-4	2007	Yap1 activation involved oxidation to the intramolecular disulfide bond, a signature of activation by peroxide, and was dependent on the Yap1 peroxide sensor Orp1/Gpx3.	Disulfides	57-66	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	163-167
33827045-6	2021	Thioredoxin reductase and glutathione reductase create new inter disulfide bonds.	Disulfides	65-74	peroxiredoxin 5	Homo sapiens	0-21
17567740-2	2007	We have shown previously in the crystal structure of the PAI-1/SMB complex that SMB, a peptide of 51 residues, is folded as a compact cysteine knot of four pairs of crossed disulfide bonds.	Disulfides	173-182	serpin family E member 1	Homo sapiens	57-62
33838181-1	2021	The lysosomal thiol reductase GILT catalyzes the reduction of disulfide bonds of protein antigens, facilitating antigen-presenting cells (APCs) to present antigen to T cells.	Disulfides	62-71	interferon gamma inducible protein 30	Mus musculus	30-34
33652022-3	2021	It has been long recognized from in vitro evidence that Txnip forms a disulfide bridge through cysteine 247 (C247) with reduced thioredoxin to inhibit the anti-oxidative properties of thioredoxin.	Disulfides	70-79	thioredoxin	Homo sapiens	184-195
17530757-5	2007	An antibody is then immobilized on the Au-NCAM via gold-thiol chemistry as a thiolated fragment of antigen-binding (Fab") prepared by direct digestion of the antibody followed by reduction of the disulfide linkage on the hinge region.	Disulfides	196-205	neural cell adhesion molecule 1	Homo sapiens	39-46
17530757-5	2007	An antibody is then immobilized on the Au-NCAM via gold-thiol chemistry as a thiolated fragment of antigen-binding (Fab") prepared by direct digestion of the antibody followed by reduction of the disulfide linkage on the hinge region.	Disulfides	196-205	FA complementation group B	Homo sapiens	116-119
17575238-5	2007	Thioredoxin activity was assayed by the insulin disulfide-reducing assay.	Disulfides	48-57	thioredoxin	Homo sapiens	0-11
33878389-2	2021	We used human growth hormone (hGH) as target protein that contains two internal disulfide bridges and an N-terminal phenylalanine.	Disulfides	80-89	gamma-glutamyl hydrolase	Homo sapiens	30-33
17409163-7	2007	To better understand the nature of this disulfide network, E1 and E2 cysteinyl residues were labeled with iodoacetamide in the native virus particle and analyzed by liquid chromatography-tandem mass spectrometry.	Disulfides	40-49	small nucleolar RNA, H/ACA box 73A	Homo sapiens	59-67
33878389-9	2021	Periplasmic expression of hGH fused to this novel C-terminal DnaX intein-based self-cleaving affinity tag made possible expression and purification of hGH protein containing disulfide bonds and free of extra amino acids.	Disulfides	174-183	gamma-glutamyl hydrolase	Homo sapiens	26-29
17511867-3	2007	RESULTS: Structural models of serine proteases PR1 from entomophagous fungus, Ver112 and VCP1 from nematophagous fungi, have been modeled using the homology modeling technique based on the crystal coordinate of the proteinase K. In combination with multiple sequence alignment, these models suggest one similar calcium-binding site and two common disulfide bridges in the three cuticle-degrading enzymes.	Disulfides	347-356	transmembrane protein 37	Homo sapiens	47-50
33878389-9	2021	Periplasmic expression of hGH fused to this novel C-terminal DnaX intein-based self-cleaving affinity tag made possible expression and purification of hGH protein containing disulfide bonds and free of extra amino acids.	Disulfides	174-183	gamma-glutamyl hydrolase	Homo sapiens	151-154
33963564-13	2021	Disulfide-bonded KCNQ1/KCNE1 constructs reported preferential association after they had reached cell surface.	Disulfides	0-9	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	17-22
17374396-6	2007	Physical characterization by velocity sedimentation revealed that this novel construct, hFcILZOX40L, was assembled into hexamers in which the Fc domains formed three disulfide-bonded dimers and the ILZ-OX40L domains formed two trimers.	Disulfides	166-175	TNF superfamily member 4	Homo sapiens	94-99
33964423-4	2021	Native A2M consists of two crescent-shaped disulfide-bridged subunit dimers which face towards each other and surround a central hollow space.	Disulfides	43-52	alpha-2-macroglobulin	Homo sapiens	7-10
17497430-11	2007	The marked conservation of cysteine residues emphasizes the importance of the intricate pattern of disulfide bonds in governing the structure of pro-VWF and regulating the function of the mature VWF protein.	Disulfides	99-108	Von Willebrand factor	Mus musculus	149-152
17497430-11	2007	The marked conservation of cysteine residues emphasizes the importance of the intricate pattern of disulfide bonds in governing the structure of pro-VWF and regulating the function of the mature VWF protein.	Disulfides	99-108	Von Willebrand factor	Mus musculus	195-198
33964423-5	2021	In native A2M, interactions across the disulfide-bridged dimers are minimal, with a single major interface between the linker (LNK) regions of oppositely positioned subunits.	Disulfides	39-48	alpha-2-macroglobulin	Homo sapiens	10-13
33601275-8	2021	MS with 18O-labeling has allowed identification of the residues involved in some cases (e.g. Cys25 from the Cys25-Cys80 disulfide in beta-2-microglobulin, with Cys149 or Cys244 of GAPDH).	Disulfides	120-129	beta-2-microglobulin	Homo sapiens	133-153
17276536-1	2007	Delivery of the hypoxia-inducible vascular endothelial growth factor (RTP-VEGF) plasmid using a novel reducible disulfide poly(amido ethylenediamine) (SS-PAED) polymer carrier was studied in vitro and in vivo.	Disulfides	112-121	vascular endothelial growth factor A	Rattus norvegicus	74-78
33893096-2	2021	gamma-Interferon-inducible lysosomal thiol reductase (GILT) enhances antigen processing within lysosomes through direct reduction of antigen disulfides and maintenance of cysteine protease activity.	Disulfides	141-151	interferon gamma inducible protein 30	Mus musculus	0-52
17092531-4	2007	Soluble, stabilized, proteolytically cleaved, trimeric gp140 proteins can be generated by engineering an intermolecular disulfide bond between gp120 and gp41 (SOS), combined with a single residue change, I559P, within gp41 (SOSIP).	Disulfides	120-129	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	143-148
33893096-2	2021	gamma-Interferon-inducible lysosomal thiol reductase (GILT) enhances antigen processing within lysosomes through direct reduction of antigen disulfides and maintenance of cysteine protease activity.	Disulfides	141-151	interferon gamma inducible protein 30	Mus musculus	54-58
33872626-4	2021	mFe(SS)/DG based on coordination between Fe3+ and disulfide-bearing ligand scavenged GSH and downregulated glutathione peroxide 4 (GPX4) to trigger ferroptosis.	Disulfides	50-59	glutathione peroxidase 4	Homo sapiens	131-135
17315952-1	2007	Alpha-conotoxins isolated from Conus venoms contain 11-19 residues and preferentially fold into the globular conformation that possesses a specific disulfide pairing pattern (C1-3, C2-4).	Disulfides	148-157	complement C2	Homo sapiens	181-185
33889136-4	2021	HCMV virions also contain an alternative non-disulfide bound heterodimer comprised of gH and UL116 whose function remains unknown.	Disulfides	45-54	gamma-glutamyl hydrolase	Homo sapiens	86-88
17101776-0	2007	Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress.	Disulfides	8-17	activating transcription factor 6	Homo sapiens	58-62
17101776-2	2007	We show here that, owing to the presence of intra- and intermolecular disulfide bridges formed between the two conserved cysteine residues in the luminal domain, ATF6 occurs in unstressed ER in monomer, dimer, and oligomer forms.	Disulfides	70-79	activating transcription factor 6	Homo sapiens	162-166
17101776-3	2007	Disulfide-bonded ATF6 is reduced upon treatment of cells with not only the reducing reagent dithiothreitol but also the glycosylation inhibitor tunicamycin, and the extent of reduction correlates with that of activation.	Disulfides	0-9	activating transcription factor 6	Homo sapiens	17-21
33889136-4	2021	HCMV virions also contain an alternative non-disulfide bound heterodimer comprised of gH and UL116 whose function remains unknown.	Disulfides	45-54	protein UL116	Human betaherpesvirus 5	93-98
33577944-6	2021	Oxidative site of PTEN exposed to CSE is via formation of a disulfide bond between Cys71 and Cys124, similar to H2O2.	Disulfides	60-69	phosphatase and tensin homolog	Homo sapiens	18-22
17302776-5	2007	RESULTS: Using compounds having similar structures but differences in reactive moieties, it was proved that the only chemical moiety that was required for inhibition of FcgammaR-mediated phagocytosis in vitro was a disulfide bond.	Disulfides	215-224	Fc gamma receptor Ia	Homo sapiens	169-177
33577944-14	2021	Oxidative mechanism of PTEN exposed to CSE was mediated by formation of a disulfide bond between Cys71and Cys124, similar to H2O2.	Disulfides	74-83	phosphatase and tensin homolog	Homo sapiens	23-27
17209570-0	2007	Isomers of human alpha-synuclein stabilized by disulfide bonds exhibit distinct structural and aggregative properties.	Disulfides	47-56	synuclein alpha	Homo sapiens	17-32
33850892-7	2021	Residues located outside the disulfide bond of TCR alpha or beta chains and forming pi stack force played favorable roles in the complex intermolecular interaction and binding free energy.	Disulfides	29-38	T cell receptor alpha joining 60 (pseudogene)	Homo sapiens	47-56
17094948-8	2006	This particular disulfide (Cys94-Cys117) is only present in BMPRII and activin receptors, suggesting that it is important for their likely shared mode of binding.	Disulfides	16-25	bone morphogenetic protein receptor type 2	Homo sapiens	60-66
17094948-8	2006	This particular disulfide (Cys94-Cys117) is only present in BMPRII and activin receptors, suggesting that it is important for their likely shared mode of binding.	Disulfides	16-25	inhibin subunit beta E	Homo sapiens	71-78
17096689-6	2006	These finding suggest that GPX isoenzymes may function to detoxify H2O2 and organic hydroperoxides using thioredoxin in vivo and may also be involved in regulation of the cellular redox homeostasis by maintaining the thiol/disulfide or NADPH/NADP balance.	Disulfides	223-232	glutathione peroxidase 2	Arabidopsis thaliana	27-30
33850892-10	2021	Conclusions: The findings of this study suggest that the hydrophobic nature of the amino acids inside or outside the disulfide bonds on the TCR may be associated with the intermolecular interaction and binding between the TCR and polypeptide.	Disulfides	117-126	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	140-143
33850892-10	2021	Conclusions: The findings of this study suggest that the hydrophobic nature of the amino acids inside or outside the disulfide bonds on the TCR may be associated with the intermolecular interaction and binding between the TCR and polypeptide.	Disulfides	117-126	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	222-225
17238830-5	2006	Cation exchange purification results in the isolation of at least two N-linked glycosylated IL-24 dimers covalently associated via intermolecular disulfide bonds.	Disulfides	146-155	interleukin 24	Homo sapiens	92-97
33850892-11	2021	The residues located outside the TCR alpha or beta single-chain disulfide bond and forming the pi-stack force showed a beneficial effect on the intermolecular interaction and binding of the complex.	Disulfides	64-73	T cell receptor alpha joining 60 (pseudogene)	Homo sapiens	33-42
33633190-2	2021	beta2GPI exists mainly in closed or open conformations and comprises of 11 disulfides distributed across five domains.	Disulfides	75-85	apolipoprotein H	Homo sapiens	0-8
17115050-3	2006	Success was achieved for GluR5, GluR6 and GluR7 with intermolecular disulfide cross-links but not by engineering the dimer interface.	Disulfides	68-77	glutamate ionotropic receptor kainate type subunit 2	Homo sapiens	32-37
17115050-3	2006	Success was achieved for GluR5, GluR6 and GluR7 with intermolecular disulfide cross-links but not by engineering the dimer interface.	Disulfides	68-77	glutamate ionotropic receptor kainate type subunit 3	Homo sapiens	42-47
17078949-2	2006	After producing recombinant full-length tenascin-X in mammalian cells, we find that this protein assembled into disulfide-linked oligomers.	Disulfides	112-121	tenascin XB	Homo sapiens	40-50
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	13-22	serpin family C member 1	Homo sapiens	84-92
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	13-22	serpin family C member 1	Homo sapiens	145-153
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	185-194	serpin family C member 1	Homo sapiens	145-153
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	185-194	serpin family C member 1	Homo sapiens	145-153
16732321-1	2006	In patients with medullary thyroid carcinoma (MTC) and type 2A multiple endocrine neoplasia (MEN2A), mutations of cysteine residues in the extracellular juxtamembrane region of the RET receptor tyrosine kinase cause the formation of covalent receptor dimers linked by intermolecular disulfide bonds between unpaired cysteines, followed by oncogenic activation of the RET kinase.	Disulfides	283-292	ret proto-oncogene	Homo sapiens	93-98
16732321-1	2006	In patients with medullary thyroid carcinoma (MTC) and type 2A multiple endocrine neoplasia (MEN2A), mutations of cysteine residues in the extracellular juxtamembrane region of the RET receptor tyrosine kinase cause the formation of covalent receptor dimers linked by intermolecular disulfide bonds between unpaired cysteines, followed by oncogenic activation of the RET kinase.	Disulfides	283-292	ret proto-oncogene	Homo sapiens	181-184
32773600-4	2021	We found disulfide HMGB1 to equally increase microglial Iba-1 immunoreactivity in lumbar spinal dorsal horn in male and female mice, but evoke higher cytokine and chemokine expression in primary microglial culture derived from males compared to females.	Disulfides	9-18	induction of brown adipocytes 1	Mus musculus	56-61
33212041-4	2021	The disulfide group of GQQ-792 binds to Cys379 and Cys380 of PGK1, resulting in occlusion of ATP from binding to PGK1.	Disulfides	4-13	phosphoglycerate kinase 1	Homo sapiens	113-117
32949584-4	2020	PNSA bound to cysteine residues C572/C598 of CT-Hsp90 with disulfide bonds and inhibits Hsp90 activity, resulting in apoptosis and growth inhibition of HCT116 cells in vitro and in vivo.	Disulfides	59-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	48-53
16813566-3	2006	Using phage display, we have identified the disulfide-constrained peptide motif CFGWC with affinity for natural human PAI-1.	Disulfides	44-53	serpin family E member 1	Homo sapiens	118-123
33196673-8	2020	It was suggested that oxidation presumably acts through stabilizing the dimer structures of artemin through formation of disulfide bridges between the subunits and strengthens its chaperoning efficacy.	Disulfides	121-130	artemin	Homo sapiens	92-99
17015729-5	2006	The DMalpha and beta-chains direct each others fate: single DMalpha chains cannot fully oxidize without DMbeta, while DMbeta forms disulfide-linked homodimers without DMalpha.	Disulfides	131-140	major histocompatibility complex, class II, DM alpha	Homo sapiens	4-11
32745482-0	2020	Novel SERPINC1 missense mutation (Cys462Tyr) causes disruption of the 279Cys-462Cys disulfide bond and leads to type I hereditary antithrombin deficiency.	Disulfides	84-93	serpin family C member 1	Homo sapiens	6-14
17015827-4	2006	We have used disulfide cross-linking technology to capture a human oxoG repair protein, 8-oxoguanine DNA glycosylase I (hOGG1) sampling an undamaged G:C base pair located adjacent to an oxoG:C base pair in DNA.	Disulfides	13-22	8-oxoguanine DNA glycosylase	Homo sapiens	120-125
17002301-10	2006	These findings imply that the Cys186-Cys209 disulfide bond is reduced in the cryptic form of TF and that activation involves formation of the disulfide.	Disulfides	44-53	coagulation factor III, tissue factor	Homo sapiens	93-95
17002301-10	2006	These findings imply that the Cys186-Cys209 disulfide bond is reduced in the cryptic form of TF and that activation involves formation of the disulfide.	Disulfides	142-151	coagulation factor III, tissue factor	Homo sapiens	93-95
32745482-10	2020	CONCLUSION: A SERPINC1 missense mutation (Cys462Tyr) causing damage to the 279Cys-462Cys disulfide bond of the AT protein appears to be the cause of Type I AT deficiency in this family.	Disulfides	89-98	serpin family C member 1	Homo sapiens	14-22
16995928-7	2006	These immunodominant regions of HIV envelope contain cysteine residues, which make disulfide bond and can interfere with the assembly of light chain and heavy chain fragment to make Fab molecule in vitro.	Disulfides	83-92	FA complementation group B	Homo sapiens	182-185
16959886-0	2006	Disulfide isomerization switches tissue factor from coagulation to cell signaling.	Disulfides	0-9	coagulation factor III, tissue factor	Homo sapiens	33-46
16959886-3	2006	The surface-accessible, extracellular Cys186-Cys209 disulfide bond of TF is critical for coagulation, and protein disulfide isomerase (PDI) disables coagulation by targeting this disulfide.	Disulfides	52-61	coagulation factor III, tissue factor	Homo sapiens	70-72
32745482-10	2020	CONCLUSION: A SERPINC1 missense mutation (Cys462Tyr) causing damage to the 279Cys-462Cys disulfide bond of the AT protein appears to be the cause of Type I AT deficiency in this family.	Disulfides	89-98	serpin family C member 1	Homo sapiens	111-113
33214850-2	2020	Several structure-activity relationship studies on both human relaxin 3 (containing 3 disulfide bonds) and its analogue A2 (two disulfide bonds) suggest that the C-terminal carboxylic acid of the tryptophan residue in the B-chain is important for RXFP3 activity.	Disulfides	86-95	relaxin 3	Homo sapiens	62-71
16935577-2	2006	C8 is composed of a disulfide-linked C8alpha-gamma heterodimer and a noncovalently associated C8beta chain.	Disulfides	20-29	complement C8 alpha chain	Homo sapiens	37-44
16877534-0	2006	Identification of disulfide bonds in the Ig-alpha/Ig-beta component of the B cell antigen receptor using the Drosophila S2 cell reconstitution system.	Disulfides	18-27	chemokine (C-X-C motif) ligand 9	Mus musculus	41-43
16877534-0	2006	Identification of disulfide bonds in the Ig-alpha/Ig-beta component of the B cell antigen receptor using the Drosophila S2 cell reconstitution system.	Disulfides	18-27	chemokine (C-X-C motif) ligand 9	Mus musculus	50-52
16877534-2	2006	We have used the Drosophila S2 cell reconstitution system for identification of disulfide bonds within and between CD79a (Ig-alpha) and CD79b (Ig-beta), the heterodimeric signal transducing element of the B cell antigen receptor (BCR).	Disulfides	80-89	chemokine (C-X-C motif) ligand 9	Mus musculus	122-124
33214850-2	2020	Several structure-activity relationship studies on both human relaxin 3 (containing 3 disulfide bonds) and its analogue A2 (two disulfide bonds) suggest that the C-terminal carboxylic acid of the tryptophan residue in the B-chain is important for RXFP3 activity.	Disulfides	128-137	relaxin 3	Homo sapiens	62-71
16877534-2	2006	We have used the Drosophila S2 cell reconstitution system for identification of disulfide bonds within and between CD79a (Ig-alpha) and CD79b (Ig-beta), the heterodimeric signal transducing element of the B cell antigen receptor (BCR).	Disulfides	80-89	chemokine (C-X-C motif) ligand 9	Mus musculus	143-145
16877534-3	2006	Cysteines 113 and 135 of Ig-alpha and Ig-beta, respectively, form the intermolecular disulfide bridge stabilizing the Ig-alpha/Ig-beta heterodimer in both S2 cells and the B cell line J558L.	Disulfides	85-94	chemokine (C-X-C motif) ligand 9	Mus musculus	25-27
32428298-0	2020	Switching the Switch: Ligand induced Disulfide Formation in HDAC8.	Disulfides	37-46	histone deacetylase 8	Homo sapiens	60-65
16877534-3	2006	Cysteines 113 and 135 of Ig-alpha and Ig-beta, respectively, form the intermolecular disulfide bridge stabilizing the Ig-alpha/Ig-beta heterodimer in both S2 cells and the B cell line J558L.	Disulfides	85-94	chemokine (C-X-C motif) ligand 9	Mus musculus	38-40
16877534-3	2006	Cysteines 113 and 135 of Ig-alpha and Ig-beta, respectively, form the intermolecular disulfide bridge stabilizing the Ig-alpha/Ig-beta heterodimer in both S2 cells and the B cell line J558L.	Disulfides	85-94	chemokine (C-X-C motif) ligand 9	Mus musculus	38-40
16877534-3	2006	Cysteines 113 and 135 of Ig-alpha and Ig-beta, respectively, form the intermolecular disulfide bridge stabilizing the Ig-alpha/Ig-beta heterodimer in both S2 cells and the B cell line J558L.	Disulfides	85-94	chemokine (C-X-C motif) ligand 9	Mus musculus	38-40
16877534-4	2006	Furthermore, using transfected S2 cells, two putative intramolecular disulfide bonds in the Ig-like domain of Ig-beta were identified.	Disulfides	69-78	chemokine (C-X-C motif) ligand 9	Mus musculus	92-94
16877534-4	2006	Furthermore, using transfected S2 cells, two putative intramolecular disulfide bonds in the Ig-like domain of Ig-beta were identified.	Disulfides	69-78	chemokine (C-X-C motif) ligand 9	Mus musculus	110-112
16877534-5	2006	Ig-betaC65 and Ig-betaC120 form the canonical Ig fold disulfide bond.	Disulfides	54-63	chemokine (C-X-C motif) ligand 9	Mus musculus	0-2
32428298-2	2020	PD-404,182 was shown to be a selective covalent inhibitor of HDAC8 that forms mixed disulfides with several cysteine residues and is also able to transform thiol groups to thiocyanates.	Disulfides	84-94	histone deacetylase 8	Homo sapiens	61-66
32428298-3	2020	Moreover, HDAC8 was shown to be regulated by a redox switch based on the reversible formation of a disulfide bond between cysteines Cys102 and Cys153.	Disulfides	99-108	histone deacetylase 8	Homo sapiens	10-15
16859704-4	2006	Despite great differences in overall size and structure, the DR5-binding peptides and antibodies shared a tripeptide motif, which was conserved within a disulfide-constrained loop of the peptides and the third complementarity determining region of the antibody heavy chains.	Disulfides	153-162	TNF receptor superfamily member 10b	Homo sapiens	61-64
32428298-4	2020	This study on the distinct effects of PD-404,182 on HDAC8 reveals that this compound induces the dose-dependent formation of intramolecular disulfide bridges.	Disulfides	140-149	histone deacetylase 8	Homo sapiens	52-57
32428298-5	2020	Therefore, the inhibition mechanism of HDAC8 by PD-404,182 involves both, covalent modification of thiols as well as ligand mediated disulfide formation.	Disulfides	133-142	histone deacetylase 8	Homo sapiens	39-44
32428298-6	2020	Moreover, this study provides a deep molecular insight into the regulation mechanism of HDAC8 involving several cysteines with graduated capability to form reversible disulfide bridges.	Disulfides	167-176	histone deacetylase 8	Homo sapiens	88-93
32815729-6	2020	At low dosages (10 and 25 mumol/g GA), disulfide-dominant covalent bonds were formed to generate myosin and actin aggregates, while MP aggregate was mostly bridged through GA-thiols or GA-tryptophan adduct when the dosages exceeded 50 mumol/g.	Disulfides	39-48	myosin heavy chain 14	Homo sapiens	97-103
16586531-1	2006	Thioredoxin superfamily members share a considerable degree of structural similarity, with a conserved CX(i)X(j)C motif at the active site, where C stand for two cysteines that alternate between a reduced thiol and oxidized disulfide states, and X(i)and X(j) are two amino acids different in each family member.	Disulfides	224-233	thioredoxin	Homo sapiens	0-11
16586531-3	2006	Thioredoxin, for example, promotes the reduction of disulfide bonds, while DsbA promotes their oxidation in prokaryotic cells.	Disulfides	52-61	thioredoxin	Homo sapiens	0-11
33066406-4	2020	The heavy (i.e., 4F2hc) and light (i.e., LAT1 and LAT2) chains belong to the solute carrier (SLC) families SLC3 and SLC7, and are covalently linked by a conserved disulfide bridge.	Disulfides	163-172	solute carrier family 3 member 2	Homo sapiens	17-22
33066406-4	2020	The heavy (i.e., 4F2hc) and light (i.e., LAT1 and LAT2) chains belong to the solute carrier (SLC) families SLC3 and SLC7, and are covalently linked by a conserved disulfide bridge.	Disulfides	163-172	solute carrier family 7 member 5	Homo sapiens	41-45
32863228-7	2020	We found that the phosphorylated (inactive) form of cofilin-2 is mechanistically linked to the formation of an extended network of fibrillar structures induced by oxidative stress via the formation of a disulfide bond between Cys39 and Cys80.	Disulfides	203-212	cofilin 2	Homo sapiens	52-61
16682620-6	2006	Recently, disulfide trapping identified a similar small-molecule site and allosteric transition in the apoptotic caspase-7 that shares only a 23% sequence identity with caspase-1.	Disulfides	10-19	caspase 7	Homo sapiens	113-122
16634638-8	2006	A covalent disulfide-linked complex between SAP97(PDZ2) and the GluR-A peptide was seen in the binding assay and in the NMR experiments performed under oxidizing conditions.	Disulfides	11-20	glutamate ionotropic receptor AMPA type subunit 1	Homo sapiens	64-70
16495342-3	2006	Genetic and structural data indicate a disulfide bond is transferred from Cys100-Cys105 directly to Pdi1p, whereas a Cys352-Cys355 disulfide bond is used to reoxidize the reduced Cys100-Cys105 pair through an internal thiol-transfer reaction.	Disulfides	39-48	peptidyl arginine deiminase 1	Homo sapiens	100-105
33110418-5	2020	For missense variants, burden in NOTCH1 achieved genome-wide significance only when restricted to constrained genes (i.e., under negative selection, Bonferroni corrected p-value = 0.004), and showed enrichment for variants affecting the extracellular domain, especially those disrupting cysteine residues forming disulfide bonds (OR = 39.8 vs. gnomAD).	Disulfides	313-322	notch 1	Mus musculus	33-39
16226036-4	2006	Activin-A, a member of transforming growth factor beta superfamily, is a homodimeric protein with nine disulfide bonds.	Disulfides	103-112	inhibin subunit beta E	Homo sapiens	0-7
32982964-2	2020	Some studies support that the central C-domain of INSL3 is proteolytically removed and that INSL3 is secreted by the testicular Leydig cells into circulation as a small heterodimer consisting of an A- and a B-chain linked by two disulfide bridges.	Disulfides	229-238	insulin like 3	Homo sapiens	92-97
16489763-0	2006	Human bradykinin B2 receptor sialylation and N-glycosylation participate with disulfide bonding in surface receptor dimerization.	Disulfides	78-87	bradykinin receptor B2	Homo sapiens	17-28
16489763-7	2006	Importantly, receptor sialylation and N-glycosylation participate with disulfide bonding in the stabilization of the cell surface human B2 receptor dimers.	Disulfides	71-80	bradykinin receptor B2	Homo sapiens	136-147
32445640-6	2020	Reduced glutathione drastically increases the warfarin sensitivity of a VKOR-like protein from Takifugu rubripes, presumably through maintaining a disulfide-bonded conformation.	Disulfides	147-156	vitamin K epoxide reductase complex subunit 1	Homo sapiens	72-76
16377632-6	2006	Reduction of protein disulfide bonds with tris(hydroxypropyl)phosphine resulted in virtually complete immobilization of the SHGFP-MUC5AC/CK intragranular pool.	Disulfides	21-30	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	130-136
32592613-9	2020	We conclude that both deglycosylation and disulfide bond formation are important for CD44 to compete with IGFBP-3 for binding HA.	Disulfides	42-51	insulin like growth factor binding protein 3	Homo sapiens	106-113
16377632-7	2006	However, when activity of the vacuolar H+-ATPase was also inhibited, disulfide reduction decreased SHGFP-MUC5AC/CK t((1/2)) while diminishing its intraluminal concentration.	Disulfides	69-78	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	105-111
16475797-0	2006	Selectivity of tryptophan residues in mediating photolysis of disulfide bridges in goat alpha-lactalbumin.	Disulfides	62-71	alpha-lactalbumin	Capra hircus	88-105
16475797-1	2006	Goat alpha-lactalbumin (GLA) contains four tryptophan (Trp) residues and four disulfide bonds.	Disulfides	78-87	alpha-lactalbumin	Capra hircus	5-22
33397549-6	2020	To overcome this dilemma, we designed disulfide cross-linking micelles (DCM) nanocarrier for delivery of miR-145 to colon cancer cells and investigated its therapeutic efficacy in vitro and in vivo.	Disulfides	38-47	microRNA 145	Homo sapiens	105-112
16303754-8	2006	Our initial studies focused on disulfide bond formation between the SNARE motifs of Bet1p and Sec22p.	Disulfides	31-40	Bet1p	Saccharomyces cerevisiae S288C	84-89
16303754-11	2006	Using this disulfide cross-linking assay, we show that inhibition of transport with anti-Sly1p antibodies blocked formation of the Bet1p-Sec22p heterodimer.	Disulfides	11-20	Bet1p	Saccharomyces cerevisiae S288C	131-136
32677157-4	2020	In addition, glutathione (GSH) depletion through disulfide-thiol exchange leads to the inactivation of glutathione peroxide 4 (GPX4), which results in a further increase in LPO content.	Disulfides	49-58	glutathione peroxidase 4	Mus musculus	127-131
32601209-6	2020	Using the approach, we confirm peroxide- and thioredoxin-related quaternary transitions to take place in cellulo and observe that the relationship between dimer-decamer transitions and intersubunit disulfide bond formation is more complex than previously thought.	Disulfides	198-207	thioredoxin	Homo sapiens	45-56
16357268-13	2006	Theoretically important findings are: 1) when heated, serum PG is capable of covalently binding to micellar casein or complexing with beta-LG in whey and then coadhering to micelles, and 2) PG that associated with micellar casein through lysine binding sites before heating is capable of developing heat-induced disulfide bonds with casein.	Disulfides	312-321	plasminogen	Bos taurus	60-62
32601215-6	2020	Using two-dimensional (2D) gel electrophoresis and a conformation-specific antibody that recognizes a correctly folded domain, we show here that shuffling of nonnative disulfide bonds to native ones in the most N-terminal region of LDL receptor (LDLR) started at a specific timing during synthesis.	Disulfides	168-177	low density lipoprotein receptor	Homo sapiens	232-244
32601215-6	2020	Using two-dimensional (2D) gel electrophoresis and a conformation-specific antibody that recognizes a correctly folded domain, we show here that shuffling of nonnative disulfide bonds to native ones in the most N-terminal region of LDL receptor (LDLR) started at a specific timing during synthesis.	Disulfides	168-177	low density lipoprotein receptor	Homo sapiens	246-250
32601215-7	2020	Deletion analysis identified a region on LDLR that assisted with disulfide shuffling in the upstream domain, thereby promoting its cotranslational folding.	Disulfides	65-74	low density lipoprotein receptor	Homo sapiens	41-45
15942931-3	2006	After oxidation to form the two-disulfide bonds, affinity chromatography using an immobilized mouse anti-human MCP-1 monoclonal antibody (mAb) was utilized for a simple and highly effective purification procedure for the proteins.	Disulfides	32-41	C-C motif chemokine ligand 2	Homo sapiens	111-116
32389478-3	2020	First, we tested the thiol-disulfide bond interchange between beta-LG and MFGM by heating raw milk (87 C, 8 min) in the presence of different reagents capable of preventing this interaction, and then evaluated the presence of beta-LG in resulting MFGM preparations by sodium dodecyl sulfate-PAGE.	Disulfides	27-36	milk fat globule EGF and factor V/VIII domain containing	Homo sapiens	74-78
17073723-2	2006	However, the high expression of active hEGF in Escherichia coli has not been successful, as the protein contains three intra-molecular disulfide bonds that are difficult to form correctly in the bacterial intracellular environment.	Disulfides	135-144	epidermal growth factor	Homo sapiens	39-43
32389478-9	2020	This indicates that disulfide formation between beta-LG and proteins in the MFGM is not required for the association, but that hydrophobic interactions and hydrogen bonding may be crucial.	Disulfides	20-29	milk fat globule EGF and factor V/VIII domain containing	Homo sapiens	76-80
32142475-4	2020	After this reaction, MIA40 is reoxidized by the sulfhydryl oxidase ALR, which couples disulfide formation by this machinery to the activity of the respiratory chain.	Disulfides	86-95	growth factor, augmenter of liver regeneration	Homo sapiens	67-70
16185653-9	2005	The activation of TPH1 by incubation with DTT was accompanied by exposure of 9 sulfhydryls out of the total 10 cysteine residues, but the cleavage of disulfide bonds seemed not to be crucial, even if it occurred.	Disulfides	150-159	tryptophan hydroxylase 1	Homo sapiens	18-22
16242719-0	2005	A single disulfide bond differentiates aggregation pathways of beta2-microglobulin.	Disulfides	9-18	beta-2-microglobulin	Homo sapiens	63-82
16242719-2	2005	The native beta-sandwich fold of beta2m has a highly conserved disulfide bond linking Cys25 and Cys80.	Disulfides	63-72	beta-2-microglobulin	Homo sapiens	33-39
16242719-3	2005	Oxidized beta2m forms needle-like amyloid fibrils at pH 2.5 in vitro, whereas reduced beta2m, at acid pH, in which the intra-chain disulfide bond is disrupted, cannot form typical fibrils.	Disulfides	131-140	beta-2-microglobulin	Homo sapiens	86-92
32380958-4	2020	Disulfide-HMGB1 triggers TLR4 receptors generating pro-inflammatory cytokine release.	Disulfides	0-9	toll like receptor 4	Homo sapiens	25-29
16242719-10	2005	Our studies suggest that the different aggregation pathways of oxidized and reduced beta2m are dictated by the formation of distinct precursor oligomeric species that are modulated by Cys25-Cys80 disulfide-bonds.	Disulfides	196-205	beta-2-microglobulin	Homo sapiens	84-90
32204009-4	2020	First, two-generation polyglutamic acid dendrimer was bonded to nattokinase (NK) and then cross-linkers containing disulfide linkages were used to obtain polymer conjugates (NK-G2)n. Then doxorubicin (Dox) was encapsulated.	Disulfides	115-124	killer cell lectin like receptor C1	Homo sapiens	174-179
16086339-3	2005	A disulfide-based anchoring group was tagged to the TTF end of the molecule in order to allow its self-assembly on gold surfaces.	Disulfides	2-11	ras homolog family member H	Homo sapiens	52-55
31913846-10	2020	Redox-mediated modification of Cys thiols of apoE2 or apoE3, especially disulfide bond formation with apoAII, affects lipid metabolism and consequently may be responsible for the diverse isoform specificity of apoE.	Disulfides	72-81	apolipoprotein A2	Homo sapiens	102-108
16274220-3	2005	Hp shares approximately 50% sequence identity with the plasma multicopper ferroxidase ceruloplasmin including conservation of residues involved in disulfide bond formation and metal coordination.	Disulfides	147-156	ceruloplasmin	Homo sapiens	86-99
32316996-0	2020	Disulfide isomerase ERp57 improves the stability and immunogenicity of H3N2 influenza virus hemagglutinin.	Disulfides	0-9	protein disulfide isomerase associated 3	Mus musculus	20-25
16221844-9	2005	Disulfide bonds formed in 5-HT3A/K81C/A304C and 5-HT3A/K81C/I305C when coexpressed with 5-HT3B.	Disulfides	0-9	5-hydroxytryptamine receptor 3B	Homo sapiens	88-94
32068386-5	2020	For one thing, it was found that the introduction of the disulfide bond in the PLGA hydrogel promoted cellular adhesion via combining fibronectin, preventing the formation of spheroids, while the introduction of polyethylene glycol monomethyl ether (mPEG) could disturb the effect of the disulfide bond on cellular adhesion, supporting spheroid formation inside the porous hydrogel.	Disulfides	57-66	fibronectin 1	Mus musculus	134-145
16156662-0	2005	Role of the hexapeptide disulfide loop in the gamma-carboxyglutamic acid domain of protein C in Ca2+-mediated structural and functional properties.	Disulfides	24-33	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	83-92
31843260-6	2020	We extend these findings by demonstrating the oxidation of free thiols on the ectodomain of hTLR4, after exposure to LPS or hyperoxia suggesting that the cysteines on the ectodomain of TLR4 could form intra- or intermolecular disulfide bonds.	Disulfides	226-235	toll like receptor 4	Homo sapiens	92-97
16166313-4	2005	In this study, we provide evidence that eukaryotically expressed His-tagged human K5 cDNA (hK5His) is exported extracellularly and maintains predicted disulfide bridging conformation in solution.	Disulfides	151-160	keratin 5	Homo sapiens	82-84
16142898-6	2005	Finally, native PRL-1 is crystallized in an oxidized form in which a disulfide is formed between the active site Cys104 and a neighboring residue Cys49, which blocks both substrate binding and catalysis.	Disulfides	69-78	protein tyrosine phosphatase 4A1	Homo sapiens	16-21
31843260-6	2020	We extend these findings by demonstrating the oxidation of free thiols on the ectodomain of hTLR4, after exposure to LPS or hyperoxia suggesting that the cysteines on the ectodomain of TLR4 could form intra- or intermolecular disulfide bonds.	Disulfides	226-235	toll like receptor 4	Homo sapiens	93-97
16014632-7	2005	Chemical shift perturbation analysis of the disulfide ubiquitin-Ubc1 complex by NMR spectroscopy reveals an ubiquitin-Ubc1 interface similar to that for the ubiquitin-E2 thioester.	Disulfides	44-53	E2 ubiquitin-conjugating protein UBC1	Saccharomyces cerevisiae S288C	64-68
32734105-3	2020	Dithiothreitol (DTT) is a typical disulfide reductant that is used as a substrate for in vitro VKOR assays.	Disulfides	34-43	vitamin K epoxide reductase complex subunit 1	Homo sapiens	95-99
16014632-7	2005	Chemical shift perturbation analysis of the disulfide ubiquitin-Ubc1 complex by NMR spectroscopy reveals an ubiquitin-Ubc1 interface similar to that for the ubiquitin-E2 thioester.	Disulfides	44-53	E2 ubiquitin-conjugating protein UBC1	Saccharomyces cerevisiae S288C	118-122
16014632-8	2005	In addition to the typical E2 catalytic domain, Ubc1 contains an ubiquitin-associated (UBA) domain, and we have utilized NMR spectroscopy to demonstrate that in this disulfide complex the UBA domain is freely accessible to non-covalently bind a second molecule of ubiquitin.	Disulfides	166-175	E2 ubiquitin-conjugating protein UBC1	Saccharomyces cerevisiae S288C	48-52
16014909-4	2005	The A21 protein contained two intramolecular disulfide bonds, the formation of which required the vaccinia virus-encoded cytoplasmic redox pathway, and was localized on the surface of the lipoprotein membrane of intracellular mature virions.	Disulfides	45-54	immunoglobulin kappa variable 2-26 (pseudogene)	Homo sapiens	4-7
31901894-9	2020	Furthermore, substitution of multiple cysteine residues of the NOTCH3 N-terminus activated proteolytic release of the first EGF-like repeat, suggesting that elimination of multiple disulfide bonds in NOTCH3 accelerates its fragmentation.	Disulfides	181-190	notch receptor 3	Homo sapiens	63-69
31901894-9	2020	Furthermore, substitution of multiple cysteine residues of the NOTCH3 N-terminus activated proteolytic release of the first EGF-like repeat, suggesting that elimination of multiple disulfide bonds in NOTCH3 accelerates its fragmentation.	Disulfides	181-190	notch receptor 3	Homo sapiens	200-206
31774080-0	2020	Time-resolved FTIR study on the structural switching of human galectin-1 by light-induced disulfide bond formation.	Disulfides	90-99	galectin 1	Homo sapiens	62-72
16008417-3	2005	1H and 31P NMR spectra following the addition of smaller amounts (&lt; 5 equiv moles) of PPh3 indicate that the reaction liberates a AuISC2Ph complex, as opposed to a SC2Ph thiol, disulfide, or anion.	Disulfides	180-189	protein phosphatase 4 catalytic subunit	Homo sapiens	89-93
15998246-0	2005	The S-thiolating activity of membrane gamma-glutamyltransferase: formation of cysteinyl-glycine mixed disulfides with cellular proteins and in the cell microenvironment.	Disulfides	102-112	gamma-glutamyltransferase light chain family member 3	Homo sapiens	38-63
15998246-4	2005	With cells presenting high levels of GGT expression, basal levels of CG-containing protein mixed disulfides are detectable, in cellular proteins, as well as in proteins of the culture medium.	Disulfides	97-107	gamma-glutamyltransferase light chain family member 3	Homo sapiens	37-40
15998246-5	2005	Stimulation of GGT activity in these cells by administration of substrates results in an increase of CG mixed disulfide formation and a concomitant decrease of GSH-containing disulfides, likely due to GGT-dependent removal of GSH from the system.	Disulfides	110-119	gamma-glutamyltransferase light chain family member 3	Homo sapiens	15-18
15998246-5	2005	Stimulation of GGT activity in these cells by administration of substrates results in an increase of CG mixed disulfide formation and a concomitant decrease of GSH-containing disulfides, likely due to GGT-dependent removal of GSH from the system.	Disulfides	110-119	gamma-glutamyltransferase light chain family member 3	Homo sapiens	201-204
15998246-5	2005	Stimulation of GGT activity in these cells by administration of substrates results in an increase of CG mixed disulfide formation and a concomitant decrease of GSH-containing disulfides, likely due to GGT-dependent removal of GSH from the system.	Disulfides	175-185	gamma-glutamyltransferase light chain family member 3	Homo sapiens	15-18
15998246-5	2005	Stimulation of GGT activity in these cells by administration of substrates results in an increase of CG mixed disulfide formation and a concomitant decrease of GSH-containing disulfides, likely due to GGT-dependent removal of GSH from the system.	Disulfides	175-185	gamma-glutamyltransferase light chain family member 3	Homo sapiens	201-204
16321931-5	2005	Overproduction of the E. coli disulfide bond isomerase DsbC, TrbB(F), DsbC(R27), or HtdT(R27), but not TraF(F) or TrhF(R27), reverses this hypersensitivity to DTT.	Disulfides	30-39	F pilus assembly periplasmic protein TrbB	Escherichia coli	61-65
16321931-9	2005	Our results indicate that TrbB(F), DsbC(R27), and HtdT(R27) are putative disulfide bond isomerases for their respective transfer systems.	Disulfides	73-82	F pilus assembly periplasmic protein TrbB	Escherichia coli	26-30
31774080-2	2020	Human galectin-1 (hGal-1), which is a lectin protein, exemplifies how both structure and function are changed by disulfide bonds; the structure and sugar-binding ability of hGal-1 are altered by the formation and cleavage of its three intra-molecular disulfide bonds.	Disulfides	113-122	galectin 1	Homo sapiens	6-16
15989945-1	2005	In this issue of Cell, show that there is a disulfide relay system in the intermembrane space (IMS) of mitochondria that is comprised of the proteins Mia40 and Erv1.	Disulfides	44-53	growth factor, augmenter of liver regeneration	Homo sapiens	160-164
31774080-2	2020	Human galectin-1 (hGal-1), which is a lectin protein, exemplifies how both structure and function are changed by disulfide bonds; the structure and sugar-binding ability of hGal-1 are altered by the formation and cleavage of its three intra-molecular disulfide bonds.	Disulfides	113-122	galectin 1	Homo sapiens	18-24
15989945-5	2005	The reduced Mia40 generated is then reoxidized by the sulfhydryl oxidase Erv1, promoting the next round of disulfide exchange.	Disulfides	107-116	growth factor, augmenter of liver regeneration	Homo sapiens	73-77
31774080-2	2020	Human galectin-1 (hGal-1), which is a lectin protein, exemplifies how both structure and function are changed by disulfide bonds; the structure and sugar-binding ability of hGal-1 are altered by the formation and cleavage of its three intra-molecular disulfide bonds.	Disulfides	113-122	galectin 1	Homo sapiens	173-179
31774080-2	2020	Human galectin-1 (hGal-1), which is a lectin protein, exemplifies how both structure and function are changed by disulfide bonds; the structure and sugar-binding ability of hGal-1 are altered by the formation and cleavage of its three intra-molecular disulfide bonds.	Disulfides	251-260	galectin 1	Homo sapiens	6-16
31774080-2	2020	Human galectin-1 (hGal-1), which is a lectin protein, exemplifies how both structure and function are changed by disulfide bonds; the structure and sugar-binding ability of hGal-1 are altered by the formation and cleavage of its three intra-molecular disulfide bonds.	Disulfides	251-260	galectin 1	Homo sapiens	18-24
15994775-5	2005	In this construct, the gp120 and gp41 moieties are covalently linked by an intermolecular disulfide bond (SOS gp140), and an I559P substitution has been added to stabilize gp41-gp41 interactions (SOSIP gp140).	Disulfides	90-99	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	23-28
31774080-2	2020	Human galectin-1 (hGal-1), which is a lectin protein, exemplifies how both structure and function are changed by disulfide bonds; the structure and sugar-binding ability of hGal-1 are altered by the formation and cleavage of its three intra-molecular disulfide bonds.	Disulfides	251-260	galectin 1	Homo sapiens	173-179
31774080-3	2020	In the present study, the dynamics of the structural change of hGal-1 by the formation of disulfide bonds were investigated by time-resolved FTIR spectroscopy combined with a modification in which its thiol groups (-SH) were replaced with S-nitrosylated groups (SNO).	Disulfides	90-99	galectin 1	Homo sapiens	63-69
16279788-2	2005	Urotensin II (U-II) is a disulfide bridged peptide hormone recently identified as the ligand of a G-protein-coupled receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	0-12
31774080-4	2020	Photodissociation of NO from SNO in reduced hGal-1 induced disulfide bond formation and transformed it into the oxidised form.	Disulfides	59-68	galectin 1	Homo sapiens	44-50
31774080-6	2020	In an examination of hGal-1 in the lactose-bound form, structural changes owing to the release of substrate lactose were also observed upon disulfide bond formation.	Disulfides	140-149	galectin 1	Homo sapiens	21-27
16104002-3	2005	This review focuses on electron microscopic evidence (1) that facilitated the identification of amino acid residues within 3-repeat Tau that promote PHF formation; and (2) provided experimental evidence for the polymerization of S-glutathionylated three-repeat Tau, a reaction that unambiguously demonstrates that disulfide-linked Tau-S-S-Tau dimer formation is not a compulsory step in filament assembly.	Disulfides	314-323	microtubule associated protein tau	Homo sapiens	132-135
31870540-3	2020	Here, a gap-closed variant of human intestinal fatty acid binding protein was generated by mutagenesis, in which the gap is locked by a disulfide bridge.	Disulfides	136-145	glutamic-oxaloacetic transaminase 2	Homo sapiens	47-73
16104002-3	2005	This review focuses on electron microscopic evidence (1) that facilitated the identification of amino acid residues within 3-repeat Tau that promote PHF formation; and (2) provided experimental evidence for the polymerization of S-glutathionylated three-repeat Tau, a reaction that unambiguously demonstrates that disulfide-linked Tau-S-S-Tau dimer formation is not a compulsory step in filament assembly.	Disulfides	314-323	microtubule associated protein tau	Homo sapiens	261-264
16104002-3	2005	This review focuses on electron microscopic evidence (1) that facilitated the identification of amino acid residues within 3-repeat Tau that promote PHF formation; and (2) provided experimental evidence for the polymerization of S-glutathionylated three-repeat Tau, a reaction that unambiguously demonstrates that disulfide-linked Tau-S-S-Tau dimer formation is not a compulsory step in filament assembly.	Disulfides	314-323	microtubule associated protein tau	Homo sapiens	261-264
16104002-3	2005	This review focuses on electron microscopic evidence (1) that facilitated the identification of amino acid residues within 3-repeat Tau that promote PHF formation; and (2) provided experimental evidence for the polymerization of S-glutathionylated three-repeat Tau, a reaction that unambiguously demonstrates that disulfide-linked Tau-S-S-Tau dimer formation is not a compulsory step in filament assembly.	Disulfides	314-323	microtubule associated protein tau	Homo sapiens	261-264
32064171-5	2020	We have previously reported that a conserved cysteine in the MXXCW motif of RET is crucial to the disulfide-bonded dimerization-linked activation of RET kinases.	Disulfides	98-107	ret proto-oncogene	Homo sapiens	76-79
15976011-2	2005	The available commercial yeast display vector pYD1 (Invitrogen) displays the protein of interest flanked on the N-terminus by Aga2, the disulfide of which binds the myristylated surface membrane protein Aga1.	Disulfides	136-145	Aga1p	Saccharomyces cerevisiae S288C	203-207
16279788-2	2005	Urotensin II (U-II) is a disulfide bridged peptide hormone recently identified as the ligand of a G-protein-coupled receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	14-18
16274250-1	2005	The structure of human epidermal growth factor (EGF, 53 amino acids) comprises three distinct loops (A, B, and C) connected correspondingly by the three native disulfide bonds, Cys(6)-Cys(20), Cys(14)-Cys(31), and Cys(33)-Cys(42).	Disulfides	160-169	epidermal growth factor	Homo sapiens	23-46
16274250-1	2005	The structure of human epidermal growth factor (EGF, 53 amino acids) comprises three distinct loops (A, B, and C) connected correspondingly by the three native disulfide bonds, Cys(6)-Cys(20), Cys(14)-Cys(31), and Cys(33)-Cys(42).	Disulfides	160-169	epidermal growth factor	Homo sapiens	48-51
15966724-0	2005	Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural modeling.	Disulfides	20-29	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	45-89
15966724-0	2005	Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural modeling.	Disulfides	20-29	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	91-99
32064171-5	2020	We have previously reported that a conserved cysteine in the MXXCW motif of RET is crucial to the disulfide-bonded dimerization-linked activation of RET kinases.	Disulfides	98-107	ret proto-oncogene	Homo sapiens	149-152
15966724-2	2005	To investigate disulfide structure in human NTPDase3, we made single and double mutants of these 10 cysteines, and analyzed their enzymatic activity, glycosylation pattern, trafficking to the cell membrane, and sensitivity to reduction.	Disulfides	15-24	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	44-52
32064171-6	2020	Reagents which bind to this cysteine may inhibit the activity of RET kinases through disulfide-bond mediated dimerization.	Disulfides	85-94	ret proto-oncogene	Homo sapiens	65-68
15966724-10	2005	The resultant theoretical 3-D model of the extracellular portion of NTPDase3, based on homology with this exopolyphosphatase, is consistent with the assignment of the disulfide bonds occurring in regions of good fold similarity between NTPDase3 and the exopolyphosphatase.	Disulfides	167-176	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	68-76
15966724-10	2005	The resultant theoretical 3-D model of the extracellular portion of NTPDase3, based on homology with this exopolyphosphatase, is consistent with the assignment of the disulfide bonds occurring in regions of good fold similarity between NTPDase3 and the exopolyphosphatase.	Disulfides	167-176	ectonucleoside triphosphate diphosphohydrolase 3	Homo sapiens	236-244
31644305-1	2020	The anterior gradient-2 (AGR2) is an endoplasmic reticulum (ER)-resident protein belonging to the protein disulfide isomerase family that mediates the formation of disulfide bonds and assists the protein quality control in the ER.	Disulfides	106-115	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	4-23
16356134-1	2005	Thioredoxin (Trx) is a redox-active protein that has been shown to regulate various cellular processes due to its thiol-disulfide exchange reaction.	Disulfides	120-129	thioredoxin	Homo sapiens	0-11
16356134-1	2005	Thioredoxin (Trx) is a redox-active protein that has been shown to regulate various cellular processes due to its thiol-disulfide exchange reaction.	Disulfides	120-129	thioredoxin	Homo sapiens	13-16
16026256-5	2005	However, our structural analysis revealed that the axonal regeneration-promoting factor exists as an oxidized form of galectin-1, containing three intramolecular disulfide bonds.	Disulfides	162-171	galectin 1	Homo sapiens	118-128
31644305-1	2020	The anterior gradient-2 (AGR2) is an endoplasmic reticulum (ER)-resident protein belonging to the protein disulfide isomerase family that mediates the formation of disulfide bonds and assists the protein quality control in the ER.	Disulfides	106-115	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	25-29
16026256-11	2005	Disulfide bond formation alters the structure of galectin-1, so as to confer the novel ability to promote axonal regeneration.	Disulfides	0-9	galectin 1	Homo sapiens	49-59
31644305-1	2020	The anterior gradient-2 (AGR2) is an endoplasmic reticulum (ER)-resident protein belonging to the protein disulfide isomerase family that mediates the formation of disulfide bonds and assists the protein quality control in the ER.	Disulfides	164-173	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	4-23
16307478-6	2005	For the catalytic cycle of TPx1, we conclude that oxidation of the peroxidatic Cys50 by the oxidising substrate is followed by the formation of an intermolecular disulfide bond between Cys50 and Cys170" of the second subunit, which is then attacked by an external electron donor such as thioredoxin or plasmoredoxin.	Disulfides	162-171	thioredoxin	Homo sapiens	287-298
31644305-1	2020	The anterior gradient-2 (AGR2) is an endoplasmic reticulum (ER)-resident protein belonging to the protein disulfide isomerase family that mediates the formation of disulfide bonds and assists the protein quality control in the ER.	Disulfides	164-173	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	25-29
31631329-6	2020	We identified that the disulfide bridge formation within the antibody light chain (LC) was impaired due to less recognition by protein disulfide isomerase (PDI).	Disulfides	23-32	protein disulfide-isomerase	Cricetulus griseus	127-154
16186819-4	2005	The THBS2 signature domain is stabilized by these interactions and by a network of 30 bound Ca(2+) ions and 18 disulfide bonds.	Disulfides	111-120	thrombospondin 2	Homo sapiens	4-9
15950652-13	2005	CONCLUSION(S): [1] Proacrosin interacts with mannose residues through binding sites located at both the N- and C-terminal portion of the protein, [2] the full-length protein is required for maximal BSA-mannose binding, and [3] binding sites are stabilized by noncovalent bonds and by disulfide linkages.	Disulfides	284-293	acrosin	Homo sapiens	19-29
31631329-6	2020	We identified that the disulfide bridge formation within the antibody light chain (LC) was impaired due to less recognition by protein disulfide isomerase (PDI).	Disulfides	23-32	protein disulfide-isomerase	Cricetulus griseus	156-159
31727740-0	2019	Roseltide rT7 is a disulfide-rich, anionic, and cell-penetrating peptide that inhibits proteasomal degradation.	Disulfides	19-28	protein tyrosine phosphatase, receptor type, C	Rattus norvegicus	10-13
15521073-1	2005	Thioredoxin reductase (TrxR) is a selenoprotein that catalyzes the reduction of the active site disulfide of thioredoxin (Trx), which regulates the redox status of the cells.	Disulfides	96-105	peroxiredoxin 5	Homo sapiens	0-21
15521073-1	2005	Thioredoxin reductase (TrxR) is a selenoprotein that catalyzes the reduction of the active site disulfide of thioredoxin (Trx), which regulates the redox status of the cells.	Disulfides	96-105	peroxiredoxin 5	Homo sapiens	23-27
15521073-1	2005	Thioredoxin reductase (TrxR) is a selenoprotein that catalyzes the reduction of the active site disulfide of thioredoxin (Trx), which regulates the redox status of the cells.	Disulfides	96-105	thioredoxin	Homo sapiens	109-120
15967877-8	2005	Although oxidation of PTEN by H2O2 led to formation of an intramolecular disulfide, oxidation of PTEN by CSNO seemed to lead to formation of a mixed disulfide.	Disulfides	73-82	phosphatase and tensin homolog	Homo sapiens	22-26
15967877-8	2005	Although oxidation of PTEN by H2O2 led to formation of an intramolecular disulfide, oxidation of PTEN by CSNO seemed to lead to formation of a mixed disulfide.	Disulfides	149-158	phosphatase and tensin homolog	Homo sapiens	97-101
15521073-1	2005	Thioredoxin reductase (TrxR) is a selenoprotein that catalyzes the reduction of the active site disulfide of thioredoxin (Trx), which regulates the redox status of the cells.	Disulfides	96-105	thioredoxin	Homo sapiens	23-26
31727740-3	2019	Here, we report the discovery of an anionic, 34-residue peptide, the disulfide-rich roseltide rT7 from Hibiscus sabdariffa (of the Malvaceae family) that penetrates cells and inhibits their proteasomal activities.	Disulfides	69-78	protein tyrosine phosphatase, receptor type, C	Rattus norvegicus	94-97
15854654-5	2005	The cyclic nature due to a disulfide bridge between Cys1 and Cys6 of vasopressin provides structural rigidity to the peptide hormone.	Disulfides	27-36	cystin 1	Homo sapiens	52-56
31796585-3	2019	Bimolecular fluorescence complementation and deep mutational scanning reveal that TAPBPR recognition is polarized toward the alpha2 domain of the peptide-binding groove, and depends on the formation of a conserved MHC-I disulfide epitope in the alpha2 domain.	Disulfides	220-229	TAP binding protein like	Homo sapiens	82-88
15862136-0	2005	[Expression, purification, and characterization of single-chain disulfide-bond Fv (ScdsFv) antibody fused with targeted superantigen SEA (D227A)].	Disulfides	64-73	S13 erythroblastosis (avian) oncogene homolog	Homo sapiens	133-136
16114871-2	2005	PANDER has the predicted secondary structure of 4 alpha-helical bundles with an up-up-down-down topology, and two disulfide bonds.	Disulfides	114-123	FAM3 metabolism regulating signaling molecule B	Mus musculus	0-6
16114871-10	2005	The third and fourth cysteines of PANDER, C91 and C229, were shown to form one disulfide bond and be functionally important.	Disulfides	79-88	FAM3 metabolism regulating signaling molecule B	Mus musculus	34-40
16114871-12	2005	Hence, helices B and C and the second disulfide bond of PANDER are essential for PANDER-induced beta-cell death.	Disulfides	38-47	FAM3 metabolism regulating signaling molecule B	Mus musculus	56-62
16114871-12	2005	Hence, helices B and C and the second disulfide bond of PANDER are essential for PANDER-induced beta-cell death.	Disulfides	38-47	FAM3 metabolism regulating signaling molecule B	Mus musculus	81-87
15823038-7	2005	Since previous studies have shown that N-glycan-bound calnexin/calreticulin are also capable of recruiting ERp57, our results suggest that N-linked glycosylation and RAP can independently and cooperatively recruit oxidoreductases to facilitate protein folding and proper disulfide bond formation.	Disulfides	271-280	LDL receptor related protein associated protein 1	Homo sapiens	166-169
31796585-6	2019	Consistently, restriction of MHC-I groove plasticity through the introduction of a disulfide bond between the alpha1/alpha2 helices abrogates TAPBPR binding, both in solution and on a cellular membrane, while intracellular binding is tolerant of many destabilizing MHC-I substitutions.	Disulfides	83-92	TAP binding protein like	Homo sapiens	142-148
31580947-1	2019	Peroxiredoxins (Prxs), scavenge cellular peroxides by forming recyclable disulfides but under high oxidative stress, hyperoxidation of their active-site Cys residue results in loss of their peroxidase activity.	Disulfides	73-83	peroxiredoxin 1	Homo sapiens	0-14
15705573-8	2005	We propose that the role of C(H)1 cysteines in immunoglobulin assembly and secretion is not simply to engage in disulfide bridges, but to direct proper folding and interact with the retention machinery.	Disulfides	112-121	SUN domain containing ossification factor	Homo sapiens	28-33
16182193-3	2005	This could enable PDI to reduce gp120 disulfide bonds, which triggers the major conformational changes in gp120 and gp41 required for virus entry.	Disulfides	38-47	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	32-37
16182193-3	2005	This could enable PDI to reduce gp120 disulfide bonds, which triggers the major conformational changes in gp120 and gp41 required for virus entry.	Disulfides	38-47	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	106-111
16008365-0	2005	Structure-activity relation of human beta-defensin 3: influence of disulfide bonds and cysteine substitution on antimicrobial activity and cytotoxicity.	Disulfides	67-76	defensin beta 103B	Homo sapiens	37-52
16008365-6	2005	We have established a structure-activity relation of the hBD-3 using synthetic derivatives differing in length, charge, disulfide connectivity, and overall hydrophobicity.	Disulfides	120-129	defensin beta 103B	Homo sapiens	57-62
15695804-1	2005	Protein disulfide isomerase (PDI) functions as an isomerase to catalyze thiol:disulfide exchange, as a chaperone to assist protein folding, and as a subunit of prolyl-4-hydroxylase and microsomal triglyceride transfer protein.	Disulfides	8-17	protein disulfide-isomerase	Oryctolagus cuniculus	29-32
31580947-5	2019	We found that hPrxI in yeast exists as a mixture of disulfide-linked dimer and reduced monomer but becomes hyperoxidized upon elevated oxidative stress as analyzed under denaturing conditions (SDS-PAGE).	Disulfides	52-61	peroxiredoxin 1	Homo sapiens	14-19
15695804-2	2005	At a lower concentration of 0.2 microm, PDI facilitated the aggregation of unfolded rabbit muscle creatine kinase (CK) and exhibited anti-chaperone activity, which was shown to be mainly due to the hydrophobic interactions between PDI and CK and was independent of the cross-linking of disulfide bonds.	Disulfides	286-295	protein disulfide-isomerase	Oryctolagus cuniculus	40-43
31436131-3	2019	RESULTS: The data show that AGR2 is induced in esophageal adenocarcinoma, where it participates in redox responsive, disulfide-dependent complexes.	Disulfides	117-126	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	28-32
15695804-2	2005	At a lower concentration of 0.2 microm, PDI facilitated the aggregation of unfolded rabbit muscle creatine kinase (CK) and exhibited anti-chaperone activity, which was shown to be mainly due to the hydrophobic interactions between PDI and CK and was independent of the cross-linking of disulfide bonds.	Disulfides	286-295	protein disulfide-isomerase	Oryctolagus cuniculus	231-234
15695804-4	2005	The inhibition effect of PDI on CK reactivation was further characterized as due to the formation of PDI-CK complexes through intermolecular disulfide bonds, a process involving Cys-36 and Cys-295 of PDI.	Disulfides	141-150	protein disulfide-isomerase	Oryctolagus cuniculus	25-28
15695804-4	2005	The inhibition effect of PDI on CK reactivation was further characterized as due to the formation of PDI-CK complexes through intermolecular disulfide bonds, a process involving Cys-36 and Cys-295 of PDI.	Disulfides	141-150	protein disulfide-isomerase	Oryctolagus cuniculus	101-104
15695804-4	2005	The inhibition effect of PDI on CK reactivation was further characterized as due to the formation of PDI-CK complexes through intermolecular disulfide bonds, a process involving Cys-36 and Cys-295 of PDI.	Disulfides	141-150	protein disulfide-isomerase	Oryctolagus cuniculus	101-104
15695804-5	2005	Two disulfide-linked complexes containing both PDI and CK were obtained, and the large, soluble aggregates around 400 kDa were composed of 1 molecule of tetrameric PDI and 2 molecules of inactive intermediate dimeric CK, whereas the smaller one, around 200 kDa, was formed by 1 dimeric PDI and 1 dimeric CK.	Disulfides	4-13	protein disulfide-isomerase	Oryctolagus cuniculus	47-50
16130044-8	2005	It is likely that the oxidative cleavage of disulfide bonds between cuticle-constituting proteins, including S100A3, results in the fragile property of cuticles.	Disulfides	44-53	S100 calcium binding protein A3	Homo sapiens	109-115
31436131-7	2019	Disulfide-driven AGR2 complex formation provides a framework for a limited number of client proteins to interact, rather than for the recruitment of multiple novel clients.	Disulfides	0-9	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	17-21
15910735-4	2005	The r(alpha)2M species demonstrated intact structure and function, as determined by subunit size, intersubunit disulfide bonds, reaction with trypsin or methylamine, and ability to undergo conformational change.	Disulfides	111-120	alpha-2-macroglobulin	Homo sapiens	4-14
15769469-9	2005	The interchain disulfide bond in the Fab fragment plays an essential role in this stabilization.	Disulfides	15-24	FA complementation group B	Homo sapiens	37-40
16511049-1	2005	Thioredoxin reductase 1 (Trr1) from Saccharomyces cerevisiae is a member of the family of pyridine nucleotide-disulfide oxidoreductases capable of reducing the redox-active disulfide bond of the cytosolic thioredoxin 1 (Trx1) and thioredoxin 2 (Trx2).	Disulfides	110-119	thioredoxin-disulfide reductase TRR1	Saccharomyces cerevisiae S288C	0-23
16511049-1	2005	Thioredoxin reductase 1 (Trr1) from Saccharomyces cerevisiae is a member of the family of pyridine nucleotide-disulfide oxidoreductases capable of reducing the redox-active disulfide bond of the cytosolic thioredoxin 1 (Trx1) and thioredoxin 2 (Trx2).	Disulfides	110-119	thioredoxin-disulfide reductase TRR1	Saccharomyces cerevisiae S288C	25-29
31557263-2	2019	Here we demonstrate that the so far unexplored Trx2 from African trypanosomes (Trypanosoma brucei) lacks protein disulfide reductase activity but functions as an effective temperature-activated and redox-regulated chaperone.	Disulfides	113-122	thioredoxin 2	Mus musculus	47-51
16511049-1	2005	Thioredoxin reductase 1 (Trr1) from Saccharomyces cerevisiae is a member of the family of pyridine nucleotide-disulfide oxidoreductases capable of reducing the redox-active disulfide bond of the cytosolic thioredoxin 1 (Trx1) and thioredoxin 2 (Trx2).	Disulfides	110-119	thioredoxin TRX1	Saccharomyces cerevisiae S288C	220-224
16511049-2	2005	NADPH, Trr1 and Trx1 (or Trx2) comprise the thioredoxin system, which is involved in several biological processes, including the reduction of disulfide bonds and response to oxidative stress.	Disulfides	142-151	thioredoxin-disulfide reductase TRR1	Saccharomyces cerevisiae S288C	7-11
16511049-2	2005	NADPH, Trr1 and Trx1 (or Trx2) comprise the thioredoxin system, which is involved in several biological processes, including the reduction of disulfide bonds and response to oxidative stress.	Disulfides	142-151	thioredoxin TRX1	Saccharomyces cerevisiae S288C	16-20
31262730-5	2019	IL-2 fragments produced after cleavage by MMP-9 remained linked by a disulfide bond and displayed a reduced affinity for all IL-2 receptor subunits and a distinct pattern and timing of signal transduction.	Disulfides	69-78	interleukin 2	Mus musculus	0-4
30762293-6	2019	In response to extracellular signals, conformational changes in the p75NTR extracellular domain (ECD) propagate to the p75NTR -DD through the disulfide-bonded transmembrane domain (TMD) and destabilize the p75NTR -DD homodimer, leading to protomer separation and exposure of binding sites on the DD surface.	Disulfides	142-151	nerve growth factor receptor	Homo sapiens	68-74
15664984-0	2005	Paired cysteine mutagenesis to establish the pattern of disulfide bonds in the functional intact secretin receptor.	Disulfides	56-65	secretin receptor	Homo sapiens	97-114
15664984-3	2005	In the present study, we determined the disulfide bonding pattern of the prototypic class B secretin receptor by applying the same paired cysteine mutagenesis approach and confirming the predicted bonding pattern with proteolytic cleavage of intact functional receptor.	Disulfides	40-49	secretin receptor	Homo sapiens	92-109
16019431-0	2005	The role of disulfide bonds in the structure and function of murine epidermal growth factor (mEGF).	Disulfides	12-21	epidermal growth factor	Mus musculus	93-97
16019431-1	2005	A systematic study using solid phase peptide synthesis has been undertaken to examine the role of the disulfide bonds in the structure and function of mEGF.	Disulfides	102-111	epidermal growth factor	Mus musculus	151-155
30762293-6	2019	In response to extracellular signals, conformational changes in the p75NTR extracellular domain (ECD) propagate to the p75NTR -DD through the disulfide-bonded transmembrane domain (TMD) and destabilize the p75NTR -DD homodimer, leading to protomer separation and exposure of binding sites on the DD surface.	Disulfides	142-151	nerve growth factor receptor	Homo sapiens	119-125
15644496-2	2005	The triggering of fusion requires cleavage of two of the nine disulfide bonds of gp120 by a cell-surface protein disulfide-isomerase (PDI).	Disulfides	62-71	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	81-86
30762293-6	2019	In response to extracellular signals, conformational changes in the p75NTR extracellular domain (ECD) propagate to the p75NTR -DD through the disulfide-bonded transmembrane domain (TMD) and destabilize the p75NTR -DD homodimer, leading to protomer separation and exposure of binding sites on the DD surface.	Disulfides	142-151	nerve growth factor receptor	Homo sapiens	119-125
15930008-3	2005	These enzymes transfer oxidizing potential to the proteins PDI or DsbA, which are responsible for directly introducing disulfide bonds into substrate proteins during oxidative protein folding in eukaryotes and prokaryotes, respectively.	Disulfides	119-128	peptidyl arginine deiminase 1	Homo sapiens	59-62
31085461-5	2019	Importantly, DOX@CCSP exhibited low drug leakage and negligible cytotoxicity in non-reductive physiological environment, while it showed rapid release and high cytotoxicity in reductive tumorous environment via the breakage of disulfide bond.	Disulfides	227-236	secretoglobin family 1A member 1	Homo sapiens	17-21
15850387-13	2005	We used PEG-mal to map the localizations of the seven free sulfhydryls and the disulfide bond of hACAT1 present in microsomal vesicles.	Disulfides	79-88	acetyl-CoA acetyltransferase 1	Homo sapiens	97-103
15741335-0	2005	Deamidation and disulfide bridge formation in human calbindin D28k with effects on calcium binding.	Disulfides	16-25	calbindin 1	Homo sapiens	52-61
15736947-7	2005	The crystal structure of the ligand free and the active site inhibitor-MJ33 bound forms of PLA2 engineered to have the disulfide bonding pattern of group-X (eng-X) are also reported and compared with the structure of group-IB and human group-X PLA2.	Disulfides	119-128	endoglin	Homo sapiens	96-99
31138621-4	2019	The outer active site, the inner active site, and a long-range noncatalytic disulfide bond are required for AtERO1"s function.	Disulfides	76-85	endoplasmic reticulum oxidoreductins 1	Arabidopsis thaliana	108-114
15706081-3	2005	A glutathione peroxidase-like protein, Gpx3, which has peroxiredoxin activity, is required for formation of the disulfide bond in Yap1.	Disulfides	112-121	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	39-43
31138621-7	2019	In vivo, both AtERO1 and AtERO2 have two distinct oxidized isoforms (Ox1 and Ox2), which are determined by the formation or breakage of the putative regulatory disulfide.	Disulfides	160-169	endoplasmic reticulum oxidoreductins 1	Arabidopsis thaliana	14-20
31082439-5	2019	This domain forms a novel 10-stranded beta-sandwich fold that includes a set of three conserved disulfide bonds, denoted the "SARAF-fold."	Disulfides	96-105	store-operated calcium entry associated regulatory factor	Homo sapiens	126-131
15641771-2	2005	Human apo A-II is distinguished from most other species by a single cysteine (Cys6), which forms a disulfide bond with other cysteine-containing apos.	Disulfides	99-108	apolipoprotein A2	Homo sapiens	6-14
15641771-3	2005	In human plasma, nearly all apo A-II occurs as disulfide-linked homodimers of 17.4 kDa.	Disulfides	47-56	apolipoprotein A2	Homo sapiens	28-36
15956686-2	2005	Like human relaxin-1 and relaxin-2, relaxin-3 is predicted to consist of a two-chain structure and three disulfide bonds in a disposition identical to that of insulin.	Disulfides	105-114	relaxin 3	Homo sapiens	36-45
15956686-4	2005	In contrast to human relaxin-1 and relaxin-2, however, relaxin-3 could not be successfully prepared by simple combination of the individual chains, thus necessitating recourse to the use of a regioselective disulfide bond formation strategy.	Disulfides	207-216	relaxin 3	Homo sapiens	55-64
15956686-5	2005	Solid phase synthesis of the separate, selectively S-protected A and B chains followed by their purification and the subsequent stepwise formation of each of the three disulfides led to the successful acquisition of human relaxin-3.	Disulfides	168-178	relaxin 3	Homo sapiens	222-231
15956687-1	2005	Relaxin-3 (R3) is the latest member of the insulin (INSL) superfamily, which is composed of peptides with diverse sequences held together by characteristic disulfide links connecting A and B peptide chains.	Disulfides	156-165	relaxin 3	Rattus norvegicus	0-13
15890022-7	2005	Third, ROS-mediated oxidation of the Cdc25s leads to an intramolecular disulfide that is readily reversible by the cellular reductant thioredoxin.	Disulfides	71-80	cell division cycle 25C	Homo sapiens	37-42
31095380-4	2019	In each cluster, and also in a particular disulfide bond isoform, an estimation of the amino acid block loadings toward PC1 and PC2 helps relate the mutations in the GI sequence to targeted synthesis of a given isoform in a given solvent system.	Disulfides	42-51	polycystin 1, transient receptor potential channel interacting	Homo sapiens	120-123
15567420-5	2005	From comparison of the 8-Cys3(LTBP-1) structure with that of the non-TGF-beta-binding 8-Cys6(fibrillin-1), we observed that a two-residue insertion in 8-Cys3(LTBP-1) increased the potential for disulfide exchange of the 2-6 disulfide bond.	Disulfides	194-203	latent transforming growth factor beta binding protein 1	Homo sapiens	30-36
15567420-5	2005	From comparison of the 8-Cys3(LTBP-1) structure with that of the non-TGF-beta-binding 8-Cys6(fibrillin-1), we observed that a two-residue insertion in 8-Cys3(LTBP-1) increased the potential for disulfide exchange of the 2-6 disulfide bond.	Disulfides	194-203	latent transforming growth factor beta binding protein 1	Homo sapiens	158-164
15567420-5	2005	From comparison of the 8-Cys3(LTBP-1) structure with that of the non-TGF-beta-binding 8-Cys6(fibrillin-1), we observed that a two-residue insertion in 8-Cys3(LTBP-1) increased the potential for disulfide exchange of the 2-6 disulfide bond.	Disulfides	224-233	latent transforming growth factor beta binding protein 1	Homo sapiens	30-36
15567420-5	2005	From comparison of the 8-Cys3(LTBP-1) structure with that of the non-TGF-beta-binding 8-Cys6(fibrillin-1), we observed that a two-residue insertion in 8-Cys3(LTBP-1) increased the potential for disulfide exchange of the 2-6 disulfide bond.	Disulfides	224-233	latent transforming growth factor beta binding protein 1	Homo sapiens	158-164
31095380-4	2019	In each cluster, and also in a particular disulfide bond isoform, an estimation of the amino acid block loadings toward PC1 and PC2 helps relate the mutations in the GI sequence to targeted synthesis of a given isoform in a given solvent system.	Disulfides	42-51	chromobox 4	Homo sapiens	128-131
30381731-8	2019	Both of LEAP-2 peptides efficiently killed bacteria, although the disulfide-type LEAP-2 showed more powerful bactericidal activity.	Disulfides	66-75	LEAP2	Anas platyrhynchos	81-87
15650396-4	2005	Thioredoxin (TRX), a key redox molecule, plays crucial roles as an antioxidant and a catalyst in protein disulfide/dithiol exchange.	Disulfides	105-114	thioredoxin	Homo sapiens	0-11
15650396-4	2005	Thioredoxin (TRX), a key redox molecule, plays crucial roles as an antioxidant and a catalyst in protein disulfide/dithiol exchange.	Disulfides	105-114	thioredoxin	Homo sapiens	13-16
15684606-8	2005	TX is limited by the reduction capacity of its vicinal sulfhydryls and needs a source of electrons from the HMPS and TRX- coupled system to reduce disulfides.	Disulfides	147-157	peroxiredoxin 5	Homo sapiens	117-120
15840825-3	2005	By selectively introducing new disulfide bonds, we locked the conformation of these strands into an active TF*FVIIa-like state.	Disulfides	31-40	coagulation factor III, tissue factor	Homo sapiens	107-109
15695517-0	2005	Misfolding of collagen X chains harboring Schmid metaphyseal chondrodysplasia mutations results in aberrant disulfide bond formation, intracellular retention, and activation of the unfolded protein response.	Disulfides	108-117	collagen type X alpha 1 chain	Homo sapiens	42-77
15642736-19	2005	Results demonstrated that PKCgamma formed disulfide bonds in response to H2O2.	Disulfides	42-51	protein kinase C gamma	Homo sapiens	26-34
30980702-0	2019	Characterization of Disulfide Bond Rebridged Fab-Drug Conjugates Prepared Using a Dual Maleimide Pyrrolobenzodiazepine Cytotoxic Payload.	Disulfides	20-29	FA complementation group B	Homo sapiens	45-48
15695509-5	2005	Three symmetrical intersubunit disulfide bonds were identified in the noncatalytic interaction domains; two in the MAM (meprin, A-5 protein, protein-tyrosine phosphatase mu) domain and one in the TRAF (tumor necrosis factor receptor-associated factor) domain.	Disulfides	31-40	protein tyrosine phosphatase receptor type M	Homo sapiens	141-172
15772310-1	2005	EGF domains are extracellular protein modules cross-linked by three intradomain disulfides.	Disulfides	80-90	epidermal growth factor	Homo sapiens	0-3
15624163-3	2005	We studied the effects of alkaline on two purified proteins, chicken insulin and bovine alpha-lactalbumin, both containing four disulfide bonds in their structure.	Disulfides	128-137	lactalbumin alpha	Bos taurus	88-105
30980702-3	2019	SG3710 was designed to rebridge two adjacent cysteines, such as those that form the canonical interchain disulfide bond between the light and heavy chain in Fab fragments.	Disulfides	105-114	FA complementation group B	Homo sapiens	157-160
16259044-7	2005	Interestingly, the present results suggest that Cu2+ catalyzes the re-formation of the disulfide bonds of the reduced CP12, leading to recovery of the fully oxidized CP12 that is then able to bind a Cu2+ ion.	Disulfides	87-96	CP12 domain-containing protein 2	Arabidopsis thaliana	118-122
15772310-2	2005	Past studies suggest the existence of two types of EGF domain with three-disulfides, human EGF-like (hEGF) domains and complement C1r-like (cEGF) domains, but to date no functional information has been related to the two different types, and they are not differentiated in sequence or structure databases.	Disulfides	73-83	epidermal growth factor	Homo sapiens	51-54
15772310-6	2005	We show that important post-translational modifications of three-disulfide EGFs, including unusual forms of glycosylation and post-translational proteolytic processing, are dependent on EGF subtype.	Disulfides	65-74	epidermal growth factor	Homo sapiens	75-78
16259044-7	2005	Interestingly, the present results suggest that Cu2+ catalyzes the re-formation of the disulfide bonds of the reduced CP12, leading to recovery of the fully oxidized CP12 that is then able to bind a Cu2+ ion.	Disulfides	87-96	CP12 domain-containing protein 2	Arabidopsis thaliana	166-170
15772310-9	2005	Based on our structural analysis of EGF domains with three-disulfide bonds and comparison to laminin and integrin-like EGF domains with an additional inter-domain disulfide, we propose that these hEGF and cEGF domains may have arisen from a four-disulfide ancestor by selective loss of different cysteine residues.	Disulfides	59-68	epidermal growth factor	Homo sapiens	36-39
30980702-6	2019	Disulfide rebridging with SG3710 is a generic approach to prepare Fab-pyrrolobenzodiazepine dimer conjugates, which does not require the Fabs to be engineered for conjugation.	Disulfides	0-9	FA complementation group B	Homo sapiens	66-69
15772310-9	2005	Based on our structural analysis of EGF domains with three-disulfide bonds and comparison to laminin and integrin-like EGF domains with an additional inter-domain disulfide, we propose that these hEGF and cEGF domains may have arisen from a four-disulfide ancestor by selective loss of different cysteine residues.	Disulfides	163-172	epidermal growth factor	Homo sapiens	196-200
15772310-9	2005	Based on our structural analysis of EGF domains with three-disulfide bonds and comparison to laminin and integrin-like EGF domains with an additional inter-domain disulfide, we propose that these hEGF and cEGF domains may have arisen from a four-disulfide ancestor by selective loss of different cysteine residues.	Disulfides	163-172	epidermal growth factor	Homo sapiens	196-200
15561148-2	2004	The latter form, which spontaneously forms loop-sheet polymers, has an open beta-sheet A and is stabilized by a disulfide bond between C79 (in the CD-loop) and C161 (at the bottom of PAI-2).	Disulfides	112-121	serpin family B member 2	Homo sapiens	183-188
15561148-6	2004	However, the loop can translocate about 54A to the bottom of PAI-2 so that the C79-C161 disulfide bond can form under oxidizing conditions.	Disulfides	88-97	serpin family B member 2	Homo sapiens	61-66
31117440-2	2019	Herein, we developed camptothecin (CPT)-conjugated prodrug (CPTP) micelles in which CPT was grafted to the poly(ethylene glycol)-poly(glutamic acid) block copolymer via a disulfide bond linker for a redox-triggered drug release.	Disulfides	171-180	ceramide-1-phosphate transfer protein	Homo sapiens	60-64
15561148-7	2004	We show also that the redox-active C79 can form a disulfide-link to the matrix protein vitronectin, suggesting that vitronectin can stabilize active PAI-2 in extracellular compartments.	Disulfides	50-59	serpin family B member 2	Homo sapiens	149-154
15561148-8	2004	PAI-2 is therefore a rare example of a redox-sensitive protein for which the activity and polymerization ability are regulated by reversible disulfide bond formation leading to major translocation of a loop and significant conformational changes in the molecule.	Disulfides	141-150	serpin family B member 2	Homo sapiens	0-5
15709773-5	2005	The disulfide-linked A-B and C-C dimers as well as the noncovalent structural unit (A-B:C)-(C:B-A) were detected, providing experimental support to the C1q model based on covalent and noncovalent associations of six heterotrimers.	Disulfides	4-13	complement C1q A chain	Homo sapiens	152-155
31184304-2	2019	In ss cells, protein disulfide isomerase A1 (PDIA1/P4HB), the most abundant ER oxidoreductase of over 17 members, can interact with proinsulin to influence disulfide maturation.	Disulfides	21-30	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	45-50
15683237-3	2005	Several lines of evidence suggest that, contrary to a recent report, human ALR is a disulfide-bridged dimer (linked via C15-C124) with two free cysteine residues (C74 and 85) per monomer.	Disulfides	84-93	growth factor, augmenter of liver regeneration	Homo sapiens	75-78
15683237-5	2005	Although the crystal structure of rat ALR shows a proximal disulfide (C62-C65) poised to interact with the FAD prosthetic group [Wu, C. K., Dailey, T. A., Dailey, H. A., Wang, B. C., and Rose, J. P. (2003) Protein Sci.	Disulfides	59-68	growth factor, augmenter of liver regeneration	Rattus norvegicus	38-41
15542644-3	2004	Treatment of DENV-2 with beta-mercaptoethanol abolished binding of Fab 1A5, indicating that disulfide bridges were required for the structural integrity of the Fab 1A5 epitope.	Disulfides	92-101	FA complementation group B	Homo sapiens	67-70
15542644-3	2004	Treatment of DENV-2 with beta-mercaptoethanol abolished binding of Fab 1A5, indicating that disulfide bridges were required for the structural integrity of the Fab 1A5 epitope.	Disulfides	92-101	FA complementation group B	Homo sapiens	160-163
31184304-2	2019	In ss cells, protein disulfide isomerase A1 (PDIA1/P4HB), the most abundant ER oxidoreductase of over 17 members, can interact with proinsulin to influence disulfide maturation.	Disulfides	21-30	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	51-55
31184304-6	2019	Furthermore, Pdia1 deletion increased accumulation of disulfide-linked high molecular weight proinsulin complexes and islet vulnerability to oxidative stress.	Disulfides	54-63	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	13-18
15297885-6	2004	We also provide evidence that the reported disulfide bond linkage between two caspase-2 monomers is dispensable for caspase-2 dimerization.	Disulfides	43-52	caspase 2	Homo sapiens	78-87
15651042-6	2005	By means of DFT (B3LYP, lacv3p**) calculations, we could show that the formation of such a triad is essential to support the proton transfer from selenol to a histidine to stabilise a selenolate anion, which is able to interact with the disulfide of thioredoxin and catalyses the reductive disulfide opening.	Disulfides	237-246	thioredoxin	Homo sapiens	250-261
31460051-0	2019	Polymerization of Oxidized DJ-1 via Noncovalent and Covalent Binding: Significance of Disulfide Bond Formation.	Disulfides	86-95	Parkinsonism associated deglycase	Homo sapiens	27-31
15651042-6	2005	By means of DFT (B3LYP, lacv3p**) calculations, we could show that the formation of such a triad is essential to support the proton transfer from selenol to a histidine to stabilise a selenolate anion, which is able to interact with the disulfide of thioredoxin and catalyses the reductive disulfide opening.	Disulfides	290-299	thioredoxin	Homo sapiens	250-261
15292369-2	2004	We recently reported that Angptl4 is a variable-sized oligomer formed by intermolecular disulfide bonds and undergoes regulated proteolytic processing upon secretion.	Disulfides	88-97	angiopoietin-like 4	Mus musculus	26-33
30853336-1	2019	BACKGROUND: Aggregation of tau into paired helical filament (PHF) is a hallmark of Alzheimer"s disease (AD), and Cys-mediated disulfide bond formation plays a vital role in tau fibrillation.	Disulfides	126-135	microtubule associated protein tau	Homo sapiens	27-30
15297466-0	2004	Functional analysis of the alpha-defensin disulfide array in mouse cryptdin-4.	Disulfides	42-51	defensin, alpha, 20	Mus musculus	67-77
15297466-3	2004	In a series of Crp4 disulfide variants whose cysteine connectivities were confirmed using NMR spectroscopy and mass spectrometry, mutagenesis did not induce loss of function.	Disulfides	20-29	defensin, alpha, 20	Mus musculus	15-19
15297466-4	2004	To the contrary, the in vitro bactericidal activities of several Crp4 disulfide variants were equivalent to or greater than those of native Crp4.	Disulfides	70-79	defensin, alpha, 20	Mus musculus	65-69
15581893-6	2005	Two anions are found at the ACX1 dimer interface and for the first time the presence of a disulfide bridge in a peroxisomal protein has been observed.	Disulfides	90-99	acyl-CoA oxidase 1	Arabidopsis thaliana	28-32
15680231-3	2005	The mechanism includes three steps with (1) formation of a sulfenic acid intermediate with a concomitant release of 1 mol of methionine per mol of enzyme; (2) formation of an intramonomeric disulfide Msr bond followed by; (3) reduction of the oxidized Msr by thioredoxin (Trx).	Disulfides	190-199	thioredoxin	Homo sapiens	259-270
15680231-3	2005	The mechanism includes three steps with (1) formation of a sulfenic acid intermediate with a concomitant release of 1 mol of methionine per mol of enzyme; (2) formation of an intramonomeric disulfide Msr bond followed by; (3) reduction of the oxidized Msr by thioredoxin (Trx).	Disulfides	190-199	thioredoxin	Homo sapiens	272-275
15297466-8	2004	Thus, rather than determining alpha-defensin bactericidal activity, the Crp4 disulfide arrangement confers essential protection from degradation by this critical activating proteinase.	Disulfides	77-86	defensin, alpha, 20	Mus musculus	72-76
30853336-1	2019	BACKGROUND: Aggregation of tau into paired helical filament (PHF) is a hallmark of Alzheimer"s disease (AD), and Cys-mediated disulfide bond formation plays a vital role in tau fibrillation.	Disulfides	126-135	microtubule associated protein tau	Homo sapiens	173-176
30853336-2	2019	While intermolecular disulfide bond between Cys residues in microtubule-binding repeat (MTBR) region facilitates tau aggregation, intramolecular disulfide bond attenuates the same, though the molecular basis for such phenomenon remains obscure.	Disulfides	21-30	microtubule associated protein tau	Homo sapiens	113-116
15492265-4	2004	SPARC comprises three domains that are independently folded by a complex pattern of disulfide bonds and have a high degree of structural conservation.	Disulfides	84-93	secreted protein acidic and cysteine rich	Homo sapiens	0-5
15931669-1	2005	The chi-conopeptides MrIA and MrIB are 13-residue peptides with two disulfide bonds that inhibit human and rat norepinephrine transporter systems and are of significant interest for the design of novel drugs involved in pain treatment.	Disulfides	68-77	solute carrier family 6 member 2	Rattus norvegicus	111-137
15492265-8	2004	The EGF-like conformation was essential for peptide FS-E function because reduction of its two disulfide bonds completely abrogated peptide activity.	Disulfides	95-104	epidermal growth factor	Homo sapiens	4-7
30853336-3	2019	Thus intramolecular disulfide-bonded tau monomer might be an excellent model to understand the unique features of aggregation-resistant tau conformer.	Disulfides	20-29	microtubule associated protein tau	Homo sapiens	37-40
30853336-3	2019	Thus intramolecular disulfide-bonded tau monomer might be an excellent model to understand the unique features of aggregation-resistant tau conformer.	Disulfides	20-29	microtubule associated protein tau	Homo sapiens	136-139
31067198-5	2019	We report here the development of a new aminopeptidase A inhibitor prodrug, NI956/QGC006, obtained by the disulfide bridge-mediated dimerization of NI929.	Disulfides	106-115	glutamyl aminopeptidase	Rattus norvegicus	40-56
15184375-2	2004	We report that peroxynitrite- and hydrogen peroxide-induced disulfides in the neuron-specific microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the ubiquitous thioredoxin reductase system composed of thioredoxin reductase, human or Escherichia coli thioredoxin, and NADPH.	Disulfides	60-70	peroxiredoxin 5	Homo sapiens	201-222
15184375-2	2004	We report that peroxynitrite- and hydrogen peroxide-induced disulfides in the neuron-specific microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the ubiquitous thioredoxin reductase system composed of thioredoxin reductase, human or Escherichia coli thioredoxin, and NADPH.	Disulfides	60-70	peroxiredoxin 5	Homo sapiens	242-263
15545361-4	2004	These results indicate that beta-LG and alpha-LA associated with MFGM proteins via disulfide bonds during the high-pressure treatment of whole milk.	Disulfides	83-92	milk fat globule EGF and factor V/VIII domain containing	Homo sapiens	65-69
31160781-2	2019	LAT1 forms a disulfide-linked heterodimer with CD98 heavy chain (CD98hc, 4F2hc or SLC3A2), but the mechanism of assembly and amino acid transport are poorly understood.	Disulfides	13-22	solute carrier family 7 member 5	Homo sapiens	0-4
15337741-2	2004	MOX has all of the residues expected to be critical for copper binding, and its cysteine residues can yield the intramolecular disulfide bond pattern observed in DBM.	Disulfides	127-136	monooxygenase DBH like 1	Homo sapiens	0-3
15337741-9	2004	MOX is N-glycosylated, is tightly membrane-associated, and forms oligomers that are not disulfide-linked.	Disulfides	88-97	monooxygenase DBH like 1	Homo sapiens	0-3
15255930-3	2004	In rABCG2-transfected HEK293 cells, rABCG2 was detected as a glycoprotein complex bridged by disulfide bonds, possibly a homodimer.	Disulfides	93-102	ATP binding cassette subfamily G member 2	Rattus norvegicus	36-42
15255930-5	2004	In rat brain capillary fraction, rABCG2 protein was also detected as a glycosylated and disulfide-linked complex.	Disulfides	88-97	ATP binding cassette subfamily G member 2	Rattus norvegicus	33-39
15282410-2	2004	The glutathione (GSH) and thioredoxin (TRX) systems have overlapping functions in thiol/disulfide redox control in both the cytoplasm and the nucleus, and it is unclear whether these are redundant or have unique functions in control of Nrf-2-dependent signaling.	Disulfides	88-97	thioredoxin	Homo sapiens	26-37
31160781-2	2019	LAT1 forms a disulfide-linked heterodimer with CD98 heavy chain (CD98hc, 4F2hc or SLC3A2), but the mechanism of assembly and amino acid transport are poorly understood.	Disulfides	13-22	solute carrier family 3 member 2	Homo sapiens	47-63
15282410-2	2004	The glutathione (GSH) and thioredoxin (TRX) systems have overlapping functions in thiol/disulfide redox control in both the cytoplasm and the nucleus, and it is unclear whether these are redundant or have unique functions in control of Nrf-2-dependent signaling.	Disulfides	88-97	thioredoxin	Homo sapiens	39-42
15138265-7	2004	Taken together, our results lead us to conclude that FANCA and FANCG uniquely respond to oxidative damage by forming complex(es) via intermolecular disulfide linkage(s), which may be crucial in forming such complexes and in determining their function.	Disulfides	148-157	FA complementation group G	Homo sapiens	63-68
31160781-2	2019	LAT1 forms a disulfide-linked heterodimer with CD98 heavy chain (CD98hc, 4F2hc or SLC3A2), but the mechanism of assembly and amino acid transport are poorly understood.	Disulfides	13-22	solute carrier family 3 member 2	Homo sapiens	73-78
30894413-4	2019	Why does the first LU domain in uPAR (DI) lack one of its consensus disulfide bonds, when the absence of this particular disulfide bond impairs the correct folding of other single LU domain-containing proteins?	Disulfides	68-77	plasminogen activator, urokinase receptor	Homo sapiens	32-36
15304512-2	2004	The N-terminal portion of the seatbelt contains a small disulfide-stabilized loop needed for heterodimer assembly and is thought to mediate hCG-LHR interactions.	Disulfides	56-65	luteinizing hormone/choriogonadotropin receptor	Homo sapiens	144-147
15357668-1	2004	We have previously described a disulfide-linked cyclic nonapeptide (inhibitory peptide-01, IP01), with the sequence CLLRMRSIC, which binds to intercellular adhesion molecule-1 (ICAM-1), and blocks binding to its counter-structure, the integrin alphaLbeta2 (leukocyte functional antigen-1, LFA-1) (Sillerud et al., J. Peptide Res.	Disulfides	31-40	integrin alpha L	Mus musculus	289-294
15193566-1	2004	The thioredoxin and glutathione systems play a central role in thiol-disulfide redox homeostasis in many organisms by providing electrons to essential enzymes, and defence against oxidative stress.	Disulfides	69-78	thioredoxin	Homo sapiens	4-15
30894413-4	2019	Why does the first LU domain in uPAR (DI) lack one of its consensus disulfide bonds, when the absence of this particular disulfide bond impairs the correct folding of other single LU domain-containing proteins?	Disulfides	121-130	plasminogen activator, urokinase receptor	Homo sapiens	32-36
15159594-2	2004	In vitro, it is possible via a reaction with 5,5"-dithiobis-(2-nitrobenzoic acid) to make a stable mixed-disulfide complex between thioredoxin from Staphylococcus aureus and one of its substrates, oxidized pI258 arsenate reductase (ArsC) from S. aureus.	Disulfides	105-114	arsenate reductase	Staphylococcus aureus	232-236
30894413-5	2019	Here, using a variety of contemporary biophysical methods, we found that reintroducing the two missing half-cystines in uPAR DI caused the spontaneous formation of the corresponding consensus 7-8 LU domain disulfide bond.	Disulfides	206-215	plasminogen activator, urokinase receptor	Homo sapiens	120-124
15159594-6	2004	In order to form a mixed disulfide between ArsC and thioredoxin, a change in the orientation of the TNB-Cys89 disulfide in the structure is necessary.	Disulfides	25-34	arsenate reductase	Staphylococcus aureus	43-47
30894413-7	2019	We conclude that the evolutionary deletion of this particular disulfide bond in uPAR DI may have enabled the assembly of a high-affinity urokinase-binding cavity involving all three LU domains in uPAR.	Disulfides	62-71	plasminogen activator, urokinase receptor	Homo sapiens	80-84
30894413-7	2019	We conclude that the evolutionary deletion of this particular disulfide bond in uPAR DI may have enabled the assembly of a high-affinity urokinase-binding cavity involving all three LU domains in uPAR.	Disulfides	62-71	plasminogen activator, urokinase receptor	Homo sapiens	196-200
15157085-2	2004	We previously showed that the eight cysteine residues of recombinant SMB (rSMB) are organized into four disulfide bonds in a linear uncrossed pattern (Cys(5)-Cys(9), Cys(19)-Cys(21), Cys(25)-Cys(31), and Cys(32)-Cys(39)).	Disulfides	104-113	small nuclear ribonucleoprotein polypeptides B and B1	Rattus norvegicus	74-78
15157085-9	2004	An experimental demonstration of the presence of alternative disulfide conformations in active rSMB is provided by the behavior of a mutant in which Asn(14) is replaced by Met.	Disulfides	61-70	small nuclear ribonucleoprotein polypeptides B and B1	Rattus norvegicus	95-99
15383153-7	2004	Monoclonal antibodies were raised against the cynomolgus CD38 ectodomain and were either species-specific or cross-reactive with human CD38, in which case they were directed against a common disulfide-requiring conformational epitope that was mapped to the C-terminal disulfide loop.	Disulfides	191-200	CD38 molecule	Homo sapiens	135-139
15157085-11	2004	These results suggest that active forms of the SMB domain may have a number of allowed disulfide bond arrangements as long as the Cys(25)-Cys(31) disulfide bond is preserved.	Disulfides	87-96	small nuclear ribonucleoprotein polypeptides B and B1	Rattus norvegicus	47-50
30894413-9	2019	In summary, elimination of the 7-8 consensus disulfide bond in the first LU domain of uPAR did have significant functional and structural consequences.	Disulfides	45-54	plasminogen activator, urokinase receptor	Homo sapiens	86-90
15157085-11	2004	These results suggest that active forms of the SMB domain may have a number of allowed disulfide bond arrangements as long as the Cys(25)-Cys(31) disulfide bond is preserved.	Disulfides	146-155	small nuclear ribonucleoprotein polypeptides B and B1	Rattus norvegicus	47-50
30892297-4	2019	Owing to the glutathione (GSH)-responsive biodegradation behavior of the disulfide-doped organosilica gatekeeper, the DOX-loaded POMSNs exhibit only 20% cell viability towards SMMC-7721 tumor cells, and almost no toxicity towards L-02 cells at a DOX concentration of 50 mug mL-1 was measured, demonstrating their selective cytotoxicity in vitro.	Disulfides	73-82	L1 cell adhesion molecule	Mus musculus	274-278
15056758-3	2004	We report here the design and synthesis of HP-1, a disulfide-bridged two-alpha-helix peptide that self-assembles to form an antiparallel twofold symmetric diheme four-alpha-helix bundle protein with a stable conformation on the NMR time-scale.	Disulfides	51-60	chromobox 5	Homo sapiens	43-47
15309367-7	2004	The percentage disulfide bond reduction increases as the urea concentration used for protein denaturation increases, giving a single-step sigmoid increment for single-domain, low-MW proteins (alpha-Lac and Lys), and a two-step sigmoid increment for multi-domain, high MW proteins (HSA and BSA).	Disulfides	15-24	lactalbumin alpha	Bos taurus	192-201
30796163-8	2019	We obtained high yields of soluble, monomeric protein by fusing the TCR extracellular domains to antibody hinge and Fc constant regions, adding a stabilizing disulfide bond between the constant domains and disrupting predicted glycosylation sites.	Disulfides	158-167	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	68-71
15224381-4	2004	The common structural feature of U-II peptides from different species is the C-terminal portion, characterized by the disulfide bridged cyclic hexapeptide Cys-Phe-Trp-Lys-Tyr-Cys.	Disulfides	118-127	urotensin 2	Homo sapiens	33-37
15039220-1	2004	IL-12 consists of two disulfide-linked subunits, p40 and p35, that form functionally active heterodimers for the induction of Th1 cells.	Disulfides	22-31	interleukin 12a	Mus musculus	57-60
30642920-9	2019	Associated structural rearrangements in the C8-3 and TIL3 modules are required to expose cysteine residues for disulfide linkage.	Disulfides	111-120	toll like receptor 5	Homo sapiens	53-57
15041637-5	2004	The crystal structure of bovine rhodopsin has the second extracellular (EC-II) loop closed over the transmembrane regions by making a disulfide linkage between Cys-110 and Cys-187, but we speculate that opening this loop may play a role in the activation process of the receptor through the cysteine linkage with helix 3.	Disulfides	134-143	rhodopsin	Bos taurus	32-41
15180957-8	2004	A circuitry model incorporating cysteine as a redox node, along with Trx1 and GSH, reveals how selective interactions between the different thiol/disulfide couples and reactive protein thiols could differentially regulate metabolic functions.	Disulfides	146-155	thioredoxin	Homo sapiens	69-73
30948772-6	2019	Moreover, PX-12 inhibited the enzymatic activity of Trx1 and the Trx1-dependent disulfide reduction of gp120.	Disulfides	80-89	thioredoxin	Homo sapiens	65-69
14656938-2	2004	In this report, we show that the oxidative regulatory responses of purified PKCdelta and PKCepsilon to cystine are recapitulated in disulfide-treated cells.	Disulfides	132-141	protein kinase C epsilon	Homo sapiens	89-99
30948772-6	2019	Moreover, PX-12 inhibited the enzymatic activity of Trx1 and the Trx1-dependent disulfide reduction of gp120.	Disulfides	80-89	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	103-108
15212960-5	2004	Here we show using U937 cells that cystatin F is secreted as a disulfide bridge-linked dimer and is not associated with endosomes intracellularly.	Disulfides	63-72	cystatin F	Homo sapiens	35-45
30867591-8	2019	Besides a disulfide bond association, LAT1 also interacts extensively with 4F2hc on the extracellular side, within the membrane, and on the intracellular side.	Disulfides	10-19	solute carrier family 7 member 5	Homo sapiens	38-42
15358050-0	2004	The formation of an intrachain disulfide bond in the leptin protein is necessary for efficient leptin secretion.	Disulfides	31-40	leptin	Homo sapiens	53-59
15358050-0	2004	The formation of an intrachain disulfide bond in the leptin protein is necessary for efficient leptin secretion.	Disulfides	31-40	leptin	Homo sapiens	95-101
15358050-9	2004	Therefore, our work indicates that the formation of an intramolecular disulfide bridge is necessary for normal processing and secretion of leptin.	Disulfides	70-79	leptin	Homo sapiens	139-145
14871470-0	2004	TMX, a human transmembrane oxidoreductase of the thioredoxin family: the possible role in disulfide-linked protein folding in the endoplasmic reticulum.	Disulfides	90-99	thioredoxin	Homo sapiens	49-60
30611847-4	2019	RESULTS: 1) 1 is a covalent inhibitor of HDAC8; 2) inhibition is reversible in the presence of reducing agents; 3) C153 in the active site and C102 are involved in the inhibition mechanism; 4) 1 modifies various cysteines in HDAC8 forming either thiocyanates or mixed disulfides with 3; 5) 1 and 5 dock in close proximity to C153 within the active site.	Disulfides	268-278	histone deacetylase 8	Homo sapiens	41-46
14976238-7	2004	The redox midpoint potential of the peroxiredoxin Q catalytic disulfide is -325 mV at pH 7.0, explaining why the wild-type protein is reduced by thioredoxin but not by glutaredoxin.	Disulfides	62-71	thioredoxin	Homo sapiens	145-156
14676218-7	2004	Furthermore Grx2 was a substrate for NADPH and thioredoxin reductase, which efficiently reduced both the active site disulfide and the GSH-glutaredoxin intermediate formed in the reduction of glutathionylated substrates.	Disulfides	117-126	peroxiredoxin 5	Homo sapiens	47-68
15155948-0	2004	Disulfide-dependent multimeric assembly of resistin family hormones.	Disulfides	0-9	resistin	Homo sapiens	43-51
15155948-6	2004	Infusion of a resistin mutant, lacking the intertrimer disulfide bonds, in pancreatic-insulin clamp studies reveals substantially more potent effects on hepatic insulin sensitivity than those observed with wild-type resistin.	Disulfides	55-64	resistin	Homo sapiens	14-22
14975452-2	2004	Herein we report that peroxynitrite-induced disulfides in porcine brain tubulin are repaired by the thioredoxin reductase system composed of rat liver thioredoxin reductase, human or Escherichia coli thioredoxin, and NADPH.	Disulfides	44-54	thioredoxin	Homo sapiens	100-111
14975452-2	2004	Herein we report that peroxynitrite-induced disulfides in porcine brain tubulin are repaired by the thioredoxin reductase system composed of rat liver thioredoxin reductase, human or Escherichia coli thioredoxin, and NADPH.	Disulfides	44-54	thioredoxin	Homo sapiens	151-162
14975452-3	2004	Disulfide bonds between the alpha-tubulin and the beta-tubulin subunits were repaired by thioredoxin reductase as determined by Western blot under nonreducing conditions.	Disulfides	0-9	thioredoxin	Homo sapiens	89-100
30611847-4	2019	RESULTS: 1) 1 is a covalent inhibitor of HDAC8; 2) inhibition is reversible in the presence of reducing agents; 3) C153 in the active site and C102 are involved in the inhibition mechanism; 4) 1 modifies various cysteines in HDAC8 forming either thiocyanates or mixed disulfides with 3; 5) 1 and 5 dock in close proximity to C153 within the active site.	Disulfides	268-278	histone deacetylase 8	Homo sapiens	225-230
14975452-4	2004	Total disulfide repair by thioredoxin reductase was assessed using a sulfhydryl-specific labeling reagent, 5-iodoacetamido-fluorescein.	Disulfides	6-15	peroxiredoxin 5	Homo sapiens	26-47
14975452-6	2004	Tubulin disulfide reduction by thioredoxin reductase restored tubulin polymerization activity that was lost after peroxynitrite was added.	Disulfides	8-17	peroxiredoxin 5	Homo sapiens	31-52
30548114-1	2019	L-Type amino acid transporter 1 (LAT1) disulfide linked to CD98 heavy chain (hc) is highly expressed in most cancer cells, but weakly expressed in normal cells.	Disulfides	39-48	solute carrier family 7 member 5	Homo sapiens	0-31
14975452-9	2004	Thiol-disulfide exchange between tubulin and thioredoxin was detected by Western blot, thereby providing further support for our observations that optimal repair of tubulin disulfides required thioredoxin.	Disulfides	6-15	thioredoxin	Homo sapiens	45-56
14975452-9	2004	Thiol-disulfide exchange between tubulin and thioredoxin was detected by Western blot, thereby providing further support for our observations that optimal repair of tubulin disulfides required thioredoxin.	Disulfides	6-15	thioredoxin	Homo sapiens	193-204
14975452-9	2004	Thiol-disulfide exchange between tubulin and thioredoxin was detected by Western blot, thereby providing further support for our observations that optimal repair of tubulin disulfides required thioredoxin.	Disulfides	173-183	thioredoxin	Homo sapiens	45-56
14975452-9	2004	Thiol-disulfide exchange between tubulin and thioredoxin was detected by Western blot, thereby providing further support for our observations that optimal repair of tubulin disulfides required thioredoxin.	Disulfides	173-183	thioredoxin	Homo sapiens	193-204
14981081-3	2004	The multimeric size of VWF can be controlled by proteolysis at the Tyr(842)-Met(843) peptide bond by ADAMTS13 or cleavage of the disulfide bonds that hold VWF multimers together by thrombospondin-1 (TSP-1).	Disulfides	129-138	Von Willebrand factor	Mus musculus	23-26
14981081-3	2004	The multimeric size of VWF can be controlled by proteolysis at the Tyr(842)-Met(843) peptide bond by ADAMTS13 or cleavage of the disulfide bonds that hold VWF multimers together by thrombospondin-1 (TSP-1).	Disulfides	129-138	Von Willebrand factor	Mus musculus	155-158
15134578-1	2004	BACKGROUND: The Lp(a) lipoprotein (Lp(a)) consists of the polymorphic glycoprotein apolipoprotein(a) (apo(a)), which is attached by a disulfide bond to apolipoprotein B (apoB).	Disulfides	134-143	apolipoprotein B	Mus musculus	152-168
30548114-1	2019	L-Type amino acid transporter 1 (LAT1) disulfide linked to CD98 heavy chain (hc) is highly expressed in most cancer cells, but weakly expressed in normal cells.	Disulfides	39-48	solute carrier family 7 member 5	Homo sapiens	33-37
15134578-1	2004	BACKGROUND: The Lp(a) lipoprotein (Lp(a)) consists of the polymorphic glycoprotein apolipoprotein(a) (apo(a)), which is attached by a disulfide bond to apolipoprotein B (apoB).	Disulfides	134-143	apolipoprotein B	Mus musculus	170-174
14607843-7	2004	In an effort to identify target proteins of TRP14, a mutant of TRP14, in which the active site cysteine (Cys(46)) was substituted with serine, was shown to form a disulfide-linked complex with LC8 cytoplasmic dynein light chain.	Disulfides	163-172	thioredoxin domain containing 17	Homo sapiens	44-49
14607843-7	2004	In an effort to identify target proteins of TRP14, a mutant of TRP14, in which the active site cysteine (Cys(46)) was substituted with serine, was shown to form a disulfide-linked complex with LC8 cytoplasmic dynein light chain.	Disulfides	163-172	thioredoxin domain containing 17	Homo sapiens	63-68
30548114-1	2019	L-Type amino acid transporter 1 (LAT1) disulfide linked to CD98 heavy chain (hc) is highly expressed in most cancer cells, but weakly expressed in normal cells.	Disulfides	39-48	solute carrier family 3 member 2	Homo sapiens	59-75
30395443-5	2019	Disulfide exchange between the mutated cysteines and the activated disulfides yielded 20 foldamer-IL4 and 20 foldamer-CypA adducts.	Disulfides	0-9	peptidylprolyl isomerase A	Homo sapiens	118-122
14570927-4	2004	We report here that Angptl4 is evolutionarily conserved among several mammalian species and that full-length Angptl4 protein is an oligomer containing intermolecular disulfide bonds.	Disulfides	166-175	angiopoietin like 4	Homo sapiens	109-116
15081871-1	2004	Intracellular activation of ricin and of the ricin A-chain (RTA) immunotoxins requires reduction of their intersubunit disulfide(s).	Disulfides	119-128	MAS related GPR family member F	Homo sapiens	60-63
30395443-5	2019	Disulfide exchange between the mutated cysteines and the activated disulfides yielded 20 foldamer-IL4 and 20 foldamer-CypA adducts.	Disulfides	67-77	peptidylprolyl isomerase A	Homo sapiens	118-122
30680044-3	2019	This allowed conjugation to a neuropeptide-Y (NPY)-inspired peptide [K4(C-betaA-),F7,L17,P34]-hNPY, acting as NPY Y1 receptor (hY1R)-targeting peptide, to form a tubugi-1-SS-NPY disulfide-linked conjugate.	Disulfides	178-187	neuropeptide Y	Homo sapiens	30-44
15145212-6	2004	RESULTS: The G-CSF/IgG-Fc and G-CSF/IgG-C(H) fusion proteins were secreted from transfected COS cells primarily as disulfide-linked homodimers.	Disulfides	115-124	colony stimulating factor 3	Homo sapiens	13-18
15145212-6	2004	RESULTS: The G-CSF/IgG-Fc and G-CSF/IgG-C(H) fusion proteins were secreted from transfected COS cells primarily as disulfide-linked homodimers.	Disulfides	115-124	colony stimulating factor 3	Homo sapiens	30-35
14732708-7	2004	The c-Myc epitope is inserted adjacent to cysteine 79 of the NR1-2a subunit; therefore, it is possible that the tag may prevent the formation of NR1 disulfide bridges.	Disulfides	149-158	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	4-9
14656938-8	2004	Demonstration of oxidative regulation of cellular PKCdelta and PKCepsilon by disulfides in this report provides evidence that redox-regulatory sites in PKCdelta and PKCepsilon may offer novel targets for development of cancer preventive or therapeutic agents that selectively inactivate PKCepsilon or stimulate PKCdelta.	Disulfides	77-87	protein kinase C epsilon	Homo sapiens	63-73
14656938-8	2004	Demonstration of oxidative regulation of cellular PKCdelta and PKCepsilon by disulfides in this report provides evidence that redox-regulatory sites in PKCdelta and PKCepsilon may offer novel targets for development of cancer preventive or therapeutic agents that selectively inactivate PKCepsilon or stimulate PKCdelta.	Disulfides	77-87	protein kinase C epsilon	Homo sapiens	165-175
14656938-8	2004	Demonstration of oxidative regulation of cellular PKCdelta and PKCepsilon by disulfides in this report provides evidence that redox-regulatory sites in PKCdelta and PKCepsilon may offer novel targets for development of cancer preventive or therapeutic agents that selectively inactivate PKCepsilon or stimulate PKCdelta.	Disulfides	77-87	protein kinase C epsilon	Homo sapiens	165-175
14687577-7	2004	Disulfide bonds can be formed in double-cysteine mutants with substitutions at positions P11 or P13 of the RCL and neighboring residues in beta-sheet A.	Disulfides	0-9	endonuclease, poly(U) specific	Homo sapiens	89-92
14687577-7	2004	Disulfide bonds can be formed in double-cysteine mutants with substitutions at positions P11 or P13 of the RCL and neighboring residues in beta-sheet A.	Disulfides	0-9	H3 histone pseudogene 6	Homo sapiens	96-99
14525956-10	2004	Based on the known three-dimensional structure of key cystine knot proteins, we postulated disulfide bondings for eight-membered ring BMP antagonists to predict their potential folding and dimerization.	Disulfides	91-100	bone morphogenetic protein 1	Homo sapiens	134-137
14750599-2	2004	Peripherin 2 and ROM1 assemble as a mixture of core noncovalent homomeric and heteromeric tetramers that further link together through disulfide bonds to form higher order oligomers.	Disulfides	135-144	retinal outer segment membrane protein 1 L homeolog	Xenopus laevis	17-21
30680044-3	2019	This allowed conjugation to a neuropeptide-Y (NPY)-inspired peptide [K4(C-betaA-),F7,L17,P34]-hNPY, acting as NPY Y1 receptor (hY1R)-targeting peptide, to form a tubugi-1-SS-NPY disulfide-linked conjugate.	Disulfides	178-187	neuropeptide Y	Homo sapiens	46-49
30680044-3	2019	This allowed conjugation to a neuropeptide-Y (NPY)-inspired peptide [K4(C-betaA-),F7,L17,P34]-hNPY, acting as NPY Y1 receptor (hY1R)-targeting peptide, to form a tubugi-1-SS-NPY disulfide-linked conjugate.	Disulfides	178-187	neuropeptide Y	Homo sapiens	95-98
30680044-3	2019	This allowed conjugation to a neuropeptide-Y (NPY)-inspired peptide [K4(C-betaA-),F7,L17,P34]-hNPY, acting as NPY Y1 receptor (hY1R)-targeting peptide, to form a tubugi-1-SS-NPY disulfide-linked conjugate.	Disulfides	178-187	neuropeptide Y	Homo sapiens	95-98
30666186-4	2018	Previously, we have shown that moderate illumination (halogen lamp, 1,500 lx, 1-5 h) of mammalian eyes provokes disulfide dimerization of recoverin, a calcium-dependent regulator of GRK1.	Disulfides	112-121	G protein-coupled receptor kinase 1	Homo sapiens	182-186
14632930-6	2003	This study was initiated to delineate the role of the disulfide bonds of hFSH beta in receptor binding of the hormone.	Disulfides	54-63	follicle stimulating hormone subunit beta	Homo sapiens	73-82
14632930-7	2003	Five intermolecular and one intramolecular disulfide peptides corresponding to the disulfide bonds found in hFSH beta were synthesized and screened along with their linear counterparts, for their ability to competitively inhibit the radiolabelled [125I]hFSH from binding to the FSH receptor containing membranes from the testis of immature rats.	Disulfides	43-52	follicle stimulating hormone subunit beta	Homo sapiens	108-117
15027856-1	2004	Urotensin II (U-II) is a disulfide-bridged undecapeptide recently identified as the ligand of an orphan G-protein-coupled receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	0-12
15027856-1	2004	Urotensin II (U-II) is a disulfide-bridged undecapeptide recently identified as the ligand of an orphan G-protein-coupled receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	14-18
14632930-7	2003	Five intermolecular and one intramolecular disulfide peptides corresponding to the disulfide bonds found in hFSH beta were synthesized and screened along with their linear counterparts, for their ability to competitively inhibit the radiolabelled [125I]hFSH from binding to the FSH receptor containing membranes from the testis of immature rats.	Disulfides	83-92	follicle stimulating hormone subunit beta	Homo sapiens	108-117
30666186-9	2018	Meanwhile, the oxidized monomer and C39D mutant of recoverin demonstrate impaired ability to bind photoreceptor membranes and regulate GRK1, whereas disulfide dimer exhibits notably improved membrane binding and GRK1 inhibition in absence of Ca2+.	Disulfides	149-158	G protein-coupled receptor kinase 1	Homo sapiens	212-216
31376820-3	2019	LAT1 (also known as SLC7A5), is defined as a heteromeric amino acid transporter (HAT) interacting with the glycoprotein CD98 (SLC3A2) through a conserved disulfide to uptake not only large neutral amino acids, but also several pharmaceutical drugs to cells.	Disulfides	154-163	solute carrier family 7 member 5	Felis catus	20-26
14607928-5	2003	MD-2 binding to TLR4 was dependent on Cys(95) and Cys(105), which might form an intramolecular disulfide bond.	Disulfides	95-104	toll like receptor 4	Homo sapiens	16-20
14992592-2	2004	The structure of endostatin is unique in that its secondary structure is mainly irregular loops and beta-sheets and contains only a small fraction of alpha-helices with two pairs of disulfide bonds in a nested pattern.	Disulfides	182-191	collagen type XVIII alpha 1 chain	Homo sapiens	17-27
14592831-6	2004	We further find that PDI facilitates thiol/disulfide rearrangement in gp120 during conformational change, whereas inhibition of this redox shuffling prevents gp41 from assuming the fusogenic 6-helix bundle conformation.	Disulfides	43-52	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	70-75
14581223-2	2003	During the folding and assembly of the P22 tailspike protein, nonnative disulfide bonds form both in vivo and in vitro.	Disulfides	72-81	calcineurin like EF-hand protein 1	Homo sapiens	39-42
30284335-6	2019	As previously observed, a crucial difference between PRDX1 and PRDX2 is on the resolution step of the catalytic cycle, the rate of disulfide formation (11 s-1 for PRDX1, 0.2 s-1 for PRDX2, independent of the oxidant) which correlates with their different sensitivity to hyperoxidation.	Disulfides	131-140	peroxiredoxin 1	Homo sapiens	53-58
30284335-6	2019	As previously observed, a crucial difference between PRDX1 and PRDX2 is on the resolution step of the catalytic cycle, the rate of disulfide formation (11 s-1 for PRDX1, 0.2 s-1 for PRDX2, independent of the oxidant) which correlates with their different sensitivity to hyperoxidation.	Disulfides	131-140	peroxiredoxin 1	Homo sapiens	163-168
30284335-8	2019	The longer lifetime of PRDX2 sulfenic acid allows it to react with other protein thiols to translate the signal via an intermediate mixed disulfide (involving its peroxidatic cysteine), whereas PRDX1 continues the cycle forming disulfide involving its resolving cysteine to function as a redox relay.	Disulfides	228-237	peroxiredoxin 1	Homo sapiens	194-199
12920126-7	2003	Another unique feature of caspase-2 is a disulfide bridge at the dimer interface, which covalently links the two monomers.	Disulfides	41-50	caspase 2	Homo sapiens	26-35
15123261-4	2004	The Ni/GGH oxidative procedure was also used to make covalent attachments to the virion by trapping with a functionalized disulfide reagent.	Disulfides	122-131	gamma-glutamyl hydrolase	Homo sapiens	7-10
12920126-9	2003	The intersubunit disulfide bridge stabilizes the dimeric form of caspase-2, whereas all other long prodomain caspases exist as monomers in solution, and dimer formation is driven by ligand binding.	Disulfides	17-26	caspase 2	Homo sapiens	65-74
30341785-4	2019	The enzymes of this class often use a CXXC active-site motif embedded in their thioredoxin-like fold to promote formation, isomerization, and reduction of a disulfide bond in their target proteins.	Disulfides	157-166	thioredoxin	Homo sapiens	79-90
12920126-10	2003	Therefore, the central disulfide bridge appears to represent a novel way of dimer stabilization in caspases.	Disulfides	23-32	caspase 2	Homo sapiens	99-107
14523092-5	2003	After expression in HEK 293 cells of such modified P2X2 or P2X4 subunits, the disulfide bond formation is evident because an ATP-evoked channel opening requires previous reduction with dithiothreitol.	Disulfides	78-87	purinergic receptor P2X 2	Homo sapiens	51-55
14673134-3	2004	The wild-type human AMH protein is synthesized as a disulfide-linked dimer of two identical 70-kDa polypeptides, which undergoes proteolytic processing to generate a 110-kDa N-terminal dimer and a bioactive 25-kDa TGF-beta-like C-terminal dimer.	Disulfides	52-61	anti-Mullerian hormone	Homo sapiens	20-23
30545068-5	2018	Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems.	Disulfides	0-9	peroxiredoxin 5	Homo sapiens	88-109
12807997-11	2003	This three-pole feature, kept by the disulfide bond in a correct spatial arrangement, appears as the key pharmacophore for the U-II receptor.	Disulfides	37-46	urotensin 2	Homo sapiens	127-131
30121965-2	2018	Characterization of intra-disulfide linked isomer will provide important information on the stability of the antibodies and better understanding of the mechanism of Fab-arm exchange.	Disulfides	26-35	FA complementation group B	Homo sapiens	165-168
12943796-1	2003	The recombinant form of the 17kDa, highly hydrophobic and disulfide-bonded hepatitis B virus X protein (HBX) was used for developing a set of monoclonal antibodies (Mab).	Disulfides	58-67	X protein	Hepatitis B virus	75-102
12943796-1	2003	The recombinant form of the 17kDa, highly hydrophobic and disulfide-bonded hepatitis B virus X protein (HBX) was used for developing a set of monoclonal antibodies (Mab).	Disulfides	58-67	X protein	Hepatitis B virus	104-107
14668347-1	2004	Mammalian heteromeric amino acid transporters (HATs) are composed of a multi-transmembrane spanning catalytic protein covalently associated with a type II glycoprotein (e.g. 4F2hc, rBAT) through a disulfide bond.	Disulfides	197-206	solute carrier family 3 member 2	Homo sapiens	174-179
30542351-4	2018	XCL1 is unique because of its lack of one of the two disulfide bonds commonly conserved in all other chemokines and thus has an unstable structure with a relatively weak chemokine activity.	Disulfides	53-62	chemokine (C motif) ligand 1	Mus musculus	0-4
15017976-4	2004	Among these redox-regulated PTPs, PTEN, Cdc25 and low molecular weight PTP are known to form a disulfide bond between two cysteines, one in the active site and the other nearby, during oxidation by H(2)O(2).	Disulfides	95-104	phosphatase and tensin homolog	Homo sapiens	34-38
15017976-4	2004	Among these redox-regulated PTPs, PTEN, Cdc25 and low molecular weight PTP are known to form a disulfide bond between two cysteines, one in the active site and the other nearby, during oxidation by H(2)O(2).	Disulfides	95-104	cell division cycle 25C	Homo sapiens	40-45
12816947-1	2003	Thioredoxin (Trx1) is a redox-active protein containing two active site cysteines (Cys-32 and Cys-35) that cycle between the dithiol and disulfide forms as Trx1 reduces target proteins.	Disulfides	137-146	thioredoxin	Homo sapiens	0-11
12816947-1	2003	Thioredoxin (Trx1) is a redox-active protein containing two active site cysteines (Cys-32 and Cys-35) that cycle between the dithiol and disulfide forms as Trx1 reduces target proteins.	Disulfides	137-146	thioredoxin	Homo sapiens	13-17
12816947-1	2003	Thioredoxin (Trx1) is a redox-active protein containing two active site cysteines (Cys-32 and Cys-35) that cycle between the dithiol and disulfide forms as Trx1 reduces target proteins.	Disulfides	137-146	thioredoxin	Homo sapiens	156-160
12816947-3	2003	Using the redox Western blot technique and matrix assisted laser desorption ionization time-of-flight mass spectrometry mass spectrometry, we determined the midpoint potential (E0) of the Trx1 active site (-230 mV) and identified a second redox-active dithiol/disulfide (Cys-62 and Cys-69) in an alpha helix proximal to the active site, which formed under oxidizing conditions.	Disulfides	260-269	thioredoxin	Homo sapiens	188-192
15011956-4	2004	In addition, the HLA-B27 heavy chain is unusual in that it has a tendency to misfold in the endoplasmic reticulum and to form disulfide linked heavy chain dimers that can be expressed on the cell surface.	Disulfides	126-135	major histocompatibility complex, class I, B	Homo sapiens	17-24
12816947-4	2003	This non-active site disulfide was not a substrate for reduction by thioredoxin reductase and delayed the reduction of the active site disulfide by thioredoxin reductase.	Disulfides	21-30	peroxiredoxin 5	Homo sapiens	148-169
30542351-5	2018	In the present study, we generated a variant form of murine XCL1 termed mXCL1-V21C/A59C that contained a second disulfide bond to stabilize its chemokine structure.	Disulfides	112-121	chemokine (C motif) ligand 1	Mus musculus	60-64
12816947-4	2003	This non-active site disulfide was not a substrate for reduction by thioredoxin reductase and delayed the reduction of the active site disulfide by thioredoxin reductase.	Disulfides	135-144	peroxiredoxin 5	Homo sapiens	148-169
30542351-5	2018	In the present study, we generated a variant form of murine XCL1 termed mXCL1-V21C/A59C that contained a second disulfide bond to stabilize its chemokine structure.	Disulfides	112-121	chemokine (C motif) ligand 1	Mus musculus	72-77
12816947-7	2003	Taken together these results suggest that the Cys-62-Cys-69 disulfide could provide a means to transiently inhibit Trx1 activity under conditions of redox signaling or oxidative stress, allowing more time for the sensing and transmission of oxidative signals.	Disulfides	60-69	thioredoxin	Homo sapiens	115-119
30425244-5	2018	Second, we show that an endogenous GluN3A disulfide bond endows GluN1/GluN3A receptors with distinct redox modulation, profoundly affecting agonist sensitivity and gating kinetics.	Disulfides	42-51	glutamate receptor, ionotropic, NMDA1 (zeta 1)	Mus musculus	64-69
12878219-8	2003	As reported for some reactive cysteine-containing enzymes, our results suggest that inactivation of NAT1 by S-nitrosothiols is due to direct attack of the highly reactive cysteine residue in the enzyme active site on the sulfur of S-nitrosothiols to form a mixed disulfide between these NO-derived oxidants and NAT1.	Disulfides	263-272	N-acetyltransferase 1	Homo sapiens	100-104
12878219-8	2003	As reported for some reactive cysteine-containing enzymes, our results suggest that inactivation of NAT1 by S-nitrosothiols is due to direct attack of the highly reactive cysteine residue in the enzyme active site on the sulfur of S-nitrosothiols to form a mixed disulfide between these NO-derived oxidants and NAT1.	Disulfides	263-272	N-acetyltransferase 1	Homo sapiens	311-315
16328790-1	2004	The role of the ferredoxin:thioredoxin system in the reversible light activation of chloroplast enzymes by thiol-disulfide interchange with thioredoxins is now well established.	Disulfides	113-122	thioredoxin	Homo sapiens	27-38
16328790-4	2004	The unique 4Fe-4S cluster enzyme ferredoxin:thioredoxin reductase (FTR) uses photosynthetically reduced ferredoxin as an electron donor to reduce the disulfide bridge of different thioredoxin isoforms.	Disulfides	150-159	thioredoxin	Homo sapiens	44-55
16328790-4	2004	The unique 4Fe-4S cluster enzyme ferredoxin:thioredoxin reductase (FTR) uses photosynthetically reduced ferredoxin as an electron donor to reduce the disulfide bridge of different thioredoxin isoforms.	Disulfides	150-159	thioredoxin	Homo sapiens	180-191
30482150-0	2018	Effect of Disulfide Bond Incorporation on the Structure and Activity of Endostatin Peptide.	Disulfides	10-19	collagen type XVIII alpha 1 chain	Homo sapiens	72-82
14530280-6	2003	The intramolecular disulfide bonds of LAP* and LAP have been determined.	Disulfides	19-28	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	38-42
14530280-6	2003	The intramolecular disulfide bonds of LAP* and LAP have been determined.	Disulfides	19-28	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	38-41
14530280-7	2003	Among the cysteine residues, amino acid 11 (Cys11) of LAP* plays key roles for determining the overall intramolecular disulfide bonds that form the basis for redox switch regulation.	Disulfides	118-127	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	54-57
14645556-11	2003	In this model, another cysteine residue in the GP(4) protein is responsible for the covalent association of GP(3) with the disulfide-linked GP(2b)/GP(4) heterodimer.	Disulfides	123-132	CD36 molecule	Homo sapiens	47-52
14645556-11	2003	In this model, another cysteine residue in the GP(4) protein is responsible for the covalent association of GP(3) with the disulfide-linked GP(2b)/GP(4) heterodimer.	Disulfides	123-132	CD36 molecule	Homo sapiens	147-152
13679368-4	2003	The extra-cellular portion of pIgR consists of five Ig-like domains (D1-D5), each of which contains 104-114 amino acids and two disulfide bonds.	Disulfides	128-137	polymeric immunoglobulin receptor	Homo sapiens	30-34
13679368-8	2003	Finally, treating pIgR with a reducing agent abolished CbpA binding, suggesting that disulfide bonding is required for the formation of CbpA-binding motif(s).	Disulfides	85-94	polymeric immunoglobulin receptor	Homo sapiens	18-22
12909633-11	2003	Our data indicate that SPTRX-2 incorporation into the FS lags well behind FS assembly, suggesting it is required during the final stages of sperm tail maturation in the testis and/or epididymis, where extensive disulfide bonding of FS proteins occurs.	Disulfides	211-220	NME/NM23 family member 8	Rattus norvegicus	23-30
12912978-4	2003	CRSBP-1 expressed in transfected cells is an approximately 120-kDa disulfide-linked homodimeric glycoprotein and exhibits dual ligand (CRS-containing growth regulators (v-sis gene product and insulin-like growth factor binding protein-3, IGFBP-3) and hyaluronic acid) binding activity.	Disulfides	67-76	lymphatic vessel endothelial hyaluronan receptor 1	Homo sapiens	0-7
12816866-0	2003	Disruption of the beta3 663-687 disulfide bridge confers constitutive activity to beta3 integrins.	Disulfides	32-41	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	18-23
12816866-0	2003	Disruption of the beta3 663-687 disulfide bridge confers constitutive activity to beta3 integrins.	Disulfides	32-41	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	82-87
12816866-5	2003	The functional analysis of cysteine mutations within the 616 to 690 region of beta3 or chimeric beta3-beta7 subunits revealed that disruption of the C663-C687 disulfide bridge endows constitutive activity to the alphaIIbbeta3 receptor.	Disulfides	159-168	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	78-107
14703797-2	2003	It is possibly that RI may have antioxidant effect by thiol-disulfide exchange reaction.	Disulfides	60-69	ribonuclease/angiogenin inhibitor 1	Mus musculus	20-22
12962478-0	2003	Human recombinant resistin protein displays a tendency to aggregate by forming intermolecular disulfide linkages.	Disulfides	94-103	resistin	Homo sapiens	18-26
12962478-6	2003	The oligomeric structure was SDS-insensitive but beta-mercaptoethanol-sensitive, pointing to the importance of disulfide linkages in resistin oligomerization.	Disulfides	111-120	resistin	Homo sapiens	133-141
12962478-8	2003	The presence of intermolecular disulfide bond(s), crucial in maintaining the global conformation of resistin, was further evident from fluorescence emission spectra.	Disulfides	31-40	resistin	Homo sapiens	100-108
12939134-8	2003	These intramolecular disulfides can then be rapidly and effectively rereduced by thioredoxin/thioredoxin reductase but not glutathione.	Disulfides	21-31	thioredoxin	Homo sapiens	81-92
12939134-8	2003	These intramolecular disulfides can then be rapidly and effectively rereduced by thioredoxin/thioredoxin reductase but not glutathione.	Disulfides	21-31	peroxiredoxin 5	Homo sapiens	93-114
12936977-3	2003	Two isoforms of hBD3 were synthesized: the first with native disulfide linkages and the second with nonnative linkages.	Disulfides	61-70	defensin beta 103B	Homo sapiens	16-20
12919322-2	2003	Together with maurotoxin, Pi1, Pi7 and HsTx1, Pi4 belongs to the alpha KTX6 subfamily of short four-disulfide-bridged scorpion toxins acting on K+ channels.	Disulfides	100-109	serpin family E member 2	Rattus norvegicus	31-34
12950113-4	2003	Recombinant human BMP (rhBMP)-7 was produced in COS-7 cells, as a processed mature disulfide-linked homodimer, with an apparent molecular weight of 36,000.	Disulfides	83-92	bone morphogenetic protein 1	Homo sapiens	18-21
12878193-9	2003	In addition, the analyses of porcine ZPB and ZPC fragments revealed that disulfide bonds within the ZP domains are divided into two groups, suggesting that the ZP domain consists of two subdomains.	Disulfides	73-82	zona pellucida glycoprotein 4	Homo sapiens	37-40
12721298-4	2003	Moreover, applying global molecular dynamic search established a theoretical prospect of generating a disulfide bond between two Sx1A transmembrane helices.	Disulfides	102-111	syntaxin 1A	Homo sapiens	129-133
12823617-6	2003	The native disulfide connectivity in HNP1, i.e. Cys1-Cys6, Cys2-Cys4 and Cys3-Cys5, is verified by mass mapping of peptide fragments generated by proteolytic digestion and Edman degradation.	Disulfides	11-20	HNP1	Homo sapiens	37-41
12823617-6	2003	The native disulfide connectivity in HNP1, i.e. Cys1-Cys6, Cys2-Cys4 and Cys3-Cys5, is verified by mass mapping of peptide fragments generated by proteolytic digestion and Edman degradation.	Disulfides	11-20	cystin 1	Homo sapiens	48-52
12810574-1	2003	Posttranslational processing of the TSH receptor (TSHR) involves proteolysis of a single chain holoreceptor into TSHR-alpha (or A) and TSHR-beta (or B) subunits, which remain associated via disulfide bonds and which may then form oligomers.	Disulfides	190-199	thyrotropin receptor	Cricetulus griseus	36-48
12810574-1	2003	Posttranslational processing of the TSH receptor (TSHR) involves proteolysis of a single chain holoreceptor into TSHR-alpha (or A) and TSHR-beta (or B) subunits, which remain associated via disulfide bonds and which may then form oligomers.	Disulfides	190-199	thyrotropin receptor	Cricetulus griseus	50-54
12787448-3	2003	G20 (MEF G140-190 G144-158) is a peptide of 69 amino acids with two disulfide bridges, which comprises multiple protective B-cell epitopes.	Disulfides	68-77	chromosome 3 open reading frame 18	Homo sapiens	0-3
12734397-5	2003	Xfz3 dimerization requires intramolecular and/or intermolecular disulfide linkages, and the N-terminal extracellular region of the receptor, including the cysteine-rich domain (CRD), is sufficient for dimerization.	Disulfides	64-73	frizzled class receptor 3 S homeolog	Xenopus laevis	0-4
12727792-13	2003	The PDI superfamily has multiple cellular roles including chaperoning assembled glycoproteins, regulating the activities of transcription factors, and regulating disulfide bond formation.	Disulfides	162-171	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	4-7
12725245-4	2003	Thermolytic digestion demonstrated three disulfide bond pairings of the EGF-like domain in HB-EGF is consistent with that of human-EGF and human-TGF-alpha.	Disulfides	41-50	epidermal growth factor	Homo sapiens	72-75
12725245-4	2003	Thermolytic digestion demonstrated three disulfide bond pairings of the EGF-like domain in HB-EGF is consistent with that of human-EGF and human-TGF-alpha.	Disulfides	41-50	heparin binding EGF like growth factor	Homo sapiens	91-97
12725245-4	2003	Thermolytic digestion demonstrated three disulfide bond pairings of the EGF-like domain in HB-EGF is consistent with that of human-EGF and human-TGF-alpha.	Disulfides	41-50	epidermal growth factor	Homo sapiens	94-97
12642668-11	2003	These disulfide bonds produce a heterogeneous array of oligomers, including some species that can form an active complex with TLR4.	Disulfides	6-15	toll like receptor 4	Homo sapiens	126-130
12533544-3	2003	Here we show that plexin-B1 and plexin-B2 undergo proteolytic processing in their extracellular portion, thereby converting single-chain precursors into non-disulfide-linked, heterodimeric receptors.	Disulfides	157-166	plexin B1	Homo sapiens	18-27
12533544-3	2003	Here we show that plexin-B1 and plexin-B2 undergo proteolytic processing in their extracellular portion, thereby converting single-chain precursors into non-disulfide-linked, heterodimeric receptors.	Disulfides	157-166	plexin B2	Homo sapiens	32-41
12496257-9	2003	Structurally, we show that oligomer formation of Acrp30 critically depends on disulfide bond formation mediated by Cys-39.	Disulfides	78-87	adiponectin, C1Q and collagen domain containing	Mus musculus	49-55
12616495-3	2003	We have previously shown that HLA-B27 is capable of forming beta(2)m-free disulfide-bonded homodimers in vitro.	Disulfides	74-83	major histocompatibility complex, class I, B	Homo sapiens	30-37
12616495-3	2003	We have previously shown that HLA-B27 is capable of forming beta(2)m-free disulfide-bonded homodimers in vitro.	Disulfides	74-83	beta-2-microglobulin	Homo sapiens	60-68
12616495-4	2003	Here we show that HLA-B27 forms disulfide-bonded homodimers in vivo by two distinct pathways.	Disulfides	32-41	major histocompatibility complex, class I, B	Homo sapiens	18-25
12458205-13	2003	In vitro reaction of these apocytochromes c with heme to yield holocytochromes c, and the tendency to form a disulfide, have implications for the different systems responsible for cytochrome c maturation in vivo in various organisms.	Disulfides	109-118	cytochrome c, somatic	Equus caballus	180-192
12218052-6	2003	We conclude that on average two of the nine disulfides of gp120 are reduced during interaction with the lymphocyte surface after CXCR4 binding prior to fusion and that cell surface PDI catalyzes this process.	Disulfides	44-54	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	58-63
12502876-2	2003	When expressed in mammalian cells, E1 and E2 form both noncovalently linked E1E2 heterodimers, believed to be properly folded, and disulfide-linked, high-molecular-weight aggregates that are misfolded.	Disulfides	131-140	small nucleolar RNA, H/ACA box 73A	Homo sapiens	35-44
12377788-0	2002	Engineering the refolding pathway and the quaternary structure of seminal ribonuclease by newly introduced disulfide bridges.	Disulfides	107-116	seminal ribonuclease	Bos taurus	66-86
12463754-2	2002	It is composed of a disulfide-linked C8alpha-gamma heterodimer and a noncovalently associated C8beta chain.	Disulfides	20-29	complement C8 alpha chain	Homo sapiens	37-44
12239218-8	2002	The formation of at least one of the disulfide bonds in the CD1d heavy chain is coupled to its glucose trimming-dependent association with ERp57, calnexin, and calreticulin.	Disulfides	37-46	CD1d molecule	Homo sapiens	60-64
12417333-1	2002	The nuclear magnetic resonance structure of the unliganded pheromone-binding protein (PBP) from Bombyx mori at pH above 6.5, BmPBP(B), consists of seven helices with residues 3-8, 16-22, 29-32, 46-59, 70-79, 84-100, and 107-124, and contains the three disulfide bridges 19-54, 50-108, and 97-117.	Disulfides	252-261	pheromone-binding protein	Bombyx mori	86-89
12351392-4	2002	TSP-1 and TSP-2 are structurally similar trimeric proteins composed of disulfide-linked 150-kDa monomers.	Disulfides	71-80	thrombospondin 2	Homo sapiens	10-15
12269810-8	2002	The former shows that disulfide-linked dimers of apolipoprotein A-II form amphipathic alpha-helices which aggregate into tetramers.	Disulfides	22-31	apolipoprotein A2	Homo sapiens	49-68
12376475-2	2002	The present structure-activity relationship studies were designed to define the role of allyl groups and the disulfide chain in mGSTP1-inducing activity of DADS.	Disulfides	109-118	glutathione S-transferase, pi 1	Mus musculus	128-134
12376475-9	2002	The role of the disulfide chain in DADS-mediated induction of mGSTP1 was further investigated by testing a pair of alkadienes (1,7-octadiene and 1,8-nonadiene) having structural similarity to DADS.	Disulfides	16-25	glutathione S-transferase, pi 1	Mus musculus	62-68
12376475-12	2002	In conclusion, the results of the present study clearly indicate that the presence of terminal allyl groups as well as the central disulfide chain is required for maximum induction of mGSTP1 in vivo by garlic-derived OSCs.	Disulfides	131-140	glutathione S-transferase, pi 1	Mus musculus	184-190
12213606-1	2002	Thioredoxins are small molecular weight disulfide oxidoreductases specialized in the reduction of disulfide bonds on other proteins.	Disulfides	40-49	thioredoxin	Homo sapiens	0-12
12163607-5	2002	A soluble form of Env, SOS gp140, can be made that has gp120 stably linked to the gp41 ectodomain by an intermolecular disulfide bond.	Disulfides	119-128	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	55-60
12362327-3	2002	Thioredoxin, a ubiquitous 12 kDa protein with a catalytically active disulfide active site (Cys-Gly-Pro-Cys), plays a central role in controlling the redox status of disulfide bonds in proteins that regulate a range of processes.	Disulfides	69-78	thioredoxin	Homo sapiens	0-11
12362327-3	2002	Thioredoxin, a ubiquitous 12 kDa protein with a catalytically active disulfide active site (Cys-Gly-Pro-Cys), plays a central role in controlling the redox status of disulfide bonds in proteins that regulate a range of processes.	Disulfides	166-175	thioredoxin	Homo sapiens	0-11
12362327-7	2002	In so doing, the usefulness of applying this method for both in vitro and in vivo analyses is discussed for thioredoxin and other disulfide proteins, especially those occurring in plants.	Disulfides	130-139	thioredoxin	Homo sapiens	108-119
12147353-3	2002	The central portion of the frog monomeric alphaM contained Cys residues positioned analogously to the Cys residues in human alpha(2)-macroglobulin (alpha(2)M), known to be involved in disulfide bridges.	Disulfides	184-193	alpha-2-macroglobulin	Homo sapiens	124-146
12147353-3	2002	The central portion of the frog monomeric alphaM contained Cys residues positioned analogously to the Cys residues in human alpha(2)-macroglobulin (alpha(2)M), known to be involved in disulfide bridges.	Disulfides	184-193	alpha-2-macroglobulin	Homo sapiens	148-157
12119401-7	2002	These data suggest that the intracellular glutathione/glutathione disulfide ratio, an indicator of the redox state of the cell, can regulate Trx functions reversibly through thiol-disulfide exchange reactions.	Disulfides	66-75	thioredoxin	Homo sapiens	141-144
11978783-0	2002	HLA-B27 misfolding is associated with aberrant intermolecular disulfide bond formation (dimerization) in the endoplasmic reticulum.	Disulfides	62-71	major histocompatibility complex, class I, B	Homo sapiens	0-7
11978783-3	2002	We report here that HLA-B27 HC also forms two types of aberrant disulfide-linked complexes (dimers) during the folding and assembly process that can be distinguished by conformation-sensitive antibodies W6/32 and HC10.	Disulfides	64-73	major histocompatibility complex, class I, B	Homo sapiens	20-27
11978783-9	2002	These results demonstrate that residues comprising the HLA-B27 B pocket result in aberrant HC folding and disulfide bond formation, and thus confer unusual properties on this molecule that are unrelated to peptide selection per se, yet may be important in disease pathogenesis.	Disulfides	106-115	major histocompatibility complex, class I, B	Homo sapiens	55-62
12070343-6	2002	Ebselen competed with disulfide substrates for reduction by Trx and, therefore, acted as an inhibitor of protein disulfide reduction by the Trx system.	Disulfides	22-31	thioredoxin	Homo sapiens	140-143
12070343-6	2002	Ebselen competed with disulfide substrates for reduction by Trx and, therefore, acted as an inhibitor of protein disulfide reduction by the Trx system.	Disulfides	113-122	thioredoxin	Homo sapiens	60-63
12070343-6	2002	Ebselen competed with disulfide substrates for reduction by Trx and, therefore, acted as an inhibitor of protein disulfide reduction by the Trx system.	Disulfides	113-122	thioredoxin	Homo sapiens	140-143
12119116-9	2002	Two sequence differences that may relate to the instability are that trout LPL lacks the disulfide bridge in the C-terminal domain and lacks Pro(258).	Disulfides	89-98	lipoprotein lipase	Homo sapiens	75-78
12031500-1	2002	Betacellulin (BTC) belongs to the epidermal growth factor (EGF) family of peptide ligands that are characterized by a six-cysteine consensus motif (EGF-motif) that forms three intra-molecular disulfide bonds, crucial for binding the ErbB receptor family.	Disulfides	192-201	betacellulin, epidermal growth factor family member	Mus musculus	14-17
12033936-2	2002	C8gamma is disulfide-linked to a C8alpha subunit that is noncovalently associated with a C8beta chain.	Disulfides	11-20	complement C8 alpha chain	Homo sapiens	33-40
12033936-9	2002	Cys40 in C8gamma, which forms the disulfide bond to C8alpha, is located in a partially disordered loop (loop 1, residues 38-52) near the opening of the calyx.	Disulfides	34-43	complement C8 alpha chain	Homo sapiens	52-59
12169016-2	2002	In oxidized thioredoxin, the two cysteines form a disulfide bond that is targeted by the enzyme thioredoxin reductase.	Disulfides	50-59	thioredoxin	Homo sapiens	12-23
12169016-2	2002	In oxidized thioredoxin, the two cysteines form a disulfide bond that is targeted by the enzyme thioredoxin reductase.	Disulfides	50-59	peroxiredoxin 5	Homo sapiens	96-117
12169016-4	2002	Thioredoxins participate in dithiol/disulfide exchange reactions with a large range of cellular substrates.	Disulfides	36-45	thioredoxin	Homo sapiens	0-12
12009900-8	2002	Examination of various compounds with Ava in positions 9,10 and/or 14,15 revealed that the Leu(9)-Gly(10) and Arg(14)-Pro(15) segments of the disulfide ring are the principal structural elements determining hMCH-1R selectivity and ability to act as a hMCH-1R antagonist.	Disulfides	142-151	melanin concentrating hormone receptor 1	Homo sapiens	207-214
12009900-8	2002	Examination of various compounds with Ava in positions 9,10 and/or 14,15 revealed that the Leu(9)-Gly(10) and Arg(14)-Pro(15) segments of the disulfide ring are the principal structural elements determining hMCH-1R selectivity and ability to act as a hMCH-1R antagonist.	Disulfides	142-151	melanin concentrating hormone receptor 1	Homo sapiens	251-258
12920851-2	2002	The resulting nanoparticle had an average of 2.7 annexin V proteins linked per CLIO nanoparticle through disulfide bonds.	Disulfides	105-114	annexin A5	Homo sapiens	49-58
11855838-4	2002	As established by enzyme cleavage, Tsk-MTX displays half-cystine pairings of the type C1-C5, C2-C6, C3-C7 and C4-C8 which, contrary to MTX, correspond to a disulfide bridge pattern common to known scorpion toxins.	Disulfides	156-165	tsukushi, small leucine rich proteoglycan	Mus musculus	35-38
11901190-3	2002	We present here the first evidence that peroxynitrite (ONOO(-)) releases zinc from the zinc-thiolate cluster of endothelial NOS (eNOS) and presumably forms disulfide bonds between the monomers.	Disulfides	156-165	nitric oxide synthase 3, endothelial cell	Mus musculus	112-127
11901190-3	2002	We present here the first evidence that peroxynitrite (ONOO(-)) releases zinc from the zinc-thiolate cluster of endothelial NOS (eNOS) and presumably forms disulfide bonds between the monomers.	Disulfides	156-165	nitric oxide synthase 3, endothelial cell	Mus musculus	129-133
11842251-5	2002	Furthermore, although most of the E1 and E2 proteins formed disulfide-linked aggregates, significant amounts of monomeric forms of the two proteins were detected by SDS-PAGE under non-reducing conditions, suggesting the presence of non-covalently associated E1 and E2.	Disulfides	60-69	small nucleolar RNA, H/ACA box 73A	Homo sapiens	34-43
12018622-0	2002	The disulfide structure of denatured epidermal growth factor: preparation of scrambled disulfide isomers.	Disulfides	4-13	epidermal growth factor	Homo sapiens	37-60
12018622-0	2002	The disulfide structure of denatured epidermal growth factor: preparation of scrambled disulfide isomers.	Disulfides	87-96	epidermal growth factor	Homo sapiens	37-60
12018622-2	2002	Under denaturing conditions and in the presence of a thiol catalyst, the native EGF denatures by shuffling its three native disulfide bonds and converts to a mixture of scrambled isomers.	Disulfides	124-133	epidermal growth factor	Homo sapiens	80-83
12018622-5	2002	The disulfide structures of eight major scrambled isomers of EGF were determined.	Disulfides	4-13	epidermal growth factor	Homo sapiens	61-64
11879648-5	2002	Further, using tandem dimers, we show that a disulfide bond between C35 in the N-terminal region and C481 in the C linker region can form either within a subunit or between subunits.	Disulfides	45-54	migration and invasion enhancer 1	Homo sapiens	68-71
11884082-6	2002	Twelve cysteine residues, forming six disulfide bonds within beta-subunit and two putative asparagine-linked glycosylation sites, are also conserved in the chicken FSH-beta-subunit.	Disulfides	38-47	follicle stimulating hormone beta subunit	Gallus gallus	164-172
11754734-0	2002	The intrachain disulfide bond of beta(2)-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH.	Disulfides	15-24	beta-2-microglobulin	Homo sapiens	33-54
11754734-2	2002	beta2M in the native state has a typical immunoglobulin fold with a buried intrachain disulfide bond.	Disulfides	86-95	beta-2-microglobulin	Homo sapiens	0-6
12884256-0	2003	Solid-state photodegradation of bovine somatotropin (bovine growth hormone): evidence for tryptophan-mediated photooxidation of disulfide bonds.	Disulfides	128-137	somatotropin	Bos taurus	39-51
12731880-1	2003	Protein disulfide isomerase (PDI) utilizes the active site sequence Cys-Gly-His-Cys (CGHC; E degrees " = -180 mV) to effect thiol-disulfide interchange during oxidative protein folding.	Disulfides	8-17	protein-disulfide isomerase	Escherichia coli	29-32
12719576-1	2003	A mutant human immunodeficiency virus (HIV) envelope protein (Env) with an engineered disulfide bond between the gp120 and gp41 subunits (SOS-Env) was expressed on cell surfaces.	Disulfides	86-95	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	113-118
12473655-8	2003	The mass spectra for the Asp(131)-Arg(153) peptides from the oxidized and reduced forms of human RNase H1 in the presence and absence of NEM showed peptide masses consistent with the formation of a disulfide bond between Cys(147) and Cys(148).	Disulfides	198-207	ribonuclease H1	Homo sapiens	97-105
12473655-9	2003	These data show that the formation of a disulfide bond between adjacent Cys(147) and Cys(148) residues results in an inactive enzyme conformation and provides further insights into the interaction between human RNase H1 and the heteroduplex substrate.	Disulfides	40-49	ribonuclease H1	Homo sapiens	211-219
12705891-0	2003	Amyloidogenic synthetic peptides of beta2-microglobulin--a role of the disulfide bond.	Disulfides	71-80	beta-2-microglobulin	Homo sapiens	36-55
12682008-2	2003	We show that PAI-2 loses its ability to polymerize following reduction of thiol groups, suggesting that an intramolecular disulfide bond is essential for the polymerization.	Disulfides	122-131	serpin family B member 2	Homo sapiens	13-18
12682008-5	2003	Reactive center loop peptide insertion experiments and binding of bis-ANS to hydrophobic cavities indicate that the C79-C161 disulfide bond stabilizes PAI-2 in a polymerogenic conformation with an open A-beta-sheet.	Disulfides	125-134	serpin family B member 2	Homo sapiens	151-156
12663761-9	2003	Non-disulfide-mediated N protein interactions were subsequently demonstrated both in vitro by the glutathione S-transferase (GST) pull-down assay and in vivo by the mammalian two-hybrid assay.	Disulfides	4-13	glutathione S-transferase kappa 1	Homo sapiens	98-123
12663761-9	2003	Non-disulfide-mediated N protein interactions were subsequently demonstrated both in vitro by the glutathione S-transferase (GST) pull-down assay and in vivo by the mammalian two-hybrid assay.	Disulfides	4-13	glutathione S-transferase kappa 1	Homo sapiens	125-128
12592025-8	2003	In the second step, rapid refolding of the oxidized heavy chains is afforded by disulfide bond-assisted folding in the presence of beta(2)-microglobulin and a specific peptide.	Disulfides	80-89	beta-2-microglobulin	Homo sapiens	131-152
12538769-9	2003	We conclude that c.460+1A&gt;G mutation of human SP-C results in disruption of disulfide-mediated folding encoded by Exon 4 leading to diversion of unprocessed proSP-C to aggresomes.	Disulfides	79-88	protein S (beta) pseudogene	Homo sapiens	160-165
12553798-1	2003	Ferredoxin:thioredoxin reductase (FTR) catalyzes the reduction of the disulfide in thioredoxin in two one-electron steps using an active site comprising a [4Fe-4S] in close proximity to a redox active disulfide.	Disulfides	70-79	thioredoxin	Homo sapiens	11-22
12553798-1	2003	Ferredoxin:thioredoxin reductase (FTR) catalyzes the reduction of the disulfide in thioredoxin in two one-electron steps using an active site comprising a [4Fe-4S] in close proximity to a redox active disulfide.	Disulfides	70-79	thioredoxin	Homo sapiens	83-94
12553798-1	2003	Ferredoxin:thioredoxin reductase (FTR) catalyzes the reduction of the disulfide in thioredoxin in two one-electron steps using an active site comprising a [4Fe-4S] in close proximity to a redox active disulfide.	Disulfides	201-210	thioredoxin	Homo sapiens	11-22
12553798-1	2003	Ferredoxin:thioredoxin reductase (FTR) catalyzes the reduction of the disulfide in thioredoxin in two one-electron steps using an active site comprising a [4Fe-4S] in close proximity to a redox active disulfide.	Disulfides	201-210	thioredoxin	Homo sapiens	83-94
12488098-7	2003	Here we evaluate the impact of this increased disulfide bridge complexity on the generation and selection of chimeric rabbit/human Fab libraries.	Disulfides	46-55	FA complementation group B	Homo sapiens	131-134
12619676-3	2003	This hypothetical protein, tentatively named Scp15, has significant similarity with p15, including conserved positions of four cysteine residues involved in the formation of essential disulfide bonds in p15.	Disulfides	184-193	cyclin-dependent kinase inhibitor 2B	Rattus norvegicus	47-50
12619676-3	2003	This hypothetical protein, tentatively named Scp15, has significant similarity with p15, including conserved positions of four cysteine residues involved in the formation of essential disulfide bonds in p15.	Disulfides	184-193	cyclin-dependent kinase inhibitor 2B	Rattus norvegicus	84-87
11754734-3	2002	The conformation and stability of recombinant beta2M in which the intrachain disulfide bond was reduced were studied by CD, tryptophan fluorescence, and one-dimensional NMR.	Disulfides	77-86	beta-2-microglobulin	Homo sapiens	46-52
11754734-7	2002	Under the same conditions, reduced beta2M did not form typical amyloid fibrils, although it inhibited fibril extension competitively, suggesting that the conformation defined by the disulfide bond is important for amyloid fibril formation of beta2M.	Disulfides	182-191	beta-2-microglobulin	Homo sapiens	35-41
11754734-7	2002	Under the same conditions, reduced beta2M did not form typical amyloid fibrils, although it inhibited fibril extension competitively, suggesting that the conformation defined by the disulfide bond is important for amyloid fibril formation of beta2M.	Disulfides	182-191	beta-2-microglobulin	Homo sapiens	242-248
30016556-5	2018	The digallanes reacted with 2 equiv of PhNCS in the presence of Na metal or at high temperatures through a unique reductive cleavage of the C=S bond to yield the disulfide-bridged digallium species [Na(THF)3 ]2 [L1 Ga(mu-S)2 GaL1 ] (5), [L2 Ga(mu-S)2 GaL2 ] (10), and [Na(DME)3 ][L2 Ga(mu-S)2 GaL2 ] (11).	Disulfides	162-171	galectin 1	Homo sapiens	225-229
12702350-0	2001	Evidence for the attachment of Hsp150/Pir2 to the cell wall of Saccharomyces cerevisiae through disulfide bridges.	Disulfides	96-105	heat shock protein HSP150	Saccharomyces cerevisiae S288C	31-37
12702350-0	2001	Evidence for the attachment of Hsp150/Pir2 to the cell wall of Saccharomyces cerevisiae through disulfide bridges.	Disulfides	96-105	heat shock protein HSP150	Saccharomyces cerevisiae S288C	38-42
12702350-1	2001	Here we present evidence that Hsp150/Pir2, a member of the Pir family of cell wall proteins, can be extracted from the purified cell walls of Saccharomyces cerevisiae by treatment with beta-mercaptoethanol, demonstrating that at least part of this protein is attached to the cell wall through disulfide bridges.	Disulfides	293-302	heat shock protein HSP150	Saccharomyces cerevisiae S288C	30-36
12702350-1	2001	Here we present evidence that Hsp150/Pir2, a member of the Pir family of cell wall proteins, can be extracted from the purified cell walls of Saccharomyces cerevisiae by treatment with beta-mercaptoethanol, demonstrating that at least part of this protein is attached to the cell wall through disulfide bridges.	Disulfides	293-302	heat shock protein HSP150	Saccharomyces cerevisiae S288C	37-41
12533669-8	2003	To conquer this hurdle, we have produced several PAI-1 mutants by replacing chosen amino acids with cysteine in the hope of creating disulfide bridges, which could make this insertion more difficult.	Disulfides	133-142	serpin family E member 1	Homo sapiens	49-54
12533669-9	2003	On the basis of the known structure of active PAI-1, we have identified amino acids that can be substituted with a cysteine residue to produce disulfide bridges linking the top and bottom parts of strands A3 and A5 as well as sites within the helix-D region.	Disulfides	143-152	serpin family E member 1	Homo sapiens	46-51
12218051-3	2002	Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors.	Disulfides	38-47	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	91-96
12218051-3	2002	Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors.	Disulfides	158-167	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	106-111
12218051-8	2002	We propose that a PDI.CD4 association at the cell surface enables PDI to reach CD4-bound virus and to reduce disulfide bonds present in the domain of gp120 that binds to CD4.	Disulfides	109-118	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	150-155
12218051-9	2002	Conformational changes resulting from the opening of gp120-disulfide loops may drive the processes of virus-cell and cell-cell fusion.	Disulfides	59-68	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	53-58
30218010-0	2018	Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges.	Disulfides	51-60	microtubule associated protein tau	Homo sapiens	4-7
12218066-2	2002	The primary structure determination of the dimeric invertebrate alpha(2)-macroglobulin (alpha(2)M) from Limulus polyphemus has been completed by determining its sites of glycosylation and disulfide bridge pattern.	Disulfides	188-197	alpha-2-macroglobulin	Homo sapiens	88-97
12218066-6	2002	The latter bridge forms the only interchain disulfide bridge in Limulus alpha(2)M.	Disulfides	44-53	alpha-2-macroglobulin	Homo sapiens	72-81
12218066-8	2002	Several peptides identified in the course of determining the disulfide bridge pattern provided evidence for the existence of two forms of Limulus alpha(2)M.	Disulfides	61-70	alpha-2-macroglobulin	Homo sapiens	146-155
12005423-3	2001	A novel method based on ion-spray mass spectrometry analysis of cyanylation-induced cleavage products of partially reduced protein with Tris(2-carboxyethyl)phosphine was needed to determine the recombinant ASP1 disulfide bond pairing.	Disulfides	211-220	odorant binding protein 1	Apis mellifera	206-210
30218010-5	2018	More interestingly, using labels linked by a disulfide bridge, we evidenced for the first time thiol disulfide exchanges between alphabeta-tubulin or MTs and Tau.	Disulfides	45-54	microtubule associated protein tau	Homo sapiens	158-161
11701933-5	2001	GILT facilitated the processing and presentation to antigen-specific T cells of protein antigens containing disulfide bonds.	Disulfides	108-117	interferon gamma inducible protein 30	Mus musculus	0-4
12677197-1	2002	Thioredoxin (Trx) is a small multifunctional protein with a redox active dithiol/disulfide in the active-site sequence Cys-Gly-Pro-Cys.	Disulfides	81-90	thioredoxin	Homo sapiens	0-11
12677197-1	2002	Thioredoxin (Trx) is a small multifunctional protein with a redox active dithiol/disulfide in the active-site sequence Cys-Gly-Pro-Cys.	Disulfides	81-90	thioredoxin	Homo sapiens	13-16
30043021-0	2018	Modulating the GSH/Trx selectivity of a fluorogenic disulfide-based thiol sensor to reveal diminished GSH levels under ER stress.	Disulfides	52-61	thioredoxin	Homo sapiens	19-22
12145281-7	2002	Dithiothreitol could reduce either the sulfenic acid or the disulfide, but the disulfide was a preferred substrate for thioredoxin, a natural electron donor.	Disulfides	79-88	thioredoxin	Homo sapiens	119-130
29429019-0	2018	An inter-subunit disulfide bond of artemin acts as a redox switch for its chaperone-like activity.	Disulfides	17-26	artemin	Homo sapiens	35-42
12206676-0	2002	Photoexcitation of tryptophan groups induces reduction of two disulfide bonds in goat alpha-lactalbumin.	Disulfides	62-71	alpha-lactalbumin	Capra hircus	86-103
12206676-1	2002	Illumination of goat alpha-lactalbumin (GLA) with 280 or 295 nm light results in tryptophan-mediated photolysis of disulfide bonds within the protein.	Disulfides	115-124	alpha-lactalbumin	Capra hircus	21-38
11483734-6	2001	Our data indicate that sf-Stk interacts with SFFV gp55 as well as gp55(P), the biologically active form of the viral glycoprotein, forming disulfide-linked complexes.	Disulfides	139-148	macrophage stimulating 1 receptor (c-met-related tyrosine kinase)	Mus musculus	26-29
11518528-8	2001	In the reduced form of PRDX5, Cys47 and Cys151 are distant of 13.8 A although these two cysteine residues are thought to be involved in peroxide reductase activity by forming an intramolecular disulfide intermediate in the oxidized enzyme.	Disulfides	193-202	peroxiredoxin 5	Homo sapiens	23-28
29429019-3	2018	According to the result of Ellman"s assay, there are nine free thiols (seven buried and two exposed) and one disulfide bond per monomer of artemin.	Disulfides	109-118	artemin	Homo sapiens	139-146
29429019-6	2018	Since the alkylation and reduction of artemin diminished its chaperone activity, it appears that its chaperoning potential depends on the formation of intermolecular disulfide bond and the presence of cysteine residues.	Disulfides	166-175	artemin	Homo sapiens	38-45
11558680-7	2001	Mass spectroscopic analysis confirmed that ANP is rapidly cleaved at the first cysteine of the disulfide ring, whereas BNP is particularly stable to such cleavage.	Disulfides	95-104	natriuretic peptide type A	Mus musculus	43-46
29619746-5	2018	RESULTS: We found that TERT enhanced the survival rate of cells under ER stress, regardless of ER stress inducers such as tunicamycin (protein glycosylation inhibitor), thapsigargin (Ca2+-ATPase inhibitor), brefeldin A (protein transport inhibitor), or dithiothreitol (disulfide bond formation inhibitor).	Disulfides	269-278	telomerase reverse transcriptase	Homo sapiens	23-27
11685454-4	2001	In addition, our data indicate the existence of covalent (disulfide-linked) heterodimers of certain HLA class I heavy chains (namely Cw1 and Cw4) and beta2m.	Disulfides	58-67	dynein light chain Tctex-type 1	Homo sapiens	133-136
11685454-4	2001	In addition, our data indicate the existence of covalent (disulfide-linked) heterodimers of certain HLA class I heavy chains (namely Cw1 and Cw4) and beta2m.	Disulfides	58-67	beta-2-microglobulin	Homo sapiens	150-156
12176051-1	2002	Members of the Quiescin-sulfhydryl oxidase (QSOX) family utilize a thioredoxin domain and a small FAD-binding domain homologous to the yeast ERV1p protein to oxidize sulfhydryl groups to disulfides with the reduction of oxygen to hydrogen peroxide.	Disulfides	187-197	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	141-146
12183582-3	2002	These results suggest that the functional domain of lactoferrin that binds to a salivary film lies in residues 473 to 538 and that the region might be concealed by disulfide bond formation between Cys481 and Cys532 in the Lf411 fragment.	Disulfides	164-173	lactotransferrin	Bos taurus	52-63
29789341-7	2018	Knockdown of Mia40, which introduces disulfide bonds into CHCH domain proteins, blocked mitochondrial import of CHCHD10.	Disulfides	37-46	coiled-coil-helix-coiled-coil-helix domain containing 10	Homo sapiens	112-119
12202536-8	2002	Consistent with oxidation"s causing this dysfunction, exposure to a disulfide-reducing agent rapidly restored the activity of the glutamate transporter in Muller cells of diabetic retinas.	Disulfides	68-77	solute carrier family 1 member 3	Rattus norvegicus	130-151
11513661-8	2001	This pre-extraction treatment cleaved disulfide linkages of the beta- and gamma-zeins and significantly reduced insoluble aggregates in zein isolates.	Disulfides	38-47	prolamin 50 kDa gamma zein	Zea mays	64-85
29789341-8	2018	Overexpression of Mia40 rescued mitochondrial import of CHCHD10 Q108P by enhancing disulfide-bond formation.	Disulfides	83-92	coiled-coil-helix-coiled-coil-helix domain containing 10	Homo sapiens	56-63
29729526-5	2018	Molecular modeling has confirmed that the twin-cysteines do form a disulfide bond in the gp120 subunit, which interacts with the V1 loop to stabilize the envelope trimer.	Disulfides	67-76	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	89-94
11437366-8	2001	Taken together these results suggest that, in isoforms containing both Cys-291 and Cys-322, a dimeric tau with an intermolecular disulfide bond through either Cys-291 or Cys-322 is presumably acting as a seed for initiation of tau polymerization.	Disulfides	129-138	microtubule associated protein tau	Homo sapiens	102-105
11437366-8	2001	Taken together these results suggest that, in isoforms containing both Cys-291 and Cys-322, a dimeric tau with an intermolecular disulfide bond through either Cys-291 or Cys-322 is presumably acting as a seed for initiation of tau polymerization.	Disulfides	129-138	microtubule associated protein tau	Homo sapiens	227-230
11335716-3	2001	Furthermore, the feasibility and desirability of introducing a disulfide bridge between CDR1 and CDR3 was investigated.	Disulfides	63-72	cerebellar degeneration related protein 1	Homo sapiens	88-92
11335716-5	2001	Mass spectrometric analyses indicated that CDR1-CDR3 disulfide formation was universal.	Disulfides	53-62	cerebellar degeneration related protein 1	Homo sapiens	43-47
12192077-0	2002	The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR.	Disulfides	12-21	beta-2-microglobulin	Homo sapiens	57-78
12102725-0	2002	A novel approach to the synthesis of EGF-like domains: a method for the one-pot regioselective formation of the three disulfide bonds of a human blood coagulation factor VII EGF-1 analogue.	Disulfides	118-127	G elongation factor mitochondrial 1	Homo sapiens	174-179
29410027-4	2018	Secreted AGR2 was defined to enhance VEGFR2 activity as evidenced by physical interaction of purified recombinant human AGR2 (rhAGR2) with rhVEGFA through the formation of a disulfide bond.	Disulfides	174-183	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	9-13
12089508-5	2002	The redox state of the thiols (disulfide versus dithiol) appeared to be regulated by thioredoxin, which is secreted by CD4(+) T cells.	Disulfides	31-40	thioredoxin	Homo sapiens	85-96
11470401-7	2001	Five chaperone proteins: BiP (Grp78); calreticulin (CRT); protein disulfide (PDI); ERp72; and Grp94, demonstrated immunoreactivity in the enlarged PSACH cisternae and the short rER channels of chondrocytes from both in-vivo and in-vitro samples.	Disulfides	66-75	peptidyl arginine deiminase 1	Homo sapiens	77-80
11433346-6	2001	Although FANCC lacks homology with conventional disulfide reductases, it functions by preventing the formation of inactivating disulfide bonds within GSTP1 during apoptosis.	Disulfides	48-57	glutathione S-transferase pi 1	Homo sapiens	150-155
12004064-2	2002	In prokaryotes, the catalytic pathway responsible for disulfide isomerization involves thioredoxin, thioredoxin reductase, and the DsbC, DsbG, and DsbD proteins.	Disulfides	54-63	thioredoxin	Homo sapiens	87-98
12004064-2	2002	In prokaryotes, the catalytic pathway responsible for disulfide isomerization involves thioredoxin, thioredoxin reductase, and the DsbC, DsbG, and DsbD proteins.	Disulfides	54-63	peroxiredoxin 5	Homo sapiens	100-121
29410027-4	2018	Secreted AGR2 was defined to enhance VEGFR2 activity as evidenced by physical interaction of purified recombinant human AGR2 (rhAGR2) with rhVEGFA through the formation of a disulfide bond.	Disulfides	174-183	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	120-124
29453085-1	2018	In this study, a redox-sensitive glioma-targeting micelle system was designed to deliver curcumin (CUR) by conjugating it to hyaluronic acid (HA-s-s-CUR, HSC) via disulfide linkage.	Disulfides	163-172	fucosyltransferase 1 (H blood group)	Homo sapiens	154-157
12081489-0	2002	Pathway of oxidative folding of alpha-lactalbumin: a model for illustrating the diversity of disulfide folding pathways.	Disulfides	93-102	lactalbumin alpha	Bos taurus	32-49
12081489-1	2002	The pathway of oxidative folding of alpha-lactalbumin (alpha LA) (four disulfide bonds) has been characterized by structural and kinetic analysis of the acid-trapped folding intermediates.	Disulfides	71-80	lactalbumin alpha	Bos taurus	36-53
11313366-3	2001	The mature hIntL was a secretory glycoprotein consisting of 295 amino acids and N-linked oligosaccharides, and its basic structural unit was a 120-kDa homotrimer in which 40-kDa polypeptides were bridged by disulfide bonds.	Disulfides	207-216	intelectin 1	Homo sapiens	11-16
29541710-5	2018	Subsequently, the addition of TrxR to the solution of the fCDs-Cu2+ complex leads to the cleavage of the disulfide bond of the fCDs, which acclaim the release of 3-mercaptopropionic acid.	Disulfides	105-114	peroxiredoxin 5	Homo sapiens	30-34
11439187-1	2001	The T cell receptor (TCR) consists of genetically diverse disulfide-linked alpha and beta chains in noncovalent association with the invariant CD3 subunits.	Disulfides	58-67	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	4-19
11439187-1	2001	The T cell receptor (TCR) consists of genetically diverse disulfide-linked alpha and beta chains in noncovalent association with the invariant CD3 subunits.	Disulfides	58-67	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	21-24
12118169-2	2002	New ideas have focused on abnormal characteristics of HLA-B27 resulting from aberrant folding, disulfide bond formation, or both, rather than a predilection for selecting arthritogenic peptides.	Disulfides	95-104	major histocompatibility complex, class I, B	Homo sapiens	54-61
12089063-2	2002	Apoptotic stimuli such as tumor necrosis factor (TNF) and reactive oxygen species (ROS) activate ASK1 in part by oxidizing Trx (forming intramolecular disulfide between C32 and C35) to release Trx from ASK1.	Disulfides	151-160	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	97-101
12089063-2	2002	Apoptotic stimuli such as tumor necrosis factor (TNF) and reactive oxygen species (ROS) activate ASK1 in part by oxidizing Trx (forming intramolecular disulfide between C32 and C35) to release Trx from ASK1.	Disulfides	151-160	thioredoxin	Homo sapiens	123-126
29412660-6	2018	Crystal structure analysis of the MIF-derived EPCALCS peptide, bound in its oxMIF-like conformation by the Fab fragment of BaxB01, revealed that this peptide adopts a curved conformation, making the central thiol protein oxidoreductase motif competent to undergo disulfide shuffling.	Disulfides	263-272	FA complementation group B	Homo sapiens	107-110
12089063-2	2002	Apoptotic stimuli such as tumor necrosis factor (TNF) and reactive oxygen species (ROS) activate ASK1 in part by oxidizing Trx (forming intramolecular disulfide between C32 and C35) to release Trx from ASK1.	Disulfides	151-160	chemokine like factor	Homo sapiens	169-172
12070343-5	2002	This rate is orders of magnitude faster than the reaction of dithiol Trx with insulin disulfides.	Disulfides	86-96	thioredoxin	Homo sapiens	69-72
29545395-8	2018	CONCLUSIONS: In the stressed heart and myocytes, PKG1alpha C42-disulfide formation contributes to PDE5 activation.	Disulfides	63-72	phosphodiesterase 5A, cGMP-specific	Mus musculus	98-102
12070343-6	2002	Ebselen competed with disulfide substrates for reduction by Trx and, therefore, acted as an inhibitor of protein disulfide reduction by the Trx system.	Disulfides	22-31	thioredoxin	Homo sapiens	60-63
11916965-3	2002	Analysis of various cysteine mutants, including mass spectrometry of tryptic peptides, indicated that the essential Cys(124) residue in the active site of PTEN specifically forms a disulfide with Cys(71) during oxidation by H(2)O(2).	Disulfides	181-190	phosphatase and tensin homolog	Homo sapiens	155-159
11359822-8	2001	Hence, human IgM carries functionally inactive IL-18 forming a disulfide-bridged complex, and this IL-18 moiety is from 10- to 100-fold higher than the conventional type 1 IL-18 in blood circulation in approximately 30% normal subjects.	Disulfides	63-72	interleukin 18	Rattus norvegicus	99-104
18432765-2	2001	BsAbs can be produced by chemically cross-linking purified antibodies or Fab fragments with reducible disulfide bonds or nonreducible thioether bonds, both of which are described in this unit.	Disulfides	102-111	FA complementation group B	Homo sapiens	73-76
29410996-2	2018	The thioredoxin system, comprised of NADPH, thioredoxin reductase (TrxR) and thioredoxin (Trx), exerts its activities via a disulfide-dithiol exchange reaction.	Disulfides	124-133	thioredoxin	Homo sapiens	4-15
11259642-7	2001	These observations, together with the biochemical probing and molecular modeling of the TGR structure, suggest a mechanism whereby the C-terminal selenotetrapeptide serves a role of a protein-linked GSSG and shuttles electrons from the disulfide center within the TR domain to either the glutaredoxin domain or Trx.	Disulfides	236-245	thioredoxin	Homo sapiens	311-314
12010514-6	2002	In addition, the recently discovered antimicrobially active human peptide LEAP-1/hepcidin, which contains four disulfide bonds, was successfully synthesized and subsequently oxidized.	Disulfides	111-120	hepcidin antimicrobial peptide	Homo sapiens	74-80
12010514-6	2002	In addition, the recently discovered antimicrobially active human peptide LEAP-1/hepcidin, which contains four disulfide bonds, was successfully synthesized and subsequently oxidized.	Disulfides	111-120	hepcidin antimicrobial peptide	Homo sapiens	81-89
29410996-2	2018	The thioredoxin system, comprised of NADPH, thioredoxin reductase (TrxR) and thioredoxin (Trx), exerts its activities via a disulfide-dithiol exchange reaction.	Disulfides	124-133	peroxiredoxin 5	Homo sapiens	44-65
12071705-8	2002	Purified B7-2 binds tightly to bacterially expressed monomeric and disulfide-linked homodimeric human CTLA-4 as shown by gel-filtration chromatography and native PAGE.	Disulfides	67-76	cytotoxic T-lymphocyte associated protein 4	Homo sapiens	102-108
11102453-0	2001	Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate.	Disulfides	65-74	perforin 1	Homo sapiens	52-61
29410996-2	2018	The thioredoxin system, comprised of NADPH, thioredoxin reductase (TrxR) and thioredoxin (Trx), exerts its activities via a disulfide-dithiol exchange reaction.	Disulfides	124-133	peroxiredoxin 5	Homo sapiens	67-71
11124937-6	2001	It introduces a cysteine at a position in NPR-A corresponding to a supplementary cysteine found in NPR-C6, another receptor of this family (a disulfide-linked dimer).	Disulfides	142-151	natriuretic peptide receptor 1	Rattus norvegicus	42-47
11124937-7	2001	Although this D435C mutation only leads to trace levels of NPR-A disulfide-linked dimer at basal state, covalent dimerization can be induced by a treatment with rat ANP or with other agonists.	Disulfides	65-74	natriuretic peptide receptor 1	Rattus norvegicus	59-64
11222958-4	2001	Sequence comparison identified several functionally and structurally conserved domains in the mosquito peroxidase, including a heme environment, a calcium binding site, and five possible disulfide bridges.	Disulfides	187-196	Peroxidase	Drosophila melanogaster	103-113
11069904-1	2001	Recent studies have shown that the G protein-coupled, extracellular calcium ([Ca(2+)](o))-sensing receptor (CaR) forms disulfide-linked dimers through cysteine residues within its extracellular domain and that dimerization of the CaR has functional implications.	Disulfides	119-128	CXADR pseudogene 1	Homo sapiens	108-111
11069904-1	2001	Recent studies have shown that the G protein-coupled, extracellular calcium ([Ca(2+)](o))-sensing receptor (CaR) forms disulfide-linked dimers through cysteine residues within its extracellular domain and that dimerization of the CaR has functional implications.	Disulfides	119-128	CXADR pseudogene 1	Homo sapiens	230-233
11069904-2	2001	In this study, we have investigated which of these disulfide linkages are essential for dimerization of the CaR and whether they are required for these functional interactions.	Disulfides	51-60	CXADR pseudogene 1	Homo sapiens	108-111
11069904-6	2001	These findings suggest that the CaR has at least two distinct types of motifs mediating dimerization and functional interactions, i.e. covalent interactions involving intermolecular disulfide bonds and noncovalent, possibly hydrophobic, interactions.	Disulfides	182-191	CXADR pseudogene 1	Homo sapiens	32-35
11087730-5	2001	EGF-II contains two of the three native disulfide bonds of EGF, Cys(14)-Cys(31) and Cys(33)-Cys(42).	Disulfides	40-49	epidermal growth factor	Homo sapiens	0-3
11087730-5	2001	EGF-II contains two of the three native disulfide bonds of EGF, Cys(14)-Cys(31) and Cys(33)-Cys(42).	Disulfides	40-49	epidermal growth factor	Homo sapiens	59-62
11087730-6	2001	However, formation of the third native disulfide (Cys(6)-Cys(20)) for EGF-II is slow and does not occur directly.	Disulfides	39-48	epidermal growth factor	Homo sapiens	70-73
11134145-6	2000	The mutation prevents the formation of the second disulfide bridge of LPL, which is an essential part of the lid covering the catalytic center.	Disulfides	50-59	lipoprotein lipase	Homo sapiens	70-73
11132158-5	2000	Like other CD2 family members, the extracellular region of Ly108 also contains an N-terminal Ig variable regionlike domain lacking any disulfide bonds and a membrane-proximal truncated C2-like domain with two conserved disulfide bonds.	Disulfides	135-144	SLAM family member 6	Mus musculus	59-64
11132158-5	2000	Like other CD2 family members, the extracellular region of Ly108 also contains an N-terminal Ig variable regionlike domain lacking any disulfide bonds and a membrane-proximal truncated C2-like domain with two conserved disulfide bonds.	Disulfides	219-228	SLAM family member 6	Mus musculus	59-64
11040037-11	2000	Thus, the functionally important amino terminus of the secretin receptor represents a structurally independent, highly folded, and disulfide-bonded domain, with a pattern that is likely critical and conserved throughout this receptor family.	Disulfides	131-140	secretin receptor	Homo sapiens	55-72
11041857-8	2000	When denatured by SDS under nonreducing conditions, a fraction of the CD39L4 protein migrates as a 110 kDa disulfide-linked dimer.	Disulfides	107-116	ectonucleoside triphosphate diphosphohydrolase 5 (inactive)	Homo sapiens	70-76
11005828-5	2000	(ii) A disulfide bond in the LHCII kinase, rather than in its substrate, may be a target component regulated by thioredoxin.	Disulfides	7-16	thioredoxin	Homo sapiens	112-123
11005828-9	2000	(iv) Upon high-light illumination of leaves, the target disulfide bond becomes exposed and thus is made available for reduction by thioredoxin, resulting in a stable inactivation of LHCII kinase.	Disulfides	56-65	thioredoxin	Homo sapiens	131-142
11029374-7	2000	GSH enhancement was not related to the redox state of the free cysteine residue (Cys-34) on HSA, however, reduction of disulfide bonds in HSA inhibited the increase in cellular GSH.	Disulfides	119-128	CD24a antigen	Mus musculus	138-141
11012661-2	2000	Thioredoxins, with a dithiol/disulfide active site (CGPC) are the major cellular protein disulfide reductases; they therefore also serve as electron donors for enzymes such as ribonucleotide reductases, thioredoxin peroxidases (peroxiredoxins) and methionine sulfoxide reductases.	Disulfides	29-38	thioredoxin	Homo sapiens	203-214
11012661-2	2000	Thioredoxins, with a dithiol/disulfide active site (CGPC) are the major cellular protein disulfide reductases; they therefore also serve as electron donors for enzymes such as ribonucleotide reductases, thioredoxin peroxidases (peroxiredoxins) and methionine sulfoxide reductases.	Disulfides	29-38	peroxiredoxin 5	Homo sapiens	228-242
11012661-9	2000	Thioredoxin reductase is a specific dimeric 70-kDa flavoprotein in bacteria, fungi and plants with a redox active site disulfide/dithiol.	Disulfides	119-128	peroxiredoxin 5	Homo sapiens	0-21
10955997-4	2000	We found that oxidative stresses including diamide and H(2)O(2) treatment cause disulfide cross-linking of NDPK inside cells.	Disulfides	80-89	cytidine/uridine monophosphate kinase 2	Homo sapiens	107-111
10955997-6	2000	This suggests that disulfide cross-linked NDPK may be a possible mechanism in the modification of cellular regulation.	Disulfides	19-28	cytidine/uridine monophosphate kinase 2	Homo sapiens	42-46
10955997-7	2000	To confirm this idea, oxidative modification of NDPK has been performed in vitro using purified human NDPK H(2)O(2) inactivated the nucleoside diphosphate (NDP) kinase activity of NDPK by producing intermolecular disulfide bonds.	Disulfides	213-222	cytidine/uridine monophosphate kinase 2	Homo sapiens	48-52
10955997-7	2000	To confirm this idea, oxidative modification of NDPK has been performed in vitro using purified human NDPK H(2)O(2) inactivated the nucleoside diphosphate (NDP) kinase activity of NDPK by producing intermolecular disulfide bonds.	Disulfides	213-222	cytidine/uridine monophosphate kinase 2	Homo sapiens	102-106
10955997-7	2000	To confirm this idea, oxidative modification of NDPK has been performed in vitro using purified human NDPK H(2)O(2) inactivated the nucleoside diphosphate (NDP) kinase activity of NDPK by producing intermolecular disulfide bonds.	Disulfides	213-222	cytidine/uridine monophosphate kinase 2	Homo sapiens	102-106
10955997-8	2000	Disulfide cross-linking of NDPK also dissociated the native hexameric structure into a dimeric form.	Disulfides	0-9	cytidine/uridine monophosphate kinase 2	Homo sapiens	27-31
10933789-0	2000	Structural studies of the high mobility group globular domain and basic tail of HMG-D bound to disulfide cross-linked DNA.	Disulfides	95-104	High mobility group protein D	Drosophila melanogaster	80-85
10933789-4	2000	To understand the interactions of the HMG domain and C-terminal tail of HMG-D with DNA in solution, a complex between a high-affinity truncated form of the protein and a disulfide cross-linked DNA fragment was studied using heteronuclear NMR techniques.	Disulfides	170-179	High mobility group protein D	Drosophila melanogaster	72-77
10801830-1	2000	The chloroplastic NADP-malate dehydrogenase is activated by reduction of its N- and C-terminal disulfides by reduced thioredoxin.	Disulfides	95-105	thioredoxin	Homo sapiens	117-128
10987366-0	2000	The thioredoxin boxes of thyroglobulin: possible implications for intermolecular disulfide bond formation in the follicle lumen.	Disulfides	81-90	thioredoxin	Homo sapiens	4-15
10833532-1	2000	Interactions between the reactive disulfide fungal metabolite, gliotoxin (GTX), and rabbit skeletal ryanodine receptor (RyR) calcium release channels have been examined.	Disulfides	34-43	LOC100009439	Oryctolagus cuniculus	120-123
10801354-5	2000	The structural comparison, an amino acid sequence alignment of the RNase T(2) enzymes, and comparison of the disulfide-bonding pattern of these enzymes show that the structure of RNase LE shown here is the basic framework of the animal/plant subfamily of RNase T(2) enzymes (including a self-incompatibility protein called S-RNase), and the structure of RNase Rh is that of the fungal subfamily of RNase T(2) enzymes (including RNase T(2)).	Disulfides	109-118	ribonuclease T2	Solanum lycopersicum	179-187
10806406-8	2000	The binding of CD38 ligands to the active site triggers therefore conformational changes that shield some backbone bonds and disulfide bridges against, respectively, proteolytic cleavage or reduction.	Disulfides	125-134	CD38 molecule	Homo sapiens	15-19
10806406-12	2000	These data have major implications in the knowledge of the CD38 structure, especially with regard to the location of disulfide bridges and their accessibility.	Disulfides	117-126	CD38 molecule	Homo sapiens	59-63
10754306-8	2000	We hypothesize that PAO-induced L-selectin shedding involves a regulatory molecule, such as protein disulfide isomerase (PDI), an enzyme that plays a role in the formation and rearrangement of disulfide bonds, contains PAO-binding, vicinal dithiol-active sites, and is expressed on the neutrophil surface.	Disulfides	100-109	selectin L	Homo sapiens	32-42
10713099-1	2000	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded, homodimeric mucin ( approximately 250 kDa) on leukocytes that binds to P-selectin on platelets and endothelial cells during the initial steps in inflammation.	Disulfides	47-56	selectin P ligand	Homo sapiens	0-32
10713099-1	2000	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded, homodimeric mucin ( approximately 250 kDa) on leukocytes that binds to P-selectin on platelets and endothelial cells during the initial steps in inflammation.	Disulfides	47-56	selectin P ligand	Homo sapiens	34-40
10713099-1	2000	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded, homodimeric mucin ( approximately 250 kDa) on leukocytes that binds to P-selectin on platelets and endothelial cells during the initial steps in inflammation.	Disulfides	47-56	selectin P	Homo sapiens	0-10
10666276-0	2000	Disulfide bonds and membrane topology of the vaccinia virus A17L envelope protein.	Disulfides	0-9	IMV membrane protein	Vaccinia virus	60-64
10666276-2	2000	Our mutagenesis studies indicated that cysteines 101 and 121 form an intramolecular disulfide bond and that cysteine 178 forms an intermolecular disulfide linking two A17L molecules.	Disulfides	145-154	IMV membrane protein	Vaccinia virus	167-171
10666276-3	2000	This arrangement of disulfide bonds has important implications for the topology of the A17L protein and supports a two-transmembrane model in which cysteines 101 and 121 are intraluminal and cysteine 178 is cytoplasmic.	Disulfides	20-29	IMV membrane protein	Vaccinia virus	87-91
10686155-1	2000	Human CD94 is a subunit of the disulfide-linked, heterodimeric natural killer (NK) cell surface receptor CD94/NKG2.	Disulfides	31-40	killer cell lectin like receptor C1	Homo sapiens	110-114
10652328-1	2000	The 79-amino acid, mature SP-B peptide contains three intramolecular disulfide bonds shared by all saposin-like proteins.	Disulfides	69-78	surfactant associated protein B	Mus musculus	26-30
10652328-2	2000	This study tested the hypothesis that the disulfide bond formed between cysteine residues 35 and 46 (residues 235 and 246 of the SP-B proprotein) is essential for proper function of SP-B.	Disulfides	42-51	surfactant associated protein B	Mus musculus	182-186
10649999-1	2000	Light generates reducing equivalents in chloroplasts that are used not only for carbon reduction, but also for the regulation of the activity of chloroplast enzymes by reduction of regulatory disulfides via the ferredoxin:thioredoxin reductase (FTR) system.	Disulfides	192-202	thioredoxin	Homo sapiens	222-233
10620363-0	2000	Disulfide bonds in big ET-1 are essential for the specific cleavage at the Trp(21)-Val(22) bond by soluble endothelin converting enzyme-1 from baculovirus/insect cells.	Disulfides	0-9	endothelin converting enzyme 1	Homo sapiens	107-137
10620363-8	2000	This result indicates that secondary/tertiary structure of big ET-1 induced by disulfide bonds is essential for the specific cleavage of the Trp(21)-Val(22) bond by ECE-1.	Disulfides	79-88	endothelin converting enzyme 1	Homo sapiens	165-170
11213471-2	2000	The protein mediating this transport is a disulfide-linked heterodimer of a light chain named xCT and a heavy chain previously known as 4F2hc.	Disulfides	42-51	solute carrier family 7 member 11	Homo sapiens	94-97
11213471-2	2000	The protein mediating this transport is a disulfide-linked heterodimer of a light chain named xCT and a heavy chain previously known as 4F2hc.	Disulfides	42-51	solute carrier family 3 member 2	Homo sapiens	136-141
10766509-6	2000	These results suggest that an intact disulfide portion of GSSG is required for the effective inhibition of caspase activity.	Disulfides	37-46	caspase 6	Homo sapiens	107-114
10585186-0	1999	Facilitating the formation of disulfide bonds in the Escherichia coli periplasm via coexpression of yeast protein disulfide isomerase.	Disulfides	30-39	protein-disulfide isomerase	Escherichia coli	106-133
10535922-3	1999	A 2.6-A resolution crystal structure of rat HBP23 in oxidized form revealed an unusual dimer structure in which the active residue Cys-52 forms a disulfide bond with conserved Cys-173 from another subunit by C-terminal tail swapping.	Disulfides	146-155	peroxiredoxin 1	Rattus norvegicus	44-49
10529171-10	1999	Additional constraints at the ends of the peptide, corresponding to the disulfide between the first and third cysteines in MCP-1, yielded further improvements in affinity.	Disulfides	72-81	C-C motif chemokine ligand 2	Homo sapiens	123-128
10766297-0	1999	Parallel syntheses of disulfide inhibitors of the thioredoxin redox system as potential antitumor agents.	Disulfides	22-31	thioredoxin	Homo sapiens	50-61
10766297-1	1999	We have reported previously that unsymmetrical disulfide inhibitors of the human thioredoxin/thioredoxin reductase redox system (hTrx/TR) possess antitumor activity.	Disulfides	47-56	thioredoxin	Homo sapiens	81-92
10766297-1	1999	We have reported previously that unsymmetrical disulfide inhibitors of the human thioredoxin/thioredoxin reductase redox system (hTrx/TR) possess antitumor activity.	Disulfides	47-56	thioredoxin	Homo sapiens	93-104
10766297-8	1999	The most potent inhibitors of the Trx system contained two heteroatoms ortho to the disulfide moiety in an aromatic functionality.	Disulfides	84-93	thioredoxin	Homo sapiens	34-37
10766297-11	1999	Bis-disulfides showed patterns of activity which depended on chain length, with optimum activity observed when the disulfide units were separated by 3.9 A, a similar distance to that separating the thioredoxin active site cysteine residues.	Disulfides	4-13	thioredoxin	Homo sapiens	198-209
10504260-0	1999	Structure and function in rhodopsin: effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase.	Disulfides	48-57	G protein-coupled receptor kinase 1	Homo sapiens	155-171
10504260-4	1999	In contrast, disulfide bonds 2-5 abolished both G(T) activation and phosphorylation by RK.	Disulfides	13-22	G protein-coupled receptor kinase 1	Homo sapiens	87-89
10508261-3	1999	Both hpH4 and mH4 (1) are selectively expressed by activated T cells and mature thymocytes, (2) are disulfide-linked dimers of two chains (29/37 kDa in humans, 25/29 kDa in mice), whose N-deglycosylation produces a single band at 20 - 21 kDa, and (3) display a low association with CD4 and the TCR.	Disulfides	100-109	prolyl 4-hydroxylase, transmembrane	Homo sapiens	5-9
10463601-0	1999	Pharmacokinetics and antitumor activity of a bivalent disulfide-stabilized Fv immunotoxin with improved antigen binding to erbB2.	Disulfides	54-63	erb-b2 receptor tyrosine kinase 2	Mus musculus	123-128
10441134-0	1999	Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin.	Disulfides	8-17	serpin family C member 1	Homo sapiens	111-123
10415716-1	1999	Differences in proteinase susceptibility between free TIMP-1 and the TIMP-1-MMP-3 complex and mutagenesis studies suggested that the residues around the disulfide bond between Cys1 and Cys70 in TIMP-1 may interact with MMPs.	Disulfides	153-162	cystin 1	Homo sapiens	176-180
10415716-1	1999	Differences in proteinase susceptibility between free TIMP-1 and the TIMP-1-MMP-3 complex and mutagenesis studies suggested that the residues around the disulfide bond between Cys1 and Cys70 in TIMP-1 may interact with MMPs.	Disulfides	153-162	matrix metallopeptidase 1	Homo sapiens	219-223
10375435-9	1999	A comparative study of recombinant human lens TTase and GST (mu and pi) on their dethiolating abilities using lens crystallin-thiol mixed disulfides showed that the lens TTase is 60-70% more efficient in the dethiolation/repair process than GST.	Disulfides	138-148	glutathione S-transferase kappa 1	Homo sapiens	56-59
10375435-10	1999	When TTase and GST were tested in conjunction for the dethiolation of thiol mixed disulfides, there was no significant enhancement of dethiolase activity.	Disulfides	82-92	glutathione S-transferase kappa 1	Homo sapiens	15-18
10318825-6	1999	Importantly, these data show that GT modification of most TCR subunits persisted until assembly of CD3alpha beta chains and formation of CD3-associated, disulfide-linked alpha beta heterodimers.	Disulfides	153-162	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	58-61
10397171-1	1999	Thioredoxin (TRX) has disulfide reducing activity and is reported to be involved in various cellular functions including the promotion of cell growth and apoptosis.	Disulfides	22-31	thioredoxin	Homo sapiens	0-11
10397171-1	1999	Thioredoxin (TRX) has disulfide reducing activity and is reported to be involved in various cellular functions including the promotion of cell growth and apoptosis.	Disulfides	22-31	thioredoxin	Homo sapiens	13-16
10698549-0	1999	Reduction of Cys36-Cys42 and Cys64-Cys74 disulfide bonds in recombinant human granulocyte colony stimulating factor.	Disulfides	41-50	colony stimulating factor 3	Homo sapiens	78-115
10698549-1	1999	The Cys36-Cys42 and Cys64-Cys74 disulfide bonds in recombinant methionyl human granulocyte colony-stimulating factor were reduced to sulfhydryls with dithiothreitol or mercury.	Disulfides	32-41	colony stimulating factor 3	Homo sapiens	79-116
10087161-9	1999	Together these data support an inhibitory mechanism, whereby cysteine -SH groups within the p56(lck) catalytic domain react with the isothiazolone ring, leading to ring opening and disulfide bond formation with the p56(lck) enzyme.	Disulfides	181-190	LCK proto-oncogene, Src family tyrosine kinase	Homo sapiens	92-100
10087161-9	1999	Together these data support an inhibitory mechanism, whereby cysteine -SH groups within the p56(lck) catalytic domain react with the isothiazolone ring, leading to ring opening and disulfide bond formation with the p56(lck) enzyme.	Disulfides	181-190	LCK proto-oncogene, Src family tyrosine kinase	Homo sapiens	96-99
10090736-10	1999	The two disulfide bridges present in the human P2Y1 receptor play a major role in the structure and stability of the receptor, to constrain the loops within the receptor, specifically stretching the EL2 over the opening of the TM cleft and thus defining the path of access to the binding site.	Disulfides	8-17	purinergic receptor P2Y1	Homo sapiens	47-60
10066809-5	1999	Both PPAE isozymes were proteins composed of two polypeptides (heavy and light chains) that are linked by disulfide linkage(s) and glycosylated serine proteases.	Disulfides	106-115	phenoloxidase-activating enzyme	Bombyx mori	5-9
10614055-12	1999	Recently, peripherin/rds-containing tetramers have been shown to form disulfide-mediated higher-order oligomers.	Disulfides	70-79	peripherin	Homo sapiens	10-20
9870313-2	1998	A biotinylated disulfide-bridged peptide mimicking the complete loop of clade B consensus V3 domain of gp120 (V3Cs), but not a biotinylated V3LAI peptide or a control beta-endorphin peptide of approximately the same molecular weight (MW), was found to bind specifically to MDM membrane proteins, in particular two proteins of 42 and 62 kDa migrating as sharp bands after electroblotting onto Immobilon, and this was specifically inhibited by anti-V3 antibodies.	Disulfides	15-24	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	103-108
11785944-4	2002	The disulfide forms of other cellular proteins rose in parallel with thioredoxin oxidation.	Disulfides	4-13	thioredoxin	Homo sapiens	69-80
14758071-5	2002	The factor was identified as oxidized galectin-1 with three intramolecular disulfide bonds and showed no lectin activity.	Disulfides	75-84	galectin 1	Homo sapiens	38-48
11825567-3	2002	The crystal structure of RAE-1beta was distorted from other MHC homologs and displayed noncanonical disulfide bonds.	Disulfides	100-109	retinoic acid early transcript beta	Mus musculus	25-34
12463512-4	2002	The method included the deposition of thin gold layers, the chemisorption of disulfides containing functional groups, and the subsequent coupling of PEG derivatives or heparin utilizing the functional groups of the disulfides.	Disulfides	215-225	progestagen associated endometrial protein	Homo sapiens	149-152
16228530-1	2002	Chloroplast NADP-dependent malate dehydrogenase (NADP-MDH, EC 1.1.1.82) is inactive in the dark and activated in the light via a reduction of specific disulfides by thiol-disulfide interchange with thioredoxin, reduced by the photosynthetic electron transfer.	Disulfides	151-161	thioredoxin	Homo sapiens	198-209
11742129-2	2002	In hemoglobin Porto Alegre (PA), the beta9 mutation induces polymerization by forming interchain disulfide bonds via the extra cysteine.	Disulfides	97-106	immunoglobulin kappa variable 1D-22 (pseudogene)	Homo sapiens	37-42
11804341-5	2001	The Cys residue of the extension peptide chain makes the disulfide bond between the two Fab domains.	Disulfides	57-66	FA complementation group B	Homo sapiens	88-91
11559704-1	2001	EndoGlyx-1, the antigen identified with the monoclonal antibody H572, is a pan-endothelial human cell surface glycoprotein complex composed of four different disulfide-bonded protein species with an apparent molecular mass of approximately 500 kDa.	Disulfides	158-167	multimerin 2	Homo sapiens	0-10
11592966-0	2001	Relative roles of albumin and ceruloplasmin in the formation of homocystine, homocysteine-cysteine-mixed disulfide, and cystine in circulation.	Disulfides	105-114	ceruloplasmin	Homo sapiens	30-43
11590138-0	2001	Disulfide connectivity of recombinant C-terminal region of human thrombospondin 2.	Disulfides	0-9	thrombospondin 2	Homo sapiens	65-81
11733994-4	2001	These connectivities prevented the release of gamma2LE1-3L4 m after BMP-1 cleavage which required in addition disulfide reshuffling by isomerases.	Disulfides	110-119	bone morphogenetic protein 1	Homo sapiens	68-73
11724947-4	2001	Here, we describe the NMR structure of BmPBP(A), which consists of a tightly packed arrangement of seven alpha-helices linked by well defined peptide segments and knitted together by three disulfide bridges.	Disulfides	189-198	pheromone-binding protein	Bombyx mori	39-44
11535606-4	2001	Here we report that when expressed alone RAMP1 is retained inside the cells where it is found in the endoplasmic reticulum and the Golgi predominantly as a disulfide-linked homodimer.	Disulfides	156-165	receptor activity modifying protein 1	Homo sapiens	41-46
11535606-6	2001	Although heterodimer formation does not involve intermolecular disulfide bonds, RAMP-CRLR association promotes the formation of intramolecular disulfide bonds within RAMP1.	Disulfides	143-152	receptor activity modifying protein 1	Homo sapiens	166-171
11747200-4	2001	The Oosp1 cDNA encodes a 202-amino acid protein that contains a 21-amino acid signal peptide sequence, 5 putative N-linked glycosylation consensus sequences, and 6 cysteines that are predicted to form 3 disulfide bonds.	Disulfides	203-212	oocyte secreted protein 1	Mus musculus	4-9
11602730-2	2001	In this protection assay-based procedure, a soluble gp140 protein with a stabilizing intermolecular disulfide bond between the gp120 and gp41 subunits (SOS gp140) was affinity bound to immobilized 2F5 under physiological conditions.	Disulfides	100-109	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	127-132
11546643-9	2001	However, there is experimental evidence that the disulfide bridge in the 4F2hc/LAT1 heterodimer plays a role in the regulation of a cation channel.	Disulfides	49-58	solute carrier family 3 member 2	Homo sapiens	73-78
11546643-9	2001	However, there is experimental evidence that the disulfide bridge in the 4F2hc/LAT1 heterodimer plays a role in the regulation of a cation channel.	Disulfides	49-58	solute carrier family 7 member 5	Homo sapiens	79-83
11573087-6	2001	The mechanism proposed here for the catalysis of arsenate reduction by pI258 ArsC involves a nucleophilic attack by Cys 10 on arsenate, the formation of a covalent intermediate and the transport of oxidative equivalents by a disulfide cascade.	Disulfides	225-234	Arsenate reductase	Staphylococcus aureus	77-81
11739896-6	2001	Two proteins comprising cysteine-containing polyionic fusion peptides, a modified Fab fragment and an alpha-glucosidase fusion, could be specifically conjugated by directed association and subsequent disulfide bond formation.	Disulfides	200-209	FA complementation group B	Homo sapiens	82-85
11739896-6	2001	Two proteins comprising cysteine-containing polyionic fusion peptides, a modified Fab fragment and an alpha-glucosidase fusion, could be specifically conjugated by directed association and subsequent disulfide bond formation.	Disulfides	200-209	sucrase-isomaltase	Homo sapiens	102-119
11455610-7	2001	We present a model for the transmembrane domain of CD3-zeta that is consistent with predictions based on mutagenesis, homology modeling, and the presence of a disulfide bond.	Disulfides	159-168	CD247 molecule	Homo sapiens	51-59
11397793-10	2001	To functionally characterize the new protein, human and mouse Grx2 proteins were expressed in Escherichia coli, and the purified proteins were shown to reduce mixed disulfides formed between GSH and S-sulfocysteine, hydroxyethyldisulfide, or cystine.	Disulfides	165-175	glutaredoxin 2 (thioltransferase)	Mus musculus	62-66
11443543-2	2001	Elsewhere we have described six disease-associated TNFRSF1A mutations, five of which disrupt extracellular cysteines involved in disulfide bonds; four other mutations have subsequently been reported.	Disulfides	129-138	TNF receptor superfamily member 1A	Homo sapiens	51-59
11467948-4	2001	TNFR-IgG is a disulfide-linked dimer of a polypeptide composed of the extracellular portion of the human type 1 (p55) tumor necrosis factor receptor (TNFR) fused to the hinge and Fc regions of the human IgG(1) heavy chain.	Disulfides	14-23	TNF receptor superfamily member 1A	Homo sapiens	0-4
11467948-4	2001	TNFR-IgG is a disulfide-linked dimer of a polypeptide composed of the extracellular portion of the human type 1 (p55) tumor necrosis factor receptor (TNFR) fused to the hinge and Fc regions of the human IgG(1) heavy chain.	Disulfides	14-23	TNF receptor superfamily member 1A	Homo sapiens	113-116
11467948-4	2001	TNFR-IgG is a disulfide-linked dimer of a polypeptide composed of the extracellular portion of the human type 1 (p55) tumor necrosis factor receptor (TNFR) fused to the hinge and Fc regions of the human IgG(1) heavy chain.	Disulfides	14-23	TNF receptor superfamily member 1A	Homo sapiens	118-148
11467948-4	2001	TNFR-IgG is a disulfide-linked dimer of a polypeptide composed of the extracellular portion of the human type 1 (p55) tumor necrosis factor receptor (TNFR) fused to the hinge and Fc regions of the human IgG(1) heavy chain.	Disulfides	14-23	TNF receptor superfamily member 1A	Homo sapiens	150-154
11447267-5	2001	We isolated a cDNA encoding a peptide, hepcidin (also referred to as LEAP-1, for liver-expressed antimicrobial peptide), that was very recently purified from human blood ultrafiltrate and from urine as a disulfide-bonded peptide exhibiting antimicrobial activity.	Disulfides	204-213	hepcidin antimicrobial peptide	Homo sapiens	39-47
11447267-5	2001	We isolated a cDNA encoding a peptide, hepcidin (also referred to as LEAP-1, for liver-expressed antimicrobial peptide), that was very recently purified from human blood ultrafiltrate and from urine as a disulfide-bonded peptide exhibiting antimicrobial activity.	Disulfides	204-213	hepcidin antimicrobial peptide	Homo sapiens	69-75
11358969-4	2001	Here we show that resistin is a disulfide-linked homodimer that can be converted to a monomer by reducing conditions.	Disulfides	32-41	resistin	Homo sapiens	18-26
11358969-9	2001	Thus, a single disulfide bond is necessary to connect two resistin subunits in a homodimer.	Disulfides	15-24	resistin	Homo sapiens	58-66
11451435-1	2001	Fragment 53--103 of bovine alpha-lactalbumin, prepared by limited peptic digestion of the protein at low pH, is a 51-residue polypeptide chain crosslinked by two disulfide bonds encompassing helix C (residues 86--98) of the native protein.	Disulfides	162-171	lactalbumin alpha	Bos taurus	27-44
11445066-4	2001	Disulfide bonds were found in the VLP which caused dimeric and trimeric VP1 linkages as demonstrated by non-reducing SDS-PAGE.	Disulfides	0-9	VHL like	Homo sapiens	34-37
11445066-5	2001	The VLP remained intact when disulfide bonds were reduced by dithiothreitol.	Disulfides	29-38	VHL like	Homo sapiens	4-7
11445066-6	2001	The VLP without disulfide bonds could be disassembled into capsomeres by EGTA alone, but those with disulfide bonds could not be disassembled by EGTA.	Disulfides	16-25	VHL like	Homo sapiens	4-7
11445066-9	2001	These results indicate that disulfide bonds play an important role in maintaining the integrity of the JC VLP by protecting calcium ions from chelation.	Disulfides	28-37	VHL like	Homo sapiens	106-109
11274154-1	2001	Macrophage stimulating protein (MSP) is secreted as 78-kDa single chain pro-MSP, which is converted to biologically active, disulfide-linked alphabeta chain MSP by cleavage at Arg(483)-Val(484).	Disulfides	124-133	macrophage stimulating 1	Homo sapiens	0-30
11274154-1	2001	Macrophage stimulating protein (MSP) is secreted as 78-kDa single chain pro-MSP, which is converted to biologically active, disulfide-linked alphabeta chain MSP by cleavage at Arg(483)-Val(484).	Disulfides	124-133	macrophage stimulating 1	Homo sapiens	32-35
11274154-1	2001	Macrophage stimulating protein (MSP) is secreted as 78-kDa single chain pro-MSP, which is converted to biologically active, disulfide-linked alphabeta chain MSP by cleavage at Arg(483)-Val(484).	Disulfides	124-133	macrophage stimulating 1	Homo sapiens	76-79
11274154-1	2001	Macrophage stimulating protein (MSP) is secreted as 78-kDa single chain pro-MSP, which is converted to biologically active, disulfide-linked alphabeta chain MSP by cleavage at Arg(483)-Val(484).	Disulfides	124-133	macrophage stimulating 1	Homo sapiens	76-79
11375523-2	2001	The disulfide-linked homodimer of the extracellular segment of human CTLA-4 and the receptor-binding domain of human B7-2 were purified and cocrystallized.	Disulfides	4-13	cytotoxic T-lymphocyte associated protein 4	Homo sapiens	69-75
11278672-2	2001	Cell wall attachment of Aga2p is mediated through two disulfide bonds to Aga1p (Cappellaro, C., Baldermann, C., Rachel, R., and Tanner, W. (1994) EMBO J.	Disulfides	54-63	Aga1p	Saccharomyces cerevisiae S288C	73-78
11278672-5	2001	Aga2p co-expressed with a 149-residue fragment of Aga1p formed a disulfide-linked complex with specific activity 43-fold higher than Aga2p expressed alone.	Disulfides	65-74	Aga1p	Saccharomyces cerevisiae S288C	50-55
11254682-5	2001	Ly49E was immunoprecipitated as a disulfide-linked homodimer with 46-kDa subunits.	Disulfides	34-43	killer cell lectin-like receptor, subfamily A, member 5	Mus musculus	0-5
11121408-7	2001	Interestingly, LAR expression significantly decreased the levels of disulfide-linked RET-MEN2A dimerization.	Disulfides	68-77	ret proto-oncogene	Homo sapiens	85-88
11121408-7	2001	Interestingly, LAR expression significantly decreased the levels of disulfide-linked RET-MEN2A dimerization.	Disulfides	68-77	ret proto-oncogene	Homo sapiens	89-94
11237737-1	2001	Reduction of disulfide bonds in human melanocortin 1 receptor (hMC1R) with increasing concentrations of DTT (dithiothreitol) resulted in a decrease in the binding of [125I]-ACTH (adrenocorticotropic hormone, L-isomer) in an uniphasic manner and a decrease in [125I]-NDP-MSH ([Nle(4),D-Phe(7)]-alpha-melanocyte stimulating hormone; D-isomer) binding in a biphasic manner.	Disulfides	13-22	melanocortin 1 receptor	Homo sapiens	38-61
11237737-1	2001	Reduction of disulfide bonds in human melanocortin 1 receptor (hMC1R) with increasing concentrations of DTT (dithiothreitol) resulted in a decrease in the binding of [125I]-ACTH (adrenocorticotropic hormone, L-isomer) in an uniphasic manner and a decrease in [125I]-NDP-MSH ([Nle(4),D-Phe(7)]-alpha-melanocyte stimulating hormone; D-isomer) binding in a biphasic manner.	Disulfides	13-22	melanocortin 1 receptor	Homo sapiens	63-68
11182766-12	2001	Eight of the ten disulfide linkages have been determined, including linkages of conserved cysteine residues not previously identified in other IGFBPs.	Disulfides	17-26	insulin-like growth factor binding protein 1	Rattus norvegicus	143-149
11460486-2	2001	More recently, a lower-resolution structure of native chicken fibrinogen has provided details about the structure of the central domain, and particularly the arrangement of disulfide bonds.	Disulfides	173-182	fibrinogen gamma chain	Gallus gallus	62-72
11693578-5	2001	The creation of intermolecular disulfide linkages between the apo-GR and associated heat shock proteins Hsp90 and Hsp70, which was evident in the presence of H2O2, was also significantly impaired after cadmium administration.	Disulfides	31-40	heat shock protein family A (Hsp70) member 1B	Rattus norvegicus	114-119
11445906-0	2001	Determination of the disulfide bond pattern of the endogenous and recombinant angiogenesis inhibitor endostatin by mass spectrometry.	Disulfides	21-30	collagen type XVIII alpha 1 chain	Homo sapiens	101-111
11778846-1	2001	Thioredoxin (TRX) is a small ubiquitous and multifunctional protein having a redox-active dithiol/disulfide within the conserved active site sequence -Cys-Gly-Pro-Cys-.	Disulfides	98-107	thioredoxin	Homo sapiens	0-11
11778846-1	2001	Thioredoxin (TRX) is a small ubiquitous and multifunctional protein having a redox-active dithiol/disulfide within the conserved active site sequence -Cys-Gly-Pro-Cys-.	Disulfides	98-107	thioredoxin	Homo sapiens	13-16
11120833-7	2000	These disulfide-stabilized bispecific Fab-scFv ("bibody") and trispecific Fab-(scFv)(2) ("tribody") heterodimers represent up to 90% of all secreted Ab fragments in the mammalian expression system and possess fully functional binding moieties.	Disulfides	6-15	FA complementation group B	Homo sapiens	38-41
11120833-7	2000	These disulfide-stabilized bispecific Fab-scFv ("bibody") and trispecific Fab-(scFv)(2) ("tribody") heterodimers represent up to 90% of all secreted Ab fragments in the mammalian expression system and possess fully functional binding moieties.	Disulfides	6-15	FA complementation group B	Homo sapiens	74-77
11209756-5	2000	Both species of PSPI-21 are composed of two chains, named chains A and B, which are linked by a disulfide bridge between Cys(146) and Cys(157).	Disulfides	96-105	Kunitz-type protease inhibitor precursor	Solanum tuberosum	16-23
11100975-6	2000	Since disulfide bonds and sulfhydryl groups have been shown to play vital roles in the assembly, organization, and function of various G-protein-coupled receptors, we report here the effect of disulfide and sulfhydryl group modifications on the agonist and antagonist binding activity of 5-HT1A receptors from bovine hippocampus.	Disulfides	6-15	5-hydroxytryptamine receptor 1A	Bos taurus	288-294
11100975-6	2000	Since disulfide bonds and sulfhydryl groups have been shown to play vital roles in the assembly, organization, and function of various G-protein-coupled receptors, we report here the effect of disulfide and sulfhydryl group modifications on the agonist and antagonist binding activity of 5-HT1A receptors from bovine hippocampus.	Disulfides	193-202	5-hydroxytryptamine receptor 1A	Bos taurus	288-294
11100975-13	2000	In addition, ligand-binding studies in presence of GTP-gamma-S, a nonhydrolyzable analogue of GTP, indicate that sulfhydryl groups (and disulfide bonds to a lesser extent) are vital for efficient coupling between the 5-HT1A receptor and the G-protein.	Disulfides	136-145	5-hydroxytryptamine receptor 1A	Bos taurus	217-223
11100975-15	2000	Our results point out that disulfide bonds and sulfhydryl groups could play an important role in ligand binding in 5-HT1A receptors.	Disulfides	27-36	5-hydroxytryptamine receptor 1A	Bos taurus	115-121
10982790-1	2000	Human thioredoxin (Trx) catalyzes intracellular disulfide reductions but has also co-cytokine activity with interleukins after leaderless secretion.	Disulfides	48-57	thioredoxin	Homo sapiens	6-17
10982790-1	2000	Human thioredoxin (Trx) catalyzes intracellular disulfide reductions but has also co-cytokine activity with interleukins after leaderless secretion.	Disulfides	48-57	thioredoxin	Homo sapiens	19-22
11082429-3	2000	Alteration of the bridging groups between the D-Cys(2) and D-Pen(4) residues of JH-54 from dithioether to disulfide revealed the importance of the relative position of the aromatic rings of the first and third residues in determining mu- and delta-affinities.	Disulfides	106-115	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	61-64
10896943-2	2000	High affinity binding of Ca(2+) to alpha-lactalbumin (LA) stabilizes the native structure and is required for the efficient generation of native protein with correct disulfide bonds from the reduced denatured state.	Disulfides	166-175	lactalbumin alpha	Bos taurus	35-52
10896943-2	2000	High affinity binding of Ca(2+) to alpha-lactalbumin (LA) stabilizes the native structure and is required for the efficient generation of native protein with correct disulfide bonds from the reduced denatured state.	Disulfides	166-175	lactalbumin alpha	Bos taurus	54-56
10942760-5	2000	This motif comprises the active site in enzymes involved in disulfide exchange reactions, including protein-disulfide isomerase (EC ) and thioredoxin.	Disulfides	60-69	thioredoxin	Homo sapiens	138-149
11068063-4	2000	Superinfection of both recombinant viruses into the cells in a spinner flask resulted in the formation of a 70kDa disulfide-bonded heterodimer detected in the supernatant by immunoblotting using anti-p40 and anti-p35 subunits antibodies.	Disulfides	114-123	annexin A1	Bos taurus	213-216
11041874-3	2000	In C8 from serum, these are arranged as a disulfide-linked C8alpha-gamma dimer that is noncovalently associated with C8beta.	Disulfides	42-51	complement C8 alpha chain	Homo sapiens	59-66
11041874-5	2000	From a comparative analysis of indels (insertions/deletions) in C8alpha and its structural homologues C8beta, C6, C7, and C9, it was determined that C8alpha contains a unique insertion (residues 159-175), which includes Cys(164) that forms the disulfide bond to C8gamma.	Disulfides	244-253	complement C8 alpha chain	Homo sapiens	149-156
11058761-3	2000	These subunits are arranged asymmetrically to form a disulfide-linked C8 alpha-gamma dimer that is noncovalently associated with C8 beta.	Disulfides	53-62	complement C8 alpha chain	Homo sapiens	70-78
10837476-1	2000	The assembly of lipoprotein(a) (Lp(a)) involves an initial noncovalent interaction between apolipoprotein (apo) B100 and apo(a), followed by the formation of a disulfide bond between apoB100 cysteine 4326 and apo(a) cysteine 4057.	Disulfides	160-169	apolipoprotein B	Mus musculus	183-190
10842173-4	2000	Analysis of the electrophoretic mobility of the membrane-bound protein in nonreducing and reducing conditions, together with cross-linking studies, indicated that the membrane-bound GlcAT-I formed active disulfide-linked dimers.	Disulfides	204-213	beta-1,3-glucuronyltransferase 3	Homo sapiens	182-189
10842173-9	2000	Our study demonstrates that GlcAT-I is organized as a homodimer as a result of disulfide bond formation mediated by Cys(33) localized in the stem region, whereas the residue Cys(301) localized in a conserved C-terminal domain is strictly required for the functional integrity of the enzyme.	Disulfides	79-88	beta-1,3-glucuronyltransferase 3	Homo sapiens	28-35
11027164-1	2000	In eukaryotic cells, protein disulfide isomerase (PDI) found in the endoplasmic reticulum (ER) catalyzes disulfide bond exchange and assists in protein folding of newly synthesized proteins.	Disulfides	29-38	protein disulfide-isomerase	Cricetulus griseus	50-53
11027164-4	2000	Increasing PDI activity in bacterial, yeast, and insect cell expression systems can lead to increased secretion of heterologous proteins containing disulfide bridges.	Disulfides	148-157	protein disulfide-isomerase	Cricetulus griseus	11-14
11009104-4	2000	We have engineered a disulfide-linked dimer of KIR2DL1 by introducing a free cysteine at the C-terminal stem region of the receptor.	Disulfides	21-30	killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 1	Homo sapiens	47-54
11009104-5	2000	The disulfide-linked KIR2DL1 dimer binds to HLA-Cw4 at a molar ratio of one dimer to one HLA-Cw4 molecule.	Disulfides	4-13	killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 1	Homo sapiens	21-28
11034317-0	2000	LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity.	Disulfides	23-32	hepcidin antimicrobial peptide	Homo sapiens	0-6
11034317-5	2000	The discovery of LEAP-1 extends the known families of mammalian peptides with antimicrobial activity by its novel disulfide motif and distinct expression pattern.	Disulfides	114-123	hepcidin antimicrobial peptide	Homo sapiens	17-23
10967136-2	2000	The rat cDNA was subsequently cloned, and ps20 was found to contain a WAP-type four-disulfide core motif, indicating it may function as a protease inhibitor.	Disulfides	84-93	WAP four-disulfide core domain 1	Rattus norvegicus	42-46
10816554-12	2000	Disulfide bonds in FucT III occur between Cys residues (Cys(81) to Cys(338) and Cys(91) to Cys(341)) at the N and C termini of the catalytic domain, bringing these ends close together in space.	Disulfides	0-9	fucosyltransferase 3 (Lewis blood group)	Homo sapiens	19-27
10913307-10	2000	Modified electrophoretic mobilities of mutant endopin 2 suggested the presence of intramolecular disulfide bonds; in addition, chemical modification suggested that Cys-374 influences the electrophoretic and conformational properties of endopin 2.	Disulfides	97-106	serpin A3-7	Bos taurus	46-55
10940639-1	2000	Betacellulin (BTC) belongs to the epidermal growth factor (EGF) family of peptide ligands that are characterised by a six-cysteine consensus motif that forms three intra-molecular disulfide bonds crucial for binding the ErbB receptor family.	Disulfides	180-189	betacellulin, epidermal growth factor family member	Mus musculus	0-12
10940639-1	2000	Betacellulin (BTC) belongs to the epidermal growth factor (EGF) family of peptide ligands that are characterised by a six-cysteine consensus motif that forms three intra-molecular disulfide bonds crucial for binding the ErbB receptor family.	Disulfides	180-189	betacellulin, epidermal growth factor family member	Mus musculus	14-17
10770945-9	2000	However, the displacement of the first disulfide in CDF causes the dimer to assume a more compact quaternary structure relative to CC chemokines, which is unique to CX(3)C chemokines.	Disulfides	39-48	LIF interleukin 6 family cytokine	Homo sapiens	52-55
10899311-4	2000	This fragment of Erv1p still binds FAD and catalyzes the formation of disulfide bonds but is no longer able to form dimers like the complete protein.	Disulfides	70-79	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	17-22
10779502-10	2000	Together, these data indicate that reaction of wild-type human Mb and H(2)O(2) differs from the corresponding reaction of other myoglobin species by formation of thiyl radicals that lead to a homodimer through intermolecular disulfide bond formation.	Disulfides	225-234	myoglobin	Homo sapiens	128-137
10891077-1	2000	Bovine seminal ribonuclease (BS-RNase) is a dimeric protein with two identical subunits linked by two disulfide bridges, each subunit showing 80% of sequence identity with pancreatic RNase A.	Disulfides	102-111	seminal ribonuclease	Bos taurus	7-27
9829974-5	1998	y+LAT-1 protein forms a approximately 135-kDa, disulfide bond-dependent heterodimer with 4F2hc in oocytes, which upon reduction results in two protein bands of approximately 85 kDa (i.e. 4F2hc) and approximately 40 kDa (y+LAT-1).	Disulfides	47-56	solute carrier family 7 member 5	Homo sapiens	2-7
9829974-5	1998	y+LAT-1 protein forms a approximately 135-kDa, disulfide bond-dependent heterodimer with 4F2hc in oocytes, which upon reduction results in two protein bands of approximately 85 kDa (i.e. 4F2hc) and approximately 40 kDa (y+LAT-1).	Disulfides	47-56	solute carrier family 3 member 2	Homo sapiens	89-94
9829974-5	1998	y+LAT-1 protein forms a approximately 135-kDa, disulfide bond-dependent heterodimer with 4F2hc in oocytes, which upon reduction results in two protein bands of approximately 85 kDa (i.e. 4F2hc) and approximately 40 kDa (y+LAT-1).	Disulfides	47-56	solute carrier family 3 member 2	Homo sapiens	187-192
9829974-5	1998	y+LAT-1 protein forms a approximately 135-kDa, disulfide bond-dependent heterodimer with 4F2hc in oocytes, which upon reduction results in two protein bands of approximately 85 kDa (i.e. 4F2hc) and approximately 40 kDa (y+LAT-1).	Disulfides	47-56	solute carrier family 7 member 7	Homo sapiens	0-7
9858782-11	1998	We now report that protein disulfide isomerase, which is known to catalyze disulfide interchange in thrombospondin-1 and change its enzyme inhibitory properties and its binding to monoclonal antibodies, was secreted by bovine aortic endothelial cells and deposited on the cell surface.	Disulfides	27-36	thrombospondin 1	Bos taurus	100-116
9794406-1	1998	CD27 belongs to TNF receptor family, and it is unique in this family for its disulfide-linked homodimerization of 55-kDa monomers.	Disulfides	77-86	CD27 molecule	Homo sapiens	0-4
9783263-3	1998	Proteolytic cleavage and disulfide bridge reduction in the DTA-DTB linker region of DTx are required for optimal ADP-ribosylation of elongation factor 2 (EF-2).	Disulfides	25-34	eukaryotic translation elongation factor 2	Homo sapiens	133-152
9783263-3	1998	Proteolytic cleavage and disulfide bridge reduction in the DTA-DTB linker region of DTx are required for optimal ADP-ribosylation of elongation factor 2 (EF-2).	Disulfides	25-34	eukaryotic translation elongation factor 2	Homo sapiens	154-158
9737963-6	1998	Mass spectrometry analysis and mutagenesis experiments demonstrate that the redox regulation is accomplished through the reversible formation of an intramolecular disulfide bridge involving the cysteines present in the PAI subdomain, whereas the RED subdomain appears quite insensitive to redox potential.	Disulfides	163-172	serpin family E member 1	Homo sapiens	219-222
29410996-2	2018	The thioredoxin system, comprised of NADPH, thioredoxin reductase (TrxR) and thioredoxin (Trx), exerts its activities via a disulfide-dithiol exchange reaction.	Disulfides	124-133	thioredoxin	Homo sapiens	44-55
29410996-2	2018	The thioredoxin system, comprised of NADPH, thioredoxin reductase (TrxR) and thioredoxin (Trx), exerts its activities via a disulfide-dithiol exchange reaction.	Disulfides	124-133	thioredoxin	Homo sapiens	67-70
29278740-1	2018	Mammalian thioredoxin reductases (TrxRs) are selenocysteine-containing proteins (selenoproteins) that propel a large number of functions through reduction of several substrates including the active site disulfide of thioredoxins (Trxs).	Disulfides	203-212	thioredoxin	Homo sapiens	216-228
9733783-4	1998	Unlike other human cystatins, cystatin F has 2 additional Cys residues, indicating the presence of an extra disulfide bridge stabilizing the N-terminal region of the molecule.	Disulfides	108-117	cystatin F	Homo sapiens	30-40
29101227-2	2018	The pre-TCR is a disulfide-linked heterodimer composed of an invariant pre-TCR alpha (pTalpha) subunit and a variable beta subunit, the latter of which is incorporated into the mature TCR in subsequent developmental progression.	Disulfides	17-26	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	8-11
9731071-8	1998	Western blot analysis of neutrophil lysates indicated that siglec-5 exists as a disulfide-linked dimer of approximately 140 kD.	Disulfides	80-89	sialic acid binding Ig like lectin 5	Homo sapiens	59-67
29101227-2	2018	The pre-TCR is a disulfide-linked heterodimer composed of an invariant pre-TCR alpha (pTalpha) subunit and a variable beta subunit, the latter of which is incorporated into the mature TCR in subsequent developmental progression.	Disulfides	17-26	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	75-78
29272095-2	2018	Here, we report on novel hyaluronic acid-shelled disulfide-cross-linked biodegradable polymersomes (HA-XPS) self-assembled from hyaluronic acid-b-poly(trimethylene carbonate-co-dithiolane trimethylene carbonate) diblock copolymer for ultrahigh-efficiency reactive encapsulation and CD44-targeted delivery of mertansine (DM1) toxin, a highly potent warhead for clinically used antibody-drug conjugates.	Disulfides	49-58	immunoglobulin heavy diversity 1-7	Homo sapiens	320-323
9722550-6	1998	The data indicate that bovine phosphodiester alpha-GlcNAcase is a 272,000-Da complex of four identical 68,000-Da glycoprotein subunits arranged as two disulfide-linked homodimers.	Disulfides	151-160	N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase	Bos taurus	30-60
9680483-4	1998	Initially, to gain an insight into the energetics of heterodimerization, we studied the stability of N-terminal disulfide-linked versions of the c-Myc and Max homodimeric LZs and c-Myc-Max heterodimeric LZ by fitting the temperature-induced denaturation curves monitored by circular dichroism spectroscopy.	Disulfides	112-121	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	145-150
29240412-8	2018	The feasibility of top-down fragmentation of disulfide-containing proteins is also demonstrated using beta2-microglobulin and a monoclonal antibody (mAb).	Disulfides	45-54	beta-2-microglobulin	Homo sapiens	102-121
9687533-0	1998	T cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-linked dimer associated with the TCR-CD3-zeta complex, recruits intracellular signaling proteins to the plasma membrane.	Disulfides	59-68	CD247 molecule	Homo sapiens	106-114
28398822-4	2018	Heightened oxidative stress evokes formation of disulfide-bound heterotrimers linking dimeric PRDX1 to monomeric FOXO3.	Disulfides	48-57	peroxiredoxin 1	Homo sapiens	94-99
9664841-7	1998	To overcome folding difficulties with the EGF1, a two-step oxidation procedure was used in which the cysteines involved in the middle, crossing, disulfide bond (Cys85-Cys102) remained protected with acetamidomethyl (Acm) groups after hydrogen fluoride treatment of the peptide resin.	Disulfides	145-154	G elongation factor mitochondrial 1	Homo sapiens	42-46
9664841-10	1998	Deuterium exchange studies suggested a very tightly packed core in EGF1 that is not accessible to the bulk solvent, likely a result from the compact structure caused by its three disulfide bonds.	Disulfides	179-188	G elongation factor mitochondrial 1	Homo sapiens	67-71
29635040-9	2018	By contrast, nearly all of the free monomers in the lysate converted to disulfide bond-linked dimers by a simple, long incubation at 4  C. These results strongly suggest that the monomer-dimer equilibrium of HSP27 was inversed between the in-cell and cell-free systems.	Disulfides	72-81	heat shock protein family B (small) member 1	Homo sapiens	208-213
9707171-6	1998	All these peptides used an oxidized Cys-X-Cys bridge to link the discontinuous sequence elements in a manner suggested by the known conserved disulfide bridges in gp120.	Disulfides	142-151	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	163-168
9653033-4	1998	Both wtMIF and MF1 were demonstrated to form an intramolecular disulfide bridge.	Disulfides	63-72	flap structure-specific endonuclease 1	Homo sapiens	15-18
29877571-2	2018	Numerous studies showed that LRPAP1 has a dual function, initially as a chaperone insuring proper formation of intermolecular disulfide bonds during biogenesis of low density lipoprotein (LDL) receptors and later as an escort protein during trafficking through the endoplasmic reticulum and the early Golgi compartment, preventing premature interaction of receptor and ligand.	Disulfides	126-135	LDL receptor related protein associated protein 1 L homeolog	Xenopus laevis	29-35
9684801-2	1998	The u-PAR is comprised of three homologous domains of approximately 90 amino acids, defined by the pattern of disulfide bonds.	Disulfides	110-119	plasminogen activator, urokinase receptor	Homo sapiens	4-9
29519368-4	2018	Dithiothreitol is a reagent that breaks disulfide bonds and effectively destroys antigenic sites for CD38 on red blood cells.	Disulfides	40-49	CD38 molecule	Homo sapiens	101-105
9575190-3	1998	Here we report that potato carboxypeptidase inhibitor (PCI), a 39-amino acid protease inhibitor with three disulfide bridges, is an antagonist of human EGF.	Disulfides	107-116	epidermal growth factor	Homo sapiens	152-155
9575190-6	1998	PCI has a special disulfide scaffold called a T-knot that is also present in several growth factors including EGF and transforming growth factor alpha.	Disulfides	18-27	epidermal growth factor	Homo sapiens	110-113
29126850-3	2017	Interchain disulfide bridging of an alphaCD3 Fab enabled installation of either the PSMA-targeting small molecule DUPA (SynFab) or the attachment of an alphaPSMA Fab (BisFab) by covalent linkage.	Disulfides	11-20	FA complementation group B	Homo sapiens	45-48
9620546-2	1998	In MEN2A mutations affecting cysteine residues in the extracellular domain of the receptor cause constitutive activation of the tyrosine kinase by the formation of disulfide-bonded homodimers.	Disulfides	164-173	ret proto-oncogene	Homo sapiens	3-8
9572853-6	1998	The complex could be degraded to a fragment containing two disulfide-linked peptides from uPA, one of which included the active site Ser, while PAI-1 was left undegraded.	Disulfides	59-68	serpin family E member 1	Homo sapiens	144-149
29126850-3	2017	Interchain disulfide bridging of an alphaCD3 Fab enabled installation of either the PSMA-targeting small molecule DUPA (SynFab) or the attachment of an alphaPSMA Fab (BisFab) by covalent linkage.	Disulfides	11-20	FA complementation group B	Homo sapiens	123-126
29241459-4	2017	A recent study published in BMC Biology demonstrates for the first time that some Erv1 proteins can function in oxidative folding independently of a Mia40 protein, providing for the first time strong evidence that the IMS disulfide relay evolved in a stepwise manner.See research article: 10.1186/s12915-017-0445-8.	Disulfides	222-231	growth factor, augmenter of liver regeneration	Homo sapiens	82-86
9679540-7	1998	A class of disulfide inhibitors of thioredoxin has been identified.	Disulfides	11-20	thioredoxin	Homo sapiens	35-46
9539778-0	1998	Activating mutations in the extracellular domain of the fibroblast growth factor receptor 2 function by disruption of the disulfide bond in the third immunoglobulin-like domain.	Disulfides	122-131	fibroblast growth factor receptor 2	Homo sapiens	56-91
29055825-4	2017	We demonstrated that mBB derivatization of H2S and H2Sn standards under alkaline conditions (pH 9.5) induced significant decreases in H2S2 and H2S3 levels and a significant increase in the H2S level in an incubation time-dependent manner.	Disulfides	134-138	histocompatibility 2, S region (C4, Slp, Bf, C2)	Mus musculus	43-46
29055825-4	2017	We demonstrated that mBB derivatization of H2S and H2Sn standards under alkaline conditions (pH 9.5) induced significant decreases in H2S2 and H2S3 levels and a significant increase in the H2S level in an incubation time-dependent manner.	Disulfides	134-138	histocompatibility 2, S region (C4, Slp, Bf, C2)	Mus musculus	51-54
9539778-8	1998	Molecular modeling also reveals that noncysteine mutations may activate FGFR2 by altering the conformation of the Ig-3 domain near the disulfide bond, preventing the formation of an intramolecular bond.	Disulfides	135-144	fibroblast growth factor receptor 2	Homo sapiens	72-77
29117860-2	2017	In fungi and animals, the sulfhydryl oxidase Erv1 "generates" disulfide bonds that are passed on to the oxidoreductase Mia40, which oxidizes substrate proteins.	Disulfides	62-71	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	45-49
9568908-1	1998	Human epidermal growth factor (hEGF) contains 53 amino acids and three disulfide bonds.	Disulfides	71-80	epidermal growth factor	Homo sapiens	6-29
9568908-1	1998	Human epidermal growth factor (hEGF) contains 53 amino acids and three disulfide bonds.	Disulfides	71-80	epidermal growth factor	Homo sapiens	31-35
29117860-9	2017	In accordance to the absence of Mia40 in many protists, our study suggests that the mitochondrial disulfide relay evolved in a stepwise reaction from an Erv1-only system to which Mia40 was added in order to improve substrate specificity.	Disulfides	98-107	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	153-157
29117860-10	2017	Graphical Abstract The mitochondrial disulfide relay evolved in a step-wise manner from an Erv1-only system.	Disulfides	37-46	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	91-95
29016988-1	2017	Once the ferredoxin/thioredoxin system was established as a mechanism linking light to the post-translational regulation of chloroplast enzymes, I considered that plants might harbor a light-independent mechanism utilizing this same enzyme chemistry based on thiol-disulfide redox transitions.	Disulfides	265-274	thioredoxin	Homo sapiens	20-31
9638971-6	1998	PSGL-1 is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with P-, L-, and E-selectin.	Disulfides	12-21	selectin P ligand	Homo sapiens	0-6
9638971-6	1998	PSGL-1 is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with P-, L-, and E-selectin.	Disulfides	12-21	selectin E	Homo sapiens	111-121
29204107-2	2017	The CD13-targeting moiety NGR was synthesized and cyclized by native chemical ligation (NCL) instead of disulfide bridging, leading to a cyclic peptide backbone: cyclo(Cys-Asn-Gly-Arg-Gly) (coNGR).	Disulfides	104-113	alanyl (membrane) aminopeptidase	Mus musculus	4-8
9485403-1	1998	The N-terminal domain of phosphoglycerate kinase (N-PGK) and domain 1 of the T-cell adhesion protein CD2 (CD2.d1) fold through rapidly formed and transiently populated intermediate states in reactions which have no kinetic complications arising from proline isomerization or disulfide bonding.	Disulfides	275-284	CD2 molecule	Homo sapiens	101-104
9485403-1	1998	The N-terminal domain of phosphoglycerate kinase (N-PGK) and domain 1 of the T-cell adhesion protein CD2 (CD2.d1) fold through rapidly formed and transiently populated intermediate states in reactions which have no kinetic complications arising from proline isomerization or disulfide bonding.	Disulfides	275-284	CD2 molecule	Homo sapiens	106-112
28878015-6	2017	Recombinant Trx1 preferentially binds to monomeric MLKL and blocks MLKL disulfide bond formation and polymerization in vitro Inhibition of MLKL polymer formation requires the reducing activity of Trx1.	Disulfides	72-81	thioredoxin	Homo sapiens	12-16
9521070-8	1998	Upon treatment of NK cells with pervanadate, the disulfide-linked p13 and additional proteins of 25, 30, 37 and 50-95 kDa were identified as KAR-associated tyrosine phosphoproteins.	Disulfides	49-58	H3 histone pseudogene 6	Homo sapiens	66-69
28878015-6	2017	Recombinant Trx1 preferentially binds to monomeric MLKL and blocks MLKL disulfide bond formation and polymerization in vitro Inhibition of MLKL polymer formation requires the reducing activity of Trx1.	Disulfides	72-81	thioredoxin	Homo sapiens	196-200
28814504-6	2017	In reconstitution studies with reduced Tim13, Mia40, and Erv1, the addition of Osm1 and fumarate completes the disulfide exchange pathway that results in Tim13 oxidation.	Disulfides	111-120	growth factor, augmenter of liver regeneration	Homo sapiens	57-61
28926961-1	2017	Bovine alpha-lactalbumin (alphaLA) has four disulfide (SS) bonds in the native form (N).	Disulfides	44-53	lactalbumin alpha	Bos taurus	7-24
9533440-7	1998	Reduction of the Fas/APO-1-derived cross-reactive peptides by dithiothreitol completely abrogated their antigenic reactivity with the anti-Fas mAb CH-11, thus indicating that the establishment of intrapeptide disulfide bonds is critical for antigenic reactivity.	Disulfides	209-218	Fas cell surface death receptor	Homo sapiens	21-26
9570526-1	1998	IL-12p70, a 70- to 75-kDa heterodimer consisting of disulfide-bonded 35-kDa (p35) and 40-kDa (p40) subunits, enhances Th1 development primarily by its ability to induce IFN-gamma production by NK and Th1 cells.	Disulfides	52-61	interleukin 12a	Mus musculus	77-80
9430729-4	1998	XRCC4 expressed in insect cells exists primarily as a disulfide-linked homodimer, although it can also form large multimers.	Disulfides	54-63	X-ray repair complementing defective repair in Chinese hamster cells 4	Mus musculus	0-5
28716990-3	2017	Oxidants induce an interprotein disulfide in PKG Ialpha (protein kinase G Ialpha) at C42, which is associated with its targeting and activation, resulting in vasodilation and blood pressure lowering.	Disulfides	32-41	protein kinase cGMP-dependent 1	Homo sapiens	45-48
9419208-3	1998	Sequence analysis revealed a TSP1 recognition motif, previously defined for the CD36 gene family of cell adhesion receptors, in conserved regions flanking the disulfide-linked cysteine residues of the V3 loop of HIV envelope glycoprotein gp120, important for HIV binding to its high affinity cellular receptor CD4.	Disulfides	159-168	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	238-243
28551108-3	2017	On the other hand, PbTx-2 activates the reduction of small disulfides such as 5,5"-dithio-bis-(2-nitrobenzoic acid) by thioredoxin reductase.	Disulfides	59-69	thioredoxin	Homo sapiens	119-130
9709808-4	1998	LTBP is required for efficient secretion and processing of latent TGF-beta and it binds to LAP via disulfide bond(s).	Disulfides	99-108	LAP	Homo sapiens	91-94
9950104-1	1998	Thioredoxin (TRX) is known to contain an active site with a redox-active disulfide and has various biological activities.	Disulfides	73-82	thioredoxin	Homo sapiens	0-11
28642368-7	2017	Specifically, disulfide-bonded FimG undergoes a 30% increase in its mechanical stability compared with its reduced counterpart, whereas the unfolding force of I91 domains experiences a decrease of 15% relative to the WT form.	Disulfides	14-23	CMS1A1	Homo sapiens	31-35
9950104-1	1998	Thioredoxin (TRX) is known to contain an active site with a redox-active disulfide and has various biological activities.	Disulfides	73-82	thioredoxin	Homo sapiens	13-16
28765527-4	2017	We found that the binding of Ca2+ to hSCGN promotes the dimerization of hSCGN via the formation of a Cys193-Cys193 disulfide bond.	Disulfides	115-124	secretagogin, EF-hand calcium binding protein	Homo sapiens	37-42
9769020-0	1998	Disulfide cross-linked Fab-aggregates: preparation and biodistribution.	Disulfides	0-9	FA complementation group B	Homo sapiens	23-26
28765527-4	2017	We found that the binding of Ca2+ to hSCGN promotes the dimerization of hSCGN via the formation of a Cys193-Cys193 disulfide bond.	Disulfides	115-124	secretagogin, EF-hand calcium binding protein	Homo sapiens	72-77
28794626-3	2017	We developed folic acid (FA)- and disulfide (SS)-polyethylene glycol (PEG)-conjugated polyethylenimine (PEI) complexed with superparamagnetic iron oxide Fe3O4 nanoparticles (SPIONs) as a siRNA-delivery system for PD-L1 knockdown.	Disulfides	34-43	CD274 molecule	Homo sapiens	213-218
9388228-5	1997	Trx2 together with thioredoxin reductase and NADPH is an efficient electron donor for the essential enzyme ribonucleotide reductase and is also able to reduce the interchain disulfide bridges of insulin.	Disulfides	174-183	thioredoxin 2	Homo sapiens	0-4
9388228-5	1997	Trx2 together with thioredoxin reductase and NADPH is an efficient electron donor for the essential enzyme ribonucleotide reductase and is also able to reduce the interchain disulfide bridges of insulin.	Disulfides	174-183	peroxiredoxin 5	Homo sapiens	19-40
28262915-0	2017	Glutathione and thioredoxin systems contribute to recombinant monoclonal antibody interchain disulfide bond reduction during bioprocessing.	Disulfides	93-102	thioredoxin	Homo sapiens	16-27
9367781-0	1997	Structure of the fifth EGF-like domain of thrombomodulin: An EGF-like domain with a novel disulfide-bonding pattern.	Disulfides	90-99	thrombomodulin	Homo sapiens	42-56
28411237-3	2017	Thioredoxin (Trx) and glutaredoxin (Grx) are ubiquitous redox proteins, catalyzing thiol-disulfide exchange reactions.	Disulfides	89-98	thioredoxin	Homo sapiens	0-11
9325298-0	1997	Conformation of factor VIIa stabilized by a labile disulfide bond (Cys-310-Cys-329) in the protease domain is essential for interaction with tissue factor.	Disulfides	51-60	coagulation factor III, tissue factor	Homo sapiens	141-154
28411237-3	2017	Thioredoxin (Trx) and glutaredoxin (Grx) are ubiquitous redox proteins, catalyzing thiol-disulfide exchange reactions.	Disulfides	89-98	thioredoxin	Homo sapiens	13-16
26856589-3	2017	In the present study, to promote the formation of the disulfide bond between the heavy and light chains, some positively charged amino acid residues were introduced near the cysteine residue for the disulfide bond at the C-terminus of CL, while some negatively charged amino acid residues were added near the cysteine residue for the disulfide bond at the C-terminus of CH1.	Disulfides	54-63	SUN domain containing ossification factor	Homo sapiens	370-373
9344598-1	1997	Thioredoxin (Trx) is an intracellular multifunctional 12-kDa protein with a reduction/oxidation (redox) active disulfide constitutively expressed by most cells of the human body.	Disulfides	111-120	thioredoxin	Homo sapiens	0-11
9344598-1	1997	Thioredoxin (Trx) is an intracellular multifunctional 12-kDa protein with a reduction/oxidation (redox) active disulfide constitutively expressed by most cells of the human body.	Disulfides	111-120	thioredoxin	Homo sapiens	13-16
9317167-8	1997	It is concluded that disulfide bond formation plays a critical role in the maintenance of antigenic structure and that the autoantibodies to IA-2/IA-2 beta in IDDM sera recognize conformational epitopes.	Disulfides	21-30	protein tyrosine phosphatase receptor type N2	Homo sapiens	146-155
9315320-6	1997	Glutaredoxin (Grx) which catalyzes GSH-dependent disulfide reduction also via a redox-active disulfide and Trx are both efficient electron donors to the human plasma glutathione peroxidase providing a mechanism by which human plasma glutathione peroxidase may reduce hydroperoxides in an environment almost free from glutathione.	Disulfides	49-58	thioredoxin	Homo sapiens	107-110
28524918-2	2017	U-II is constrained by a disulfide bridge that induces a beta-turn structure and binds pseudo-irreversibly to UTR and is believed to result in a structural rearrangement of the receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	0-4
15739495-2	1997	Insulin contains 51 amino acids and two intrachain disulfide bridges.	Disulfides	51-60	insulin	Bos taurus	0-7
15739495-4	1997	The results show that the conformation of insulin has changed before cleavage of the disulfide bonds to A and B chains.	Disulfides	85-94	insulin	Bos taurus	42-49
28524918-2	2017	U-II is constrained by a disulfide bridge that induces a beta-turn structure and binds pseudo-irreversibly to UTR and is believed to result in a structural rearrangement of the receptor.	Disulfides	25-34	urotensin 2 receptor	Homo sapiens	110-113
28524918-4	2017	Here we describe a series of U-II peptidomimetics incorporating a non-reducible disulfide bond structural surrogate to investigate the feasibility that native U-II binds to the G protein-coupled receptor through disulfide bond shuffling as a mechanism of covalent interaction.	Disulfides	212-221	urotensin 2	Homo sapiens	159-163
9268350-5	1997	Of the mutations introduced, the greatest functional disturbances, reflected in Ki increases of 2-4 orders of magnitude, are generated by changes that disrupt the Cys1-Cys70 disulfide bond and by substitution of Ala for Thr2.	Disulfides	174-183	cystin 1	Homo sapiens	163-167
28524918-5	2017	Disubstituted 1,2,3-triazoles were designed with the aid of computational modeling as a non-reducible mimic of the disulfide bridge (Cys5-Cys10) in U-II.	Disulfides	115-124	urotensin 2	Homo sapiens	148-152
28441474-3	2017	Hydrothermally synthesized MoS2 nanoflakes were modified with generation 5 (G5) poly(amidoamine) dendrimers partially functionalized with lipoic acid via disulfide bond.	Disulfides	154-163	mago homolog, exon junction complex core component	Mus musculus	27-31
9250594-3	1997	Highly purified tryptic peptides from native and disulfide-bond-reduced alpha-La were obtained by reverse phase chromatography.	Disulfides	49-58	lactalbumin alpha	Bos taurus	72-80
9444979-6	1997	Reduction and subsequent alkylation of disulfide bridges of defensins greatly decreased the C1q binding ability but complement activation (C4b binding) remained high.	Disulfides	39-48	complement C1q A chain	Homo sapiens	92-95
27744031-7	2017	Interestingly, these 2 products remained linked with disulfide bonds and presented as a dimerized form, TSLP (29-124 + 131-159).	Disulfides	53-62	thymic stromal lymphopoietin	Homo sapiens	104-108
9272623-0	1997	Synthesis, solution structure, binding activity, and cGMP activation of human guanylin and its disulfide isomer.	Disulfides	95-104	guanylate cyclase activator 2A	Homo sapiens	78-86
9272623-1	1997	Guanylin is a recently isolated peptide consisting of 15 amino acid residues with four cysteines, which may form two intramolecular disulfide bridges, and stimulates intestinal membrane guanylate cyclase.	Disulfides	132-141	guanylate cyclase activator 2A	Homo sapiens	0-8
9272623-2	1997	The position of the disulfide linkages of guanylin was predicted from its structural similarity to a heat stable enterotoxin which is thought to be responsible for secretory diarrhoea.	Disulfides	20-29	guanylate cyclase activator 2A	Homo sapiens	42-50
9272623-7	1997	In contrast, the disulfide isomer of guanylin shows only a single conformation with an elongated curved plate-like structure.	Disulfides	17-26	guanylate cyclase activator 2A	Homo sapiens	37-45
9272623-10	1997	Both binding and cGMP assays indicated that the relevant form of disulfide bridges in the intact guanylin was as predicted.	Disulfides	65-74	guanylate cyclase activator 2A	Homo sapiens	97-105
28521463-1	2017	Endoplasmic reticulum (ER) protein ERp46 is a member of the protein disulfide isomerase family of oxidoreductases, which facilitates the reduction of disulfides in proteins and their folding.	Disulfides	150-160	thioredoxin domain containing 5	Homo sapiens	35-40
28289087-9	2017	We show here that the A. oris membrane-spanning protein VKOR employs two pairs of exoplasmic cysteine residues, including the canonical CXXC thioredoxinlike motif, to oxidize MdbA via a disulfide relay mechanism.	Disulfides	186-195	putative DNA-binding protein	Escherichia coli	175-179
9108027-3	1997	Although the mechanism and structure of thioredoxin reductase from Escherichia coli are distinct (M(r) approximately 35,000), this enzyme must be placed in the same family because there are significant amino acid sequence similarities with the other two enzymes, the presence of a redox-active disulfide, and the substrate specificities.	Disulfides	294-303	peroxiredoxin 5	Homo sapiens	40-61
28375144-5	2017	Crystallographic data for shrimp thioredoxin (LvTrx) obtained under different redox conditions reveal a dimeric arrangement mediated by a disulfide bond through residue Cys73 and other hydrophobic interactions located in the crystallographic interface, as reported for human Trx.	Disulfides	138-147	thioredoxin	Homo sapiens	33-44
9092813-4	1997	We examine the hypothesis that, in spite of these differences, cripto can adopt the characteristic EGF-like 1-3, 2-4, 5-6 disulfide bond pattern.	Disulfides	122-131	epidermal growth factor	Homo sapiens	99-102
28375144-5	2017	Crystallographic data for shrimp thioredoxin (LvTrx) obtained under different redox conditions reveal a dimeric arrangement mediated by a disulfide bond through residue Cys73 and other hydrophobic interactions located in the crystallographic interface, as reported for human Trx.	Disulfides	138-147	thioredoxin	Homo sapiens	48-51
27825521-0	2017	Au nanoparticles/hollow molybdenum disulfide microcubes based biosensor for microRNA-21 detection coupled with duplex-specific nuclease and enzyme signal amplification.	Disulfides	35-44	microRNA 21	Homo sapiens	76-87
9063752-5	1997	The missense mutation at codon 306 (TGC --> GGC) involves the substitution of Cys306 by Gly306 which causes the disruption of a disulfide bond between Cys281 and Cys306 and affects the normal configuration of the fifth domain of apoH that appears to be critical for clustering positively charged amino acids along with four hydrophobic amino acids sequence.	Disulfides	128-137	apolipoprotein H	Homo sapiens	229-233
28077339-3	2017	Here, we cloned and characterized the first disulfide-bridged toxin peptide St20 from the non-buthidae scorpion Scorpiops tibetanus.	Disulfides	44-53	sulfotransferase family 2A member 1	Rattus norvegicus	76-80
9406241-0	1997	Redox active disulfides: the thioredoxin system as a drug target.	Disulfides	13-23	thioredoxin	Homo sapiens	29-40
9406241-3	1997	We originally determined the disulfides to be weak reversible inhibitors of thioredoxin reductase.	Disulfides	29-39	thioredoxin	Homo sapiens	76-87
8978667-0	1996	Dimerization of TWIK-1 K+ channel subunits via a disulfide bridge.	Disulfides	49-58	potassium two pore domain channel subfamily K member 1	Homo sapiens	16-22
28077339-9	2017	Together, our results showed that St20 is the first disulfide-bridged toxin peptide from the non-buthidae scorpion Scorpiops tibetanus with immunosuppressive and anti-inflammatory activities, suggesting that toxins from non-buthidae scorpions might be a new source of peptide drug discovery towards human diseases.	Disulfides	52-61	sulfotransferase family 2A member 1	Rattus norvegicus	34-38
8978667-2	1996	Here we show that TWIK-1 subunits can self-associate to give dimers containing an interchain disulfide bridge.	Disulfides	93-102	potassium two pore domain channel subfamily K member 1	Homo sapiens	18-24
28011677-4	2017	N-acetylcysteine (NAC), an FDA-approved anti-mucolytic agent, is a possible new treatment strategy for TTP, as it was demonstrated to reduce disulfide bonds in VWF, thereby decreasing VWF multimers size and hence their prothrombotic potential.	Disulfides	141-150	Von Willebrand factor	Mus musculus	160-163
8931546-1	1996	Proteins with the thioredoxin fold have widely differing stabilities of the disulfide bond that can be formed between the two cysteines at their active site sequence motif Cys1-Xaa2-Yaa3-Cys4.	Disulfides	76-85	thioredoxin	Homo sapiens	18-29
8931546-1	1996	Proteins with the thioredoxin fold have widely differing stabilities of the disulfide bond that can be formed between the two cysteines at their active site sequence motif Cys1-Xaa2-Yaa3-Cys4.	Disulfides	76-85	cystin 1	Homo sapiens	172-176
8931546-2	1996	This is believed to be regulated not by varying the disulfide bond itself, but by modulating the stability of the dithiol form of the protein through interactions with the ionized form of the Cys1 thiol group.	Disulfides	52-61	cystin 1	Homo sapiens	192-196
8931546-3	1996	A consistent relationship between disulfide bond stability and Cys1 thiol pKa value is found here for DsbA, thioredoxin, and the N-terminal thioredoxin-like domain of protein disulfide isomerase (PDI a), which has a very low thiol pKa value of 4.5.	Disulfides	34-43	cystin 1	Homo sapiens	63-67
8931546-3	1996	A consistent relationship between disulfide bond stability and Cys1 thiol pKa value is found here for DsbA, thioredoxin, and the N-terminal thioredoxin-like domain of protein disulfide isomerase (PDI a), which has a very low thiol pKa value of 4.5.	Disulfides	34-43	thioredoxin	Homo sapiens	108-119
28061386-3	2017	Here we show, using biochemical analysis coupled with electron microscopy, that sAg nanoparticle disassembly requires both reducing agent to disrupt intermolecular disulfide bonds, and detergent to disrupt hydrophobic interactions that stabilize the nanoparticle.	Disulfides	164-173	S-antigen visual arrestin	Homo sapiens	80-83
8931546-3	1996	A consistent relationship between disulfide bond stability and Cys1 thiol pKa value is found here for DsbA, thioredoxin, and the N-terminal thioredoxin-like domain of protein disulfide isomerase (PDI a), which has a very low thiol pKa value of 4.5.	Disulfides	34-43	thioredoxin	Homo sapiens	140-151
27856252-10	2017	The results indicate that cross-linking significantly affects properties of Tpm and actin-myosin interaction and can explain, at least partly, the role of the interchain disulfide cross-linking of cardiac Tpm in human heart diseases.	Disulfides	170-179	myosin heavy chain 14	Homo sapiens	90-96
8944748-2	1996	Reduction-carboxamidomethylation of HDL3 entirely converts the disulfide-linked apoA-II dimers into monomers, without affecting the structure, composition and particle size distribution of HDL3.	Disulfides	63-72	apolipoprotein A2	Homo sapiens	80-87
8896764-0	1996	Disulfide bond formation between the n-terminal region of p56LCK and the cytoplasmic domain of CD8 studied by electrospray ionization and matrix-assisted desorption/ionization time-of-flight mass spectrometry.	Disulfides	0-9	LCK proto-oncogene, Src family tyrosine kinase	Homo sapiens	58-64
26916602-8	2017	Myosin was involved in gel formation through non-disulfide covalent bond.	Disulfides	49-58	myosin heavy chain 14	Homo sapiens	0-6
8810647-3	1996	Because S-nitrosylation of vicinal thiols promotes disulfide formation, we determined whether exposure to NO results in modulation of the catalytic activity of NO synthase and whether disulfide reduction catalyzed by thioredoxin/thioredoxin reductase (T/TR) and/or by glutaredoxin restores the catalytic activity of NO synthase in pulmonary artery endothelial cells (PAEC).	Disulfides	184-193	thioredoxin	Homo sapiens	217-228
27958302-6	2016	Both IgL 1 and 2 adopt the classical Ig domain conformation comprised of two layers of beta-sheets possessing antiparallel beta-strands with each being anchored by a pair of cysteines forming a disulfide bond.	Disulfides	194-203	immunoglobulin lambda like polypeptide 1	Homo sapiens	5-16
8810647-12	1996	Thioredoxin-regulated reversal of NO-induced modulation of NO synthase protein suggests that an oxidative conformational change in vicinal thiols, resulting in the formation of intramolecular or intermolecular disulfides or both, is involved.	Disulfides	210-220	thioredoxin	Homo sapiens	0-11
8806454-7	1996	Immunochemical and SDS-PAGE gel analyses of laminin heterotrimers demonstrated that glial laminin contained the beta 2 and gamma 1 chains in disulfide-bonded heterotrimeric complexes with a 360-kDa chain, a 320-kDa chain, or a postulated approximately 200-kDa chain.	Disulfides	141-150	tubulin beta 4B class IVb	Homo sapiens	112-130
8799121-4	1996	Here we demonstrate that these mutations promote dimerization of the Neu receptor through the formation of disulfide bonds, resulting in its constitutive activation.	Disulfides	107-116	erb-b2 receptor tyrosine kinase 2	Mus musculus	69-72
27683653-1	2016	Pyrrolobenzodiazepine (PBD)-dimer is a DNA minor groove alkylator, and its CD22 THIOMAB antibody drug conjugate (ADC) demonstrated, through a disulfide linker, an efficacy in tumor reduction for more than 7 weeks with minimal body weight loss in xenograft mice after a single 0.5-1 mg/kg i.v.	Disulfides	142-151	CD22 antigen	Mus musculus	75-79
8799121-9	1996	These observations suggest that oncogenic activation of Neu results from constitutive disulfide bond-dependent dimerization.	Disulfides	86-95	erb-b2 receptor tyrosine kinase 2	Mus musculus	56-59
27687729-0	2016	Forkhead Box O3A (FOXO3) and the Mitochondrial Disulfide Relay Carrier (CHCHD4) Regulate p53 Protein Nuclear Activity in Response to Exercise.	Disulfides	47-56	coiled-coil-helix-coiled-coil-helix domain containing 4	Mus musculus	72-78
8756708-2	1996	Two of the domains, a and a", which are homologous to thioredoxin and active in catalysis of disulfide bond formation, have been identified and characterized previously.	Disulfides	93-102	thioredoxin	Homo sapiens	54-65
27687729-0	2016	Forkhead Box O3A (FOXO3) and the Mitochondrial Disulfide Relay Carrier (CHCHD4) Regulate p53 Protein Nuclear Activity in Response to Exercise.	Disulfides	47-56	transformation related protein 53, pseudogene	Mus musculus	89-92
27733683-0	2016	Homodimerization of the Lymph Vessel Endothelial Receptor LYVE-1 through a Redox-labile Disulfide Is Critical for Hyaluronan Binding in Lymphatic Endothelium.	Disulfides	88-97	lymphatic vessel endothelial hyaluronan receptor 1	Homo sapiens	58-64
8889834-0	1996	Reversible affinity labeling of opioid receptors via disulfide bonding: discriminative labeling of mu and delta subtypes by chemically activated thiol-containing enkephalin analogs.	Disulfides	53-62	proenkephalin	Rattus norvegicus	162-172
27733683-3	2016	An unusual feature of LYVE-1 not found in other HA receptors is the potential to form disulfide-linked homodimers.	Disulfides	86-95	lymphatic vessel endothelial hyaluronan receptor 1	Homo sapiens	22-28
18966590-1	1996	Nanogram quantities of cobalt (II) in 200 ml of water were quantitatively collected at pH 4 on a precipitate of disulfide, which is an oxidation product of dithiol (toluene-3,4-dithiol).	Disulfides	112-121	prolyl 4-hydroxylase, transmembrane	Homo sapiens	87-91
27733683-8	2016	Finally, we demonstrate the Cys-201 interchain disulfide is highly labile, and selective reduction with TCEP-HCl disrupts LYVE-1 homodimers, ablating HA binding.	Disulfides	47-56	lymphatic vessel endothelial hyaluronan receptor 1	Homo sapiens	122-128
8654563-4	1996	Analysis by SDS-PAGE and rotary shadowing electron microscopy indicated that TSP1 and TSP2 are disulfide bonded trimers whereas TSP3 is a disulfide-bonded pentamer.	Disulfides	95-104	tumor suppressor region 1	Mus musculus	77-81
27733683-10	2016	They also mark LYVE-1 as the first Link protein superfamily member requiring covalent homodimerization for function and suggest the interchain disulfide acts as a redox switch in vivo.	Disulfides	143-152	lymphatic vessel endothelial hyaluronan receptor 1	Homo sapiens	15-21
27694578-5	2016	Here, we show that ERdj5, a mammalian ER disulfide reductase, which we reported to be involved in the ER-associated degradation of misfolded proteins, activates the pump function of SERCA2b by reducing its luminal disulfide bond.	Disulfides	41-50	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	19-24
8634257-3	1996	Previous studies have suggested that disulfide-linked homodimers of peripherin/rds and rom-1 can associate noncovalently to form higher order structures.	Disulfides	37-46	retinal outer segment membrane protein 1	Bos taurus	87-92
27716795-9	2016	Together, these results provide a mechanism for conservation of disulfide linkage proximal glycosylation adjacent to the variable domains of gp120 and begin to explain how this could be exploited to enhance the immunogenicity of those regions.	Disulfides	64-73	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	141-146
8603822-0	1996	Improved tumor detection by anti-CEA chimeric Fab oligomers with disulfide linkages in a pancreatic-carcinoma-xenograft model.	Disulfides	65-74	FA complementation group B	Homo sapiens	46-49
27588831-7	2016	The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect.	Disulfides	4-13	chemokine like factor	Homo sapiens	37-40
8619605-4	1996	The ability of isolated rat liver mitochondria to reduce disulfides was examined by the reduction of 5,5"-dithiobis-(2 nitro-benzoic acid) (DTNB), the reaction catalyzed by thioredoxin reductase and glutathione reductase.	Disulfides	57-67	glutathione-disulfide reductase	Rattus norvegicus	199-220
27588831-7	2016	The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect.	Disulfides	4-13	migration and invasion enhancer 1	Homo sapiens	45-48
8745405-2	1996	In contrast to the wild-type enzyme, an engineered mutant of TS (T155C/E188C/C244T), TSMox, in which two subunits are crosslinked by disulfide bridges between residues 155-188" and 188-155" does not show this behavior.	Disulfides	133-142	thymidylate synthetase	Homo sapiens	61-63
27588831-7	2016	The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect.	Disulfides	4-13	thioredoxin	Homo sapiens	75-79
27588831-7	2016	The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect.	Disulfides	4-13	thioredoxin	Homo sapiens	119-123
27588831-7	2016	The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect.	Disulfides	187-196	chemokine like factor	Homo sapiens	37-40
27588831-7	2016	The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect.	Disulfides	187-196	migration and invasion enhancer 1	Homo sapiens	45-48
8555200-1	1996	The pH dependence of the 13C chemical shifts of the side-chain carboxyl carbons of all Asp and Glu residues in the reduced and oxidized states of human thioredoxin and in a mixed disulfide complex of human thioredoxin with a target peptide from the transcription factor NF kappa B has been investigated by multidimensional triple-resonance NMR spectroscopy.	Disulfides	179-188	thioredoxin	Homo sapiens	206-217
11012214-10	1996	Two disulfide bonds (Cys7-Cys151 and Cys29-Cys85) located in the N-terminal domain of TPO have an important effect on its biological activity.	Disulfides	4-13	thrombopoietin like 1	Rattus norvegicus	86-89
27588831-7	2016	The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect.	Disulfides	187-196	thioredoxin	Homo sapiens	75-79
27588831-7	2016	The disulfide bond formation between C32 and C35 within the active site of TRX1 is the main factor responsible for the TRX1 dissociation upon its oxidation as the formation of the second disulfide bond between noncatalytic cysteines C62 and C69 did not have any additional effect.	Disulfides	187-196	thioredoxin	Homo sapiens	119-123
27588831-9	2016	Furthermore, our data show that the catalytic site of TRX1 interacts with ASK1-TBD region containing cysteine C200 and that the oxidative stress induces intramolecular disulfide bond formation within ASK1-TBD and affects its structure in regions directly involved and/or important for TRX1 binding.	Disulfides	168-177	thioredoxin	Homo sapiens	54-58
27588831-9	2016	Furthermore, our data show that the catalytic site of TRX1 interacts with ASK1-TBD region containing cysteine C200 and that the oxidative stress induces intramolecular disulfide bond formation within ASK1-TBD and affects its structure in regions directly involved and/or important for TRX1 binding.	Disulfides	168-177	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	200-204
27588831-9	2016	Furthermore, our data show that the catalytic site of TRX1 interacts with ASK1-TBD region containing cysteine C200 and that the oxidative stress induces intramolecular disulfide bond formation within ASK1-TBD and affects its structure in regions directly involved and/or important for TRX1 binding.	Disulfides	168-177	thioredoxin	Homo sapiens	285-289
27629822-8	2016	Remarkably, yeast naturally contains Thr-Ser variants (Tsa1 and Tsa2, respectively) with distinct oligomeric stabilities in their disulfide states.	Disulfides	130-139	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	55-59
11012214-13	1996	These findings indicate that the region essential for TPO activity is the N-terminal domain, which contains two disulfide bonds.	Disulfides	112-121	thrombopoietin like 1	Rattus norvegicus	54-57
27018805-5	2016	Papain digestion and reduction of the disulfide linkage at the hinge region was used to generate Fab and Fc fragments.	Disulfides	38-47	FA complementation group B	Homo sapiens	97-100
8527452-5	1995	The very low stabilities of these disulfide bonds, which destabilize the protein structures, account for the efficiency with which PDI and each of the isolated domains can introduce disulfide bonds into proteins.	Disulfides	34-43	protein-disulfide isomerase	Escherichia coli	131-134
8527452-5	1995	The very low stabilities of these disulfide bonds, which destabilize the protein structures, account for the efficiency with which PDI and each of the isolated domains can introduce disulfide bonds into proteins.	Disulfides	182-191	protein-disulfide isomerase	Escherichia coli	131-134
8747428-0	1995	Conformational changes of alpha-lactalbumin induced by the stepwise reduction of its disulfide bridges: the effect of the disulfide bridges on the structural stability of the protein in sodium dodecyl sulfate solution.	Disulfides	85-94	lactalbumin alpha	Bos taurus	26-43
8747428-0	1995	Conformational changes of alpha-lactalbumin induced by the stepwise reduction of its disulfide bridges: the effect of the disulfide bridges on the structural stability of the protein in sodium dodecyl sulfate solution.	Disulfides	122-131	lactalbumin alpha	Bos taurus	26-43
8747428-1	1995	Four disulfide bridges of bovine alpha-lactalbumin (alpha-lact) were selectively reduced to obtain its derivatives with three, two, and zero disulfide bridges (designated as 3SS, 2SS, and 0SS alpha-lact, respectively).	Disulfides	5-14	lactalbumin alpha	Bos taurus	33-50
27342776-3	2016	Because PDE5 inhibition elevates cGMP and protects from doxorubicin-induced injury, we reasoned that this may be because it limits PKG Ialpha disulfide formation.	Disulfides	142-151	phosphodiesterase 5A, cGMP-specific	Mus musculus	8-12
8747434-0	1995	The superreactive disulfide bonds in alpha-lactalbumin and lysozyme.	Disulfides	18-27	lactalbumin alpha	Bos taurus	37-54
8747434-2	1995	The local conformation around the surface disulfide in ELZ seems to be more similar to that in hen egg-white lysozyme than in alpha-lactalbumin.	Disulfides	42-51	lactalbumin alpha	Bos taurus	126-143
8747434-4	1995	The torsion energy on each of the disulfides in three alpha-lactalbumin and eight c-type lysozymes whose native conformations have been experimentally or theoretically analyzed was calculated, and it was found that torsion imposed on the surface disulfide between Cys 6 and Cys 120 in alpha-lactalbumin is a main cause of the superreactivity and all of lysozymes, including the Ca(2+)-binding ones, have no such strained surface bond.	Disulfides	34-44	lactalbumin alpha	Bos taurus	54-71
8747434-4	1995	The torsion energy on each of the disulfides in three alpha-lactalbumin and eight c-type lysozymes whose native conformations have been experimentally or theoretically analyzed was calculated, and it was found that torsion imposed on the surface disulfide between Cys 6 and Cys 120 in alpha-lactalbumin is a main cause of the superreactivity and all of lysozymes, including the Ca(2+)-binding ones, have no such strained surface bond.	Disulfides	34-44	lactalbumin alpha	Bos taurus	285-302
8747434-4	1995	The torsion energy on each of the disulfides in three alpha-lactalbumin and eight c-type lysozymes whose native conformations have been experimentally or theoretically analyzed was calculated, and it was found that torsion imposed on the surface disulfide between Cys 6 and Cys 120 in alpha-lactalbumin is a main cause of the superreactivity and all of lysozymes, including the Ca(2+)-binding ones, have no such strained surface bond.	Disulfides	34-43	lactalbumin alpha	Bos taurus	54-71
8747434-4	1995	The torsion energy on each of the disulfides in three alpha-lactalbumin and eight c-type lysozymes whose native conformations have been experimentally or theoretically analyzed was calculated, and it was found that torsion imposed on the surface disulfide between Cys 6 and Cys 120 in alpha-lactalbumin is a main cause of the superreactivity and all of lysozymes, including the Ca(2+)-binding ones, have no such strained surface bond.	Disulfides	34-43	lactalbumin alpha	Bos taurus	285-302
27113713-6	2016	Moreover, Fc-gp130 could automatically form dimers by the disulfide bond.	Disulfides	58-67	interleukin 6 cytokine family signal transducer	Homo sapiens	13-18
8561853-4	1995	The results of proton NMR studies of the reduced form of these proteins suggest that the heme environments of the unmodified monomer and disulfide dimer derivatives of iso-1 ferrocytochrome c are similar and indicate that treatment of the thionitrobenzoate-derivatized and disulfide dimer forms of the protein with sodium dithionite results in cleavage of the disulfide bonds at position 102.	Disulfides	273-282	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	168-173
8561853-4	1995	The results of proton NMR studies of the reduced form of these proteins suggest that the heme environments of the unmodified monomer and disulfide dimer derivatives of iso-1 ferrocytochrome c are similar and indicate that treatment of the thionitrobenzoate-derivatized and disulfide dimer forms of the protein with sodium dithionite results in cleavage of the disulfide bonds at position 102.	Disulfides	273-282	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	168-173
8561853-5	1995	Circular dichroism studies reveal that only the disulfide dimer form of iso-1 ferricytochrome c exhibits a Soret CD spectrum which differs from the native, unmodified monomer in that the intensity of the negative band at approximately 420 nm is diminished in the spectrum of the dimer relative to the spectrum of the monomer.	Disulfides	48-57	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	72-77
27009048-7	2016	Hence, SO2 exerted its vasodilatory effects at least partly by promoting disulfide-dependent dimerization of sGC and PKG, resulting in an activated sGC/cGMP/PKG pathway in blood vessels.	Disulfides	73-82	guanylate cyclase 1 soluble subunit beta 2	Rattus norvegicus	109-112
27009048-7	2016	Hence, SO2 exerted its vasodilatory effects at least partly by promoting disulfide-dependent dimerization of sGC and PKG, resulting in an activated sGC/cGMP/PKG pathway in blood vessels.	Disulfides	73-82	guanylate cyclase 1 soluble subunit beta 2	Rattus norvegicus	148-151
26887678-5	2016	RESULTS: Loss of native disulfide in cyclic (cT20-T21) and linear peptides (T20-T21pep) derived from the C-terminal hGH disulfide during the first 60 min of reaction was greater than loss of the C-terminal disulfide in hGH itself.	Disulfides	24-33	serine protease 50	Homo sapiens	45-49
7559385-4	1995	In this study we show that DnaJ, like thioredoxin, protein-disulfide isomerase, and DsbA, possesses an active dithiol/disulfide group and catalyzes protein disulfide formation (oxidative renaturation of reduced RNase), reduction (reduction of insulin disulfides), and isomerization (refolding of randomly oxidized RNase).	Disulfides	59-68	DnaJ	Escherichia coli	27-31
7559385-4	1995	In this study we show that DnaJ, like thioredoxin, protein-disulfide isomerase, and DsbA, possesses an active dithiol/disulfide group and catalyzes protein disulfide formation (oxidative renaturation of reduced RNase), reduction (reduction of insulin disulfides), and isomerization (refolding of randomly oxidized RNase).	Disulfides	118-127	DnaJ	Escherichia coli	27-31
7559385-4	1995	In this study we show that DnaJ, like thioredoxin, protein-disulfide isomerase, and DsbA, possesses an active dithiol/disulfide group and catalyzes protein disulfide formation (oxidative renaturation of reduced RNase), reduction (reduction of insulin disulfides), and isomerization (refolding of randomly oxidized RNase).	Disulfides	118-127	protein-disulfide isomerase	Escherichia coli	51-78
26887678-7	2016	At longer reaction times (&gt;240 min), native disulfides in both hGH and cT20-T21 were regenerated.	Disulfides	47-57	serine protease 50	Homo sapiens	74-78
29997815-2	2016	The site-selective functionalization of (a) the peptide hormone somatostatin, (b) the interchain disulfide of bovine insulin and (c) functionalization of the proteins GFP and lysozyme with allyl sulfones proceeds in aqueous solution.	Disulfides	97-106	insulin	Bos taurus	117-124
7556625-0	1995	Expression and disulfide-bond connectivity of the second ligand-binding repeat of the human LDL receptor.	Disulfides	15-24	low density lipoprotein receptor	Homo sapiens	92-104
7556625-1	1995	The human LDL receptor (LDLR) has a binding domain which consists of seven contiguous ligand-binding (LB) repeats, each approximately 40 amino acids long with three disulfide bonds.	Disulfides	165-174	low density lipoprotein receptor	Homo sapiens	10-22
7556625-1	1995	The human LDL receptor (LDLR) has a binding domain which consists of seven contiguous ligand-binding (LB) repeats, each approximately 40 amino acids long with three disulfide bonds.	Disulfides	165-174	low density lipoprotein receptor	Homo sapiens	24-28
7556625-4	1995	We suggest that the first two LB repeats of the LDLR, with their unique disulfide-bonding pattern, serve as a structural paradigm for other LB repeats.	Disulfides	72-81	low density lipoprotein receptor	Homo sapiens	48-52
26195288-3	2016	Our previous results show that the MED10a, MED28, and MED32 Mediator subunits form various types of covalent oligomers linked by intermolecular disulfide bonds in vitro.	Disulfides	144-153	mediator of RNA polymerase II transcription subunit-like protein	Arabidopsis thaliana	54-59
24214390-1	1995	Fast-atom bombardment mass spectrometry was used to study disulfide bonding patterns in heat-denatured human recombinant macrophage colony stimulating factor (rhM-CSF).	Disulfides	58-67	colony stimulating factor 2	Homo sapiens	163-166
24214390-3	1995	Native rhM-CSF is a homodimer with intramolecular disulfide linkages between Cys7-Cys90, Cys48-Cys139, and Cys102-Cys146 and intermolecular linkages between Cys31-Cys31, and the pairs Cys157 and Cys159.	Disulfides	50-59	colony stimulating factor 2	Homo sapiens	11-14
24214390-6	1995	When heated for 5 min the disulfide bonds of rhM-CSF are completely scrambled and lead to nonnative intramolecular disulfide bonds between Cys48-Cys102 and Cys90-Cys102 and one intermolecular disulfide bond between Cys102-Cys102.	Disulfides	26-35	colony stimulating factor 2	Homo sapiens	49-52
24214390-6	1995	When heated for 5 min the disulfide bonds of rhM-CSF are completely scrambled and lead to nonnative intramolecular disulfide bonds between Cys48-Cys102 and Cys90-Cys102 and one intermolecular disulfide bond between Cys102-Cys102.	Disulfides	115-124	colony stimulating factor 2	Homo sapiens	49-52
27138491-7	2016	The mutation leads to the substitution of a highly conserved FBN1 cysteine residue (p.Cys1111Arg), which is likely to severely perturb the FBN1 structure because of an alteration of the disulfide bond pattern in the calcium-binding epidermal growth factor-like (cbEGF) 12 domain.	Disulfides	186-195	fibrillin 1	Homo sapiens	61-65
24214390-6	1995	When heated for 5 min the disulfide bonds of rhM-CSF are completely scrambled and lead to nonnative intramolecular disulfide bonds between Cys48-Cys102 and Cys90-Cys102 and one intermolecular disulfide bond between Cys102-Cys102.	Disulfides	115-124	colony stimulating factor 2	Homo sapiens	49-52
7541042-4	1995	We demonstrate CTLA-4 is a homodimer interconnected by one disulfide bond in the extracellular domain at cysteine residue 120.	Disulfides	59-68	cytotoxic T-lymphocyte associated protein 4	Homo sapiens	15-21
27138491-7	2016	The mutation leads to the substitution of a highly conserved FBN1 cysteine residue (p.Cys1111Arg), which is likely to severely perturb the FBN1 structure because of an alteration of the disulfide bond pattern in the calcium-binding epidermal growth factor-like (cbEGF) 12 domain.	Disulfides	186-195	fibrillin 1	Homo sapiens	139-143
27138491-9	2016	An analysis of nMFS-associated mutations from the UMD-FBN1 database indicates that those de novo mutations altering disulfide bonds or Ca(2+) binding sites of the cbEGF domains encoded by exons 25-33, and a lack of phenotypic heterogeneity may be associated with an increased risk for nMFS.	Disulfides	116-125	fibrillin 1	Homo sapiens	54-58
26944735-6	2016	In the absence of NEM, BMP-1 has a higher tendency to form aggregates, but after aggregate removal, C185 and C186 are almost quantitatively engaged in the vicinal disulfide bond and BMP-1 activity remains unchanged.	Disulfides	163-172	bone morphogenetic protein 1	Homo sapiens	23-28
7762072-1	1995	A C164Y somatic mutation in the H-2Kb class I molecule causes a disruption of the alpha 2 domain disulfide bond and results in a loss of H-2Kb cell surface expression by the 69.9.15 cell line.	Disulfides	97-106	histocompatibility 2, K1, K region	Mus musculus	32-37
26944735-9	2016	A rare vicinal disulfide bond in the catalytic domain could be confirmed for the first time by mass spectrometry along with nine other proposed disulfide linkages of mature BMP-1.	Disulfides	144-153	bone morphogenetic protein 1	Homo sapiens	173-178
26435004-9	2016	Furthermore, we observed that disulfide bridges in eotaxin, epidermal growth factor, and periostin were also decreased in the lungs of house dust mite-challenged ERp57-deleted mice.	Disulfides	30-39	epidermal growth factor	Mus musculus	60-83
7730378-9	1995	It was presently found that the effects of saposin C on phosphatidylserine liposomes and on glucosylceramidase activity are markedly reduced when the three disulfide bonds are irreversibly disrupted.	Disulfides	156-165	glucosylceramidase beta	Homo sapiens	92-110
7613471-3	1995	The positions of these disulfide bonds are conserved in factor V and ceruloplasmin except that the second disulfide bond in the A3 domain is missing in both factor V and ceruloplasmin.	Disulfides	23-32	ceruloplasmin	Homo sapiens	69-82
26435004-9	2016	Furthermore, we observed that disulfide bridges in eotaxin, epidermal growth factor, and periostin were also decreased in the lungs of house dust mite-challenged ERp57-deleted mice.	Disulfides	30-39	protein disulfide isomerase associated 3	Mus musculus	162-167
26415097-8	2016	We show that in vitro and in vivo exposure to hydrogen peroxide induces the formation of a disulfide bond in Mss51 involving CPX motif heme-coordinating cysteines.	Disulfides	91-100	Mss51p	Saccharomyces cerevisiae S288C	109-114
26760765-6	2016	Mass spectroscopy revealed that cysteines 2 and 8 can form a disulfide bridge in native VDAC3.	Disulfides	61-70	voltage dependent anion channel 3	Homo sapiens	88-93
7880821-2	1995	Previous mutagenesis studies have indicated the requirement of a tertiary structure in the intradiscal region with a disulfide bond between Cys-110 and Cys-187 for the correct assembly and/or function of rhodopsin.	Disulfides	117-126	rhodopsin	Bos taurus	204-213
26719247-4	2015	In contrast, the gp120 subunits of the native-like SOSIP.664 trimer almost exclusively retained the canonical disulfide bond pattern.	Disulfides	110-119	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	17-22
7812965-0	1995	Rapid and specific uptake of anti-Tac disulfide-stabilized Fv by interleukin-2 receptor-bearing tumors.	Disulfides	38-47	interleukin 2	Mus musculus	65-78
26719247-7	2015	The same factors may also be relevant to the production and purification of monomeric gp120 proteins that are free of aberrant disulfide bonds.	Disulfides	127-136	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	86-91
7818530-0	1995	Lipoprotein lipase: role of intramolecular disulfide bonds in enzyme catalysis.	Disulfides	43-52	lipoprotein lipase	Homo sapiens	0-18
26719252-7	2015	Using the redesigned subtype B and C trimer representatives as respective foundations, we further stabilized the NFL TD trimers by engineering an intraprotomer disulfide linkage in the prebridging sheet, I201C-A433C (CC), that locks the gp120 in the receptor nontriggered state.	Disulfides	160-169	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	237-242
7818530-8	1995	The conservation of catalytic function despite the disruption of the only disulfide bridge in the C-terminal domain of LPL indicates that the two domains can function independently of each other in enzyme catalysis.	Disulfides	74-83	lipoprotein lipase	Homo sapiens	119-122
26729099-1	2015	Human leukocytic antigen-B27 heavy chain (HLA-B27 HC) has the tendency to fold slowly, in turn gradually forming a homodimer, (B27-HC)2 via a disulfide linkage to activate killer cells and T-helper 17 cells and inducing endoplasmic reticulum (ER) stress to trigger the IL-23/IL-17 axis for pro-inflammatory reactions.	Disulfides	142-151	major histocompatibility complex, class I, B	Homo sapiens	42-49
7835433-5	1995	Furthermore, as isolated the thioredoxin domains of CaBP1 and CaBP2 were in disulfide form as judged by stoichiometric oxidation of 2 and 3 mol of NADPH in CaBP1 and CaBP2, respectively.	Disulfides	76-85	calcium binding protein 1	Rattus norvegicus	52-57
7835433-7	1995	This showed that CaBP1 and CaBP2, like PDI, have a much higher redox potential than wild type thioredoxin (-270 mV) in agreement with a role in formation of protein disulfide bonds.	Disulfides	165-174	calcium binding protein 1	Rattus norvegicus	17-22
7835433-7	1995	This showed that CaBP1 and CaBP2, like PDI, have a much higher redox potential than wild type thioredoxin (-270 mV) in agreement with a role in formation of protein disulfide bonds.	Disulfides	165-174	protein-disulfide isomerase	Escherichia coli	39-42
26729099-1	2015	Human leukocytic antigen-B27 heavy chain (HLA-B27 HC) has the tendency to fold slowly, in turn gradually forming a homodimer, (B27-HC)2 via a disulfide linkage to activate killer cells and T-helper 17 cells and inducing endoplasmic reticulum (ER) stress to trigger the IL-23/IL-17 axis for pro-inflammatory reactions.	Disulfides	142-151	interleukin 23 subunit alpha	Homo sapiens	269-274
7843232-1	1995	Interleukin-12 (IL-12) is a cytokine that has regulatory effects on T and natural killer (NK) cells and is composed of two disulfide-bonded subunits, p40 and p35.	Disulfides	123-132	interleukin 12a	Mus musculus	158-161
26458166-5	2015	Molecular docking of PTT onto gp120 argued that, with sufficient linker length, the peptide SH could approach and disrupt several alternative gp120 disulfides.	Disulfides	148-158	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	142-147
26458166-8	2015	Overall, the results are consistent with the view that the binding of PTT positions the peptide SH group to interfere with conserved disulfides clustered proximal to the CD4 binding site in gp120, leading to disulfide exchange in gp120 and possibly gp41, rearrangement of the Env spike, and ultimately disruption of the viral membrane.	Disulfides	133-143	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	190-195
26458166-8	2015	Overall, the results are consistent with the view that the binding of PTT positions the peptide SH group to interfere with conserved disulfides clustered proximal to the CD4 binding site in gp120, leading to disulfide exchange in gp120 and possibly gp41, rearrangement of the Env spike, and ultimately disruption of the viral membrane.	Disulfides	133-143	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	230-235
7476356-0	1995	Measurement of equilibrium midpoint potentials of thiol/disulfide regulatory groups on thioredoxin-activated chloroplast enzymes.	Disulfides	56-65	thioredoxin	Homo sapiens	87-98
26458166-8	2015	Overall, the results are consistent with the view that the binding of PTT positions the peptide SH group to interfere with conserved disulfides clustered proximal to the CD4 binding site in gp120, leading to disulfide exchange in gp120 and possibly gp41, rearrangement of the Env spike, and ultimately disruption of the viral membrane.	Disulfides	133-142	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	190-195
26458166-8	2015	Overall, the results are consistent with the view that the binding of PTT positions the peptide SH group to interfere with conserved disulfides clustered proximal to the CD4 binding site in gp120, leading to disulfide exchange in gp120 and possibly gp41, rearrangement of the Env spike, and ultimately disruption of the viral membrane.	Disulfides	133-142	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	230-235
26676779-11	2015	Disulfide cross-linking based on ectopic Cys residues showed that the contacts between Gag proteins on the membrane are similar to the known contacts in virus-like particles.	Disulfides	0-9	Pr76 polyprotein precursor	Rous sarcoma virus	87-90
7896508-4	1994	It was confirmed by amino acid microsequencing of cysteine-containing fragments derived from thermolytic digestion that the pattern of three disulfide bond pairings in synthetic HB-EGF(44-86) was consistent with that of EGF and transforming growth factor-alpha (TGF-alpha).	Disulfides	141-150	heparin binding EGF like growth factor	Homo sapiens	178-184
7896748-5	1994	Porcine ATIII showed high sequence similarity to other mammalian ATIIIs, including the reactive site, heparin-binding basic amino acid residues, and disulfide bonds.	Disulfides	149-158	serpin family C member 1	Homo sapiens	8-13
7929094-10	1994	Furthermore, mutations in Cys-1 and Cys-4 also prevented intrachain disulfide bond formation within the C-propeptide.	Disulfides	68-77	cystin 1	Homo sapiens	26-31
26379215-2	2015	A water-in-oil emulsion is generated feasibly from a mixture of water and a solution of disulfide-containing hyperbranched PEGylated poly(amido amine)s, poly(BAC2-AMPD1)-PEG, in chloroform.	Disulfides	88-97	adenosine monophosphate deaminase 1	Homo sapiens	163-168
28955804-2	2016	Thioredoxin 1 (Trx1) is an important reducing enzyme that cleaves disulfides in proteins and acts as an S-denitrosylase.	Disulfides	66-76	thioredoxin	Homo sapiens	0-13
8050492-9	1994	These results indicate that ERp61 may be involved in disulfide bond formation for such proteins.	Disulfides	53-62	protein disulfide isomerase associated 3	Mus musculus	28-33
28955804-2	2016	Thioredoxin 1 (Trx1) is an important reducing enzyme that cleaves disulfides in proteins and acts as an S-denitrosylase.	Disulfides	66-76	thioredoxin	Homo sapiens	15-19
8038212-5	1994	Employment of nonreducing conditions decreased the electrophoretic mobility of the complex to a 60 kDa species suggesting that the native PACAP receptor exists in a compact conformation stabilized by intramolecular disulfide bridges.	Disulfides	215-224	adenylate cyclase activating polypeptide 1	Sus scrofa	138-143
26453009-5	2015	The non-active disulfide switches the alpha3-helix of TRX, composed of residues Cys62 to Glu70, to a bulging loop and dramatically changes the environment of the TRX residues involved in the interaction with its reductase and other cellular substrates.	Disulfides	15-24	thioredoxin	Homo sapiens	54-57
8038212-6	1994	Disulfide bonds are also important for the ligand binding activity of the PACAP receptor since pretreatment of the membranes with dithiothreitol led to complete inhibition of PACAP binding and to 61% dissociation of the ligand-receptor complex.	Disulfides	0-9	adenylate cyclase activating polypeptide 1	Sus scrofa	74-79
8038212-6	1994	Disulfide bonds are also important for the ligand binding activity of the PACAP receptor since pretreatment of the membranes with dithiothreitol led to complete inhibition of PACAP binding and to 61% dissociation of the ligand-receptor complex.	Disulfides	0-9	adenylate cyclase activating polypeptide 1	Sus scrofa	175-180
26453009-5	2015	The non-active disulfide switches the alpha3-helix of TRX, composed of residues Cys62 to Glu70, to a bulging loop and dramatically changes the environment of the TRX residues involved in the interaction with its reductase and other cellular substrates.	Disulfides	15-24	thioredoxin	Homo sapiens	162-165
8176746-3	1994	Only elimination of the whole EF hand domain or its single disulfide bond decreased production and secretion indicating that the C-terminal region of BM-40 is essential for correct folding.	Disulfides	59-68	secreted protein acidic and cysteine rich	Homo sapiens	150-155
26418532-7	2015	We show that both molecules inhibit PTEN via oxidative mechanisms resulting in the formation of the same intramolecular disulfide, therefore enabling the reactivation of PTEN under reductive conditions.	Disulfides	120-129	phosphatase and tensin homolog	Homo sapiens	36-40
8188714-3	1994	Instead, the role of PDI is limited to disulfide bond formation as demonstrated for the folding of the denatured and reduced Fab fragment.	Disulfides	39-48	FA complementation group B	Homo sapiens	125-128
7513556-3	1994	The present study investigates the effect of DsbA on the well-characterized disulfide-coupled refolding processes of BPTI and of alpha-lactalbumin.	Disulfides	76-85	lactalbumin alpha	Bos taurus	129-146
7513556-6	1994	Neither did DsbA catalyze the intramolecular rearrangements observed in the three disulfide-bonded "molten globule" form of alpha-lactalbumin at neutral pH.	Disulfides	82-91	lactalbumin alpha	Bos taurus	124-141
8139027-10	1994	The binding activity of apo H is destroyed upon reduction, indicating that 1 or more of its 22 disulfide bonds are required for interaction with rHBsAg.	Disulfides	95-104	apolipoprotein H	Homo sapiens	24-29
8139571-5	1994	Substitution for both cysteines in sqt-1 also resulted in an LRol phenotype, demonstrating that disulfide bonding is important for normal function but not required for assembly.	Disulfides	96-105	Cuticle collagen sqt-1	Caenorhabditis elegans	35-40
8119694-1	1994	In all vertebrate species studied, the complex, disulfide-linked structure of fibrinogen is essentially the same: a hexamer assembled from three different subunits (A alpha, B beta, gamma)2.	Disulfides	48-57	fibrinogen gamma chain	Gallus gallus	78-88
7510745-4	1994	Exchanging the disulfide-linked C8 alpha-gamma dimer in human C8 with one from rabbit was found to be sufficient to overcome restriction by human Es.	Disulfides	15-24	complement C8 alpha chain	Homo sapiens	32-40
8177377-5	1994	SDS-PAGE of hydrophobically labeled DS-AChE revealed the presence of a disulfide bonded hydrophobic membrane anchor of about 20 kDa.	Disulfides	71-80	acetylcholinesterase	Rattus norvegicus	39-43
8117284-2	1994	Immunoreactive BMP-2 protein was found to be a homodimer of an 18 kDa BMP-2 polypeptide linked through disulfide bridge(s).	Disulfides	103-112	bone morphogenetic protein 2 S homeolog	Xenopus laevis	15-20
8117284-2	1994	Immunoreactive BMP-2 protein was found to be a homodimer of an 18 kDa BMP-2 polypeptide linked through disulfide bridge(s).	Disulfides	103-112	bone morphogenetic protein 2 S homeolog	Xenopus laevis	70-75
8119487-4	1994	SPARC also inhibits cell cycle progression in vitro, in part through a cationic, disulfide-bonded region that is homologous to a repeated domain in the cytokine inhibitor, follistatin.	Disulfides	81-90	secreted protein acidic and cysteine rich	Homo sapiens	0-5
7893813-4	1994	The tetrapeptides found in the redox site of thioredoxin were optimized to conformers in which the two sulfur atoms were in van der Waals contact, so that a disulfide bond may be formed during the function.	Disulfides	157-166	thioredoxin	Homo sapiens	45-56
8223649-12	1993	Furthermore, a minor species was identified which contains Cys1 and Cys98 in a modified form, thereby hindering the formation of a disulfide bridge between these two residues.	Disulfides	131-140	cystin 1	Homo sapiens	59-63
8395501-6	1993	Therefore, in the normal thioredoxin-catalyzed reduction pathway, Cys-46 is the nucleophile required to attack the disulfide of the substrate and Cys-49 serves to cleave the mixed disulfide intermediate, thus allowing for the release of oxidized thioredoxin and the reduced target enzyme.	Disulfides	180-189	thioredoxin	Homo sapiens	25-36
8274513-2	1993	The modified protein has PEG polymer molecules attached to the backbone by the newly formed disulfide bonds, which are readily cleaved to regenerate the native protein under mild reducing conditions.	Disulfides	92-101	progestagen associated endometrial protein	Homo sapiens	25-28
8413323-6	1993	SDS-PAGE analyses revealed that the NK2.1 antigen is expressed at the cell surface as a N-glycosylated disulfide-linked protein dimer with approximately 65 kD subunits.	Disulfides	103-112	serine (or cysteine) peptidase inhibitor, clade B, member 9f	Mus musculus	36-41
7688570-12	1993	These results suggest that EGF can react with the reactive thiol ester of proteinase-activated alpha 2M by nucleophilic attack of the alpha-amino group and to a lesser extent by sulfide-disulfide exchange with the free SH of the cleaved thiol ester.	Disulfides	186-195	alpha-2-macroglobulin	Homo sapiens	95-103
8262907-8	1993	Our study shows that the disulfide-bond pairings of [-32-153]M-CSF that is expressed and post-translationally modified in mammalian cells are identical to those of Escherichia coli-derived [3-153]M-CSF with only one intermolecular disulfide bond, namely, Cys31-Cys31.	Disulfides	231-240	colony stimulating factor 1	Homo sapiens	61-66
8325331-0	1993	The extended hinge region of IgG3 is not required for high phagocytic capacity mediated by Fc gamma receptors, but the heavy chains must be disulfide bonded.	Disulfides	140-149	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	29-33
8511589-2	1993	Binding of IL-6 to IL-6R induced disulfide-linked homodimerization of gp130.	Disulfides	33-42	interleukin 6 cytokine family signal transducer	Homo sapiens	70-75
8461340-0	1993	Charge-remote fragmentation in a disulfide-containing peptide, [Pen]-enkephalin, under fast atom bombardment collisionally activated dissociation conditions.	Disulfides	33-42	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	64-67
8461340-1	1993	Fast atom bombardment collisionally activated dissociation tandem mass spectrometry (FAB CAD MS/MS) of a disulfide-containing peptide, [2-D-penicillamine, 5-D-penicillamine]- enkephalin ([Pen]-enkephalin), is described.	Disulfides	105-114	FA complementation group B	Homo sapiens	85-88
8461340-1	1993	Fast atom bombardment collisionally activated dissociation tandem mass spectrometry (FAB CAD MS/MS) of a disulfide-containing peptide, [2-D-penicillamine, 5-D-penicillamine]- enkephalin ([Pen]-enkephalin), is described.	Disulfides	105-114	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	188-191
8461340-2	1993	Unlike those of most other disulfide-containing peptides investigated, CAD of the native, unreduced protonated molecule of [Pen]-enkephalin yields a relatively large number of fragment ions.	Disulfides	27-36	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	124-127
8461340-7	1993	Comparison of the CAD spectra of derivatized and underivatized [Pen]-enkephalin suggests that charge-remote fragmentation plays a significant role in the high-energy dissociation of this disulfide-bonded peptide.	Disulfides	187-196	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	64-67
8437217-5	1993	As has already been described, if the Cys at position -7 is mutated, disulfide-linked HBe homodimers which have both HBe antigenicity and HBc antigenicity are expressed.	Disulfides	69-78	keratin 88, pseudogene	Homo sapiens	138-141
8094405-5	1993	In contrast, mature single-positive T cells expressed fully assembled surface TCR complexes containing disulfide-linked heterodimers consisting of transgenic TCR beta chains and endogenous TCR alpha chains.	Disulfides	103-112	T cell receptor beta chain	Mus musculus	158-166
8094405-5	1993	In contrast, mature single-positive T cells expressed fully assembled surface TCR complexes containing disulfide-linked heterodimers consisting of transgenic TCR beta chains and endogenous TCR alpha chains.	Disulfides	103-112	T cell receptor alpha chain	Mus musculus	189-198
8454579-8	1993	(2) The remaining disulfide linkage linked Cys 31 of one subunit to Cys 31 of the second subunit of M-CSF.	Disulfides	18-27	colony stimulating factor 1	Homo sapiens	100-105
1460414-7	1992	The molecular mass of MASP was estimated to be 83 kD with two polypeptides of heavy (66 kD) and light (L) (31 kD) chains linked by disulfide bonds.	Disulfides	131-140	MBL associated serine protease 1	Homo sapiens	22-26
1358967-1	1992	CD27 is a disulfide-linked 120-kDa homodimer expressed on the majority of peripheral T cells at variable density that belongs to the recently defined nerve growth factor receptor family.	Disulfides	10-19	CD27 molecule	Homo sapiens	0-4
1401917-0	1992	Human pre-B and B cell membrane mu-chains are noncovalently associated with a disulfide-linked complex containing a product of the B29 gene.	Disulfides	78-87	CD79b molecule	Homo sapiens	131-134
1401917-2	1992	Studies of murine B cells conducted in several laboratories, including our own, suggest that products of the mb-1 (IgM-alpha or IgD-alpha) and B29 (Ig-beta, Ig-gamma) genes occur as disulfide-linked alpha/beta and alpha/gamma heterodimers that are noncovalently associated with mIgM and mIgD.	Disulfides	182-191	histocompatibility 2, M region locus 1	Mus musculus	109-113
1401917-2	1992	Studies of murine B cells conducted in several laboratories, including our own, suggest that products of the mb-1 (IgM-alpha or IgD-alpha) and B29 (Ig-beta, Ig-gamma) genes occur as disulfide-linked alpha/beta and alpha/gamma heterodimers that are noncovalently associated with mIgM and mIgD.	Disulfides	182-191	CD79b molecule	Homo sapiens	143-146
1401917-2	1992	Studies of murine B cells conducted in several laboratories, including our own, suggest that products of the mb-1 (IgM-alpha or IgD-alpha) and B29 (Ig-beta, Ig-gamma) genes occur as disulfide-linked alpha/beta and alpha/gamma heterodimers that are noncovalently associated with mIgM and mIgD.	Disulfides	182-191	chemokine (C-X-C motif) ligand 9	Mus musculus	115-117
1445335-2	1992	The cysteines at positions 58 and 105 of active IL-2 form an intramolecular disulfide bond while that at position 125 remains as a free form.	Disulfides	76-85	interleukin 2	Mus musculus	48-52
1327135-0	1992	Folding topology of the disulfide-bonded dimeric DNA-binding domain of the myogenic determination factor MyoD.	Disulfides	24-33	myogenic differentiation 1	Mus musculus	105-109
1327135-4	1992	There is a naturally occurring cysteine at residue 135 in mouse MyoD that when oxidized to a disulfide induces MyoD-bHLH to form a symmetric homodimer with a defined tertiary structure as judged by sedimentation equilibrium ultracentrifugation and NMR spectroscopy.	Disulfides	93-102	myogenic differentiation 1	Mus musculus	64-68
1327135-4	1992	There is a naturally occurring cysteine at residue 135 in mouse MyoD that when oxidized to a disulfide induces MyoD-bHLH to form a symmetric homodimer with a defined tertiary structure as judged by sedimentation equilibrium ultracentrifugation and NMR spectroscopy.	Disulfides	93-102	myogenic differentiation 1	Mus musculus	111-115
1390929-4	1992	The purified arylsulfatase B migrated as a single polypeptide of 58 kDa on non-reducing SDS-PAGE, indicating that the three chains are linked by disulfide bonds.	Disulfides	145-154	arylsulfatase B	Homo sapiens	13-28
1356981-0	1992	Effects of hemin and porphyrin compounds on intersubunit disulfide formation of heme-regulated eIF-2 alpha kinase and the regulation of protein synthesis in reticulocyte lysates.	Disulfides	57-66	eukaryotic translation initiation factor 2A	Oryctolagus cuniculus	95-106
1440533-4	1992	All of these protein Cs were two chain form linked by disulfide bond as well as human protein C and activated by thrombin-thrombomodulin complex.	Disulfides	54-63	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	13-22
1379254-10	1992	The apparent molecular weight of the IGF-II/M6P receptor (220,000 kilos without reduction of disulfide bonds) varied among the different tissues: in brain the receptor was of lower molecular weight than in other organs.	Disulfides	93-102	insulin like growth factor 2	Homo sapiens	37-43
1312829-1	1992	Splicing at an alternate 3"-acceptor site results in deletion of a CCCAG in the 5"-sequence of the exon coding for the NH2-terminal immunoglobulin-like disulfide loop of the heparin-binding fibroblast growth factor receptor (flg) alpha isoform.	Disulfides	152-161	filaggrin	Homo sapiens	225-228
1312472-4	1992	One of them expressed a non-disulfide-linked gamma/delta TcR using the 60-kDa gamma chain, whereas, the other expressed a disulfide-linked gamma/delta TcR.	Disulfides	28-37	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	57-60
1312472-4	1992	One of them expressed a non-disulfide-linked gamma/delta TcR using the 60-kDa gamma chain, whereas, the other expressed a disulfide-linked gamma/delta TcR.	Disulfides	122-131	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	151-154
1312472-5	1992	A T cell line was derived from a patient with sarcoma and expressed a disulfide-linked gamma/delta TcR, whereas, a T cell line derived from a patient with melanoma expressed a non-disulfide-linked gamma chain of 62 kDa.	Disulfides	70-79	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	99-102
1312472-11	1992	These results demonstrate that both disulfide- and non-disulfide-linked gamma/delta TcR are expressed on T cell lines and clones derived from TIL from solid tumors.	Disulfides	36-45	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	84-87
1312472-11	1992	These results demonstrate that both disulfide- and non-disulfide-linked gamma/delta TcR are expressed on T cell lines and clones derived from TIL from solid tumors.	Disulfides	55-64	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	84-87
1312472-12	1992	Non-disulfide-linked gamma/delta TcR using the 56-66-kDa gamma chain are frequently found on TIL-derived T cell lines and clones.	Disulfides	4-13	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	33-36
1737006-4	1992	These peptides can form only one of the native disulfide bonds, C-1 to C-11 in the case of Apa-1 and C-3 to C-15 in the case of Apa-2.	Disulfides	47-56	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	64-75
1517016-1	1992	To further elucidate the role of the disulfide bonds in determining the protein folding of recombinant human epidermal growth factor (r-HuEGF) we studied the structure of reduced and oxidized r-HuEGF using circular dichroism (CD).	Disulfides	37-46	epidermal growth factor	Homo sapiens	109-132
1569370-19	1992	The putative lipid-binding domains of LPL and HL, the disulfide-bridging cysteine residues, catalytic residues, and N-linked glycosylation sites of LPL, HL, and PL all lie within regions having a CI of 0.8 or higher.	Disulfides	54-63	lipoprotein lipase	Homo sapiens	148-151
1727607-7	1992	Thus a disulfide loop at the V3 portion of gp160 is required for cleavage into gp120 and gp41, presumably because the loop is required for proper tertiary structure.	Disulfides	7-16	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	79-84
1837811-4	1991	Furthermore, the TcR-gamma combinatorial repertoire appears to be even more limited by the fact that particular V gamma genes are preferentially used in TcR-gamma 1 or TcR-gamma 2 derived receptors, i.e. in disulfide-linked or non-disulfide-linked TcR-gamma delta receptors.	Disulfides	207-216	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	17-20
1837811-4	1991	Furthermore, the TcR-gamma combinatorial repertoire appears to be even more limited by the fact that particular V gamma genes are preferentially used in TcR-gamma 1 or TcR-gamma 2 derived receptors, i.e. in disulfide-linked or non-disulfide-linked TcR-gamma delta receptors.	Disulfides	207-216	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	153-156
1837811-4	1991	Furthermore, the TcR-gamma combinatorial repertoire appears to be even more limited by the fact that particular V gamma genes are preferentially used in TcR-gamma 1 or TcR-gamma 2 derived receptors, i.e. in disulfide-linked or non-disulfide-linked TcR-gamma delta receptors.	Disulfides	207-216	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	153-156
1837811-4	1991	Furthermore, the TcR-gamma combinatorial repertoire appears to be even more limited by the fact that particular V gamma genes are preferentially used in TcR-gamma 1 or TcR-gamma 2 derived receptors, i.e. in disulfide-linked or non-disulfide-linked TcR-gamma delta receptors.	Disulfides	207-216	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	153-156
1837811-4	1991	Furthermore, the TcR-gamma combinatorial repertoire appears to be even more limited by the fact that particular V gamma genes are preferentially used in TcR-gamma 1 or TcR-gamma 2 derived receptors, i.e. in disulfide-linked or non-disulfide-linked TcR-gamma delta receptors.	Disulfides	231-240	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	17-20
1837811-4	1991	Furthermore, the TcR-gamma combinatorial repertoire appears to be even more limited by the fact that particular V gamma genes are preferentially used in TcR-gamma 1 or TcR-gamma 2 derived receptors, i.e. in disulfide-linked or non-disulfide-linked TcR-gamma delta receptors.	Disulfides	231-240	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	153-156
1799225-1	1991	A method has been developed to prepare, purify, and fully characterize poly-iodinated insulin-like growth factor II (IGF-II) which can then be catalytically deiodinated to produce IGF-II with its native disulfide bonded structure.	Disulfides	203-212	insulin like growth factor 2	Homo sapiens	86-123
1799225-1	1991	A method has been developed to prepare, purify, and fully characterize poly-iodinated insulin-like growth factor II (IGF-II) which can then be catalytically deiodinated to produce IGF-II with its native disulfide bonded structure.	Disulfides	203-212	insulin like growth factor 2	Homo sapiens	117-123
1799225-7	1991	Purified poly-iodinated IGF-II was deiodinated by hydrogenolysis, over a prereduced palladium (II) oxide catalyst to form IGF-II with its native disulfide bonds intact, as shown by peptide mapping.	Disulfides	145-154	insulin like growth factor 2	Homo sapiens	24-30
1680927-5	1991	The rat NKR-P1 Ag shares several features with the mouse Ly-49 Ag, including selective cell surface expression on NK cells, homology to the C-type lectins, expression as a type II integral membrane protein, and disulfide-linked homodimeric structure.	Disulfides	211-220	killer cell lectin-like receptor subfamily B member 1C	Mus musculus	8-14
1836739-4	1991	Unexpectedly, the antibody showed cross-reactivity to the human CD3 epsilon molecule and detected a disulfide-linked 20 kDa dimeric form of human CD3 epsilon, which is a novel family component of the CD3 complex and is associated closely with the CD3 zeta-zeta homodimer as well as TCR alpha beta or TCR gamma delta.	Disulfides	100-109	CD3 epsilon subunit of T-cell receptor complex	Homo sapiens	64-75
1836739-4	1991	Unexpectedly, the antibody showed cross-reactivity to the human CD3 epsilon molecule and detected a disulfide-linked 20 kDa dimeric form of human CD3 epsilon, which is a novel family component of the CD3 complex and is associated closely with the CD3 zeta-zeta homodimer as well as TCR alpha beta or TCR gamma delta.	Disulfides	100-109	CD3 epsilon subunit of T-cell receptor complex	Homo sapiens	146-157
1875954-4	1991	Fab/c made by papain digestion was able to active complement in haemolytic assays; this activity was lost after cleavage of its accessible disulfide bonds.	Disulfides	139-148	FA complementation group B	Homo sapiens	0-3
1713450-7	1991	Carboxymethylation of hIGFBP-3 suggests that all 18 cysteines are involved in disulfide linkages.	Disulfides	78-87	insulin like growth factor binding protein 3	Homo sapiens	22-30
1906475-5	1991	Based on the deduced amino acid sequence and immunochemical analysis of proteolytic fragments of NG2, the extracellular region can be divided into three domains: an amino terminal cysteine-containing domain which is stabilized by intrachain disulfide bonds, a serine-glycine-containing domain to which chondroitin sulfate chains are attached, and another cysteine-containing domain.	Disulfides	241-250	chondroitin sulfate proteoglycan 4	Rattus norvegicus	97-100
2037582-0	1991	The integrity of the cysteine 186-cysteine 209 bond of the second disulfide loop of tissue factor is required for binding of factor VII.	Disulfides	66-75	coagulation factor III, tissue factor	Homo sapiens	84-97
2037582-2	1991	The functional significance of the two disulfide bonded loops in the surface domain of TF has been analyzed using site-directed mutagenesis to selectively preclude covalent stabilization of these loops by pairwise substitution of serine residues for cysteines.	Disulfides	39-48	coagulation factor III, tissue factor	Homo sapiens	87-89
1932345-1	1991	Thioredoxin, a disulfide-containing protein having a highly conservative structure, is present in all types of organisms that are phylogenetically distant from one another.	Disulfides	15-24	thioredoxin	Homo sapiens	0-11
1917296-3	1991	A variety of procedures have been demonstrated using the related model peptides Ac-Cys-Pro-D Val-Cys-NH2 and Ac-Pen-Pro-D Val-Cys-NH2 (which both readily assume a type II beta-turn conformation that becomes stabilized by a 14-membered disulfide-containing intramolecular ring), and oxytocin (conformationally mobile 20-membered disulfide ring).	Disulfides	235-244	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	112-115
1917296-3	1991	A variety of procedures have been demonstrated using the related model peptides Ac-Cys-Pro-D Val-Cys-NH2 and Ac-Pen-Pro-D Val-Cys-NH2 (which both readily assume a type II beta-turn conformation that becomes stabilized by a 14-membered disulfide-containing intramolecular ring), and oxytocin (conformationally mobile 20-membered disulfide ring).	Disulfides	328-337	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	112-115
1965778-6	1990	Leucinthiol-enkephalin became bound covalently to this receptor-thiol group via disulfide formation after prolonged incubation.	Disulfides	80-89	proenkephalin	Rattus norvegicus	12-22
2215480-12	1990	Moreover, the formation of inter-molecular disulfide bond(s) linked by two pairs of cystein residues is essential for the expression of the biological activity of mouse IL-5.	Disulfides	43-52	interleukin 5	Mus musculus	169-173
2188973-3	1990	Protein disulfide-isomerase contains two redox-active disulfides/molecule which were reduced by NADPH and calf thioredoxin reductase (Km approximately 35 microM).	Disulfides	54-64	thioredoxin	Homo sapiens	111-122
2188973-4	1990	The isomerase was a poor substrate for NADPH and Escherichia coli thioredoxin reductase, but the addition of E. coli thioredoxin resulted in rapid reduction of two disulfides/molecule.	Disulfides	164-174	thioredoxin	Homo sapiens	66-77
2188973-4	1990	The isomerase was a poor substrate for NADPH and Escherichia coli thioredoxin reductase, but the addition of E. coli thioredoxin resulted in rapid reduction of two disulfides/molecule.	Disulfides	164-174	thioredoxin	Homo sapiens	117-128
2188973-6	1990	Fluorescence measurements demonstrated that thioredoxin--(SH)2 reduced the disulfides of the isomerase and allowed the kinetics of the reaction to be followed; the reaction was also catalyzed by calf thioredoxin reductase.	Disulfides	75-85	thioredoxin	Homo sapiens	200-211
2188973-7	1990	Equilibrium measurements showed that the apparent redox potential of the active site disulfide/dithiols of the thioredoxin domains of protein disulfide-isomerase was about 30 mV higher than the disulfide/dithiol of E. coli thioredoxin.	Disulfides	85-94	thioredoxin	Homo sapiens	111-122
2188973-7	1990	Equilibrium measurements showed that the apparent redox potential of the active site disulfide/dithiols of the thioredoxin domains of protein disulfide-isomerase was about 30 mV higher than the disulfide/dithiol of E. coli thioredoxin.	Disulfides	85-94	protein-disulfide isomerase	Escherichia coli	134-161
2188973-7	1990	Equilibrium measurements showed that the apparent redox potential of the active site disulfide/dithiols of the thioredoxin domains of protein disulfide-isomerase was about 30 mV higher than the disulfide/dithiol of E. coli thioredoxin.	Disulfides	85-94	thioredoxin	Homo sapiens	223-234
2188973-7	1990	Equilibrium measurements showed that the apparent redox potential of the active site disulfide/dithiols of the thioredoxin domains of protein disulfide-isomerase was about 30 mV higher than the disulfide/dithiol of E. coli thioredoxin.	Disulfides	142-151	thioredoxin	Homo sapiens	111-122
2188973-7	1990	Equilibrium measurements showed that the apparent redox potential of the active site disulfide/dithiols of the thioredoxin domains of protein disulfide-isomerase was about 30 mV higher than the disulfide/dithiol of E. coli thioredoxin.	Disulfides	142-151	thioredoxin	Homo sapiens	223-234
2335203-2	1990	The chromogranin B protein was found to be encoded by 5 exons which correspond to the cleaved signal peptide, the short N-terminal sequence preceding the disulfide-bonded loop structure, the disulfide-bonded loop structure itself, the large, variable region comprising approximately 90% of the protein, and the conserved C-terminal sequence.	Disulfides	154-163	chromogranin B	Mus musculus	4-18
2335203-2	1990	The chromogranin B protein was found to be encoded by 5 exons which correspond to the cleaved signal peptide, the short N-terminal sequence preceding the disulfide-bonded loop structure, the disulfide-bonded loop structure itself, the large, variable region comprising approximately 90% of the protein, and the conserved C-terminal sequence.	Disulfides	191-200	chromogranin B	Mus musculus	4-18
2306116-3	1990	In addition, glutathione reductase was able to catalyze the reduction of the disulfide-linked dimer of oncomodulin.	Disulfides	77-86	glutathione-disulfide reductase	Rattus norvegicus	13-34
2306116-3	1990	In addition, glutathione reductase was able to catalyze the reduction of the disulfide-linked dimer of oncomodulin.	Disulfides	77-86	oncomodulin	Rattus norvegicus	103-114
1692242-10	1990	A similar reversal can be effected by cyanylation, with NaCN, of methylamine-treated alpha 2M in which the liberated thiols have first been converted to mixed disulfides by reaction with dithiobis(nitrobenzoic acid).	Disulfides	159-169	alpha-2-macroglobulin	Homo sapiens	85-93
2297694-4	1990	Immunoprecipitation analysis, enzyme-linked immunosorbent assays, and the lectin-binding properties of gp90 on lectin affinity columns indicated that it is a Mr approximately 180,000 disulfide-linked dimer, probably related to the transferrin receptor.	Disulfides	183-192	galectin 3 binding protein	Homo sapiens	103-107
2300577-3	1990	It is disulfide-linked to the central core and contains a binding site for the vitamin K-dependent protein S.	Disulfides	6-15	protein S	Homo sapiens	79-108
2302230-6	1990	Analogously, only C8bp/HRF that has been disulfide-reduced reacts with these antibodies.	Disulfides	41-50	tumor protein, translationally-controlled 1	Homo sapiens	18-26
33822598-2	2021	A critical role for expulsion of the RCL hinge from a native stabilizing interaction with the hydrophobic core in the activation mechanism has been proposed from reports that antithrombin variants that block this change through engineered disulfide bonds block activation.	Disulfides	239-248	serpin family C member 1	Homo sapiens	175-187
8535250-0	1995	Thrombin-binding affinities of different disulfide-bonded isomers of the fifth EGF-like domain of thrombomodulin.	Disulfides	41-50	thrombomodulin	Homo sapiens	98-112
8535250-1	1995	The fifth EGF-like domain of thrombomodulin (TM), both with and without the amino acids that connect the fifth domain to the sixth domain, has been synthesized and refolded to form several different disulfide-bonded isomers.	Disulfides	199-208	thrombomodulin	Homo sapiens	29-43
7925367-7	1994	Based on the knowledge of the location of the five disulfide bonds in the structure of pig pancreatic alpha-amylase, the possible disulfide bridges were established for each of these groups of homologous alpha-amylases.	Disulfides	51-60	amylase, alpha 2A (pancreatic)	Sus scrofa	91-115
34775124-7	2022	The GSH consumption by disulfide, CA and Fe3+, downregulates GPX4 and generates  OH, which accelerate lipid peroxides (LPO) accumulation and consequently enhances ferroptosis.	Disulfides	23-32	glutathione peroxidase 4	Homo sapiens	61-65
34788052-2	2021	The 1,2,3-Dithiazole scaffold was predicted to inhibit LAT1 by the formation of an intermolecular disulfide bond with the thiolate group of cysteine(s).	Disulfides	98-107	solute carrier family 7 member 5	Homo sapiens	55-59
34873834-9	2022	It is revealed that the disulfide-stapled peptides can be constrained into a native-like conformation and thus exhibit an improved binding potency to IL-17Rb as compared to their unstapled counterpart.	Disulfides	24-33	interleukin 17 receptor B	Homo sapiens	150-157
34455077-3	2021	The thioredoxin system, comprised of TrxR Trx and NADPH, exerts its activities via a disulfide-dithiol exchange reaction.	Disulfides	85-94	thioredoxin	Homo sapiens	4-15
34455077-3	2021	The thioredoxin system, comprised of TrxR Trx and NADPH, exerts its activities via a disulfide-dithiol exchange reaction.	Disulfides	85-94	thioredoxin	Homo sapiens	42-45
34852234-3	2021	Our results show that CypA forms an intramolecular disulfide bond between Cys115 and Cys161 upon oxidative stress and the oxidized cysteines in CypA are recycled to a reduced state by peroxiredoxin-2 (PRDX2).	Disulfides	51-60	peptidylprolyl isomerase A	Homo sapiens	22-26
34591491-1	2021	The study aims to investigate the in vivo distribution, antitumor effect, and safety of cell membrane-penetrating peptide-modified disulfide bond copolymer nanoparticles loaded with small-interfering RNA (siRNA) targeting epidermal growth factor receptor (EGFR) and bromodomain-containing protein 4 (BRD4) in triple-negative breast cancer (TNBC).	Disulfides	131-140	epidermal growth factor receptor	Mus musculus	222-254
34591491-1	2021	The study aims to investigate the in vivo distribution, antitumor effect, and safety of cell membrane-penetrating peptide-modified disulfide bond copolymer nanoparticles loaded with small-interfering RNA (siRNA) targeting epidermal growth factor receptor (EGFR) and bromodomain-containing protein 4 (BRD4) in triple-negative breast cancer (TNBC).	Disulfides	131-140	epidermal growth factor receptor	Mus musculus	256-260
34591491-1	2021	The study aims to investigate the in vivo distribution, antitumor effect, and safety of cell membrane-penetrating peptide-modified disulfide bond copolymer nanoparticles loaded with small-interfering RNA (siRNA) targeting epidermal growth factor receptor (EGFR) and bromodomain-containing protein 4 (BRD4) in triple-negative breast cancer (TNBC).	Disulfides	131-140	bromodomain containing 4	Mus musculus	266-298
34591491-1	2021	The study aims to investigate the in vivo distribution, antitumor effect, and safety of cell membrane-penetrating peptide-modified disulfide bond copolymer nanoparticles loaded with small-interfering RNA (siRNA) targeting epidermal growth factor receptor (EGFR) and bromodomain-containing protein 4 (BRD4) in triple-negative breast cancer (TNBC).	Disulfides	131-140	bromodomain containing 4	Mus musculus	300-304
34679128-4	2021	Initially, we boosted the expression of 17 candidate trimers by truncating gp41 and introducing a gp120-gp41 SOS disulfide to prevent gp120 shedding.	Disulfides	113-122	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	98-103
34679128-4	2021	Initially, we boosted the expression of 17 candidate trimers by truncating gp41 and introducing a gp120-gp41 SOS disulfide to prevent gp120 shedding.	Disulfides	113-122	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	134-139
34665595-2	2021	To design functional heme enzymes, we used myoglobin (Mb) as a model protein and introduced an artificial CXXC motif into the heme distal pocket by F46C and L49C mutations, which forms a de novo disulfide bond, as confirmed by the X-ray crystal structure.	Disulfides	195-204	myoglobin	Homo sapiens	43-52
34729312-4	2021	Herein, novel tumor microenvironments (TME)-activated metal-organic frameworks involving Fe & Cu ions bridged by disulfide bonds with PEGylation (FCSP MOFs) were developed, which would be degraded specifically under the redox TME, simultaneously achieving GSH-depletion induced GPX4 inactivation and releasing Fe ions to produce ROS via Fenton reaction, therefore causing ferroptosis.	Disulfides	113-122	glutathione peroxidase 4	Homo sapiens	278-282
34616733-1	2021	Augmenter of liver regeneration (ALR) is a critical multi-isoform protein with its longer isoform, located in the mitochondrial intermembrane space, being part of the mitochondrial disulfide relay system (DRS).	Disulfides	181-190	growth factor, augmenter of liver regeneration	Homo sapiens	0-31
34616733-1	2021	Augmenter of liver regeneration (ALR) is a critical multi-isoform protein with its longer isoform, located in the mitochondrial intermembrane space, being part of the mitochondrial disulfide relay system (DRS).	Disulfides	181-190	growth factor, augmenter of liver regeneration	Homo sapiens	33-36
34575960-11	2021	TRX can remove NO-like glutathione and break down the disulfide bridge.	Disulfides	54-63	thioredoxin	Homo sapiens	0-3
34339733-10	2021	Surprisingly, fibrils composed of compact tau disaggregate upon reduction, highlighting the importance of the intramolecular disulfide bond for fibril stability.	Disulfides	125-134	microtubule associated protein tau	Homo sapiens	42-45
34174476-5	2021	The mature CG42782, Met75C and Acp54A1 peptides each have a cyclic structure formed by a disulfide bond, which will reduce conformational freedom and enhance metabolic stability.	Disulfides	89-98	Accessory gland protein 54A1	Drosophila melanogaster	31-38
34341191-4	2021	Using fluorescence polarization, isothermal titration calorimetry and X-ray crystallography, it is shown that synthetic peptides containing either phosphorylated Thr869 or Ser542 can indeed interact with 14-3-3, with the latter capable of forming an interprotein disulfide bond with 14-3-3sigma: a hitherto unreported phenomenon.	Disulfides	263-272	stratifin	Homo sapiens	283-294
34449533-6	2021	ACPA reactivity to citrullinated alpha-enolase peptides was found to depend on peptide length and peptide conformation, favouring cyclic (disulfide bond) conformations for long peptides and linear peptides for truncated ones.	Disulfides	138-147	enolase 1	Homo sapiens	33-46
34098544-4	2021	In all of them, the native structure is stabilized by a disulfide bridge between the sulphur atoms of the cysteine residues 25 (at B strand) and 80 (at F strand), which has been considered fundamental in b2m fibrillogenesis.	Disulfides	56-65	beta-2-microglobulin	Homo sapiens	204-207
34098544-5	2021	Here, we use extensive Discrete Molecular Dynamics simulations of a full atomistic structure-based model to explore the role of this disulfide bridge as a modulator of the folding space of b2m.	Disulfides	133-142	beta-2-microglobulin	Homo sapiens	189-192
34203497-6	2021	Vimentin oxidation can induce disulfide crosslinking, implying the close proximity of Cys328 from neighboring dimers in certain vimentin conformations, supported by our computational models.	Disulfides	30-39	vimentin	Homo sapiens	0-8
34061528-0	2021	Selective, Modular Probes for Thioredoxins Enabled by Rational Tuning of a Unique Disulfide Structure Motif.	Disulfides	82-91	thioredoxin	Homo sapiens	30-42
34061528-8	2021	This design process delivered the first disulfide probes with excellent stability to monothiols yet high selectivity for the key redox-active protein effector, thioredoxin.	Disulfides	40-49	thioredoxin	Homo sapiens	160-171
34061528-9	2021	We anticipate that further applications of these novel disulfide triggers will deliver unique probes targeting cellular thioredoxins.	Disulfides	55-64	thioredoxin	Homo sapiens	120-132
35583206-4	2022	Upon accumulation in the tumor site, however, the micelles demonstrated tumor microenvironment (TME) triggered photoactive formed-PPA (a photosensitizer) and NLG919 (an indoleamine 2,3-dioxygenase (IDO) inhibitor) release because the amide bonds of PGA-Cys-PPA and the disulfide linkage of Cys were sensitive to pH and GSH, respectively.	Disulfides	269-278	indoleamine 2,3-dioxygenase 1	Homo sapiens	169-196
35583206-4	2022	Upon accumulation in the tumor site, however, the micelles demonstrated tumor microenvironment (TME) triggered photoactive formed-PPA (a photosensitizer) and NLG919 (an indoleamine 2,3-dioxygenase (IDO) inhibitor) release because the amide bonds of PGA-Cys-PPA and the disulfide linkage of Cys were sensitive to pH and GSH, respectively.	Disulfides	269-278	indoleamine 2,3-dioxygenase 1	Homo sapiens	198-201
35421616-0	2022	Disulfide-Mediated Elongation of Amyloid Fibrils of alpha-Synuclein For Use in Producing Self-Healing Hydrogel and Dye-Absorbing Aerogel.	Disulfides	0-9	synuclein alpha	Homo sapiens	52-67
35421616-3	2022	Here, we have demonstrated the full extension of AFs of alpha-synuclein (alphaS) by introducing a cysteine residue to its C-terminus which prevents the shear-induced fragmentation of AFs via site-directed disulfide bond formation on the exposed surface of AFs.	Disulfides	205-214	synuclein alpha	Homo sapiens	56-71
35421616-10	2022	In this study, we have demonstrated the full extension of alpha-synuclein amyloid fibrils by introducing a cysteine residue to its C-terminus by forming site-directed disulfide bonds on the exposed surface of amyloid fibrils for the first time.	Disulfides	167-176	synuclein alpha	Homo sapiens	58-73
35416493-3	2022	Defective transport of cystine into epithelial cells of renal tubules occurs because of mutations of the transport heterodimer, including protein b0,+AT (encoded by SLC7A9) and rBAT (encoded by SLC3A1) linked through a covalent disulfide bond.	Disulfides	228-237	solute carrier family 3 member 1	Rattus norvegicus	194-200
35613580-5	2022	We further demonstrate that Rad6 and its human homolog UBE2A are redox regulated by forming a reversible disulfide with the E1 ubiquitin-activating enzyme (Uba1).	Disulfides	105-114	ubiquitin like modifier activating enzyme 1	Homo sapiens	156-160
10880278-11	2000	In addition, bands of molecular mass 150 and 200 kD were present that appeared to be disulfide-bonded complexes of SPARC monomers.	Disulfides	85-94	secreted protein acidic and cysteine rich	Homo sapiens	115-120
10813841-0	2000	Disulfide bond plasticity in epidermal growth factor.	Disulfides	0-9	epidermal growth factor	Mus musculus	29-52
10813841-1	2000	Epidermal growth factor (EGF) has a (1-3,2-4,5-6) disulfide-bonding pattern.	Disulfides	50-59	epidermal growth factor	Mus musculus	0-23
10813841-1	2000	Epidermal growth factor (EGF) has a (1-3,2-4,5-6) disulfide-bonding pattern.	Disulfides	50-59	epidermal growth factor	Mus musculus	25-28
10813841-3	2000	Biological data from EGF and at least one EGF-like domain show that disulfide bond isomers have significant bioactivity and suggests that the EGF fold can accommodate alternate disulfide-bonding patterns.	Disulfides	68-77	epidermal growth factor	Mus musculus	21-24
10813841-3	2000	Biological data from EGF and at least one EGF-like domain show that disulfide bond isomers have significant bioactivity and suggests that the EGF fold can accommodate alternate disulfide-bonding patterns.	Disulfides	68-77	epidermal growth factor	Mus musculus	42-45
10813841-3	2000	Biological data from EGF and at least one EGF-like domain show that disulfide bond isomers have significant bioactivity and suggests that the EGF fold can accommodate alternate disulfide-bonding patterns.	Disulfides	68-77	epidermal growth factor	Mus musculus	42-45
10813841-3	2000	Biological data from EGF and at least one EGF-like domain show that disulfide bond isomers have significant bioactivity and suggests that the EGF fold can accommodate alternate disulfide-bonding patterns.	Disulfides	177-186	epidermal growth factor	Mus musculus	21-24
10813841-3	2000	Biological data from EGF and at least one EGF-like domain show that disulfide bond isomers have significant bioactivity and suggests that the EGF fold can accommodate alternate disulfide-bonding patterns.	Disulfides	177-186	epidermal growth factor	Mus musculus	42-45
10813841-3	2000	Biological data from EGF and at least one EGF-like domain show that disulfide bond isomers have significant bioactivity and suggests that the EGF fold can accommodate alternate disulfide-bonding patterns.	Disulfides	177-186	epidermal growth factor	Mus musculus	42-45
10813841-4	2000	The disulfide bonds in murine EGF were altered to seven different patterns and structures were calculated incorporating all the restraints from the highest resolution restraint set available (Tejero et al., 1996).	Disulfides	4-13	epidermal growth factor	Mus musculus	30-33
10813841-10	2000	These results suggest that the EGF backbone fold has the unique property of accommodating several different disulfide-bonding patterns.	Disulfides	108-117	epidermal growth factor	Mus musculus	31-34
10867016-12	2000	As the 10 cysteines of the three known FGF-BPs are positionally conserved, the disulfide bond pattern of bovine FGF-BP may be regarded as representative for the FGF-BP family.	Disulfides	79-88	fibroblast growth factor-binding protein 1	Bos taurus	39-45
10867016-12	2000	As the 10 cysteines of the three known FGF-BPs are positionally conserved, the disulfide bond pattern of bovine FGF-BP may be regarded as representative for the FGF-BP family.	Disulfides	79-88	fibroblast growth factor-binding protein 1	Bos taurus	112-118
15012197-1	2000	Thioredoxins, the ubiquitous small proteins with a redox active disulfide bridge, are important regulatory elements in plant metabolism.	Disulfides	64-73	thioredoxin	Homo sapiens	0-12
10847613-11	2000	These data suggest that the relative participation of the thioltransferase (glutaredoxin) and thioredoxin systems in overall cellular disulfide reduction is cell line specific.	Disulfides	134-143	thioredoxin	Homo sapiens	94-105
10834548-1	2000	PURPOSE: Platelet-derived growth factor basic 30-kD disulfide-bonded dimer of A and B chains (PDGF-AA, PDGF AB, PDGF-BB) and a cytokine, promoting wound healing by its mitogenicity for fibroblast and by stimulating the production of fibronectin and hyaluronic acid.	Disulfides	52-61	fibronectin 1	Rattus norvegicus	233-244
10806394-11	2000	These results indicate that galectin-1 promotes axonal regeneration only in the oxidized form containing three intramolecular disulfide bonds, not in the reduced form which exhibits lectin activity.	Disulfides	126-135	galectin 1	Homo sapiens	28-38
10793134-7	2000	Filament formation is associated with, and may be dependent on, disulfide bridge formation between the hnRNP proteins.	Disulfides	64-73	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	103-108
10938586-6	2000	The results obtained show that the 41 degrees C stress leads to formation of intermolecular disulfide bonds between apo-GR and associated heat shock proteins (Hsp90, Hsp70).	Disulfides	92-101	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
10734121-2	2000	The encoded protein, designated as Asc-1 (asc-type amino acid transporter 1), was found to be structurally related to recently identified mammalian amino acid transporters for the transport systems L, y(+)L, x(C)(-), and b(0,+), which are linked, via a disulfide bond, to the type II membrane glycoproteins, 4F2 heavy chain (4F2hc), or rBAT (related to b(0,+) amino acid transporter).	Disulfides	253-262	solute carrier family 3 member 2	Homo sapiens	308-323
10734121-2	2000	The encoded protein, designated as Asc-1 (asc-type amino acid transporter 1), was found to be structurally related to recently identified mammalian amino acid transporters for the transport systems L, y(+)L, x(C)(-), and b(0,+), which are linked, via a disulfide bond, to the type II membrane glycoproteins, 4F2 heavy chain (4F2hc), or rBAT (related to b(0,+) amino acid transporter).	Disulfides	253-262	solute carrier family 3 member 2	Homo sapiens	325-330
10734121-5	2000	The band shifted to 33 kDa in the reducing condition, confirming that Asc-1 and 4F2hc are linked via a disulfide bond.	Disulfides	103-112	solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2	Mus musculus	80-85
10669787-3	2000	Therefore, we examined the formation of a disulfide bond in the recombinant Shh-N and identified three kinds of disulfides with a combination of peptide mapping and NH(2)-terminal amino acid sequencing analysis.	Disulfides	42-51	sonic hedgehog	Mus musculus	76-79
10669787-3	2000	Therefore, we examined the formation of a disulfide bond in the recombinant Shh-N and identified three kinds of disulfides with a combination of peptide mapping and NH(2)-terminal amino acid sequencing analysis.	Disulfides	112-122	sonic hedgehog	Mus musculus	76-79
10669787-4	2000	Among them, one type of the Shh-N containing a disulfide bond of Cys-103/Cys-184 could be separated from the other Shh-Ns using reverse phase HPLC and had no activity of alkaline phosphatase induction in C3H10T1/2 cells.	Disulfides	47-56	sonic hedgehog	Mus musculus	28-31
10669787-7	2000	These results suggested that Shh-N was synthesized as an active form whose three cysteine residues did not form disulfide and inactivated finally by forming a disulfide bond between Cys-103 and Cys-184.	Disulfides	112-121	sonic hedgehog	Mus musculus	29-32
10669787-7	2000	These results suggested that Shh-N was synthesized as an active form whose three cysteine residues did not form disulfide and inactivated finally by forming a disulfide bond between Cys-103 and Cys-184.	Disulfides	159-168	sonic hedgehog	Mus musculus	29-32
10636927-1	2000	Formation of disulfide-cross-linked multimers containing fibrillin-1.	Disulfides	13-22	fibrillin 1	Gallus gallus	57-68
10636927-4	2000	Sequential extractions and pulse-chase labeling of organ cultures of embryonic chick aortae revealed rapid formation of disulfide-cross-linked aggregates containing fibrillin-1.	Disulfides	120-129	fibrillin 1	Gallus gallus	165-176
10636927-8	2000	One cysteine residue (Cys(204)) in the first hybrid domain of fibrillin-1 was found to occur as a free thiol and is therefore a good candidate for intermolecular disulfide bonding in initial steps of the assembly process.	Disulfides	162-171	fibrillin 1	Gallus gallus	62-73
10666628-1	2000	Human epidermal growth factor (hEGF), a 6.2 kDa protein of 53 amino acids with three internal disulfide bridges, has been crystallized by the hanging-drop method.	Disulfides	94-103	epidermal growth factor	Homo sapiens	6-29
10666628-1	2000	Human epidermal growth factor (hEGF), a 6.2 kDa protein of 53 amino acids with three internal disulfide bridges, has been crystallized by the hanging-drop method.	Disulfides	94-103	epidermal growth factor	Homo sapiens	31-35
11213488-3	2000	We found that small proportions of c-Ret and Ret-MEN2B and a large proportion of MEN2A were dimerized due to disulfide bonds and that high kinase activity resided in these fractions.	Disulfides	109-118	ret proto-oncogene	Homo sapiens	45-48
11213488-3	2000	We found that small proportions of c-Ret and Ret-MEN2B and a large proportion of MEN2A were dimerized due to disulfide bonds and that high kinase activity resided in these fractions.	Disulfides	109-118	ret proto-oncogene	Homo sapiens	49-54
11213488-3	2000	We found that small proportions of c-Ret and Ret-MEN2B and a large proportion of MEN2A were dimerized due to disulfide bonds and that high kinase activity resided in these fractions.	Disulfides	109-118	ret proto-oncogene	Homo sapiens	81-86
11213488-4	2000	The UV-induced activation of c-Ret and superactivation of Ret-MEN2A and Ret-MEN2B were then shown to be closely associated with promotion of the disulfide bond-mediated dimerization of the Ret proteins.	Disulfides	145-154	ret proto-oncogene	Homo sapiens	31-34
11213488-4	2000	The UV-induced activation of c-Ret and superactivation of Ret-MEN2A and Ret-MEN2B were then shown to be closely associated with promotion of the disulfide bond-mediated dimerization of the Ret proteins.	Disulfides	145-154	ret proto-oncogene	Homo sapiens	58-61
11213488-4	2000	The UV-induced activation of c-Ret and superactivation of Ret-MEN2A and Ret-MEN2B were then shown to be closely associated with promotion of the disulfide bond-mediated dimerization of the Ret proteins.	Disulfides	145-154	ret proto-oncogene	Homo sapiens	62-67
11213488-4	2000	The UV-induced activation of c-Ret and superactivation of Ret-MEN2A and Ret-MEN2B were then shown to be closely associated with promotion of the disulfide bond-mediated dimerization of the Ret proteins.	Disulfides	145-154	ret proto-oncogene	Homo sapiens	58-61
11213488-4	2000	The UV-induced activation of c-Ret and superactivation of Ret-MEN2A and Ret-MEN2B were then shown to be closely associated with promotion of the disulfide bond-mediated dimerization of the Ret proteins.	Disulfides	145-154	ret proto-oncogene	Homo sapiens	76-81
11213488-4	2000	The UV-induced activation of c-Ret and superactivation of Ret-MEN2A and Ret-MEN2B were then shown to be closely associated with promotion of the disulfide bond-mediated dimerization of the Ret proteins.	Disulfides	145-154	ret proto-oncogene	Homo sapiens	58-61
10662484-6	2000	We now report the stable, high-level expression of soluble, disulfide-bonded human uteroglobin without antibiotic selection.	Disulfides	60-69	secretoglobin family 1A member 1	Homo sapiens	83-94
10623724-5	2000	To try to develop recombinant proteins that are better antigenic mimics of the native envelope glycoprotein complex, we have introduced a disulfide bond between the C-terminal region of gp120 and the immunodominant segment of the gp41 ectodomain.	Disulfides	138-147	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	186-191
10623724-7	2000	The association of gp120 with gp41 is now stabilized by the supplementary intermolecular disulfide bond, which forms with approximately 50% efficiency.	Disulfides	89-98	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	19-24
10637293-4	2000	Before UV irradiation, small percentages of c-Ret (3-4%) and Ret-MEN2B (1-2%) and large percentages of Ret-MEN2A (30-40%) were dimerized through disulfide bonds.	Disulfides	145-154	ret proto-oncogene	Homo sapiens	107-112
10637293-5	2000	These dimerized Ret proteins were preferentially autophosphorylated, suggesting a close relation between up-regulated kinase activity and disulfide bond-mediated dimerization of Ret proteins.	Disulfides	138-147	ret proto-oncogene	Homo sapiens	16-19
10637293-5	2000	These dimerized Ret proteins were preferentially autophosphorylated, suggesting a close relation between up-regulated kinase activity and disulfide bond-mediated dimerization of Ret proteins.	Disulfides	138-147	ret proto-oncogene	Homo sapiens	178-181
10611489-5	1999	The disulfide linkages were identical in the protein obtained by periplasmic expression in Escherichia coli and in the native BmPBP.	Disulfides	4-13	pheromone-binding protein	Bombyx mori	126-131
10593884-6	1999	This suggests that, during the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.	Disulfides	67-76	steroid sulfatase	Homo sapiens	48-52
10593884-6	1999	This suggests that, during the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase.	Disulfides	67-76	steroid sulfatase	Homo sapiens	148-152
10578068-3	1999	The complete amino acid sequence of p15 was determined and it was shown to be a hydrophilic protein composed of 118 amino acid residues with two intramolecular disulfide bridges.	Disulfides	160-169	cyclin-dependent kinase inhibitor 2B	Rattus norvegicus	36-39
10549279-6	1999	Further, PDI1 is required for the net formation of disulfide bonds in newly synthesized CPY, indicating that PDI functions as an oxidase in vivo.	Disulfides	51-60	peptidyl arginine deiminase 1	Homo sapiens	9-13
10504260-5	1999	Disulfide bond 6 resulted in enhanced G(T) activation but abolished phosphorylation by RK, suggesting the structure recognized by G(T) was stabilized in this mutant by cross-linking of the C-terminus to the cytoplasmic end of helix VI.	Disulfides	0-9	G protein-coupled receptor kinase 1	Homo sapiens	87-89
10391944-6	1999	Biochemical analysis indicated that Ig-Hepta is a highly glycosylated protein and exists as a disulfide-linked dimer.	Disulfides	94-103	adhesion G protein-coupled receptor F5	Rattus norvegicus	36-44
10382764-1	1999	Interleukin-12 (IL-12) is a heterodimeric cytokine composed of two disulfide-bonded subunits, p35 and p40, which has important regulatory effects on T cells and natural killer (NK) cells.	Disulfides	67-76	interleukin 12a	Mus musculus	94-97
10329650-0	1999	The N-terminal disulfide linkages of human insulin-like growth factor-binding protein-6 (hIGFBP-6) and hIGFBP-1 are different as determined by mass spectrometry.	Disulfides	15-24	insulin like growth factor binding protein 1	Homo sapiens	103-111
10329650-5	1999	Numbering IGFBP-6 cysteines sequentially from the N terminus, the first three disulfide linkages are Cys1-Cys2, Cys3-Cys4, and Cys5-Cys6.	Disulfides	78-87	cystin 1	Homo sapiens	101-105
10329650-8	1999	Disulfide linkages of IGFBP-1 were partially determined and show that Cys1 is not linked to Cys2 and Cys3 is not linked to Cys4.	Disulfides	0-9	insulin like growth factor binding protein 1	Homo sapiens	22-29
10329650-8	1999	Disulfide linkages of IGFBP-1 were partially determined and show that Cys1 is not linked to Cys2 and Cys3 is not linked to Cys4.	Disulfides	0-9	cystin 1	Homo sapiens	70-74
10329650-9	1999	Analogous with IGFBP-3, IGFBP-5, and IGFBP-6, Cys9-Cys11 and Cys10-Cys12 of IGFBP-1 are also disulfide-linked.	Disulfides	93-102	insulin like growth factor binding protein 3	Homo sapiens	15-22
10329650-9	1999	Analogous with IGFBP-3, IGFBP-5, and IGFBP-6, Cys9-Cys11 and Cys10-Cys12 of IGFBP-1 are also disulfide-linked.	Disulfides	93-102	insulin like growth factor binding protein 1	Homo sapiens	76-83
10350608-2	1999	We have shown that p70 exists predominantly as p45 and p40 fragments which are linked by disulfide bonds.	Disulfides	89-98	septin 3	Rattus norvegicus	55-58
10187802-3	1999	The large interaction interface in the TIMP-1.MMP-3 complex includes a contiguous region of TIMP-1 around the disulfide bond between Cys1 and Cys70 that inserts into the active site of MMP-3.	Disulfides	110-119	cystin 1	Homo sapiens	133-137
10098518-1	1999	Guanylin and uroguanylin are small peptides containing two disulfide bonds that activate membrane guanylate cyclase-receptors in the intestine, kidney and other epithelia.	Disulfides	59-68	guanylate cyclase activator 2A	Homo sapiens	0-8
10383197-12	1999	Structural comparison of the PDI b domain with thioredoxin and PDI a reveals several features important for thiol-disulfide exchange activity.	Disulfides	114-123	thioredoxin	Homo sapiens	47-58
10100850-2	1999	So far, it has been found exclusively in plasma, covalently linked to C8alpha by disulfide bridging.	Disulfides	81-90	complement C8 alpha chain	Homo sapiens	70-77
10049754-4	1999	The D631Y mutation activated Ret by inducing its disulfide-linked dimerization in the transfectant as observed for multiple endocrine neoplasia (MEN) 2A mutations at cysteine 609, 611, 618, 620, 630, or 634.	Disulfides	49-58	ret proto-oncogene	Homo sapiens	29-32
10049754-4	1999	The D631Y mutation activated Ret by inducing its disulfide-linked dimerization in the transfectant as observed for multiple endocrine neoplasia (MEN) 2A mutations at cysteine 609, 611, 618, 620, 630, or 634.	Disulfides	49-58	ret proto-oncogene	Homo sapiens	124-152
10049754-5	1999	Further mutation analysis suggested that cysteine 630 or 634 could be involved in the disulfide-linked Ret dimerization induced by the D631Y mutation.	Disulfides	86-95	ret proto-oncogene	Homo sapiens	103-106
10195449-4	1999	We previously confirmed that the synthetic EGF-like peptides SDGF(38-80) and AR(44-84), corresponding to the EGF-like domain of mouse SDGF and human AR, respectively, formed similar disulfide bond patterns to that of EGF.	Disulfides	182-191	epidermal growth factor	Mus musculus	43-46
10024465-9	1999	Bovine alpha-lactalbumin, 14 kDa with four disulfide bonds, required complete renaturation prior to the removal of a reducing agent.	Disulfides	43-52	lactalbumin alpha	Bos taurus	7-24
9878049-2	1999	We recently have identified the vertebrate proteins which mediate Na+-independent exchange of large neutral amino acids corresponding to transport system L. This transporter consists of a novel amino acid permease-related protein (LAT1 or AmAT-L-lc) which for surface expression and function requires formation of disulfide-linked heterodimers with the glycosylated heavy chain of the h4F2/CD98 surface antigen.	Disulfides	314-323	solute carrier family 7 member 5	Homo sapiens	231-235
9878049-2	1999	We recently have identified the vertebrate proteins which mediate Na+-independent exchange of large neutral amino acids corresponding to transport system L. This transporter consists of a novel amino acid permease-related protein (LAT1 or AmAT-L-lc) which for surface expression and function requires formation of disulfide-linked heterodimers with the glycosylated heavy chain of the h4F2/CD98 surface antigen.	Disulfides	314-323	H4 clustered histone 14	Homo sapiens	385-389
9878049-2	1999	We recently have identified the vertebrate proteins which mediate Na+-independent exchange of large neutral amino acids corresponding to transport system L. This transporter consists of a novel amino acid permease-related protein (LAT1 or AmAT-L-lc) which for surface expression and function requires formation of disulfide-linked heterodimers with the glycosylated heavy chain of the h4F2/CD98 surface antigen.	Disulfides	314-323	solute carrier family 3 member 2	Homo sapiens	390-394
9886847-1	1999	Human thioredoxin (hTrx) is a cellular redox-active protein that catalyzes dithiol/disulfide exchange reactions, thus controlling multiple biological functions, including cell growth-promoting activity.	Disulfides	83-92	thioredoxin	Homo sapiens	6-17
9886847-1	1999	Human thioredoxin (hTrx) is a cellular redox-active protein that catalyzes dithiol/disulfide exchange reactions, thus controlling multiple biological functions, including cell growth-promoting activity.	Disulfides	83-92	thioredoxin	Homo sapiens	19-23
10210188-1	1999	In addition to the Cys-Xaa-Xaa-Cys motif at position 30-33, DsbA, the essential catalyst for disulfide bond formation in the bacterial periplasm shares with other oxidoreductases of the thioredoxin family a cis-proline in proximity of the active site residues.	Disulfides	93-102	thioredoxin	Homo sapiens	186-197
9857064-3	1998	The mutant-type leptin lacking a C-terminal disulfide bond reduced food intake at doses of more than 15 pmol/mouse, which was as effective as the wild-type leptin.	Disulfides	44-53	leptin	Mus musculus	16-22
9879991-7	1998	We now report that each mutation induces a constitutive catalytic activity due to the aberrant disulfide homodimerization of RET.	Disulfides	95-104	ret proto-oncogene	Homo sapiens	125-128
9792673-3	1998	Peptides derived from SPARC domain IV, which contains a disulfide-bonded EF-hand sequence and binds to endothelial cells, mimicked the effect of native SPARC.	Disulfides	56-65	secreted protein acidic and cysteine rich	Homo sapiens	22-27
9792673-3	1998	Peptides derived from SPARC domain IV, which contains a disulfide-bonded EF-hand sequence and binds to endothelial cells, mimicked the effect of native SPARC.	Disulfides	56-65	secreted protein acidic and cysteine rich	Homo sapiens	152-157
9844746-0	1998	Occurrence of bovine spleen CD38/NAD+glycohydrolase disulfide-linked dimers.	Disulfides	52-61	CD38 molecule	Bos taurus	28-32
9786864-6	1998	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.	Disulfides	15-24	leptin receptor	Homo sapiens	46-61
9685721-4	1998	The binding free energy of the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+ is close to that of the molten globule state of disulfide-intact alpha-lactalbumin.	Disulfides	35-44	lactalbumin alpha	Bos taurus	53-70
9685721-4	1998	The binding free energy of the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+ is close to that of the molten globule state of disulfide-intact alpha-lactalbumin.	Disulfides	35-44	lactalbumin alpha	Bos taurus	160-177
9685721-4	1998	The binding free energy of the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+ is close to that of the molten globule state of disulfide-intact alpha-lactalbumin.	Disulfides	143-152	lactalbumin alpha	Bos taurus	53-70
9685721-4	1998	The binding free energy of the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+ is close to that of the molten globule state of disulfide-intact alpha-lactalbumin.	Disulfides	143-152	lactalbumin alpha	Bos taurus	160-177
9685721-6	1998	The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL.	Disulfides	10-19	lactalbumin alpha	Bos taurus	54-71
9685721-6	1998	The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL.	Disulfides	36-45	lactalbumin alpha	Bos taurus	54-71
9685721-6	1998	The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL.	Disulfides	36-45	lactalbumin alpha	Bos taurus	171-188
9685721-6	1998	The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL.	Disulfides	36-45	lactalbumin alpha	Bos taurus	54-71
9685721-6	1998	The fully disulfide-reduced and two-disulfide-reduced alpha-lactalbumins were found to bind more strongly with GroEL in the absence of Ca2+ than the two-disulfide-reduced alpha-lactalbumin in the presence of Ca2+, thus indicating that the unfolding of the beta-domain of alpha-lactalbumin leads to stronger interaction with GroEL.	Disulfides	36-45	lactalbumin alpha	Bos taurus	171-188
9688530-4	1998	In addition, we have found that cyclization of the first loop peptide by disulfide linkage and blocking the C-terminus of the peptide by amidation increases the activity of this peptide to block MCP-1 binding and chemotaxis.	Disulfides	73-82	C-C motif chemokine ligand 2	Homo sapiens	195-200
9632693-3	1998	Here, we provide evidence that this abnormal processing results from defective initial folding of the secreted FAF gelsolin due to the lack of the Cys188-Cys201 disulfide bond, normally formed next to the FAF mutation site.	Disulfides	161-170	gelsolin	Homo sapiens	115-123
9603915-0	1998	Calnexin associates with monomeric and oligomeric (disulfide-linked) CD3delta proteins in murine T lymphocytes.	Disulfides	51-60	calnexin	Mus musculus	0-8
9603915-1	1998	The antigen-binding receptor expressed on most T lymphocytes consists of disulfide-linked clonotypic alphabeta heterodimers noncovalently associated with monomeric CD3gamma,delta,epsilon proteins and disulfide-linked zeta zeta homodimers, collectively referred to as the T cell antigen receptor (TCR) complex.	Disulfides	73-82	T cell receptor alpha variable 6-3	Mus musculus	271-294
9603915-1	1998	The antigen-binding receptor expressed on most T lymphocytes consists of disulfide-linked clonotypic alphabeta heterodimers noncovalently associated with monomeric CD3gamma,delta,epsilon proteins and disulfide-linked zeta zeta homodimers, collectively referred to as the T cell antigen receptor (TCR) complex.	Disulfides	73-82	T cell receptor alpha variable 6-3	Mus musculus	296-299
9603915-2	1998	Here, we examined and compared the disulfide linkage status of newly synthesized TCR proteins in murine CD4(+)CD8(+) thymocytes and splenic T cells.	Disulfides	35-44	T cell receptor alpha variable 6-3	Mus musculus	81-84
9603915-7	1998	Finally, these studies show that calnexin associates with both monomeric and disulfide-linked CD3delta proteins in murine T cells.	Disulfides	77-86	calnexin	Mus musculus	33-41
9603915-8	1998	The data in the current report demonstrate that CD3delta proteins exist as both monomeric and disulfide-linked molecules in murine T cells that differentially associate with partner TCR chains in CD4(+)CD8(+) thymocytes and splenic T cells.	Disulfides	94-103	T cell receptor alpha variable 6-3	Mus musculus	182-185
9604936-4	1998	In some crystals, the catalytic Cys-430 forms a disulfide bond with the invariant Cys-384, suggesting that Cdc25 may be self-inhibited during oxidative stress.	Disulfides	48-57	cell division cycle 25C	Homo sapiens	107-112
9605422-5	1998	The disulfides caused reversible thioalkylation of hTrx at the redox catalytic site as shown by the fact that there was no thioalkylation of a mutant hTrx where both the catalytic site Cys32 and Cys35 residues were replaced by Ser.	Disulfides	4-14	thioredoxin	Homo sapiens	51-55
9605422-6	1998	In addition, the disulfides caused a slower irreversible inactivation of hTrx as a substrate for reduction by TR, with half-lives for III-2 of 30 min, for IV-2 of 4 hr, and for IX-2 (t-butyl 2-mercaptoimidazolyl disulfide) of 24 hr.	Disulfides	17-27	thioredoxin	Homo sapiens	73-77
9605422-7	1998	This irreversible inactivation of hTrx occurred at concentrations of the disulfides an order of magnitude below those that inhibited TR, and involved the Cys73 of hTrx, which is outside the conserved redox catalytic site, as shown by the resistance to inactivation of a mutant hTrx where Cys73 was replaced by Ser.	Disulfides	73-83	thioredoxin	Homo sapiens	34-38
9605422-8	1998	Electrophoretic and mass spectral analyses of the products of the reaction between the disulfides and hTrx show that modification of 1-3 Cys residues of the protein occurred in a concentration-dependent fashion.	Disulfides	87-97	thioredoxin	Homo sapiens	102-106
9521781-1	1998	Thioredoxin reduction in plant chloroplasts is catalyzed by a unique class of disulfide reductases which use a one-electron donor, [Fe2S2]2+,+ ferredoxin, and has an active site involving a disulfide in close proximity to a [Fe4S4]2+ cluster.	Disulfides	78-87	thioredoxin	Homo sapiens	0-11
9521781-2	1998	In this study, spinach ferredoxin:thioredoxin reductase (FTR) reduced with stoichiometric amounts of reduced benzyl viologen or frozen under turnover conditions in the presence of thioredoxin is shown to exhibit a slowly relaxing S = 1/2 resonance (g = 2.11, 2.00, 1.98) identical to that of a modified form of the enzyme in which one of the cysteines of the active-site disulfide is alkylated with N-ethylmaleimide (NEM-FTR).	Disulfides	371-380	thioredoxin	Homo sapiens	34-45
9521781-2	1998	In this study, spinach ferredoxin:thioredoxin reductase (FTR) reduced with stoichiometric amounts of reduced benzyl viologen or frozen under turnover conditions in the presence of thioredoxin is shown to exhibit a slowly relaxing S = 1/2 resonance (g = 2.11, 2.00, 1.98) identical to that of a modified form of the enzyme in which one of the cysteines of the active-site disulfide is alkylated with N-ethylmaleimide (NEM-FTR).	Disulfides	371-380	thioredoxin	Homo sapiens	180-191
9521781-8	1998	The catalytic mechanism involves novel S-based cluster chemistry to facilitate electron transfer to the active-site disulfide resulting in covalent attachment of the electron-transfer cysteine and generation of the free interchange cysteine that is required for the thiol-disulfide interchange reaction with thioredoxin.	Disulfides	116-125	thioredoxin	Homo sapiens	308-319
9521781-8	1998	The catalytic mechanism involves novel S-based cluster chemistry to facilitate electron transfer to the active-site disulfide resulting in covalent attachment of the electron-transfer cysteine and generation of the free interchange cysteine that is required for the thiol-disulfide interchange reaction with thioredoxin.	Disulfides	272-281	thioredoxin	Homo sapiens	308-319
9521722-2	1998	In a crystal, seminal RNase is a homodimer joined by two "antiparallel" intersubunit disulfide bonds between Cys-31 from one subunit and Cys-32" from the other and having composite active sites arising from the "swap" of residues 1-20 from each subunit.	Disulfides	85-94	seminal ribonuclease	Bos taurus	14-27
9502784-8	1998	Finally, the C609W HSCR mutation exerts a dual effect on RET since it leads to a decrease of the receptor at the cell surface and converted RET51 into a constitutively activated kinase due to the formation of disulfide-linked homodimers.	Disulfides	209-218	ret proto-oncogene	Homo sapiens	57-60
9502784-8	1998	Finally, the C609W HSCR mutation exerts a dual effect on RET since it leads to a decrease of the receptor at the cell surface and converted RET51 into a constitutively activated kinase due to the formation of disulfide-linked homodimers.	Disulfides	209-218	ret proto-oncogene	Homo sapiens	140-145
9468514-8	1998	Sequence analysis revealed that ps20 protein contains a WAP-type "four-disulfide core" motif and is a novel member of the WAP signature protein family composed primarily of secreted serine protease inhibitors.	Disulfides	71-80	WAP four-disulfide core domain 1	Rattus norvegicus	32-36
9451015-6	1998	Each of the precursors of MUC2, MUC5AC, MUC5B, and MUC6 formed a single species of disulfide-linked homo-oligomer within 1 h after pulse labeling.	Disulfides	83-92	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	32-38
9842742-1	1998	Guanylin 99-115 is a small human peptide hormone with two disulfide bonds.	Disulfides	58-67	guanylate cyclase activator 2A	Homo sapiens	0-8
9450496-0	1997	Repression of c-myc gene expression by the thiol and disulfide forms of the cytoprotector amifostine.	Disulfides	53-62	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	14-19
9450496-9	1997	An exposure of cells to 40 microM of the disulfide form of amifostine was the most effective in repressing c-myc, i.e. 27% of control level.	Disulfides	41-50	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	107-112
9450496-10	1997	A concentration of 4 mM of the disulfide form reduced gene expression to 45% of the control level, while the thiol form was less effective, with 4 mM and 40 microM concentrations reducing c-myc gene expression to 65% and 46% of control levels, respectively.	Disulfides	31-40	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	188-193
11596194-2	1997	The fully-protected peptide-resin was cleaved with anhydrous HF.--SH of Cys in [Cys5,9] SP(4-11) was protected with Acm, then deprotected through Iodine oxidation method, the disulfide bridge cyclization was formed subsequently.	Disulfides	175-184	tachykinin 1	Mus musculus	88-90
9348303-4	1997	In this report, we demonstrate for the first time that pT alpha-containing pre-TCR complexes are expressed at low levels on the surface of primary thymocytes and that these pre-TCR complexes comprise a disulfide-linked pT alpha-TCR-beta heterodimer associated not only with CD3-gamma and -epsilon, as previously reported, but also with zeta and delta.	Disulfides	202-211	T cell receptor alpha variable 6-3	Mus musculus	79-82
9348303-4	1997	In this report, we demonstrate for the first time that pT alpha-containing pre-TCR complexes are expressed at low levels on the surface of primary thymocytes and that these pre-TCR complexes comprise a disulfide-linked pT alpha-TCR-beta heterodimer associated not only with CD3-gamma and -epsilon, as previously reported, but also with zeta and delta.	Disulfides	202-211	T cell receptor alpha variable 6-3	Mus musculus	177-180
9404661-4	1997	The second method generated a disulfide-linked FVS191cys-dgRTA from a FVS191cys, the FVS191 with an additional C-terminal cysteine, and a deglycosylated RTA (dgRTA).	Disulfides	30-39	MAS related GPR family member F	Homo sapiens	59-62
9336411-3	1997	The aims of this study were to examine the expression of different disulfide-bonded isoforms of TSP1 in inflammatory environments in which elastase and cathepsin G are present in variable amounts, and to determine the relationship between these proteinases and their potential inhibitor.	Disulfides	67-76	cathepsin G	Homo sapiens	152-163
9403340-2	1997	In the present study, we examined the immunosuppressive properties of a derivative of sLFA-3, a dimeric form of the first domain (D1) of sLFA-3, named sD1Hcys dimer which was made by oxidative binding of the two D1 molecules through disulfide bonds formed between the SH side chains of a cysteine which was added to the C-terminal of the D1 domain.	Disulfides	233-242	CUP2Q35	Homo sapiens	151-154
9278433-3	1997	CAP11 is a homodimer of G1LRKKFRKTRKRIQKLGRKIGKTGRKVWKAWREYGQIPYPCRI43 joined with one disulfide bond.	Disulfides	87-96	cathelicidin antimicrobial peptide	Cavia porcellus	0-5
9278443-6	1997	Reduction and alkylation of disulfide bonds in MAGP-1 did not destroy its type VI collagen-binding properties, indicating that the binding site was likely to be in the cysteine-free, N-terminal domain of MAGP-1.	Disulfides	28-37	microfibril associated protein 2	Homo sapiens	47-53
9300824-3	1997	Like normal HB-EGF, SF HB-EGF contains the signal peptide, the propeptide, the heparin-binding domain and the first two conservative disulfide loops of the EGF unit.	Disulfides	133-142	heparin binding EGF like growth factor	Homo sapiens	23-29
9181583-5	1997	Overproduction of the dnaKJ operon in trxB cells decreased the formation of disulfide-bonded SPARC multimers in the aggregated material but not in its soluble counterpart.	Disulfides	76-85	secreted protein acidic and cysteine rich	Homo sapiens	93-98
9210480-0	1997	Mutational analysis of extracellular cysteine residues of rat secretin receptor shows that disulfide bridges are essential for receptor function.	Disulfides	91-100	secretin receptor	Rattus norvegicus	62-79
9171290-4	1997	The same spatial distribution of disulfide bridges can be observed in both domains of the secretory leukocyte protease inhibitor (SLPI), another elastase inhibitor.	Disulfides	33-42	antileukoproteinase	Bos taurus	90-128
9171290-4	1997	The same spatial distribution of disulfide bridges can be observed in both domains of the secretory leukocyte protease inhibitor (SLPI), another elastase inhibitor.	Disulfides	33-42	antileukoproteinase	Bos taurus	130-134
9166907-4	1997	Helix lengths and disulfide pattern are in agreement with leptin as a member of the short-helix cytokine family.	Disulfides	18-27	leptin	Mus musculus	58-64
9109671-11	1997	Further, binding affinities to the IGF binding protein 1 and a soluble IGF type I receptor, respectively, were severely lowered in both disulfide mutant proteins compared to the native IGF-I molecule.	Disulfides	136-145	insulin like growth factor binding protein 1	Homo sapiens	35-56
9109401-3	1997	Here we show that treatment of erythrocytes with the thiol-oxidizing agent diamide leads to the formation of PTP disulfides (PTP-band 3 mixed disulfides) and inhibition of dephosphorylation, allowing the accumulation of band 3 phosphotyrosine.	Disulfides	113-123	cell division cycle 25C	Homo sapiens	109-112
9109401-3	1997	Here we show that treatment of erythrocytes with the thiol-oxidizing agent diamide leads to the formation of PTP disulfides (PTP-band 3 mixed disulfides) and inhibition of dephosphorylation, allowing the accumulation of band 3 phosphotyrosine.	Disulfides	113-123	cell division cycle 25C	Homo sapiens	125-128
9109401-3	1997	Here we show that treatment of erythrocytes with the thiol-oxidizing agent diamide leads to the formation of PTP disulfides (PTP-band 3 mixed disulfides) and inhibition of dephosphorylation, allowing the accumulation of band 3 phosphotyrosine.	Disulfides	142-152	cell division cycle 25C	Homo sapiens	109-112
9122230-3	1997	The Cys-282 --&gt; Tyr mutation in HH patients would be expected to disrupt the function of the HLA-H gene product by altering a critical disulfide bridge.	Disulfides	138-147	major histocompatibility complex, class I, H (pseudogene)	Homo sapiens	96-101
9125187-1	1997	In higher plants, light enhances the activity of chloroplast fructose-1,6-bisphosphatase via a cascade of thiol/disulfide exchanges.	Disulfides	112-121	fructose-1,6-bisphosphatase, cytosolic	Brassica napus	61-88
9062118-8	1997	The cysteine-specific spin-label, methanethiosulfonate spin-label (MTSSL), was attached to yeast iso-1-cytochrome c at the single naturally occurring cysteine102, and the emphasis for this work was on this disulfide-attached spin-labeled prototype.	Disulfides	206-215	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	97-102
9037018-5	1997	Western blot analysis indicated that the native form of Drosophila PTTH was a single 66-kDa polypeptide with N-linked carbohydrate chains and intrachain disulfide bonds.	Disulfides	153-162	Prothoracicotropic hormone	Drosophila melanogaster	67-71
9012462-6	1997	We have reported previously that mutations of Cys-634 constitutively activate the RET transforming potential by causing a disulfide bridge-mediated homodimerization.	Disulfides	122-131	ret proto-oncogene	Homo sapiens	82-85
9119370-5	1997	Since the bacterially expressed protein of nucleoredoxin showed oxidoreductase activity of the insulin disulfide bonds with kinetics similar to that of thioredoxin, it may be a redox regulator of the nuclear proteins, such as transcription factors.	Disulfides	103-112	thioredoxin	Homo sapiens	152-163
9006964-4	1997	In the absence of Ig H chain expression, these export-incompetent Ig L chains remain bound to BiP as partially folded monomers with only one of the two internal disulfide bonds being formed.	Disulfides	161-170	immunoglobulin lambda locus	Homo sapiens	66-70
9003812-0	1997	Functional consequences of disulfide bond formation in gelsolin.	Disulfides	27-36	gelsolin	Homo sapiens	55-63
9003812-1	1997	Gelsolin is an actin monomer binding and filament severing protein synthesized in plasma and cytoplasmic forms differing by an N-terminal amino acid extension and a disulfide bond between Cys-188 and Cys-201.	Disulfides	165-174	gelsolin	Homo sapiens	0-8
9003812-3	1997	The results indicate that the disulfide bond in domain 2 of gelsolin influences the transmission of information from C-terminal regulatory sites to functional sites in the N-terminus.	Disulfides	30-39	gelsolin	Homo sapiens	60-68
9000515-3	1997	Meanwhile, in the cells producing delta beta1S gamma1 dimer, the level of endogenous alpha1 beta1 gamma1 was reduced but the level of monomeric alpha1 was increased, suggesting that alpha1 was recruited to trimer formation with the delta beta1S gamma1 dimer without disulfide-bonding.	Disulfides	266-275	hemoglobin, beta adult major chain	Mus musculus	40-45
9143692-4	1997	TRX is a small multifunctional protein that has a redox-active disulfide/dithiol within the conserved active site sequence: Cys-Gly-Pro-Cys.	Disulfides	63-72	thioredoxin	Homo sapiens	0-3
9143695-1	1997	The pre-T cell receptor (pre-TCR) that minimally consists of the TCR beta chain and the disulfide-linked pre-T cell receptor alpha (pT alpha) chain in association with signal-transducing CD3 molecules rescues from programmed cell death cells with productive TCR beta rearrangements.	Disulfides	88-97	T cell receptor alpha variable 6-3	Mus musculus	29-32
8943311-14	1996	Deacylation of affinity-purified ASGP-Rs with hydroxylamine results in the spontaneous formation of dimers through reversible disulfide bonds, indicating that deacylation concomitantly generates free thiol groups.	Disulfides	126-135	mucin 4, cell surface associated	Rattus norvegicus	33-37
8986137-6	1996	We have recently shown by X-ray crystallography that Trx forms a dimer that is stabilized by an intermolecular Cys73-Cys73 disulfide bond.	Disulfides	123-132	thioredoxin	Homo sapiens	53-56
8997498-0	1996	Disulfide bonds and free SH-group in pig kidney aminopeptidase P.	Disulfides	0-9	X-prolyl aminopeptidase 2	Sus scrofa	48-64
8920951-2	1996	The seven cysteine residues in CSF-1(256) form three intrachain disulfide bonds (Cys7-Cys90, Cys48-Cys139, and Cys 102-Cys146), and one interchain disulfide bond (Cys31-Cys31).	Disulfides	64-73	colony stimulating factor 1	Homo sapiens	31-36
8920951-2	1996	The seven cysteine residues in CSF-1(256) form three intrachain disulfide bonds (Cys7-Cys90, Cys48-Cys139, and Cys 102-Cys146), and one interchain disulfide bond (Cys31-Cys31).	Disulfides	147-156	colony stimulating factor 1	Homo sapiens	31-36
8920951-7	1996	Furthermore, disruption of the interchain disulfide bond led to efficient cell surface expression of monomeric CSF-1.	Disulfides	42-51	colony stimulating factor 1	Homo sapiens	111-116
8892940-4	1996	Epitope mapping revealed eight continuous epitopes accessible on the surface of a predicted structural model for the monomeric and the disulfide-linked dimeric forms of p23.	Disulfides	135-144	RAS related	Homo sapiens	169-172
8934442-4	1996	The consequences of the apo Cys6-Cys6 disulfide bridge in apoAII for human HDL structure and function are not known.	Disulfides	38-47	apolipoprotein A2	Homo sapiens	58-64
8934442-10	1996	Overall, reduction of the disulfide bridge of apoAII probably does not have a major effect in the determination of HDL particle size in vivo.	Disulfides	26-35	apolipoprotein A2	Homo sapiens	46-52
8871643-3	1996	The variants of human IgA differ in their H and L chain disulfide-bonding pattern; in IgA1, IgA2(n), and IgA2 m(2), a disulfide bond connects a cysteine residue in CH1 of the H chain with the L chains while human IgA2 m(1) has been reported to lack a covalent bond between the H and L chains.	Disulfides	118-127	SUN domain containing ossification factor	Homo sapiens	164-167
8855939-0	1996	Disulfide structure and N-glycosylation sites of an extracellular domain of granulocyte-colony stimulating factor receptor.	Disulfides	0-9	colony stimulating factor 3 receptor	Homo sapiens	76-122
8828477-5	1996	Our data revealed that disruption of either disulfide bond 7-31 or 59-87 in the alpha-subunit markedly reduced the dimer formation with LH beta-subunit in both CHO and GH3 cells, whereas it did not significantly affect the assembly of FSH.	Disulfides	44-53	lutropin subunit beta	Cricetulus griseus	136-143
8816772-1	1996	The disulfide bonding pattern of the fourth and fifth epidermal growth factor (EGF)-like domains within the smallest active fragment of thrombomodulin have been determined.	Disulfides	4-13	epidermal growth factor	Homo sapiens	54-77
8816772-1	1996	The disulfide bonding pattern of the fourth and fifth epidermal growth factor (EGF)-like domains within the smallest active fragment of thrombomodulin have been determined.	Disulfides	4-13	thrombomodulin	Homo sapiens	136-150
8806751-4	1996	The noncovalent interaction between the disulfide-bonded dimers is stronger in the "closed-trap" than in the "open-trap" conformation of alpha 2-macroglobulin.	Disulfides	40-49	alpha-2-macroglobulin	Homo sapiens	137-158
8930126-0	1996	Renaturation of SPARC expressed in Escherichia coli requires isomerization of disulfide bonds for recovery of biological activity.	Disulfides	78-87	secreted protein acidic and cysteine rich	Homo sapiens	16-21
8703941-0	1996	The plasma and cytoplasmic forms of human gelsolin differ in disulfide structure.	Disulfides	61-70	gelsolin	Homo sapiens	42-50
8703941-5	1996	We have used a combination of cysteine-specific modification with 4-vinylpyridine, HPLC peptide mapping methods, and mass spectrometry to analyze the disulfide structures of human plasma and cytoplasmic gelsolin.	Disulfides	150-159	gelsolin	Homo sapiens	203-211
8703941-7	1996	Cys residues 188 and 201 in domain 2 of plasma gelsolin were disulfide linked.	Disulfides	61-70	gelsolin	Homo sapiens	47-55
35595959-8	2022	Prediction of three-dimensional (3D) structure of the proteins showed that p.Cys620Tyr mutation altered the disulfide bond of ZP2 protein and may affect its function.	Disulfides	108-117	LOW QUALITY PROTEIN: zona pellucida sperm-binding protein 2	Cricetulus griseus	126-129
35471205-0	2022	Structural and functional regulations by a disulfide bond designed in myoglobin like human neuroglobin.	Disulfides	43-52	myoglobin	Homo sapiens	70-79
35471205-1	2022	An artificial disulfide bond (Cys46-Cys61) was designed in the heme distal site of myoglobin, which regulates the conformation of the heme distal His64 and the protein reactivity, as confirmed by X-ray crystallography, EPR, and kinetic UV-vis studies.	Disulfides	14-23	myoglobin	Homo sapiens	83-92
35020809-2	2022	The cysteine residues of VWF monomers form intra- and inter-molecular disulfide bonds that regulate its structural conformation, multimer distribution and ultimately its hemostatic activity.	Disulfides	70-79	Von Willebrand factor	Mus musculus	25-28
35020809-9	2022	Accelerated VWF clearance and impaired VWF secretion contributed to the fully expressed homozygous phenotype with impaired secretion arising due to disordered disulfide connectivity.	Disulfides	159-168	Von Willebrand factor	Mus musculus	39-42
35448610-3	2022	Here, we solved a high-resolution crystal structure of the extracellular cysteine-rich domain (CRD) of yeast Wsc1, which shows the characteristic PAN/Apple domain fold with two of the four Wsc1 disulfide bridges being conserved in other PAN domain cores.	Disulfides	194-203	Slg1p	Saccharomyces cerevisiae S288C	109-113
35448610-3	2022	Here, we solved a high-resolution crystal structure of the extracellular cysteine-rich domain (CRD) of yeast Wsc1, which shows the characteristic PAN/Apple domain fold with two of the four Wsc1 disulfide bridges being conserved in other PAN domain cores.	Disulfides	194-203	Slg1p	Saccharomyces cerevisiae S288C	189-193
35225603-4	2022	Cysteine-cysteine (Cys-Cys) disulfide bonds are intrinsically unstable in endogenous reductive environment, while cysteine-penicillamine (Cys-Pen) disulfide bonds show satisfactory stability.	Disulfides	147-156	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	142-145
35225603-5	2022	We envisioned the Cys-Pen disulfide as a potential ligand-induced covalent bonding warhead, and this disulfide could reconstruct with the protein cysteine in the vicinity of the peptide binding site to form a new disulfide.	Disulfides	101-110	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	22-25
35225603-5	2022	We envisioned the Cys-Pen disulfide as a potential ligand-induced covalent bonding warhead, and this disulfide could reconstruct with the protein cysteine in the vicinity of the peptide binding site to form a new disulfide.	Disulfides	213-222	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	22-25
35225603-7	2022	Both proteins were successfully modified by Cys-Pen disulfide and formed new disulfides between proteins and peptides.	Disulfides	77-87	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	48-51
35225603-8	2022	The new disulfide was then analyzed to confirm it was a newly formed disulfide bond between Pen of the ligand and a protein Cys near the ligand binding site.	Disulfides	8-17	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	92-95
8759006-1	1996	Adult T cell leukemia-derived factor (ADF) is a human thioredoxin (Trx) and is a disulfide reducing protein with various biological functions.	Disulfides	81-90	thioredoxin	Homo sapiens	38-41
8759006-1	1996	Adult T cell leukemia-derived factor (ADF) is a human thioredoxin (Trx) and is a disulfide reducing protein with various biological functions.	Disulfides	81-90	thioredoxin	Homo sapiens	54-65
8759006-1	1996	Adult T cell leukemia-derived factor (ADF) is a human thioredoxin (Trx) and is a disulfide reducing protein with various biological functions.	Disulfides	81-90	thioredoxin	Homo sapiens	67-70
35225603-8	2022	The new disulfide was then analyzed to confirm it was a newly formed disulfide bond between Pen of the ligand and a protein Cys near the ligand binding site.	Disulfides	69-78	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	92-95
26418532-7	2015	We show that both molecules inhibit PTEN via oxidative mechanisms resulting in the formation of the same intramolecular disulfide, therefore enabling the reactivation of PTEN under reductive conditions.	Disulfides	120-129	phosphatase and tensin homolog	Homo sapiens	170-174
35210360-4	2022	The crystal structure of COA7, determined to 2.4 A resolution, reveals a banana-shaped molecule composed of five helix-turn-helix (alpha/alpha) repeats, tethered by disulfide bonds.	Disulfides	165-174	cytochrome c oxidase assembly factor 7	Homo sapiens	25-29
35210360-5	2022	COA7 interacts transiently with the copper metallochaperones SCO1 and SCO2 and catalyzes the reduction of disulfide bonds within these proteins, which are crucial for copper relay to COX2.	Disulfides	106-115	cytochrome c oxidase assembly factor 7	Homo sapiens	0-4
26119781-2	2015	One of its component, Trx, is involved in redox homeostasis and many cellular biological processes through participating in disulfide reduction, S-nitrosylation/S-denitrosylation reactions and protein-protein interactions.	Disulfides	124-133	thioredoxin	Homo sapiens	22-25
35340291-5	2022	Specialized chaperones with thioredoxin (Trx) domains catalyze the redox functions necessary for breaking incorrect and forming correct disulfide bonds in proteins.	Disulfides	136-145	thioredoxin	Homo sapiens	28-39
8678907-5	1996	That the inactivation of GSTP1-1 by captan and captafol involves the formation of disulfide bonds between the four cysteinil groups of the enzymes was confirmed by the SDS-PAGE experiments on nondenaturant conditions.	Disulfides	82-91	glutathione S-transferase pi 1	Homo sapiens	25-32
8678907-6	1996	In fact, on SDS-PAGE, GSTP1-1 as well as the cys47ala, cys101ala, and cys47ala/cys101ala GSTP1-1 mutants treated with captan and captafol showed several extra bands, with apparent molecular masses higher and lower than the molecular mass of native GSTP1-1 (23.5 kDa), indicating that both intra- and inter-subunit disulfide bonds were formed.	Disulfides	314-323	glutathione S-transferase pi 1	Homo sapiens	22-29
35340291-5	2022	Specialized chaperones with thioredoxin (Trx) domains catalyze the redox functions necessary for breaking incorrect and forming correct disulfide bonds in proteins.	Disulfides	136-145	thioredoxin	Homo sapiens	41-44
35340291-8	2022	Activity based crosslinkers that rely on the nucleophilic cysteines on Trx domains and the disulfide bond forming cysteines on clients provide an easily scalable method to trap and identify the substrates of Trx-domain containing chaperones.	Disulfides	91-100	thioredoxin	Homo sapiens	208-211
26216883-3	2015	Here, we show that two additional cysteine residues located in the non-helical head domain of K14, Cys-4 and Cys-40, also participate in inter-keratin disulfide bonding and tandemly play a key role complementary to that of Cys-367 in the assembly, organization, and dynamics of keratin filaments in skin keratinocytes in primary culture.	Disulfides	151-160	keratin 14	Homo sapiens	94-97
35340291-9	2022	The cell permeable crosslinker divinyl sulfone (DVSF) is active only in the presence of nucleophilic cysteines in proteins and, therefore, traps Trx domains with their substrates, as they form mixed disulfide bonds during the course of their catalytic activity.	Disulfides	199-208	thioredoxin	Homo sapiens	145-148
8858566-2	1996	To examine its role in DNA repair, we have been studying the interaction of PARP with other nuclear proteins using disulfide cross-linking, initiated by sodium tetrathionate (NaTT).	Disulfides	115-124	poly [ADP-ribose] polymerase 1	Cricetulus griseus	76-80
35163331-8	2022	Overall, this work will help to further understand the working mechanism of AtPDI11 in catalyzing disulfide formation in plants.	Disulfides	98-107	thioredoxin family protein	Arabidopsis thaliana	76-83
26085143-3	2015	Here we identify ERdj5 as an ER enzyme that reduces SV40"s disulfide bonds, a reaction important for its ER membrane transport and infection.	Disulfides	59-68	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	17-22
34609517-8	2022	Furthermore, AtPDI2/5 work synergistically with PDI-M/S members in relaying disulfide bonds from AtERO1 to substrates.	Disulfides	76-85	endoplasmic reticulum oxidoreductins 1	Arabidopsis thaliana	97-103
26187352-7	2015	Therefore, a correlation exists between the N-terminal loop and anti-cancer properties of endostatin fragment and a disulfide loop may be more promising than a Zn binding loop for inhibiting tumor growth.	Disulfides	116-125	collagen type XVIII alpha 1 chain	Homo sapiens	90-100
26214018-9	2015	The sulfhydryl oxidase Erv1 generates the disulfide pairs de novo using either molecular oxygen or, cytochrome c and other proteins as terminal electron acceptors that eventually link this folding process to respiration.	Disulfides	42-51	growth factor, augmenter of liver regeneration	Homo sapiens	23-27
25704664-3	2015	ERp57 is a member of the protein disulfide isomerase (PDI) family and facilitates correct folding of newly synthesized glycoproteins by rearrangement of native disulfide bonds.	Disulfides	33-42	protein disulfide isomerase associated 3	Mus musculus	0-5
25704664-3	2015	ERp57 is a member of the protein disulfide isomerase (PDI) family and facilitates correct folding of newly synthesized glycoproteins by rearrangement of native disulfide bonds.	Disulfides	33-42	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	54-57
26230708-0	2015	Phylogeny of the Vitamin K 2,3-Epoxide Reductase (VKOR) Family and Evolutionary Relationship to the Disulfide Bond Formation Protein B (DsbB) Family.	Disulfides	100-109	vitamin K epoxide reductase complex subunit 1	Homo sapiens	17-48
26230708-0	2015	Phylogeny of the Vitamin K 2,3-Epoxide Reductase (VKOR) Family and Evolutionary Relationship to the Disulfide Bond Formation Protein B (DsbB) Family.	Disulfides	100-109	vitamin K epoxide reductase complex subunit 1	Homo sapiens	50-54
26119103-5	2015	The double-cysteine mutant alpha-synCC, with a disulfide linking beta1 and beta2, is aggregation-incompetent and inhibits aggregation and toxicity of wild-type alpha-syn.	Disulfides	47-56	synuclein alpha	Homo sapiens	27-36
26236235-5	2015	In this review we focus on the role of cGMP-dependent protein kinase (PKG) Ia disulfide dimerisation, an oxidative modification that is induced by oxidants that directly activates the enzyme, discussing how this impacts on the cardiovascular system.	Disulfides	78-87	protein kinase cGMP-dependent 1	Homo sapiens	70-73
26168158-0	2015	Intradomain Confinement of Disulfides in the Folding of Two Consecutive Modules of the LDL Receptor.	Disulfides	27-37	low density lipoprotein receptor	Homo sapiens	87-99
26168158-3	2015	Despite the enormous number of disulfide combinations possible, LDLR oxidative folding leads to a single native species with 30 unique intradomain disulfides.	Disulfides	147-157	low density lipoprotein receptor	Homo sapiens	64-68
26168158-4	2015	Previous folding studies of the LDLR have shown that non native disulfides are initially formed that lead to compact species.	Disulfides	64-74	low density lipoprotein receptor	Homo sapiens	32-36
26168158-11	2015	Reduction of incredibly large disulfide combinatorial spaces, such as that in the LDLR, by intradomain confinement of disulfide bond formation might be also essential for the efficient folding of other homologous disulfide-rich receptors.	Disulfides	30-39	low density lipoprotein receptor	Homo sapiens	82-86
26168158-11	2015	Reduction of incredibly large disulfide combinatorial spaces, such as that in the LDLR, by intradomain confinement of disulfide bond formation might be also essential for the efficient folding of other homologous disulfide-rich receptors.	Disulfides	118-127	low density lipoprotein receptor	Homo sapiens	82-86
26013822-6	2015	To develop an LRP1 inhibitor that does not dissociate at low pH, we introduced a disulfide bond between the second and third helices in the RAP D3 domain.	Disulfides	81-90	LDL receptor related protein associated protein 1	Homo sapiens	140-143
26013822-7	2015	By combining this disulfide bond with elimination of key histidine residues, we generated a stable RAP molecule that is resistant to both pH- and heat-induced denaturation.	Disulfides	18-27	LDL receptor related protein associated protein 1	Homo sapiens	99-102
25712700-2	2015	Since HB-EGF has three intra-molecular disulfide bonds, a high expression pattern of active HB-EGF in an E. coli expression system was not successfully established.	Disulfides	39-48	heparin binding EGF like growth factor	Homo sapiens	6-12
26039939-9	2015	The results indicate that Cys910 in wild-type NaV1.2 has a free thiol and conversely suggest that in NaV1.2[C912A] and NaV1.2[C918A], Cys910 is disulfide-bonded to Cys918 and Cys912, respectively.	Disulfides	144-153	neuron navigator 1	Rattus norvegicus	46-50
25877331-4	2015	All the corresponding recombinant proteins form various types of covalent oligomers linked by intermolecular disulfide bonds that are reduced in vitro by the thioredoxin (TRX) and/or glutathione/glutaredoxin (GRX) systems.	Disulfides	109-118	thioredoxin	Homo sapiens	158-169
25877331-4	2015	All the corresponding recombinant proteins form various types of covalent oligomers linked by intermolecular disulfide bonds that are reduced in vitro by the thioredoxin (TRX) and/or glutathione/glutaredoxin (GRX) systems.	Disulfides	109-118	thioredoxin	Homo sapiens	171-174
25772009-0	2015	Light-induced disulfide dimerization of recoverin under ex vivo and in vivo conditions.	Disulfides	14-23	recoverin	Bos taurus	40-49
25772009-2	2015	Here, we demonstrate that prolonged intense illumination (halogen bulb, 1500 lx, 1-5 h) of mammalian eyes under ex vivo (cow) or in vivo (rabbit) conditions induces disulfide dimerization of recoverin, a Ca(2+)-dependent inhibitor of rhodopsin kinase.	Disulfides	165-174	recoverin	Oryctolagus cuniculus	191-200
25772009-3	2015	Western blotting and mass spectrometry analysis of retinal extracts reveals illumination time-dependent accumulation of disulfide homodimers of recoverin and its higher order disulfide cross-linked species, including a minor fraction of mixed disulfides with intracellular proteins (tubulins, etc.).	Disulfides	120-129	recoverin	Bos taurus	144-153
25772009-7	2015	A comparison of ex vivo levels of disulfide homodimers of bovine recoverin with redox dependence of its in vitro thiol-disulfide equilibrium (glutathione redox pair) gives the lowest estimate of redox potential in rod outer segments under illumination from -160 to -155 mV.	Disulfides	34-43	recoverin	Bos taurus	65-74
25772009-7	2015	A comparison of ex vivo levels of disulfide homodimers of bovine recoverin with redox dependence of its in vitro thiol-disulfide equilibrium (glutathione redox pair) gives the lowest estimate of redox potential in rod outer segments under illumination from -160 to -155 mV.	Disulfides	119-128	recoverin	Bos taurus	65-74
25772009-8	2015	Chemical crosslinking and dynamic light scattering data demonstrate an increased propensity of disulfide dimer of bovine recoverin to multimerization/aggregation.	Disulfides	95-104	recoverin	Bos taurus	121-130
25772009-9	2015	Overall, the oxidative stress caused by the prolonged intense illumination of retina might affect rhodopsin desensitization via concerted disulfide dimerization of recoverin and arrestin.	Disulfides	138-147	rhodopsin	Bos taurus	98-107
25772009-9	2015	Overall, the oxidative stress caused by the prolonged intense illumination of retina might affect rhodopsin desensitization via concerted disulfide dimerization of recoverin and arrestin.	Disulfides	138-147	recoverin	Bos taurus	164-173
25784287-9	2015	Royalisin and royalisin D lost their antimicrobial activities when the intra-disulfide bonds were reduced by DDT.	Disulfides	77-86	defensin-1	Apis mellifera	0-9
25784287-9	2015	Royalisin and royalisin D lost their antimicrobial activities when the intra-disulfide bonds were reduced by DDT.	Disulfides	77-86	defensin-1	Apis mellifera	14-23
25784287-10	2015	The intra-disulfide bond plays a more important role than the extra stretch of 11 amino acid residues at the C-terminus of royalisin in terms of the antimicrobial properties of the native royalisin.	Disulfides	10-19	defensin-1	Apis mellifera	188-197
25866208-0	2015	Structures of the Ets Protein DNA-binding Domains of Transcription Factors Etv1, Etv4, Etv5, and Fev: DETERMINANTS OF DNA BINDING AND REDOX REGULATION BY DISULFIDE BOND FORMATION.	Disulfides	154-163	ETS variant transcription factor 5	Homo sapiens	87-91
25870246-5	2015	MHC class I HC folding is linked to the assembly of MHC class I molecules because only fully disulfide-bonded class I HCs efficiently assemble with beta2-microglobulin.	Disulfides	93-102	beta-2-microglobulin	Homo sapiens	148-167
25874934-1	2015	Thioredoxins are small soluble proteins that contain a redox-active disulfide (CXXC).	Disulfides	68-77	thioredoxin	Homo sapiens	0-12
25874934-2	2015	These disulfides are tuned to oxidizing or reducing potentials depending on the function of the thioredoxin within the cell.	Disulfides	6-16	thioredoxin	Homo sapiens	96-107
26182355-4	2015	In the present study, we examined the requirement and role for the individual disulfide bonds of Tim9 on cell viability, complex formation and stability using yeast genetic, biochemical and biophysical methods.	Disulfides	78-87	protein transporter TIM9	Saccharomyces cerevisiae S288C	97-101
26182355-5	2015	Loss of the Tim9 inner disulfide bond led to a temperature-sensitive phenotype and degradation of both Tim9 and Tim10.	Disulfides	23-32	protein transporter TIM9	Saccharomyces cerevisiae S288C	12-16
26182355-5	2015	Loss of the Tim9 inner disulfide bond led to a temperature-sensitive phenotype and degradation of both Tim9 and Tim10.	Disulfides	23-32	protein transporter TIM9	Saccharomyces cerevisiae S288C	103-107
26182355-7	2015	Formation of both disulfide bonds is not essential for Tim9 function, but it can facilitate the formation and improve the stability of the hexameric Tim9-Tim10 complex.	Disulfides	18-27	protein transporter TIM9	Saccharomyces cerevisiae S288C	149-153
25501500-1	2015	The human endothelin converting enzyme-1 (hECE-1) is a homodimer linked by a single disulfide bridge and has been identified as an important target for Alzheimer"s disease.	Disulfides	84-93	endothelin converting enzyme 1	Homo sapiens	10-40
25501500-1	2015	The human endothelin converting enzyme-1 (hECE-1) is a homodimer linked by a single disulfide bridge and has been identified as an important target for Alzheimer"s disease.	Disulfides	84-93	endothelin converting enzyme 1	Homo sapiens	42-48
25722499-7	2015	In fact, our "3-FAB" probe 2 was proven to be highly useful to investigate the stability and reactivity of the self-immolative disulfide linker system in human blood plasma by 19F NMR.	Disulfides	127-136	FA complementation group B	Homo sapiens	16-19
25422905-4	2015	Gd reveals a classical lipocalin fold including two disulfide bridges, which is however unusually compact and lacks a pronounced central pocket inside the beta-barrel, in line with its low affinity for hydrophobic ligands.	Disulfides	52-61	progestagen associated endometrial protein	Homo sapiens	0-2
25715249-6	2015	We show here that circulating Prdx1 and 2 are present exclusively as disulfide-linked homodimers.	Disulfides	69-78	peroxiredoxin 1	Homo sapiens	30-41
25715249-7	2015	Inflammatory stimuli also induce in vitro release of Prdx1 and 2 as disulfide-linked homodimers.	Disulfides	68-77	peroxiredoxin 1	Homo sapiens	53-64
25212829-8	2015	The structure and disulfide network of the protein and chemical stability of the claMP Tag and EGF components were characterized.	Disulfides	18-27	long intergenic non-protein coding RNA 1194	Homo sapiens	87-90
25603346-1	2015	ShK, from the sea anemone Stichodactyla helianthus, is a 35-residue disulfide-rich peptide that blocks the voltage-gated potassium channel Kv1.3 at ca.	Disulfides	68-77	sedoheptulokinase	Mus musculus	0-3
24911456-12	2015	These studies are the first to demonstrate that lung cancer chemotherapy agents increase procoagulant activity on endothelial cells and A549 cells by tissue factor decryption through a disulfide bond formation in a PDI-dependent mechanism.	Disulfides	185-194	coagulation factor III, tissue factor	Homo sapiens	150-163
25398878-4	2014	These results, combined with the monomeric size of Prx3 observed under non-reducing conditions, suggested that Prx3 is a Grx3/GSH-dependent 1-Cys Prx and oxidized without forming intermolecular disulfide bonds.	Disulfides	194-203	peroxiredoxin 3	Mus musculus	111-115
25231459-2	2014	Trx1 is a key reductase that reduces specific disulfide bonds and other cysteine post-translational modifications.	Disulfides	46-55	thioredoxin	Homo sapiens	0-4
25231459-6	2014	The wild-type Trx1 contains a conserved C32XXC35 motif, and the C32 thiol initiates the reduction of a target disulfide bond by forming an intermolecular disulfide with one of the oxidized target cysteines, resulting in a transient Trx1-target protein complex.	Disulfides	110-119	thioredoxin	Homo sapiens	14-18
25231459-6	2014	The wild-type Trx1 contains a conserved C32XXC35 motif, and the C32 thiol initiates the reduction of a target disulfide bond by forming an intermolecular disulfide with one of the oxidized target cysteines, resulting in a transient Trx1-target protein complex.	Disulfides	110-119	thioredoxin	Homo sapiens	232-236
25231459-6	2014	The wild-type Trx1 contains a conserved C32XXC35 motif, and the C32 thiol initiates the reduction of a target disulfide bond by forming an intermolecular disulfide with one of the oxidized target cysteines, resulting in a transient Trx1-target protein complex.	Disulfides	154-163	thioredoxin	Homo sapiens	14-18
25231459-6	2014	The wild-type Trx1 contains a conserved C32XXC35 motif, and the C32 thiol initiates the reduction of a target disulfide bond by forming an intermolecular disulfide with one of the oxidized target cysteines, resulting in a transient Trx1-target protein complex.	Disulfides	154-163	thioredoxin	Homo sapiens	232-236
25231459-7	2014	The reduction is rapidly consummated by the donation of a C35 proton to the target molecule, forming a Trx1 C32-C35 disulfide, and results in the concurrent release of the target protein containing reduced thiols.	Disulfides	116-125	migration and invasion enhancer 1	Homo sapiens	58-61
25231459-7	2014	The reduction is rapidly consummated by the donation of a C35 proton to the target molecule, forming a Trx1 C32-C35 disulfide, and results in the concurrent release of the target protein containing reduced thiols.	Disulfides	116-125	thioredoxin	Homo sapiens	103-107
25231459-7	2014	The reduction is rapidly consummated by the donation of a C35 proton to the target molecule, forming a Trx1 C32-C35 disulfide, and results in the concurrent release of the target protein containing reduced thiols.	Disulfides	116-125	chemokine like factor	Homo sapiens	108-111
25231459-7	2014	The reduction is rapidly consummated by the donation of a C35 proton to the target molecule, forming a Trx1 C32-C35 disulfide, and results in the concurrent release of the target protein containing reduced thiols.	Disulfides	116-125	migration and invasion enhancer 1	Homo sapiens	112-115
25393952-6	2014	Cys47 and Cys101, the most reactive sulfhydryls of GSTP1-1, are mainly involved in a redox interaction which leads to the formation of an intra-chain disulfide bridge.	Disulfides	150-159	glutathione S-transferase pi 1	Homo sapiens	51-58
24328910-4	2014	RECENT ADVANCES: The thioredoxin (Trx) system, which is predominantly expressed in pulmonary epithelia in the newborn lung, acts as an antioxidant system; however, it is increasingly recognized as a key redox regulator of signal transduction and gene expression via thiol-disulfide exchange reactions.	Disulfides	272-281	thioredoxin	Homo sapiens	21-32
24328910-4	2014	RECENT ADVANCES: The thioredoxin (Trx) system, which is predominantly expressed in pulmonary epithelia in the newborn lung, acts as an antioxidant system; however, it is increasingly recognized as a key redox regulator of signal transduction and gene expression via thiol-disulfide exchange reactions.	Disulfides	272-281	thioredoxin	Homo sapiens	34-37
25205656-3	2014	In particular, the IL2 cytokine and the disulfide-linked maytansinoid DM1 microtubular inhibitor could be coupled to the F8 antibody, directed against the alternatively spliced EDA domain of fibronectin, in a site-specific manner, yielding a chemically defined product with selective tumor-homing performance and potent anticancer activity in vivo, as tested in two different immunocompetent mouse models.	Disulfides	40-49	fibronectin 1	Mus musculus	191-202
25182596-11	2014	Results of processing assays suggested that these residues were redox active and formation of a disulfide bond between them was necessary for the activity of recombinant Arabidopsis Plsp1.	Disulfides	96-105	plastidic type i signal peptidase 1	Arabidopsis thaliana	182-187
8662950-5	1996	The degree to which bovine somatotropin is stabilized by disulfide bonds was examined using CSI-based quantitative thermal denaturation kinetics profiles generated under reducing and nonreducing conditions.	Disulfides	57-66	somatotropin	Bos taurus	27-39
8662950-6	1996	All of the conformational epitopes unfolded faster under reducing conditions indicating that the two disulfide bonds within the somatotropin molecule impart some degree of global stabilization.	Disulfides	101-110	somatotropin	Bos taurus	128-140
24094148-8	2014	Disulfide HMGB1 effect on NMDA-induced Ca(2+) influx was prevented by 3-O-methylsphingomyelin (3-O-MS) and 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo [3,4-d] pyrimidine, (PP2) selective inhibitors of neutral sphingomyelinase and Src-family Tyr kinases, respectively.	Disulfides	0-9	neuropeptide Y receptor Y6	Mus musculus	176-179
24094148-8	2014	Disulfide HMGB1 effect on NMDA-induced Ca(2+) influx was prevented by 3-O-methylsphingomyelin (3-O-MS) and 4-amino-5-(4-chlorophenyl)-7-(t-butyl) pyrazolo [3,4-d] pyrimidine, (PP2) selective inhibitors of neutral sphingomyelinase and Src-family Tyr kinases, respectively.	Disulfides	0-9	Rous sarcoma oncogene	Mus musculus	234-237
8805557-1	1996	BACKGROUND: Human thioredoxin reduces the disulfide bonds of numerous proteins in vitro, and can activate transcription factors such as NFkB in vivo.	Disulfides	42-51	thioredoxin	Homo sapiens	18-29
8805557-4	1996	Surprisingly, thioredoxin is dimeric in all four structures; the dimer is linked through a disulfide bond between Cys73 of each monomer, except in Cys73--&gt;Ser where a hydrogen bond occurs.	Disulfides	91-100	thioredoxin	Homo sapiens	14-25
24094148-9	2014	Disulfide HMGB1, but not 3S-HMGB1, increased Tyr(1472) phosphorylation of the NR2B subunit of the NMDAR, which is known to increase Ca(2+) channel permeability.	Disulfides	0-9	glutamate receptor, ionotropic, NMDA2B (epsilon 2)	Mus musculus	78-82
8805557-9	1996	This nucleophilicity, in tum, is thought to be necessary for the role of thioredoxin in disulfide-bond reduction.	Disulfides	88-97	thioredoxin	Homo sapiens	73-84
24094148-9	2014	Disulfide HMGB1, but not 3S-HMGB1, increased Tyr(1472) phosphorylation of the NR2B subunit of the NMDAR, which is known to increase Ca(2+) channel permeability.	Disulfides	0-9	glutamate receptor, ionotropic, NMDA1 (zeta 1)	Mus musculus	98-103
25220457-3	2014	Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction.	Disulfides	65-74	peroxiredoxin 5	Homo sapiens	23-44
25220457-3	2014	Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction.	Disulfides	65-74	thioredoxin	Homo sapiens	23-34
8724352-1	1996	Canine relaxin (cRlx) was synthesized by a combination of solid-phase methods and sequential site-directed disulfide bond formation.	Disulfides	107-116	prorelaxin	Canis lupus familiaris	7-14
25220457-3	2014	Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction.	Disulfides	65-74	peroxiredoxin 5	Homo sapiens	281-302
25220457-3	2014	Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction.	Disulfides	65-74	thioredoxin	Homo sapiens	45-56
8649415-0	1996	Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding.	Disulfides	35-44	interleukin 3	Homo sapiens	6-25
8649415-0	1996	Human interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity binding.	Disulfides	35-44	interleukin 3	Homo sapiens	21-25
25220457-3	2014	Here, we show that the thioredoxin reductase-thioredoxin protein disulfide-reducing system is present on synaptic vesicles and that it is functional and responsible for the reduction of the interchain disulfide of botulinum neurotoxin serotypes A, C, and E. Specific inhibitors of thioredoxin reductase or thioredoxin prevent intoxication of cultured neurons in a dose-dependent manner and are also very effective inhibitors of the paralysis of the neuromuscular junction.	Disulfides	201-210	peroxiredoxin 5	Homo sapiens	23-44
8649415-4	1996	We show here that human IL-3 induces heterodimerization of IL-3R alpha and beta c and that disulfide linkage of these chains is involved in receptor activation but not high-affinity binding.	Disulfides	91-100	interleukin 3	Homo sapiens	24-28
8649415-7	1996	IL-3-induced receptor dimers were disulfide and nondisulfide linked and were dependent on IL-3 interacting with both IL-3R alpha and beta c.	Disulfides	34-43	interleukin 3	Homo sapiens	0-4
24895313-9	2014	The three disulfide bridges hepcidin analog demonstrated bactericidal activity, against B. subtilis ATCC 11779 and S. aureus ATCC 6538 strains, at the concentration of 15 muM (50 microg/ml) or above at pH 6.2.	Disulfides	10-19	hepcidin antimicrobial peptide	Homo sapiens	28-36
8649415-7	1996	IL-3-induced receptor dimers were disulfide and nondisulfide linked and were dependent on IL-3 interacting with both IL-3R alpha and beta c.	Disulfides	34-43	colony stimulating factor 2 receptor subunit beta	Homo sapiens	133-139
8649415-10	1996	Two-dimensional gel electrophoresis and Western blotting (immunoblotting) demonstrated the presence of both IL-3R alpha and beta c in the disulfide-linked complexes.	Disulfides	138-147	colony stimulating factor 2 receptor subunit beta	Homo sapiens	124-130
8649415-12	1996	Following IL-3 stimulation, only the disulfide-linked heterodimers exhibited reactivity with antiphosphotyrosine antibodies, with beta c but not IL-3R alpha being the phosphorylated species.	Disulfides	37-46	interleukin 3	Homo sapiens	10-14
8649415-12	1996	Following IL-3 stimulation, only the disulfide-linked heterodimers exhibited reactivity with antiphosphotyrosine antibodies, with beta c but not IL-3R alpha being the phosphorylated species.	Disulfides	37-46	colony stimulating factor 2 receptor subunit beta	Homo sapiens	130-136
8645729-0	1996	FTIR studies of recombinant human granulocyte-macrophage colony-stimulating factor in aqueous solutions: secondary structure, disulfide reduction and thermal behavior.	Disulfides	126-135	colony stimulating factor 2	Homo sapiens	34-82
8645729-1	1996	Fourier transform infrared spectroscopy (FTIR) has been used to investigate the secondary structure, disulfide reduction and thermal behavior of recombinant human granulocyte-macrophage colony-stimulating factor (rhGM-CSF) in aqueous solutions.	Disulfides	101-110	colony stimulating factor 2	Homo sapiens	163-211
24920818-6	2014	Destabilization of the gp120 conformation by deletion of single disulfide bonds preferentially enhanced responses to the cryptic I-Ak motif-containing sequences, as reported by T-cell proliferation or cytokine secretion.	Disulfides	64-73	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	23-28
24997578-4	2014	The bicyclic tetrapeptides disulfide showed potent HDAC1 and HDAC4 inhibition and p21 promoting activity.	Disulfides	27-36	histone deacetylase 4	Homo sapiens	61-66
8652598-5	1996	Since the 40 kDa protein (p40) can only be detected under reducing conditions, it probably originates from reduction of disulfide bonds in p70.	Disulfides	120-129	septin 3	Rattus norvegicus	26-29
8639545-0	1996	Inhibition of human cytomegalovirus UL80 protease by specific intramolecular disulfide bond formation.	Disulfides	77-86	capsid maturation protease	Human betaherpesvirus 5	36-40
8639545-1	1996	A symmetrically substituted disulfide compound, CL13933, was identified as a potent inhibitor of human cytomegalovirus UL80 protease.	Disulfides	28-37	capsid maturation protease	Human betaherpesvirus 5	119-123
8639546-0	1996	Flavins inhibit human cytomegalovirus UL80 protease via disulfide bond formation.	Disulfides	56-65	capsid maturation protease	Human betaherpesvirus 5	38-42
24997578-4	2014	The bicyclic tetrapeptides disulfide showed potent HDAC1 and HDAC4 inhibition and p21 promoting activity.	Disulfides	27-36	H3 histone pseudogene 16	Homo sapiens	82-85
24863694-2	2014	The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress.	Disulfides	126-136	thioredoxin	Homo sapiens	4-15
8631806-11	1996	Mass spectrometric analysis combined with site-directed mutagenesis of each of the four cysteine residues of the recombinant protein revealed that p41 is a dimer of p33 cross-linked at Cys-198 via a disulfide bond.	Disulfides	199-208	erythrocyte membrane protein band 4.1	Bos taurus	147-150
24863694-2	2014	The thioredoxin (Trx) and glutaredoxin (Grx) systems are two central systems upholding the sulfhydryl homeostasis by reducing disulfides and mixed disulfides within the cell and thereby protecting against oxidative stress.	Disulfides	126-136	thioredoxin	Homo sapiens	17-20
24791606-5	2014	The MMAE rebridging reagent was also conjugated to the interchain disulfide of a Fab derived from proteolytic digestion of TRA, to give a homogeneous single drug conjugated product.	Disulfides	66-75	FA complementation group B	Homo sapiens	81-84
8636094-10	1996	Thus, despite an identical active site disulfide motif and a similar secondary structure and tertiary fold, Grx3 and Grx1 display large functional differences in in vitro protein disulfide oxido-reduction reactions.	Disulfides	179-188	glutaredoxin 3	Homo sapiens	108-112
24933654-5	2014	In the purified system we also observe a requirement for oxidation, as the effect of resveratrol on ATM signaling is substantially reduced by agents that prevent disulfide bond formation in ATM.	Disulfides	162-171	ATM serine/threonine kinase	Homo sapiens	100-103
24933654-5	2014	In the purified system we also observe a requirement for oxidation, as the effect of resveratrol on ATM signaling is substantially reduced by agents that prevent disulfide bond formation in ATM.	Disulfides	162-171	ATM serine/threonine kinase	Homo sapiens	190-193
8631927-0	1996	The molecular pathway for the regulation of phosphoribulokinase by thioredoxin f. Phosphoribulokinase (PRK) is one of several plant enzymes that is regulated by thiol-disulfide exchange as mediated by thioredoxin, which contains spatially vicinal, redox-active cysteinyl residues.	Disulfides	167-176	thioredoxin	Homo sapiens	67-78
8631927-0	1996	The molecular pathway for the regulation of phosphoribulokinase by thioredoxin f. Phosphoribulokinase (PRK) is one of several plant enzymes that is regulated by thiol-disulfide exchange as mediated by thioredoxin, which contains spatially vicinal, redox-active cysteinyl residues.	Disulfides	167-176	thioredoxin	Homo sapiens	201-212
24515870-2	2014	Here, we surprisingly found that a fraction of KLRG1 molecules expressed in the murine A5 T-cell line and in IL-2-activated NK cells forms disulfide-linked heteromers with the transferrin receptor (TfR).	Disulfides	139-148	killer cell lectin-like receptor subfamily G, member 1	Mus musculus	47-52
8631927-3	1996	268, 18411-18414), our laboratory identified Cys-46 of thioredoxin f (Trx), as opposed to the other candidate Cys-49, as the primary nucleophile that attacks the disulfide of target proteins.	Disulfides	162-171	thioredoxin	Homo sapiens	55-68
8631927-3	1996	268, 18411-18414), our laboratory identified Cys-46 of thioredoxin f (Trx), as opposed to the other candidate Cys-49, as the primary nucleophile that attacks the disulfide of target proteins.	Disulfides	162-171	thioredoxin	Homo sapiens	70-73
8631927-4	1996	The goal of the present study was to identify which of the two redox-active cysteinyl residues of PRK (Cys-16 or Cys-55) is paired with Cys-46 of Trx in the interprotein disulfide intermediate of the overall oxidation-reduction pathway.	Disulfides	170-179	thioredoxin	Homo sapiens	146-149
24515870-2	2014	Here, we surprisingly found that a fraction of KLRG1 molecules expressed in the murine A5 T-cell line and in IL-2-activated NK cells forms disulfide-linked heteromers with the transferrin receptor (TfR).	Disulfides	139-148	interleukin 2	Mus musculus	109-113
8745396-6	1996	The unique beta-sheet structures of the bound peptides are specified by the presence of disulfide bridges in the peptides because a corresponding linear thrombomodulin fragment folds into a sheet structure with a different backbone topology.	Disulfides	88-97	thrombomodulin	Homo sapiens	153-167
24713928-6	2014	The creation of a disulfide bond within the A2 domain of VWF was found to render VWF multimers resistant to proteolysis by plasma proteases under flow.	Disulfides	18-27	Von Willebrand factor	Mus musculus	57-60
8561803-1	1996	Using transfection of NIH 3T3 cells, we have recently demonstrated that multiple endocrine neoplasia (MEN) 2A mutations activate the c-Ret protein by inducing its disulfide-linked homodimerization on the cell surface.	Disulfides	163-172	ret proto-oncogene	Homo sapiens	135-138
24713928-6	2014	The creation of a disulfide bond within the A2 domain of VWF was found to render VWF multimers resistant to proteolysis by plasma proteases under flow.	Disulfides	18-27	Von Willebrand factor	Mus musculus	81-84
24855952-0	2014	Interaction of circadian clock proteins CRY1 and PER2 is modulated by zinc binding and disulfide bond formation.	Disulfides	87-96	cryptochrome circadian regulator 1	Homo sapiens	40-44
8543831-2	1996	Thioredoxin is one of the major redox-regulatory molecules which because of its dithiol/disulfide exchange activity determines the oxidation state of protein thiols.	Disulfides	88-97	thioredoxin	Homo sapiens	0-11
24706752-6	2014	CHFI-123, which lacks 34 amino acid residues at the C terminus and the fourth and fifth disulfide bridges, inhibited FXIIa with a Ki of 116 +- 16 nm.	Disulfides	88-97	trypsin/factor XIIA inhibitor	Zea mays	0-4
8552654-0	1996	The peptide binding site of the substance P (NK-1) receptor localized by a photoreactive analogue of substance P: presence of a disulfide bond.	Disulfides	128-137	tachykinin receptor 1	Homo sapiens	45-59
24778250-3	2014	Moreover, the l-cystine reduction with TRP14 was in contrast to that of Trx1 fully maintained in the presence of a protein disulfide substrate of Trx1 such as insulin, suggesting that TRP14 is a more dedicated l-cystine reductase compared with Trx1.	Disulfides	123-132	thioredoxin	Homo sapiens	146-150
9075580-2	1996	It belongs to a superfamily of proteins including Ly-6, elapid snake venom toxins, and urokinase receptor (UPAR); the members of the superfamily have a similar structure that includes four (in mammals five) disulfide bridges that maintain a three-dimensional conformation consisting of a central core, three finger-like "loops" extending from it and a small loop near the coboxyl end.	Disulfides	207-216	plasminogen activator, urokinase receptor	Homo sapiens	107-111
24778250-3	2014	Moreover, the l-cystine reduction with TRP14 was in contrast to that of Trx1 fully maintained in the presence of a protein disulfide substrate of Trx1 such as insulin, suggesting that TRP14 is a more dedicated l-cystine reductase compared with Trx1.	Disulfides	123-132	thioredoxin domain containing 17	Homo sapiens	184-189
24778250-3	2014	Moreover, the l-cystine reduction with TRP14 was in contrast to that of Trx1 fully maintained in the presence of a protein disulfide substrate of Trx1 such as insulin, suggesting that TRP14 is a more dedicated l-cystine reductase compared with Trx1.	Disulfides	123-132	thioredoxin	Homo sapiens	146-150
24582612-7	2014	Three new BChE mutants (E364-532, E377-516, and E535) were predicted to have a more stable dimer structure with the desirable cross-subunit disulfide bond(s) and, therefore, a different distribution of the oligomeric forms and a prolonged biological half-life.	Disulfides	140-149	butyrylcholinesterase	Homo sapiens	10-14
8674151-1	1996	Mammalian pancreatic ribonuclease (RNase) was conjugated chemically via a disulfide bond to human or murine epidermal growth factor (EGF).	Disulfides	74-83	epidermal growth factor	Mus musculus	108-131
8674151-1	1996	Mammalian pancreatic ribonuclease (RNase) was conjugated chemically via a disulfide bond to human or murine epidermal growth factor (EGF).	Disulfides	74-83	epidermal growth factor	Mus musculus	133-136
24577496-2	2014	At neutral pH, diselenides are found to mix with disulfides and form dynamic combinatorial libraries of diselenides, disulfides, and selenenylsulfides.	Disulfides	49-59	Mix paired-like homeobox	Homo sapiens	40-43
21043655-3	1996	Upon reduction, MDP-1 no longer bound to the 94kDa protein indicating an epitope requiring at least one disulfide bond.	Disulfides	104-113	magnesium dependent phosphatase 1	Homo sapiens	16-21
21043655-8	1996	Following chymotrypsin digestion, MDP-1 bound to a cleaved GP IIIa protein (nonreduced M, = 122 kDa) consistent with opening of the major disulfide loop.	Disulfides	138-147	magnesium dependent phosphatase 1	Homo sapiens	34-39
8527452-1	1995	The dithiol/disulfide active sites of each of the two isolated thioredoxin-like domains of protein disulfide isomerase (PDI) expressed in Escherichia coli have been characterized in order to understand their catalytic mechanisms and their functions in PDI.	Disulfides	12-21	protein-disulfide isomerase	Escherichia coli	91-118
8527452-1	1995	The dithiol/disulfide active sites of each of the two isolated thioredoxin-like domains of protein disulfide isomerase (PDI) expressed in Escherichia coli have been characterized in order to understand their catalytic mechanisms and their functions in PDI.	Disulfides	12-21	protein-disulfide isomerase	Escherichia coli	120-123
24577496-2	2014	At neutral pH, diselenides are found to mix with disulfides and form dynamic combinatorial libraries of diselenides, disulfides, and selenenylsulfides.	Disulfides	117-127	Mix paired-like homeobox	Homo sapiens	40-43
24357333-1	2014	Urotensin II (U-II) is a disulfide bridged peptide hormone identified as the ligand of a G protein-coupled receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	14-18
8590802-5	1995	In chondrocytes, the wild-type virally encoded CMP is able to form disulfide bonded trimers and to assemble into filaments.	Disulfides	67-76	matrilin 1, cartilage matrix protein	Gallus gallus	47-50
24422500-1	2014	Mammalian thioredoxin reductase (TR) is a pyridine nucleotide disulfide oxidoreductase that uses the rare amino acid selenocysteine (Sec) in place of the more commonly used amino acid cysteine (Cys) in the redox-active tetrapeptide Gly-Cys-Sec-Gly motif to catalyze thiol/disulfide exchange reactions.	Disulfides	62-71	peroxiredoxin 5	Homo sapiens	10-31
8590802-6	1995	Filaments also form with CMP whose Cys455 and Cys457 in the tail domain were mutagenized to prevent interchain disulfide bond formation.	Disulfides	111-120	matrilin 1, cartilage matrix protein	Gallus gallus	25-28
24422500-1	2014	Mammalian thioredoxin reductase (TR) is a pyridine nucleotide disulfide oxidoreductase that uses the rare amino acid selenocysteine (Sec) in place of the more commonly used amino acid cysteine (Cys) in the redox-active tetrapeptide Gly-Cys-Sec-Gly motif to catalyze thiol/disulfide exchange reactions.	Disulfides	62-71	peroxiredoxin 5	Homo sapiens	33-35
7578129-4	1995	Conversely, the solution structure of TNFR differs from the crystal structure in its distribution of disulfide rotamers and in the orientation of its unique indole side chain (tryptophan-107).	Disulfides	101-110	TNF receptor superfamily member 1A	Homo sapiens	38-42
7578147-2	1995	Site-directed mutagenesis was used to probe the contribution of each of the seven disulfide bonds of bovine pancreatic phospholipase A2 (PLA2, overexpressed in Escherichia coli) to the structure, conformational stability, and catalytic function of the enzyme.	Disulfides	82-91	LOC104974671	Bos taurus	119-135
24422500-9	2014	This experimental observation most likely means that the selenolate is the nucleophile initially attacking the disulfide bond of Trx because a complex resulted only when Cys was present in the second position of the dyad.	Disulfides	111-120	thioredoxin	Homo sapiens	129-132
7578147-9	1995	(iii) The effects of deleting disulfide bonds on the catalytic function of PLA2 are small, except the disulfide bond C29-C45 which connects the calcium binding loop with the helix C. However, the conformation and conformational stability of the C29A-C45A mutant was found to decrease by a factor of 10 or greater.	Disulfides	30-39	LOC104974671	Bos taurus	75-79
23939310-5	2014	MAJOR CONCLUSIONS: Two Prx oxidation products accumulate in cells under increased oxidative stress: an intermolecular disulfide and a hyperoxidized form.	Disulfides	118-127	periaxin	Homo sapiens	23-26
24274902-0	2014	Cross-linking of thioredoxin reductase by the sulfur mustard analogue mechlorethamine (methylbis(2-chloroethyl)amine) in human lung epithelial cells and rat lung: selective inhibition of disulfide reduction but not redox cycling.	Disulfides	187-196	peroxiredoxin 5	Homo sapiens	17-38
7579443-3	1995	Western blotting showed that the STK transcript is translated into a single-chain precursor and then cleaved into a 165-kD disulfide-linked heterodimer composed of a 35-kD alpha-chain and a 144-kD beta-chain.	Disulfides	123-132	macrophage stimulating 1 receptor (c-met-related tyrosine kinase)	Mus musculus	33-36
23899494-1	2014	The thioredoxin (Trx) system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin, is a key antioxidant system in defense against oxidative stress through its disulfide reductase activity regulating protein dithiol/disulfide balance.	Disulfides	181-190	thioredoxin	Homo sapiens	4-15
8838414-1	1995	During the time course of disulfide bond formation by iodine oxidation (in a methanolic and hydrochloric acid solution) of a cysteinyl(S-acetamidomethyl)-glutaminyl tridecapeptide, we observed by ESI, FAB mass spectrometry (pseudo-molecular ion and ion-fragments) and 1H-NMR a side reaction due to a shift of the Acm leaving group from cysteine to the carboxamide side chain of glutamine.	Disulfides	26-35	FA complementation group B	Homo sapiens	201-204
7592581-2	1995	Studies based upon fluorescent labeling of free cysteine residues have suggested that cysteine 3734 of the 4 carboxyl-terminal cysteines of apoB (Cys-3734, Cys-3890, Cys-4190, and Cys-4326) is the most likely candidate to form a disulfide bond with apo(a).	Disulfides	229-238	apolipoprotein B	Mus musculus	140-144
7548065-0	1995	Disulfide bridges of a cysteine-rich repeat of the LDL receptor ligand-binding domain.	Disulfides	0-9	low density lipoprotein receptor	Homo sapiens	51-63
7548065-4	1995	As a first step toward an understanding of the structure and function of LB repeats, we have expressed the amino-terminal ligand-binding repeat (LB1) of the human LDLR as a recombinant peptide (rLB1) and have determined its disulfide-pairing scheme.	Disulfides	224-233	low density lipoprotein receptor	Homo sapiens	163-167
23899494-1	2014	The thioredoxin (Trx) system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin, is a key antioxidant system in defense against oxidative stress through its disulfide reductase activity regulating protein dithiol/disulfide balance.	Disulfides	181-190	thioredoxin	Homo sapiens	17-20
24174213-2	2014	Human IL24 possesses three N glycosylation sites and a disulfide bridge.	Disulfides	55-64	interleukin 24	Homo sapiens	6-10
8528067-3	1995	The disulfide bonding pattern of the folded, oxidized domain was (1-3, 2-4, 5-6), which is the same as that found in EGF protein.	Disulfides	4-13	epidermal growth factor	Homo sapiens	117-120
8528067-9	1995	The C-terminal loop formed by the disulfide bond between C372 and C386 in TM4 is five amino acids longer than the analogous loop between C33 and C42 of EGF protein.	Disulfides	34-43	epidermal growth factor	Homo sapiens	152-155
24295216-0	2013	Identification of disulfide bond formation between MitoNEET and glutamate dehydrogenase 1.	Disulfides	18-27	CDGSH iron sulfur domain 1	Homo sapiens	51-59
7629235-7	1995	Reduction of disulfide bridges with reducing agents (dithiothreitol and cysteine) increased the specific binding of CRH to its myometrial receptor, and the action of dithiothreitol affected the two most basic receptor isoforms.	Disulfides	13-22	corticotropin releasing hormone	Homo sapiens	116-119
7629235-8	1995	These results suggest the presence of multiple isoforms of CRH receptors that may have different properties and functions and the presence of disulfide bridges within the myometrial CRH receptor, which are important, but not critical, for the receptor binding.	Disulfides	142-151	corticotropin releasing hormone	Homo sapiens	182-185
24295216-0	2013	Identification of disulfide bond formation between MitoNEET and glutamate dehydrogenase 1.	Disulfides	18-27	glutamate dehydrogenase 1	Homo sapiens	64-89
24295216-4	2013	MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator.	Disulfides	52-61	CDGSH iron sulfur domain 1	Homo sapiens	0-8
7635203-0	1995	Structural role of disulfide bridges in the cyclic ADP-ribose related bifunctional ectoenzyme CD38.	Disulfides	19-28	CD38 molecule	Homo sapiens	94-98
24295216-4	2013	MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator.	Disulfides	52-61	glutamate dehydrogenase 1	Homo sapiens	39-43
7635203-7	1995	These data demonstrate that none of the cysteine residues plays any direct catalytic role in CD38 and Aplysia proteins, and that disulfide bridges are essential for maintaining the monomeric, catalytically active structure of CD38.	Disulfides	129-138	CD38 molecule	Homo sapiens	226-230
25593981-6	2014	The small heat shock protein HSP27 was found to be covalently dimerized via oxidized disulfide bonds and precipitated in para-nuclear protein aggregates.	Disulfides	85-94	heat shock protein family B (small) member 1	Homo sapiens	29-34
7608548-2	1995	During transcytosis, a disulfide bond forms between pIgR and pIgA, resulting in secretion of a covalently linked complex.	Disulfides	23-32	polymeric immunoglobulin receptor	Homo sapiens	52-56
7608548-5	1995	The function of transfected pIgR was confirmed by measuring vectorial transcytosis of 125I-labeled pIgA and its disulfide bonding to pIgR.	Disulfides	112-121	polymeric immunoglobulin receptor	Homo sapiens	28-32
7608548-5	1995	The function of transfected pIgR was confirmed by measuring vectorial transcytosis of 125I-labeled pIgA and its disulfide bonding to pIgR.	Disulfides	112-121	polymeric immunoglobulin receptor	Homo sapiens	133-137
7608548-8	1995	However, disulfide bonding was observed only with human pIgR, and was found to occur mainly inside the cell.	Disulfides	9-18	polymeric immunoglobulin receptor	Homo sapiens	56-60
24790958-6	2013	Click chemistry conjugation of Cy5.5 at the B-chain N-terminus, with conservation of the disulfide bonds, yielded analogs displaying appropriate selective binding affinity and ability to activate RXFP1 and/or RXFP2 in vitro.	Disulfides	89-98	relaxin family peptide receptor 1	Homo sapiens	196-201
7539801-10	1995	These findings indicate that residues in the bait region appear to be necessary for noncovalent association of 360-kDa disulfide-linked dimers to give tetrameric alpha 2M and suggest a role for the bait region in normal alpha 2M in coupling bait region cleavage to the sequence of conformational changes that result in thiol ester activation and ultimately proteinase trapping.	Disulfides	119-128	alpha-2-macroglobulin	Homo sapiens	162-170
7539801-10	1995	These findings indicate that residues in the bait region appear to be necessary for noncovalent association of 360-kDa disulfide-linked dimers to give tetrameric alpha 2M and suggest a role for the bait region in normal alpha 2M in coupling bait region cleavage to the sequence of conformational changes that result in thiol ester activation and ultimately proteinase trapping.	Disulfides	119-128	alpha-2-macroglobulin	Homo sapiens	220-228
24490732-2	2013	The ability of both AGR2 and ERp57/GRP58 to catalyze the formation of disulfide bonds in proteins is the parameter most important for assigning them to a PDI family.	Disulfides	70-79	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	20-24
7749633-2	1995	The antigenicity was lost upon reduction of TR by NADPH indicating a large conformational change upon reduction of the redox-active disulfide in the enzyme.	Disulfides	132-141	peroxiredoxin 5	Bos taurus	44-46
24018861-0	2013	On-line electrochemical reduction of disulfide bonds: improved FTICR-CID and -ETD coverage of oxytocin and hepcidin.	Disulfides	37-46	hepcidin antimicrobial peptide	Homo sapiens	107-115
7738685-6	1995	Chicken apolipoprotein VLDL-II, an 82-amino acid protein with a disulfide crosslink at residue 75 (the sole cysteine residue), existed as a homodimer of 9.5 kDa subunits and, to a lesser extent, as a monomer.	Disulfides	64-73	very low density lipoprotein receptor	Gallus gallus	23-27
24018861-2	2013	Here we present an on-line/electrochemistry/ESI-FTICR-MS approach, which was applied to the analysis of the primary structure of oxytocin, containing one disulfide bridge, and of hepcidin, containing four disulfide bridges.	Disulfides	205-214	hepcidin antimicrobial peptide	Homo sapiens	179-187
24324475-4	2013	Indeed, 4 out of 11 enzymes of the cycle were shown to have a low activity in the dark and to be activated in the light through thioredoxin-dependent reduction of regulatory disulfide bonds.	Disulfides	174-183	thioredoxin	Homo sapiens	128-139
2605244-8	1989	Ca2+ or Mg2+ was able to prevent this disulfide formation in the RLC of myosin by 50% at a free ion concentration of 1.1 X 10(-8) and 4.0 X 10(-7) M, respectively, at 25 degrees C and pH 7.6.	Disulfides	38-47	integrin subunit alpha 9	Homo sapiens	65-68
24040747-0	2013	Unequivocal determination of site-specific protein disulfide bond reduction potentials by top-down FTICR MS: characterization of the N- and C-terminal redox-active sites in human thioredoxin 1.	Disulfides	51-60	thioredoxin	Homo sapiens	179-192
2605244-9	1989	Intrachain disulfide formation of RLC never occurred in myosin at 0 degree C.(ABSTRACT TRUNCATED AT 250 WORDS)	Disulfides	11-20	integrin subunit alpha 9	Homo sapiens	34-37
7627128-2	1995	Using oligonucleotide-directed mutagenesis of hM-CSF (1-149aa) cDNA, we have substituted Ser31 for Cys31 which forms intermolecular disulfide bond in native hM-CSF.	Disulfides	132-141	colony stimulating factor 1	Homo sapiens	46-52
7627128-2	1995	Using oligonucleotide-directed mutagenesis of hM-CSF (1-149aa) cDNA, we have substituted Ser31 for Cys31 which forms intermolecular disulfide bond in native hM-CSF.	Disulfides	132-141	colony stimulating factor 1	Homo sapiens	157-163
23669023-1	2013	Interferon-gamma-inducible-lysosomal thiol reductase (GILT) plays a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction.	Disulfides	166-175	interferon gamma inducible protein 30	Mus musculus	54-58
7786412-1	1995	The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers.	Disulfides	139-148	colony stimulating factor 2	Homo sapiens	90-96
7786412-1	1995	The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers.	Disulfides	139-148	peptidyl arginine deiminase 1	Homo sapiens	107-110
2674141-9	1989	CTSE contains 7 cysteine residues, of which 6 were localized by comparative maximal alignment analysis with pepsinogen A to conserved residues that form intrachain disulfide bonds.	Disulfides	164-173	cathepsin E	Homo sapiens	0-4
23774033-1	2013	The penultimate event in the intoxication of mammalian cells by ricin toxin is the reduction, in the endoplasmic reticulum (ER), of the intermolecular disulfide bond that links ricin"s enzymatic (RTA) and binding (RTB) subunits.	Disulfides	151-160	MAS related GPR family member F	Homo sapiens	196-199
2674141-11	1989	We suspect that this residue forms an interchain disulfide bond and thereby determines the dimerization of CTSE proenzyme molecules that is observed under native conditions.	Disulfides	49-58	cathepsin E	Homo sapiens	107-111
2752977-5	1989	125I-Labeled monomeric hamster PL-II (Mr, 22,000) formed a disulfide-bonded complex (Mr, 720,000 by gel filtration and 360,000 by SDS-PAGE) when incubated in vitro with serum of male, nonpregnant female, or pregnant hamsters.	Disulfides	59-68	prolactin family 3, subfamily b, member 1	Mus musculus	31-36
2752977-11	1989	These similarities and the ability of hamster PL-II to form a disulfide-bonded complex with alpha 2-macroglobulin in vitro suggest that the major circulating form of PL-II in the hamster may be a disulfide-bonded complex of one or more PL monomers with alpha 2-macroglobulin or a related plasma protein.	Disulfides	62-71	prolactin family 3, subfamily b, member 1	Mus musculus	46-51
2752977-11	1989	These similarities and the ability of hamster PL-II to form a disulfide-bonded complex with alpha 2-macroglobulin in vitro suggest that the major circulating form of PL-II in the hamster may be a disulfide-bonded complex of one or more PL monomers with alpha 2-macroglobulin or a related plasma protein.	Disulfides	196-205	prolactin family 3, subfamily b, member 1	Mus musculus	46-51
7861137-4	1995	Involvement of ANF-R2 receptors in the modulation of nicotinic currents was further supported by the significant loss of this inhibitory activity after the cleavage of the disulfide-bridged structure of C-ANF.	Disulfides	172-181	natriuretic peptide A	Bos taurus	15-18
7861137-4	1995	Involvement of ANF-R2 receptors in the modulation of nicotinic currents was further supported by the significant loss of this inhibitory activity after the cleavage of the disulfide-bridged structure of C-ANF.	Disulfides	172-181	natriuretic peptide A	Bos taurus	205-208
7532281-3	1995	The 170-kDa Ret protein present on the cell surface of transformed cells was highly phosphorylated on tyrosine and formed disulfide-linked homodimers.	Disulfides	122-131	ret proto-oncogene	Homo sapiens	12-15
23929130-2	2013	Functional disulfide bridging of the single interchain disulfide bond of a trastuzumab Fab fragment yields a homogeneous antibody-drug conjugate bearing a thiomaleamic acid linker.	Disulfides	11-20	FA complementation group B	Homo sapiens	87-90
7876079-2	1995	Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism involving transfer of electrons from NADPH via FAD to a redox-active disulfide.	Disulfides	198-207	thioredoxin	Homo sapiens	6-17
7876079-2	1995	Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism involving transfer of electrons from NADPH via FAD to a redox-active disulfide.	Disulfides	198-207	thioredoxin	Homo sapiens	102-113
7876079-11	1995	The inactivation of the disulfide reducing activity of thioredoxin reductase and thioredoxin with a concomitant large increase of the NADPH oxidase activity producing reactive oxygen intermediates may mediate effects of DNCB on cells in vivo.	Disulfides	24-33	thioredoxin	Homo sapiens	55-66
2504035-3	1989	Demonstration of the hinge disulfides in the Fc portion clearly indicated that in IgG2b the primary peptic cleavage occurs on the NH2-terminal side of the inter-heavy chain disulfide bridge.	Disulfides	27-37	immunoglobulin heavy constant gamma 2B	Mus musculus	82-87
2504035-3	1989	Demonstration of the hinge disulfides in the Fc portion clearly indicated that in IgG2b the primary peptic cleavage occurs on the NH2-terminal side of the inter-heavy chain disulfide bridge.	Disulfides	27-36	immunoglobulin heavy constant gamma 2B	Mus musculus	82-87
2497183-4	1989	The invariant IgV disulfide loop has been replaced by a unique, short loop involving an unusual cysteine which is conserved in the CD8 alpha-chains of man, mouse, and rat.	Disulfides	18-27	CD8a molecule	Homo sapiens	131-140
7876079-11	1995	The inactivation of the disulfide reducing activity of thioredoxin reductase and thioredoxin with a concomitant large increase of the NADPH oxidase activity producing reactive oxygen intermediates may mediate effects of DNCB on cells in vivo.	Disulfides	24-33	thioredoxin	Homo sapiens	81-92
23929130-2	2013	Functional disulfide bridging of the single interchain disulfide bond of a trastuzumab Fab fragment yields a homogeneous antibody-drug conjugate bearing a thiomaleamic acid linker.	Disulfides	55-64	FA complementation group B	Homo sapiens	87-90
23769672-0	2013	ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor.	Disulfides	67-77	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	0-5
7862635-8	1995	We conclude that gamma IIH is a thiol oxidation product of gamma II-crystallin and is a dimer containing an intermolecular disulfide crosslink.	Disulfides	123-132	G protein subunit gamma 7	Bos taurus	17-25
2523387-1	1989	Heparitinase digestion of the hydrophobic membrane-associated heparan sulfate proteoglycans (HSPG) of fetal human lung fibroblasts yields core proteins of various sizes: i.e. monomeric core proteins of 125, 90, 64, 48, and 35 kDa and a disulfide-linked dimeric core protein composed of approximately 35-kDa subunits.	Disulfides	236-245	syndecan 2	Homo sapiens	62-91
2523387-1	1989	Heparitinase digestion of the hydrophobic membrane-associated heparan sulfate proteoglycans (HSPG) of fetal human lung fibroblasts yields core proteins of various sizes: i.e. monomeric core proteins of 125, 90, 64, 48, and 35 kDa and a disulfide-linked dimeric core protein composed of approximately 35-kDa subunits.	Disulfides	236-245	syndecan 2	Homo sapiens	93-97
7849038-7	1995	Binding of the disulfide-bonded dimers of Gin to a recombination site was strongly reduced, suggesting that the subunits need to reorient in order to form a stable protein-DNA complex.	Disulfides	15-24	recombinase family protein	Escherichia phage Mu	42-45
23769672-0	2013	ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor.	Disulfides	67-77	low density lipoprotein receptor	Homo sapiens	105-117
23769672-3	2013	Here we identify a number of endogenous substrates that form mixed disulfides with ERdj5, greatly expanding its client repertoire.	Disulfides	67-77	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	83-88
23769672-4	2013	ERdj5 previously had been thought to exclusively reduce disulfides in proteins destined for dislocation to the cytosol for degradation.	Disulfides	56-66	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	0-5
23769672-6	2013	Our results demonstrate that the crucial role of ERdj5 is to reduce non-native disulfides formed during productive folding and that this requirement is dependent on its interaction with BiP.	Disulfides	79-89	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	49-54
7834639-1	1995	Thioredoxin (TRX), a disulfide-reducing intracellular dithiol enzyme, is synthesized by both normal liver cells and the hepatocarcinoma cell line HepG2.	Disulfides	21-30	thioredoxin	Homo sapiens	0-11
2653437-1	1989	Mercuric reductase, with FAD and a reducible disulfide at the active site, catalyzes the two-electron reduction of Hg(II) by NADPH.	Disulfides	45-54	2,4-dienoyl-CoA reductase 1	Homo sapiens	125-130
23769672-7	2013	Hence, ERdj5 acts as the ER reductase, both preparing misfolded proteins for degradation and catalyzing the folding of proteins that form obligatory non-native disulfides.	Disulfides	160-170	DnaJ heat shock protein family (Hsp40) member C10	Homo sapiens	7-12
7834639-1	1995	Thioredoxin (TRX), a disulfide-reducing intracellular dithiol enzyme, is synthesized by both normal liver cells and the hepatocarcinoma cell line HepG2.	Disulfides	21-30	thioredoxin	Homo sapiens	13-16
23434438-0	2013	Disulfide reduction abolishes tissue factor cofactor function.	Disulfides	0-9	coagulation factor III, tissue factor	Homo sapiens	30-43
7815553-5	1995	In all cases, the glycoproteins that activate EpoR are processed to cell surfaces as disulfide-bonded dimers.	Disulfides	85-94	erythropoietin receptor	Mus musculus	46-50
2603816-5	1989	It has been shown from the sequence of kallikrein that Arg(-1)-Ile(1) and Arg(87)-Gln(88) bonds are hydrolyzed with trypsin on rapid activation of prokallikrein and the formation of disulfide-linked two chain kallikrein.	Disulfides	182-191	kallikrein related peptidase 4	Homo sapiens	39-49
2603816-5	1989	It has been shown from the sequence of kallikrein that Arg(-1)-Ile(1) and Arg(87)-Gln(88) bonds are hydrolyzed with trypsin on rapid activation of prokallikrein and the formation of disulfide-linked two chain kallikrein.	Disulfides	182-191	kallikrein related peptidase 4	Homo sapiens	150-160
23434438-1	2013	BACKGROUND: Tissue factor (TF), an in vivo initiator of blood coagulation, is a transmembrane protein and has two disulfides in the extracellular domain.	Disulfides	114-124	coagulation factor III, tissue factor	Homo sapiens	12-25
23434438-1	2013	BACKGROUND: Tissue factor (TF), an in vivo initiator of blood coagulation, is a transmembrane protein and has two disulfides in the extracellular domain.	Disulfides	114-124	coagulation factor III, tissue factor	Homo sapiens	27-29
2493819-6	1989	The disulfide reductants dithiothreitol and 2-mercaptoethanol both inhibited GP acrosin, as did the sulfhydryl reactant, iodoacetic acid.	Disulfides	4-13	acrosin	Cavia porcellus	80-87
7827133-7	1995	Modification of gamma II-crystallin by methylglyoxal produced an overall loss of positive charge and an increase in molecular weight and non-disulfide covalent crosslinking.	Disulfides	141-150	G protein subunit gamma 7	Bos taurus	16-24
23434438-4	2013	METHODS: The status of disulfides in recombinant TF1-263 and natural placental TF in their non-reduced native and reduced forms was determined by mass-spectrometry.	Disulfides	23-33	coagulation factor III, tissue factor	Homo sapiens	49-51
23434438-8	2013	CONCLUSION: The reduction of TF disulfides (with or without alkylation) eliminates TF regulation of factor VIIa catalytic function in both membrane dependent FX activation and membrane independent synthetic substrate hydrolysis.	Disulfides	32-42	coagulation factor III, tissue factor	Homo sapiens	29-31
23434438-8	2013	CONCLUSION: The reduction of TF disulfides (with or without alkylation) eliminates TF regulation of factor VIIa catalytic function in both membrane dependent FX activation and membrane independent synthetic substrate hydrolysis.	Disulfides	32-42	coagulation factor III, tissue factor	Homo sapiens	83-85
2473333-2	1989	The disulfide structures of ET-3 and sarafotoxin S6b were found to be identical with that of ET-1 (type A) but distinct from that of apamin (type B).	Disulfides	4-13	endothelin 3	Homo sapiens	28-32
8573606-3	1995	MEN 2A mutations involved cysteine residues in the extracellular domain and induced disulfide-linked homodimerization of the Ret protein on the cell surface, leading to activation of its intrinsic tyrosine kinase.	Disulfides	84-93	ret proto-oncogene	Homo sapiens	0-6
23538787-0	2013	Synthesis of the IGF-II-like hormone vesiculin using regioselective formation of disulfide bonds.	Disulfides	81-90	insulin-like growth factor 2	Mus musculus	17-23
8573606-3	1995	MEN 2A mutations involved cysteine residues in the extracellular domain and induced disulfide-linked homodimerization of the Ret protein on the cell surface, leading to activation of its intrinsic tyrosine kinase.	Disulfides	84-93	ret proto-oncogene	Homo sapiens	125-128
3198118-3	1988	GPIIb-IIIa is a heterodimer complex composed of GPIIb (the alpha subunit), which consists of two disulfide-linked heavy and light chains, and GPIIIa (the beta subunit), which is a single polypeptide chain.	Disulfides	97-106	integrin subunit alpha 2b	Homo sapiens	0-5
23553626-4	2013	Either breaking the disulfide bond or deleting the disulfide bond-occluded segment in the W1 beta4-beta1 loop inhibited rolling cell adhesion supported by the low-affinity interaction between MAdCAM-1 and inactive alpha4beta7 but negligibly affected firm cell adhesion supported by the high-affinity interaction between MAdCAM-1 and Mn(2+)-activated alpha4beta7.	Disulfides	51-60	mucosal vascular addressin cell adhesion molecule 1	Homo sapiens	192-200
3198118-3	1988	GPIIb-IIIa is a heterodimer complex composed of GPIIb (the alpha subunit), which consists of two disulfide-linked heavy and light chains, and GPIIIa (the beta subunit), which is a single polypeptide chain.	Disulfides	97-106	integrin subunit alpha 2b	Homo sapiens	48-53
3182800-13	1988	The beta-hairpin structure of the processing region was found to (i) interact with the activation peptide of the procathepsin D in a beta-structure and (ii) place the Cys residue in the processing region within disulfide linkage distance to Cys-27 of cathepsin D light chain.	Disulfides	211-220	cathepsin D	Bos taurus	116-127
7947765-2	1994	The peptide corresponds to amino acid residues Glu408-Glu426 of thrombomodulin and contains the third disulfide loop of EGF5 and its linker to EGF6.	Disulfides	102-111	thrombomodulin	Homo sapiens	64-78
7979362-2	1994	Thioredoxins undergo reversible redox change through a disulfide group (S-S--&gt;2 SH).	Disulfides	55-64	thioredoxin	Homo sapiens	0-12
23553626-4	2013	Either breaking the disulfide bond or deleting the disulfide bond-occluded segment in the W1 beta4-beta1 loop inhibited rolling cell adhesion supported by the low-affinity interaction between MAdCAM-1 and inactive alpha4beta7 but negligibly affected firm cell adhesion supported by the high-affinity interaction between MAdCAM-1 and Mn(2+)-activated alpha4beta7.	Disulfides	51-60	mucosal vascular addressin cell adhesion molecule 1	Homo sapiens	320-328
23464809-8	2013	The results of the present study identified an HJV/RGMc molecular species containing four disulfide linkages.	Disulfides	90-99	hemojuvelin BMP co-receptor	Homo sapiens	47-50
7929403-3	1994	We have used site-directed mutagenesis of RTA cDNA to convert Cys171 to Ser and to introduce a disulfide bond into RTA by converting Ser215 and Met255 to Cys residues.	Disulfides	95-104	MAS related GPR family member F	Homo sapiens	42-45
7929403-3	1994	We have used site-directed mutagenesis of RTA cDNA to convert Cys171 to Ser and to introduce a disulfide bond into RTA by converting Ser215 and Met255 to Cys residues.	Disulfides	95-104	MAS related GPR family member F	Homo sapiens	115-118
7929403-4	1994	Mutant RTA was expressed in Escherichia coli and directed to the oxidizing environment of the periplasmic space where the Cys215-Cys255 disulfide bond was formed.	Disulfides	136-145	MAS related GPR family member F	Homo sapiens	7-10
7929403-5	1994	The disulfide-containing RTA mutant had an in vitro catalytic activity similar to that of an identical form of recombinant RTA that lacked the S215C and M255C mutations.	Disulfides	4-13	MAS related GPR family member F	Homo sapiens	25-28
3255380-6	1988	Analysis of the near-ultraviolet spectra of factor IX and prothrombin suggests that several aromatic amino acid residues and the disulfide bond present in their gamma-carboxyglutamic acid-containing regions are exposed to solvent and are perturbed by the above pH adjustment and Ca2+ addition.	Disulfides	129-138	coagulation factor II, thrombin	Bos taurus	58-69
7929403-5	1994	The disulfide-containing RTA mutant had an in vitro catalytic activity similar to that of an identical form of recombinant RTA that lacked the S215C and M255C mutations.	Disulfides	4-13	MAS related GPR family member F	Homo sapiens	123-126
2458152-9	1988	Both non-disulfide-bonded and disulfide-bonded vitronectin bound to antibody-Sepharose from a mixture of vitronectin and thrombin-antithrombin III.	Disulfides	30-39	vitronectin	Homo sapiens	47-58
7929403-7	1994	Incubation of this holotoxin with increasing concentrations of dithiothreitol showed that the interchain disulfide bond joining RTA and RTB was more readily reduced than the intrachain disulfide bond in RTA.	Disulfides	105-114	MAS related GPR family member F	Homo sapiens	128-131
23464809-8	2013	The results of the present study identified an HJV/RGMc molecular species containing four disulfide linkages.	Disulfides	90-99	hemojuvelin BMP co-receptor	Homo sapiens	51-55
7929403-7	1994	Incubation of this holotoxin with increasing concentrations of dithiothreitol showed that the interchain disulfide bond joining RTA and RTB was more readily reduced than the intrachain disulfide bond in RTA.	Disulfides	185-194	MAS related GPR family member F	Homo sapiens	203-206
7929403-8	1994	Ricin in which the RTA moiety contained the disulfide bond was 15-18-fold less cytotoxic to HeLa or Vero cells than ricin in which the RTA did not contain the stabilizing disulfide cross-link.	Disulfides	44-53	MAS related GPR family member F	Homo sapiens	19-22
2458152-9	1988	Both non-disulfide-bonded and disulfide-bonded vitronectin bound to antibody-Sepharose from a mixture of vitronectin and thrombin-antithrombin III.	Disulfides	30-39	vitronectin	Homo sapiens	105-116
7929403-9	1994	Since these ricin molecules had identical RTB cell binding and RTA catalytic activities, we suggest that the observed reduction in cytotoxicity caused by the introduced disulfide bond resulted from a constraint on the unfolding of RTA, indicating that such unfolding is necessary for the membrane translocation of RTA during its entry into the cytosol.	Disulfides	169-178	MAS related GPR family member F	Homo sapiens	63-66
23592195-0	2013	Characterization of disulfide linkages in recombinant human granulocyte-colony stimulating factor.	Disulfides	20-29	colony stimulating factor 3	Homo sapiens	60-97
7929403-9	1994	Since these ricin molecules had identical RTB cell binding and RTA catalytic activities, we suggest that the observed reduction in cytotoxicity caused by the introduced disulfide bond resulted from a constraint on the unfolding of RTA, indicating that such unfolding is necessary for the membrane translocation of RTA during its entry into the cytosol.	Disulfides	169-178	MAS related GPR family member F	Homo sapiens	231-234
7929403-9	1994	Since these ricin molecules had identical RTB cell binding and RTA catalytic activities, we suggest that the observed reduction in cytotoxicity caused by the introduced disulfide bond resulted from a constraint on the unfolding of RTA, indicating that such unfolding is necessary for the membrane translocation of RTA during its entry into the cytosol.	Disulfides	169-178	MAS related GPR family member F	Homo sapiens	231-234
2850146-3	1988	Of these 29 amino acids, three are cysteines, suggesting a more extensive disulfide-bond mediated secondary structure for TGF-beta 2,442 than for TGF-beta 2,414.	Disulfides	74-83	transforming growth factor beta 2	Homo sapiens	122-132
23592195-2	2013	The reported major disulfide (S-S) linkages in mature human G-CSF are C36 -C42 and C64 -C74 , leaving C17 as a free cysteine, which could potentially result in S-S scrambling.	Disulfides	19-28	colony stimulating factor 3	Homo sapiens	60-65
23592195-2	2013	The reported major disulfide (S-S) linkages in mature human G-CSF are C36 -C42 and C64 -C74 , leaving C17 as a free cysteine, which could potentially result in S-S scrambling.	Disulfides	19-28	cytokine like 1	Homo sapiens	102-105
3165051-1	1988	Platelet-derived growth factor (PDGF), a potent mitogen for mesenchymal cells, consists of PDGF-1 and PDGF-2 polypeptide chains which are linked by disulfide bonds.	Disulfides	148-157	platelet derived growth factor subunit A	Homo sapiens	91-97
7937748-0	1994	One disulfide bond in front of the second heavy chain constant region is necessary and sufficient for effector functions of human IgG3 without a genetic hinge.	Disulfides	4-13	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	130-134
7937748-6	1994	The results indicate that a hinge spacer region is not necessary, but the correct alignment of the two second heavy chain constant regions in the IgG3 molecule by a minimum of one disulfide bond is necessary and sufficient for effector functions.	Disulfides	180-189	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	146-150
3165051-1	1988	Platelet-derived growth factor (PDGF), a potent mitogen for mesenchymal cells, consists of PDGF-1 and PDGF-2 polypeptide chains which are linked by disulfide bonds.	Disulfides	148-157	platelet derived growth factor subunit B	Homo sapiens	102-108
23418776-4	2013	The state-dependent formation of a disulfide bridge between Cys3 and an endogenous cysteine residue at position 723 in the C-terminal C-linker suggests that the N-terminal tail of HERG can also get into close proximity with the C-linker structures located at the bottom of helix S6.	Disulfides	35-44	potassium voltage-gated channel subfamily H member 2	Homo sapiens	180-184
3260917-6	1988	One heterodimer, composed of disulfide-linked 41- to 45-kDa protein (including a V gamma/C gamma 4 component), is expressed on a T cell hybridoma, DN-1.21, which was derived from fused splenic CD3+, CD4-, CD8- T cells.	Disulfides	29-38	CD4 antigen	Mus musculus	199-202
7727388-0	1994	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.	Disulfides	4-13	natriuretic peptide receptor 3	Homo sapiens	60-90
7727388-3	1994	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.	Disulfides	76-85	natriuretic peptide receptor 3	Homo sapiens	53-58
7524419-0	1994	Disulfide bond formation by methanethiolation of the thiol ester sulfhydryl group of alpha 2M.	Disulfides	0-9	alpha-2-macroglobulin	Homo sapiens	85-93
23515283-4	2013	Clusterin, an 80-kDa disulfide-linked heterodimeric protein, has been functionally implicated in several physiological processes including lipid transport; however, little is known about its effect on hepatic lipogenesis.	Disulfides	21-30	clusterin	Mus musculus	0-9
8082769-0	1994	The disulfide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans-Golgi network.	Disulfides	4-13	chromogranin B	Rattus norvegicus	22-36
23526702-1	2013	Urotensin II (U-II) is a disulfide bridged peptide hormone identified as the ligand of a G-protein-coupled receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	0-12
8082769-2	1994	Reduction of the single, highly conserved intramolecular disulfide bond of chromogranin B by exposure of intact PC12 cells to the thiol reducing agent dithiothreitol has previously been shown to cause its missorting to the constitutive pathway of secretion.	Disulfides	57-66	chromogranin B	Rattus norvegicus	75-89
8082769-4	1994	This implies that the loop in the chromogranin B polypeptide that is formed by the disulfide bond has a critical role in the membrane recognition of aggregated chromogranin B during secretory granule formation.	Disulfides	83-92	chromogranin B	Rattus norvegicus	34-48
8082769-4	1994	This implies that the loop in the chromogranin B polypeptide that is formed by the disulfide bond has a critical role in the membrane recognition of aggregated chromogranin B during secretory granule formation.	Disulfides	83-92	chromogranin B	Rattus norvegicus	160-174
2969292-6	1988	Further analyses indicated that the CD8-class I MHC association is due, in part at least, to disulfide bonding, which may be susceptible to cleavage during processing of cell lysates.	Disulfides	93-102	CD8a molecule	Homo sapiens	36-39
23526702-1	2013	Urotensin II (U-II) is a disulfide bridged peptide hormone identified as the ligand of a G-protein-coupled receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	14-18
2967296-1	1988	The T cell antigen receptor (TCR) consists of a disulfide-linked TCR-alpha/beta heterodimer that is both structurally and functionally associated with a set of four non-covalently linked membrane proteins termed CD3-gamma, -delta, -epsilon, and -zeta.	Disulfides	48-57	CD3 gamma subunit of T-cell receptor complex	Homo sapiens	212-250
23443659-7	2013	Active ATPZs were found to promote the oxidation of the two cysteine residues within 4-R Tau by a redox cycling mechanism, resulting in the formation of a disulfide-containing compact monomer that was refractory to fibrillization.	Disulfides	155-164	microtubule associated protein tau	Homo sapiens	89-92
3042032-7	1988	The purified PH-20 protein exists in three forms separable on SDS-polyacrylamide gel electrophoresis: a major form with a molecular mass of 64 kDa, a minor form of 56 kDa, and an endoproteolytically cleaved form composed of two disulfide-linked fragments of 41-48 kDa and 27 kDa.	Disulfides	228-237	hyaluronidase PH-20	Cavia porcellus	13-18
7519475-6	1994	Antigenicity of the PlA1 fusion protein in reduced glutathione increases with time; moreover, the addition of oxidized glutathione accelerates this process, presumably because of formation of the native disulfide bonds.	Disulfides	203-212	POU class 2 homeobox 3	Homo sapiens	20-24
7983162-6	1994	The predominant components of annexin II were basic, with pI of 6.5-8.5, and some of them formed disulfide-linked monomeric multimers under non-reducing conditions.	Disulfides	97-106	annexin A2	Homo sapiens	30-40
23443659-8	2013	Moreover, the ATPZs facilitated intermolecular disulfide formation between 3-R Tau monomers, leading to dimers that were capable of fibrillization.	Disulfides	47-56	microtubule associated protein tau	Homo sapiens	79-82
7515504-1	1994	Decapentaplegic Vg-related protein 6 (DVR-6 or bone morphogenetic protein BMP-6) is a member of the DVR subgroup of the transforming growth factor beta superfamily, a large group of multifunctional signaling polypeptides that are expressed as secreted disulfide-bonded dimers proteolytically cleaved from larger precursors.	Disulfides	252-261	bone morphogenetic protein 6	Mus musculus	74-79
23449976-5	2013	As a secreted multimeric protein, CTRP11 forms disulfide-linked oligomers.	Disulfides	47-56	complement C1q like 4	Homo sapiens	34-40
7515683-5	1994	However, correct disulfide bonds are formed very efficiently when insulin-like growth factor binding protein 1 is added in equimolar amounts to IGF-I to the refolding mixture.	Disulfides	17-26	insulin like growth factor binding protein 1	Homo sapiens	66-110
3401446-1	1988	Ca2+ stimulates disulfide cross-linking between the S100b beta-subunit and the microtubule-associated tau(2) protein.	Disulfides	16-25	S100 calcium binding protein B	Bos taurus	52-57
3401446-6	1988	The difference in the effects of Ca2+ and Zn2+ on the reactivity of Cys-84 beta in S100b was confirmed when we observed that Ca2+ and Zn2+ have opposite actions on the formation of disulfide bridges between Cys-84 beta of the S100b beta-subunit and sulfhydryl groups on the microtubule-associated tau(2) protein.	Disulfides	181-190	S100 calcium binding protein B	Bos taurus	83-88
3067188-1	1988	PDGF isolated from platelets and forms of PDGF produced by cells transformed with the v-sis gene (PDGF B chain) or U-20S osteosarcoma cells which express the PDGF A chain gene are known to be processed as disulfide-linked dimers of approximately 30 kd.	Disulfides	205-214	platelet derived growth factor subunit A	Homo sapiens	158-170
23516120-11	2013	Targets of Trx, such as phosphoribulokinase, glyceraldehyde-3-phosphate dehydrogenase, transketolase, and sedoheptulose-1,7-bisphosphatase have at least one regulatory disulfide bridge which supports the conclusion that the identified proteins undergo reversible thiol oxidation.	Disulfides	168-177	thioredoxin	Homo sapiens	11-14
8196600-3	1994	A constitutively active (factor-independent) mutant of the erythropoietin receptor (EPO-R), R129C in the exoplasmic domain, forms disulfide-linked homodimers, suggesting that the wild-type EPO-R is activated by ligand-induced homodimerization.	Disulfides	130-139	erythropoietin receptor	Homo sapiens	59-82
8196600-3	1994	A constitutively active (factor-independent) mutant of the erythropoietin receptor (EPO-R), R129C in the exoplasmic domain, forms disulfide-linked homodimers, suggesting that the wild-type EPO-R is activated by ligand-induced homodimerization.	Disulfides	130-139	erythropoietin receptor	Homo sapiens	84-89
8172900-3	1994	Apa-1 contains the native disulfide bond between Cys1 and Cys11.	Disulfides	26-35	cystin 1	Homo sapiens	49-53
3481677-0	1987	Determination of isoelectric point value of 3-mercaptopyruvate sulfurtransferase by isoelectric focusing using ribonuclease A-glutathione mixed disulfides as standards.	Disulfides	144-154	mercaptopyruvate sulfurtransferase	Rattus norvegicus	44-80
23416356-5	2013	We developed a whole protein mixed disulfide interaction assay that showed that Ost6p could form mixed disulfide bonds with selected cysteines in pre-reduced yeast Gas1p, a model glycoprotein substrate of Ost3p and Ost6p.	Disulfides	35-44	dolichyl-diphosphooligosaccharide--protein glycotransferase	Saccharomyces cerevisiae S288C	80-85
2445737-6	1987	By studying the binding of C8 to the 1-112 disulfide-bonded part of hCG-beta (hCG-beta core) recombined with hCG-alpha, we were able to confirm that C8 binds to a region including or near to Asp112.	Disulfides	43-52	chorionic gonadotropin subunit beta 3	Homo sapiens	68-76
2445737-6	1987	By studying the binding of C8 to the 1-112 disulfide-bonded part of hCG-beta (hCG-beta core) recombined with hCG-alpha, we were able to confirm that C8 binds to a region including or near to Asp112.	Disulfides	43-52	chorionic gonadotropin subunit beta 3	Homo sapiens	78-86
8069231-3	1994	The recovery of all the 5,5"-dithio-bis(2-nitro-benzoic acid)-titratable thiol groups as well as the original catalytic activity of GST P1-1 after treatment of the inhibited enzyme with dithiothreitol indicates that two disulfide bridges per dimer, likely between Cys47 and Cys101, have been formed during the reaction with calvatic acid.	Disulfides	220-229	glutathione S-transferase pi 1	Homo sapiens	132-140
23416356-5	2013	We developed a whole protein mixed disulfide interaction assay that showed that Ost6p could form mixed disulfide bonds with selected cysteines in pre-reduced yeast Gas1p, a model glycoprotein substrate of Ost3p and Ost6p.	Disulfides	35-44	1,3-beta-glucanosyltransferase GAS1	Saccharomyces cerevisiae S288C	164-169
8045680-4	1994	The antigen belongs to the three-disulfide epidermal growth factor (EGF) family based on the alignment of the six cysteines.	Disulfides	33-42	epidermal growth factor	Homo sapiens	43-66
23416356-5	2013	We developed a whole protein mixed disulfide interaction assay that showed that Ost6p could form mixed disulfide bonds with selected cysteines in pre-reduced yeast Gas1p, a model glycoprotein substrate of Ost3p and Ost6p.	Disulfides	35-44	dolichyl-diphosphooligosaccharide--protein glycotransferase OST3	Saccharomyces cerevisiae S288C	205-210
8045680-4	1994	The antigen belongs to the three-disulfide epidermal growth factor (EGF) family based on the alignment of the six cysteines.	Disulfides	33-42	epidermal growth factor	Homo sapiens	68-71
23416356-5	2013	We developed a whole protein mixed disulfide interaction assay that showed that Ost6p could form mixed disulfide bonds with selected cysteines in pre-reduced yeast Gas1p, a model glycoprotein substrate of Ost3p and Ost6p.	Disulfides	35-44	dolichyl-diphosphooligosaccharide--protein glycotransferase	Saccharomyces cerevisiae S288C	215-220
8045680-6	1994	Furthermore, disulfide pairing would produce a non-EGF pattern.	Disulfides	13-22	epidermal growth factor	Homo sapiens	51-54
23416356-5	2013	We developed a whole protein mixed disulfide interaction assay that showed that Ost6p could form mixed disulfide bonds with selected cysteines in pre-reduced yeast Gas1p, a model glycoprotein substrate of Ost3p and Ost6p.	Disulfides	103-112	dolichyl-diphosphooligosaccharide--protein glycotransferase	Saccharomyces cerevisiae S288C	80-85
23416356-5	2013	We developed a whole protein mixed disulfide interaction assay that showed that Ost6p could form mixed disulfide bonds with selected cysteines in pre-reduced yeast Gas1p, a model glycoprotein substrate of Ost3p and Ost6p.	Disulfides	103-112	1,3-beta-glucanosyltransferase GAS1	Saccharomyces cerevisiae S288C	164-169
23416356-5	2013	We developed a whole protein mixed disulfide interaction assay that showed that Ost6p could form mixed disulfide bonds with selected cysteines in pre-reduced yeast Gas1p, a model glycoprotein substrate of Ost3p and Ost6p.	Disulfides	103-112	dolichyl-diphosphooligosaccharide--protein glycotransferase OST3	Saccharomyces cerevisiae S288C	205-210
23416356-6	2013	A complementary peptide affinity chromatography assay for mixed disulfide bond formation showed that Ost3p could also form mixed disulfide bonds with cysteines in selected reduced tryptic peptides from Gas1p.	Disulfides	64-73	dolichyl-diphosphooligosaccharide--protein glycotransferase OST3	Saccharomyces cerevisiae S288C	101-106
7509003-2	1994	The Env-Sea oncoprotein is synthesized as a precursor of 155 kDa which undergoes proteolytic processing to generate a disulfide-linked complex of the proteins gp85 and gp70.	Disulfides	118-127	S13 erythroblastosis (avian) oncogene homolog	Homo sapiens	8-11
3498943-2	1987	It is a disulfide-bonded heterodimer in which either the alpha or alpha" polypeptide chain encoded by Ly-2 is covalently linked to the beta polypeptide chain encoded by Ly-3.	Disulfides	8-17	CD8 antigen, beta chain 1	Mus musculus	169-173
23416356-6	2013	A complementary peptide affinity chromatography assay for mixed disulfide bond formation showed that Ost3p could also form mixed disulfide bonds with cysteines in selected reduced tryptic peptides from Gas1p.	Disulfides	129-138	dolichyl-diphosphooligosaccharide--protein glycotransferase OST3	Saccharomyces cerevisiae S288C	101-106
23416356-6	2013	A complementary peptide affinity chromatography assay for mixed disulfide bond formation showed that Ost3p could also form mixed disulfide bonds with cysteines in selected reduced tryptic peptides from Gas1p.	Disulfides	129-138	1,3-beta-glucanosyltransferase GAS1	Saccharomyces cerevisiae S288C	202-207
3040761-8	1987	P24 co-migrated with GP Ib beta on reduced gels (Mr = 24,000) and also on nonreduced gels (when GP Ib beta is disulfide-linked to GP Ib alpha and migrates with Mr = 170,000).	Disulfides	110-119	glycoprotein Ib platelet subunit beta	Homo sapiens	96-106
8017105-2	1994	Under normal conditions, the vacuolar enzyme carboxypeptidase Y (CPY) and the secretory stress-protein hsp150 acquired disulfide bonds in the endoplasmic reticulum (ER).	Disulfides	119-128	heat shock protein HSP150	Saccharomyces cerevisiae S288C	103-109
23416356-7	2013	Together, these assays showed that the thioredoxin-like active sites of Ost3p and Ost6p could form transient mixed disulfide bonds with cysteines in a model substrate glycoprotein, consistent with the function of Ost3p and Ost6p in modulating N-glycosylation substrate selection by OTase in vivo.	Disulfides	115-124	dolichyl-diphosphooligosaccharide--protein glycotransferase OST3	Saccharomyces cerevisiae S288C	72-77
8017105-3	1994	Treatment of living cells with the reducing agent dithiothreitol (DTT) prevented disulfide formation of newly synthesized CPY and hsp150, resulting in retention of the proteins in the ER.	Disulfides	81-90	heat shock protein HSP150	Saccharomyces cerevisiae S288C	130-136
23416356-7	2013	Together, these assays showed that the thioredoxin-like active sites of Ost3p and Ost6p could form transient mixed disulfide bonds with cysteines in a model substrate glycoprotein, consistent with the function of Ost3p and Ost6p in modulating N-glycosylation substrate selection by OTase in vivo.	Disulfides	115-124	dolichyl-diphosphooligosaccharide--protein glycotransferase	Saccharomyces cerevisiae S288C	82-87
23416356-7	2013	Together, these assays showed that the thioredoxin-like active sites of Ost3p and Ost6p could form transient mixed disulfide bonds with cysteines in a model substrate glycoprotein, consistent with the function of Ost3p and Ost6p in modulating N-glycosylation substrate selection by OTase in vivo.	Disulfides	115-124	dolichyl-diphosphooligosaccharide--protein glycotransferase OST3	Saccharomyces cerevisiae S288C	213-218
3476488-3	1987	Human TGF-beta 2 consists of two disulfide-linked, identical subunits.	Disulfides	33-42	transforming growth factor beta 2	Homo sapiens	6-16
23416356-7	2013	Together, these assays showed that the thioredoxin-like active sites of Ost3p and Ost6p could form transient mixed disulfide bonds with cysteines in a model substrate glycoprotein, consistent with the function of Ost3p and Ost6p in modulating N-glycosylation substrate selection by OTase in vivo.	Disulfides	115-124	dolichyl-diphosphooligosaccharide--protein glycotransferase	Saccharomyces cerevisiae S288C	223-228
7509599-3	1994	We tested if, in analogy with these redox enzymes, IGFBP-3 could catalyze the isomerization of intramolecular disulfide bridges in protein substrates.	Disulfides	110-119	insulin like growth factor binding protein 3	Homo sapiens	51-58
23416107-3	2013	Here we present a crystal structure of a Ub E1-E2(Ubc4)/Ub/ATP Mg complex that was stabilized by induction of a disulfide bond between the E1 and E2 active sites.	Disulfides	112-121	ubiquitin conjugating enzyme E2 D2	Homo sapiens	50-54
7508448-10	1994	In marked contrast, the oxidation of an additional 6 methionyl residues and a single tryptophanyl residue fractured the alpha 2 M homotetramer across its non-covalent axis into two pairs of disulfide-linked dimers.	Disulfides	190-199	alpha-2-macroglobulin	Homo sapiens	120-129
8307998-0	1994	Assignment of disulfide bonds in corticotropin-releasing factor-binding protein.	Disulfides	14-23	corticotropin releasing hormone	Homo sapiens	33-63
8307998-2	1994	The integrity of the disulfide bonds in the binding protein is essential for this activity as reduction abolishes the protein"s ability to bind corticotropin-releasing factor.	Disulfides	21-30	corticotropin releasing hormone	Homo sapiens	144-174
2966924-3	1987	Like the full-length CSF-1 precursor, the truncated polypeptide was rapidly assembled through disulfide bonds immediately after synthesis and acquired asparagine-linked oligosaccharide chains that underwent progressive post-translational modifications during intracellular transport.	Disulfides	94-103	colony stimulating factor 1 (macrophage)	Mus musculus	21-26
23428047-0	2013	Single-molecule studies of disulfide bond reduction pathways used by human thioredoxin.	Disulfides	27-36	thioredoxin	Homo sapiens	75-86
8300576-12	1994	The results indicate that both CaBP2 and CaBP1 can catalyze the formation of disulfide bonds and protein disulfide isomerization and may thus be involved in the folding of nascent proteins in the secretory pathway.	Disulfides	77-86	calcium binding protein 1	Rattus norvegicus	41-46
8300576-12	1994	The results indicate that both CaBP2 and CaBP1 can catalyze the formation of disulfide bonds and protein disulfide isomerization and may thus be involved in the folding of nascent proteins in the secretory pathway.	Disulfides	105-114	calcium binding protein 1	Rattus norvegicus	41-46
23428047-1	2013	Disulfide bond reduction pathways used by human thioredoxin (hTrx) are studied at the single molecule level using a recombinant protein (I27SS)8.	Disulfides	0-9	thioredoxin	Homo sapiens	48-59
23428047-1	2013	Disulfide bond reduction pathways used by human thioredoxin (hTrx) are studied at the single molecule level using a recombinant protein (I27SS)8.	Disulfides	0-9	thioredoxin	Homo sapiens	61-65
7762432-3	1994	The antimicrobial sequence was found to consist mainly of a loop of 18 amino acid residues formed by a disulfide bond between cysteine residues 20 and 37 of human lactoferrin, or 19 and 36 of bovine lactoferrin.	Disulfides	103-112	lactotransferrin	Bos taurus	163-174
23428047-5	2013	Earlier FC-AFM studies observed one disulfide reduction pathway used by hTrx and suggested an additional electron tunneling mechanism.	Disulfides	36-45	thioredoxin	Homo sapiens	72-76
23428047-7	2013	By analyzing the data using exponential fits and dwell time histograms two disulfide reduction pathways used by hTrx are resolved.	Disulfides	75-84	thioredoxin	Homo sapiens	112-116
23186364-0	2013	Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40.	Disulfides	0-9	growth factor, augmenter of liver regeneration	Homo sapiens	45-48
7747886-7	1994	As a first step towards structural investigations, we have determined the disulfide cross-links of the first domain of uPAR.	Disulfides	74-83	plasminogen activator, urokinase receptor	Homo sapiens	119-123
8131222-11	1994	This suggests that GST P1-1 is inhibited by disulfide formation in the case of 5-GSDA, while this oxidative pathway also substantially contributes to the inactivation by dopamine.	Disulfides	44-53	glutathione S-transferase pi 1	Homo sapiens	19-27
23118027-0	2013	The immunoglobulin domain of the sodium channel beta3 subunit contains a surface-localized disulfide bond that is required for homophilic binding.	Disulfides	91-100	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	48-53
7903251-2	1993	To elucidate the role of disulfide bridges for the allosteric interaction of these agonists we mutated the cysteine residues in the ligand-binding NMDAR1 (NR1 or zeta) subunit of the rodent NMDA receptor and co-expressed the resulting mutants with the NR2B (epsilon 2) subunit in Xenopus oocytes.	Disulfides	25-34	glutamate ionotropic receptor NMDA type subunit 1 L homeolog	Xenopus laevis	147-153
7903251-2	1993	To elucidate the role of disulfide bridges for the allosteric interaction of these agonists we mutated the cysteine residues in the ligand-binding NMDAR1 (NR1 or zeta) subunit of the rodent NMDA receptor and co-expressed the resulting mutants with the NR2B (epsilon 2) subunit in Xenopus oocytes.	Disulfides	25-34	glutamate ionotropic receptor NMDA type subunit 1 L homeolog	Xenopus laevis	155-203
23118027-6	2013	We now confirm the presence of the disulfide bond in beta3 using mass spectrometry, and we show that its integrity is essential for the association of the full-length, membrane-anchored beta3 subunit with itself.	Disulfides	35-44	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	53-58
23118027-6	2013	We now confirm the presence of the disulfide bond in beta3 using mass spectrometry, and we show that its integrity is essential for the association of the full-length, membrane-anchored beta3 subunit with itself.	Disulfides	35-44	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	186-191
23325480-8	2013	Thiol-disulfide exchange involving this disulfide is implicated in TF activation with the formation of the disulfide bond corresponding with the active conformation of TF and free thiol or thiol-modified forms corresponding with encryption.	Disulfides	6-15	coagulation factor III, tissue factor	Homo sapiens	67-69
8241510-1	1993	CD27, a transmembrane disulfide-linked 55-kD homodimer, belongs to the nerve growth factor-receptor family, a group of homologous molecules involved in lymphocyte differentiation and selection.	Disulfides	22-31	CD27 molecule	Homo sapiens	0-4
23325480-8	2013	Thiol-disulfide exchange involving this disulfide is implicated in TF activation with the formation of the disulfide bond corresponding with the active conformation of TF and free thiol or thiol-modified forms corresponding with encryption.	Disulfides	6-15	coagulation factor III, tissue factor	Homo sapiens	168-170
7693702-1	1993	The formation of disulfide bonds in Escherichia coli is catalyzed by periplasmic protein disulfide-isomerase (DsbA).	Disulfides	17-26	protein-disulfide isomerase	Escherichia coli	81-108
23325480-8	2013	Thiol-disulfide exchange involving this disulfide is implicated in TF activation with the formation of the disulfide bond corresponding with the active conformation of TF and free thiol or thiol-modified forms corresponding with encryption.	Disulfides	40-49	coagulation factor III, tissue factor	Homo sapiens	67-69
23325480-8	2013	Thiol-disulfide exchange involving this disulfide is implicated in TF activation with the formation of the disulfide bond corresponding with the active conformation of TF and free thiol or thiol-modified forms corresponding with encryption.	Disulfides	40-49	coagulation factor III, tissue factor	Homo sapiens	168-170
23325480-8	2013	Thiol-disulfide exchange involving this disulfide is implicated in TF activation with the formation of the disulfide bond corresponding with the active conformation of TF and free thiol or thiol-modified forms corresponding with encryption.	Disulfides	40-49	coagulation factor III, tissue factor	Homo sapiens	67-69
23325480-8	2013	Thiol-disulfide exchange involving this disulfide is implicated in TF activation with the formation of the disulfide bond corresponding with the active conformation of TF and free thiol or thiol-modified forms corresponding with encryption.	Disulfides	40-49	coagulation factor III, tissue factor	Homo sapiens	168-170
8232327-0	1993	Human IgG3 can adopt the disulfide bond pattern characteristic for IgG1 without resembling it in complement mediated cell lysis.	Disulfides	25-34	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	6-10
8232327-1	1993	In this paper we describe the construction of mouse-human IgG3 mutant antibodies resembling IgG1 in their disulfide bond pattern between the heavy and light chain (H-L) and between the two heavy chains (H-H).	Disulfides	106-115	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	58-62
8232327-6	1993	This suggests that IgG3 can adopt the H-L disulfide bond pattern of IgG1 without obtaining the CML activity characteristic for IgG1.	Disulfides	42-51	immunoglobulin heavy constant gamma 3 (G3m marker)	Homo sapiens	19-23
23325480-9	2013	Although the exact mechanism by which TF de-encryption occurs remains a subject of debate, thiol blockade and inhibition of oxidoreductases show an important role for thiol-disulfide reactions in platelet-independent pathways of coagulation in vitro and in vivo.	Disulfides	173-182	coagulation factor III, tissue factor	Homo sapiens	38-40
23178719-4	2013	By using specific inhibitors of the various cytosolic protein disulfides reducing systems, we show here that the NADPH-thioredoxin reductase-thioredoxin redox system is the main responsible for this disulfide reduction.	Disulfides	62-72	thioredoxin	Homo sapiens	119-130
8402912-0	1993	A novel disulfide-linked heterodimer on pre-T cells consists of the T cell receptor beta chain and a 33 kd glycoprotein.	Disulfides	8-17	T cell receptor beta chain	Mus musculus	68-94
23178719-4	2013	By using specific inhibitors of the various cytosolic protein disulfides reducing systems, we show here that the NADPH-thioredoxin reductase-thioredoxin redox system is the main responsible for this disulfide reduction.	Disulfides	62-72	thioredoxin	Homo sapiens	141-152
7691976-1	1993	Macrophage stimulating protein (MSP) is a member of a family of proteins characterized by a triple disulfide loop structure (kringle).	Disulfides	99-108	macrophage stimulating 1	Homo sapiens	0-30
23178719-4	2013	By using specific inhibitors of the various cytosolic protein disulfides reducing systems, we show here that the NADPH-thioredoxin reductase-thioredoxin redox system is the main responsible for this disulfide reduction.	Disulfides	62-71	thioredoxin	Homo sapiens	119-130
7691976-1	1993	Macrophage stimulating protein (MSP) is a member of a family of proteins characterized by a triple disulfide loop structure (kringle).	Disulfides	99-108	macrophage stimulating 1	Homo sapiens	32-35
23178719-4	2013	By using specific inhibitors of the various cytosolic protein disulfides reducing systems, we show here that the NADPH-thioredoxin reductase-thioredoxin redox system is the main responsible for this disulfide reduction.	Disulfides	62-71	thioredoxin	Homo sapiens	141-152
25206370-2	2013	Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer.	Disulfides	71-80	thioredoxin	Homo sapiens	95-106
8415618-8	1993	Similar to these findings, both mAb 197 and mAb 4D8 precipitated a 12-kDa disulfide-linked homodimeric protein from digitonin lysates of 125I-labeled human neutrophils after induction of Fc gamma RI expression with interferon gamma but not from unstimulated neutrophils.	Disulfides	74-83	Fc gamma receptor Ia	Homo sapiens	187-198
8344427-4	1993	Thioredoxin, which has higher reducing activity of protein disulfides than PDI, catalyzed the reduction with lower efficiency.	Disulfides	59-69	thioredoxin	Homo sapiens	0-11
2482755-0	1987	Appearance of neoantigen in mouse IgG1 upon reduction of interchain disulfide bridges: assessment of local and general conformational rearrangements using monoclonal antibody and small-angle X-ray scattering.	Disulfides	68-77	LOC105243590	Mus musculus	34-38
25206370-2	2013	Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer.	Disulfides	71-80	thioredoxin	Homo sapiens	108-111
25206370-2	2013	Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer.	Disulfides	71-80	thioredoxin	Homo sapiens	195-199
23461131-1	2013	Human epididymis protein 4 (HE4) is a member of the "four-disulfide core" family that comprises a heterogeneous group of small acid- and heat-stable proteins of divergent function.	Disulfides	58-67	WAP four-disulfide core domain 2	Homo sapiens	0-26
3478092-6	1987	Reduction of interchain disulfide bonds in the growth hormone receptor did not alter its elution from gel filtration columns, but intact, high molecular weight receptor constituents were separated from lower molecular weight degradation products.	Disulfides	24-33	growth hormone receptor	Rattus norvegicus	47-70
8321214-3	1993	Moreover, the mutant chains formed disulfide-bonded heterodimers with the PDGF B chain in NIH 3T3 cells heterodimer underwent the same processing and secretion as PDGF-AB.	Disulfides	35-44	platelet derived growth factor, B polypeptide	Mus musculus	74-80
8397784-4	1993	In contrast, IGF-II folds mainly into a single form with all three disulfide bonds correctly formed.	Disulfides	67-76	insulin like growth factor 2	Homo sapiens	13-19
3298238-9	1987	When the comparison is restricted inside the disulfide bond-containing core (residues 1-110), the beta-subunit of eCG is highly homologous to hCG beta (66%).	Disulfides	45-54	chorionic gonadotropin subunit beta 3	Homo sapiens	142-150
23461131-1	2013	Human epididymis protein 4 (HE4) is a member of the "four-disulfide core" family that comprises a heterogeneous group of small acid- and heat-stable proteins of divergent function.	Disulfides	58-67	WAP four-disulfide core domain 2	Homo sapiens	28-31
22920903-4	2013	Disulfide forming/ isomerizing enzymes like thioredoxin (Trx), protein disulfide isomerase (PDI), which are chaperone proteins, are implicated into transnitrosation reactions, which are the transfer of  NO from one cysteine residue to another one.	Disulfides	0-9	thioredoxin	Homo sapiens	44-55
3475130-5	1987	The purified hTGF-beta 2 has a molecular weight of 24,000 when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and consists of two disulfide-linked, apparently identical polypeptide chains, with a molecular weight of 13,000.	Disulfides	153-162	transforming growth factor beta 2	Homo sapiens	13-24
8491204-0	1993	Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathways.	Disulfides	17-26	chromogranin B	Rattus norvegicus	35-49
22920903-4	2013	Disulfide forming/ isomerizing enzymes like thioredoxin (Trx), protein disulfide isomerase (PDI), which are chaperone proteins, are implicated into transnitrosation reactions, which are the transfer of  NO from one cysteine residue to another one.	Disulfides	0-9	thioredoxin	Homo sapiens	57-60
8491204-0	1993	Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathways.	Disulfides	17-26	chromogranin B	Rattus norvegicus	51-66
8491204-1	1993	The role of the single, highly conserved disulfide bond in chromogranin B (secretogranin I) on the sorting of this regulated secretory protein to secretory granules was investigated in the neuroendocrine cell line PC12.	Disulfides	41-50	chromogranin B	Rattus norvegicus	59-73
22801966-3	2013	Human tissue factor disulfide mutants have been proposed as a model for encrypted tissue factor, but poor expression of these mutants hampers research into tissue factor decryption.	Disulfides	20-29	coagulation factor III, tissue factor	Homo sapiens	6-19
8491204-1	1993	The role of the single, highly conserved disulfide bond in chromogranin B (secretogranin I) on the sorting of this regulated secretory protein to secretory granules was investigated in the neuroendocrine cell line PC12.	Disulfides	41-50	chromogranin B	Rattus norvegicus	75-90
8491204-7	1993	We conclude that the sorting of CgB in the TGN to secretory granules is dependent upon the integrity of its single disulfide bond.	Disulfides	115-124	chromogranin B	Rattus norvegicus	32-35
3552731-0	1987	Mode of disulfide bond formation of a heat-stable enterotoxin (STh) produced by a human strain of enterotoxigenic Escherichia coli.	Disulfides	8-17	saitohin	Homo sapiens	63-66
3552731-1	1987	To determine the modes of three disulfide linkages in the heat-stable enterotoxin (STh) produced by a human strain of enterotoxigenic Escherichia coli, we synthesized STh(6-18), which consists of 13 amino acid residues and has the same intramolecular disulfide linkages as native STh [(1985) FEBS Lett.	Disulfides	32-41	saitohin	Homo sapiens	83-86
3552731-3	1987	Synthesis of the peptide with different modes of disulfide bond formation provided three peptides consistent with standard STh(6-18) in their physicochemical and biological properties, thereby indicating that the disulfide bonds in STh(6-18) are Cys-Cys-Glu-Leu-Cys-Cys-Asn-Pro-Ala-Cys-Thr-Gly-Cys.	Disulfides	49-58	saitohin	Homo sapiens	232-235
3552731-3	1987	Synthesis of the peptide with different modes of disulfide bond formation provided three peptides consistent with standard STh(6-18) in their physicochemical and biological properties, thereby indicating that the disulfide bonds in STh(6-18) are Cys-Cys-Glu-Leu-Cys-Cys-Asn-Pro-Ala-Cys-Thr-Gly-Cys.	Disulfides	213-222	saitohin	Homo sapiens	123-126
3552731-3	1987	Synthesis of the peptide with different modes of disulfide bond formation provided three peptides consistent with standard STh(6-18) in their physicochemical and biological properties, thereby indicating that the disulfide bonds in STh(6-18) are Cys-Cys-Glu-Leu-Cys-Cys-Asn-Pro-Ala-Cys-Thr-Gly-Cys.	Disulfides	213-222	saitohin	Homo sapiens	232-235
3647766-3	1987	Two large disulfide-linked peptides were also produced very slowly, which accompanied the increase in kallikrein activity.	Disulfides	10-19	kallikrein related peptidase 4	Homo sapiens	102-112
3794723-1	1987	A two-step chromatographic procedure has been developed for the purification of ovine pineal arylalkylamine N-acetyltransferase (EC 2.3.1.87), based on the principles of disulfide exchange and anion exchange.	Disulfides	170-179	aralkylamine N-acetyltransferase	Homo sapiens	93-127
2948951-6	1987	A sixth protein, identified in nonreduced 125I-HSPG preparations, appeared as a non-HS chain-bearing Mr 35,000 peptide which was disulfide-linked to an HS chain-bearing peptide of similar size.	Disulfides	129-138	syndecan 2	Homo sapiens	47-51
3528149-9	1986	The following evidence suggests that disulfide bonds mediate the association between the glucocorticoid receptor and the nuclear matrix.	Disulfides	37-46	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	89-112
2423515-3	1986	In particular, the BPTI produced by E. coli had three disulfide bonds that appeared to be identical to those found in native BPTI, as assayed by sensitivity to iodoacetate, dithiothreitol, and urea.	Disulfides	54-63	spleen trypsin inhibitor I	Bos taurus	19-23
2428763-1	1986	The eicosapeptide (Gly88,90) 82-101 hCG-beta was synthesized by the fragment condensation of the nonapeptide (Gly88,90) 82-90 and the undecapeptide 91-101 followed by iodine oxidation to make the disulfide loop.	Disulfides	196-205	chorionic gonadotropin subunit beta 3	Homo sapiens	36-44
3733321-2	1986	The conformation of the cyclic peptide Ac-Cys-Leu-Gla-Gla-Pro-Cys-NHMe, representing the 18-23 disulfide loop of bovine prothrombin, was studied by energy minimization with the ECEPP (Empirical Conformational Energy Program for Peptides) algorithm.	Disulfides	95-104	coagulation factor II, thrombin	Bos taurus	120-131
2937786-4	1986	Probing the reactivity of the disulfide bonds in thrombin-modified proteins indicated that the thrombin cleavage induces a conformational change in the protein.	Disulfides	30-39	coagulation factor II, thrombin	Bos taurus	49-57
2937786-4	1986	Probing the reactivity of the disulfide bonds in thrombin-modified proteins indicated that the thrombin cleavage induces a conformational change in the protein.	Disulfides	30-39	coagulation factor II, thrombin	Bos taurus	95-103
3458201-4	1986	Analysis of the amino acid sequence by several computer programs shows that alpha 1B exhibits internal duplication and consists of five repeating structural domains, each containing about 95 amino acids and one disulfide bond.	Disulfides	211-220	alpha-1-B glycoprotein	Homo sapiens	76-84
2949543-1	1986	Active plasma kallikrein (Mr = 90,000) can be separated by reduction of the disulfide bridges into a heavy-chain (Mr = 45,000) and a light-chain (Mr = 36,000).	Disulfides	76-85	kallikrein related peptidase 4	Homo sapiens	14-24
4066714-0	1985	Sulfhydryl/disulfide forms of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase.	Disulfides	11-20	3-hydroxy-3-methylglutaryl-CoA reductase	Rattus norvegicus	40-87
4079377-0	1985	Covalent chromatography by thiol-disulfide interchange of the highly-purified non-transformed rat liver glucocorticoid-receptor.	Disulfides	33-42	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	104-127
2413033-0	1985	Intersubunit disulfides of the follitropin receptor.	Disulfides	13-23	follicle stimulating hormone receptor	Homo sapiens	31-51
2866732-4	1985	Urea gel electrophoresis revealed that the heterogeneity of lysyl oxidase persists after reduction and alkylation, indicating that disulfide isomers are not the bases of the enzyme heterogeneity.	Disulfides	131-140	lysyl oxidase	Bos taurus	60-73
3929075-1	1985	Bacterial IgA1 proteases have substrate specificity for human IgA1 immunoglobulin, and cleave both the heavy (alpha) chains where they are paired by disulfide bonds in the hinge region.	Disulfides	149-158	immunoglobulin heavy constant alpha 1	Homo sapiens	10-14
3929075-1	1985	Bacterial IgA1 proteases have substrate specificity for human IgA1 immunoglobulin, and cleave both the heavy (alpha) chains where they are paired by disulfide bonds in the hinge region.	Disulfides	149-158	immunoglobulin heavy constant alpha 1	Homo sapiens	62-66
3989305-3	1985	Plasmin degraded pro-HNP in vitro to HNP, which was also isolated from the urine of patients and which contained disulfide-linked polypeptides of beta 60, alpha 38, and alpha 26, and noncovalently bound polypeptide of beta 17.	Disulfides	113-122	kallikrein related peptidase 8	Homo sapiens	37-40
2408618-1	1985	A fragment of rat transforming growth factor alpha (TGF alpha) comprising the third disulfide loop (residues 34-43) was selected as a potential antigenic and receptor binding region.	Disulfides	84-93	transforming growth factor alpha	Rattus norvegicus	18-50
2408618-1	1985	A fragment of rat transforming growth factor alpha (TGF alpha) comprising the third disulfide loop (residues 34-43) was selected as a potential antigenic and receptor binding region.	Disulfides	84-93	transforming growth factor alpha	Rattus norvegicus	52-61
4000128-8	1985	Both native and hinge-disulfide-cleaved IgG experienced similar percentage increases in phi L when bound in SpA complexes.	Disulfides	22-31	surfactant protein A2	Homo sapiens	108-111
3886572-3	1985	Starting from Bowman"s Acetone Insoluble factor, designated Ai, AA and SBTIAA, the Bowman-Birk inhibitor (BBI) was found to be a protein molecule consisting of a chain of 71 amino acids cross linked by 7 disulfide bonds, with a tendency to self-associate.	Disulfides	204-213	Bowman-Birk type proteinase inhibitor	Glycine max	83-104
3886572-3	1985	Starting from Bowman"s Acetone Insoluble factor, designated Ai, AA and SBTIAA, the Bowman-Birk inhibitor (BBI) was found to be a protein molecule consisting of a chain of 71 amino acids cross linked by 7 disulfide bonds, with a tendency to self-associate.	Disulfides	204-213	Bowman-Birk type proteinase inhibitor	Glycine max	106-109
3874157-6	1985	Their elevated concentration within this space may facilitate a low affinity binding interaction between Ly-2 and Ly-3 which is later stabilized by interchain disulfide bond formation.	Disulfides	159-168	CD8 antigen, beta chain 1	Mus musculus	114-118
3917281-2	1985	Previous work on an analytical scale has shown that PC-1 consists of two apparently identical disulfide-bonded polypeptides, each of Mr 115,000.	Disulfides	94-103	minisatellite 6 hypermutable	Mus musculus	52-56
6541480-3	1984	The predominant species ANF-II, which may represent the native form of ANF, has the following sequence: (H2N)-G-P-R-S-L-R-R-S-S-C-F-G-G-R-I-D-R-I-G-A-Q-S-G-L-G-C-N-S-F-R-Y-(COO H) in which Cys-10 and Cys-26 are disulfide linked.	Disulfides	211-220	natriuretic peptide A	Rattus norvegicus	24-27
6541480-3	1984	The predominant species ANF-II, which may represent the native form of ANF, has the following sequence: (H2N)-G-P-R-S-L-R-R-S-S-C-F-G-G-R-I-D-R-I-G-A-Q-S-G-L-G-C-N-S-F-R-Y-(COO H) in which Cys-10 and Cys-26 are disulfide linked.	Disulfides	211-220	natriuretic peptide A	Rattus norvegicus	71-74
6610676-9	1984	Consequently, the NH2-terminal portion (residues 1-21) and the disulfide-linked core region (residues 22-57) in intact C3a serve primarily to stabilize ordered conformation in the COOH-terminal region (residues 58-77) and thereby orient side chains at the essential active site for optimal receptor interaction.	Disulfides	63-72	complement C3	Homo sapiens	119-122
6697984-2	1984	Three disulfide bonds were assigned to Cys-4-Cys-9, Cys-56-Cys-172, and Cys-189-Cys-197 by digestion of intact prolactin with S. aureus protease.	Disulfides	6-15	prolactin	Mus musculus	111-120
6696429-2	1984	The data indicate that NADP-malate dehydrogenase, purified to homogeneity from corn leaves, is activated by a net transfer of reducing equivalents from thioredoxin m, reduced by dithiothreitol, to enzyme disulfide groups, thereby yielding oxidized thioredoxin m and reduced enzyme.	Disulfides	204-213	LOC101027257	Zea mays	152-163
6696429-2	1984	The data indicate that NADP-malate dehydrogenase, purified to homogeneity from corn leaves, is activated by a net transfer of reducing equivalents from thioredoxin m, reduced by dithiothreitol, to enzyme disulfide groups, thereby yielding oxidized thioredoxin m and reduced enzyme.	Disulfides	204-213	LOC101027257	Zea mays	248-259
6387982-8	1984	The crystalline structure of C3a provides valuable new information regarding the alpha helical regions and identifies the arrangement of intra-chain disulfide linkages.	Disulfides	149-158	complement C3	Homo sapiens	29-32
6584866-7	1983	Conserved among the three zymogens are 10 Cys residues that form five disulfide bonds in bovine chymotrypsinogens A and B and the residues that are required for zymogen activation, substrate binding, and catalytic activity.	Disulfides	70-79	chymotrypsinogen A	Bos taurus	96-121
6313673-6	1983	The data indicate, therefore, that the CCK receptor possesses subunit structure whereby an Mr = 76,000 binding subunit is linked to an Mr = 40,000 nonbinding subunit by a disulfide bond.	Disulfides	171-180	cholecystokinin	Mus musculus	39-42
6352703-1	1983	A hybrid molecule was constructed by covalently linking, by a disulfide bridge, the hormone insulin to the binding subunit B of the plant toxin ricin (specificity: Gal, GalNAc).	Disulfides	62-71	insulin	Canis lupus familiaris	92-99
6224554-8	1983	These findings indicate that the formation of mixed disulfide bonds in the tumor Hex B increases the net negative charge and results in the appearance of a heat-labile form.	Disulfides	52-61	hexosaminidase subunit beta	Homo sapiens	81-86
6885778-0	1983	Inactivation of cathepsin B by active site-directed disulfide exchange.	Disulfides	52-61	cathepsin B	Homo sapiens	16-27
6885778-2	1983	The ability of cystamine, bis-N-aminoethyl disulfide, to inactivate cathepsin B by disulfide exchange is considerably enhanced by the addition of hydrophobic residues which apparently occupy secondary binding sites in the extended active center of the protease.	Disulfides	43-52	cathepsin B	Homo sapiens	68-79
7150567-1	1982	Limited tryptic fragmentation of disulfide-intact bovine neurophysins I and II (NP-I and -II, respectively) has been found to cause selective disruption of both hormone binding and neurophysin self-association.	Disulfides	33-42	arginine vasopressin	Bos taurus	57-78
7175439-4	1982	It has a 135,000 mol wt and contains disulfide bonded labeled polypeptide chains of 75,000 and 31,000 mol wt, which presumably represent the beta and a fragment of the alpha-chain of C3b*.	Disulfides	37-46	complement C3	Homo sapiens	183-186
7096338-2	1982	In order to learn at what stage the disulfide bonds of albumin are formed during its biosynthesis, we perfused rat livers with iodoacetamide and then isolated the intracellular precursor, proalbumin, from organelles known to be in the pathway of albumin synthesis and secretion.	Disulfides	36-45	albumin	Rattus norvegicus	55-62
6180832-1	1982	A disulfide-linked conjugate between asialofetuin (ASF) and the toxic A chain (RTA) of ricin is as potent a toxin for cultured rat hepatocytes as our previously described conjugate between ASF and fragment A of diphtheria toxin (DTA).	Disulfides	2-11	RT1 class I, locus A	Rattus norvegicus	79-82
7096304-3	1982	beta 2-Toxin consisted of two dissimilar polypeptides, a (120 amino acid residues) and B (60 amino acid residues) chains, crosslinked by an interchain disulfide bond.	Disulfides	151-160	hemoglobin, beta adult minor chain	Mus musculus	0-6
7199205-1	1982	A 180,000-dalton single-chain molecule (human pro-C3) is the precursor of the third component of human complement (C3), a disulfide-linked two-chain protein.	Disulfides	122-131	complement C3	Homo sapiens	103-117
7342602-3	1981	Cystamine (bis-aminoethyl disulfide) inactivates cathepsin B by formation of a mixed disulfide.	Disulfides	26-35	cathepsin B	Homo sapiens	49-60
7410831-3	1980	Sulfhydryl analysis reveals that two disulfide bonds, both presumed to be situated in the C3 alpha subunit, are broken: one at 2.2 x 10(-2) M and one at 3.5 x 10(-2) M NaBH4.	Disulfides	37-46	complement C3	Homo sapiens	90-98
6154706-2	1980	By limited proteolysis, plasma kallikrein cleaves high Mr kininogen to liberate kinin and gives a molecule containing two disulfide-linked polypeptide chains.	Disulfides	122-131	kallikrein related peptidase 4	Homo sapiens	31-41
6995531-0	1980	Coupling of delta 5,3-ketosteroid isomerase to human placental lactogen with intermolecular disulfide bond formation.	Disulfides	92-101	hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1	Homo sapiens	12-43
88474-1	1979	Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and beta 1H globulin (beta 1H) cleaved the alpha-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact beta-chain (C3bi).	Disulfides	197-206	complement C3	Homo sapiens	18-21
88474-1	1979	Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and beta 1H globulin (beta 1H) cleaved the alpha-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact beta-chain (C3bi).	Disulfides	197-206	complement factor I	Homo sapiens	45-60
88474-1	1979	Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and beta 1H globulin (beta 1H) cleaved the alpha-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact beta-chain (C3bi).	Disulfides	197-206	complement factor I	Homo sapiens	62-68
88474-1	1979	Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and beta 1H globulin (beta 1H) cleaved the alpha-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact beta-chain (C3bi).	Disulfides	197-206	complement factor H	Homo sapiens	74-90
88474-1	1979	Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and beta 1H globulin (beta 1H) cleaved the alpha-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact beta-chain (C3bi).	Disulfides	197-206	complement factor H	Homo sapiens	74-81
88474-1	1979	Treatment of 125I-C3b bound to EAC1423b with C3b inactivator (C3bINA) and beta 1H globulin (beta 1H) cleaved the alpha-chain of C3b into 65,000- and 42,000-dalton fragments, both of which remained disulfide-bonded to the intact beta-chain (C3bi).	Disulfides	197-206	complement C3	Homo sapiens	45-48
36924-2	1979	Circular dichroic spectra were measured for three analogues of deamino-oxytocin of different ring sizes where the disulfide group of oxytocin is replaced by the (CH2)n group.	Disulfides	114-123	oxytocin/neurophysin I prepropeptide	Homo sapiens	133-141
8483943-3	1993	Along the molecular twofold axis, the Fab arms are joined by an interchain disulfide bond between the two light chains.	Disulfides	75-84	FA complementation group B	Homo sapiens	38-41
8466908-0	1993	Pathway of disulfide-coupled unfolding and refolding of bovine alpha-lactalbumin.	Disulfides	11-20	lactalbumin alpha	Bos taurus	63-80
8466908-1	1993	alpha-Lactalbumin"s four disulfide bonds have been used to probe the nature of its native, molten globule, and unfolded states.	Disulfides	25-34	lactalbumin alpha	Bos taurus	0-17
8466909-0	1993	Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin.	Disulfides	35-44	lactalbumin alpha	Bos taurus	77-94
8466909-1	1993	Specific three- and two-disulfide intermediates that accumulate transiently during reduction of the disulfide bonds of Ca(2+)-bound bovine alpha-lactalbumin have been trapped, isolated, and characterized.	Disulfides	24-33	lactalbumin alpha	Bos taurus	139-156
8466909-1	1993	Specific three- and two-disulfide intermediates that accumulate transiently during reduction of the disulfide bonds of Ca(2+)-bound bovine alpha-lactalbumin have been trapped, isolated, and characterized.	Disulfides	100-109	lactalbumin alpha	Bos taurus	139-156
8466909-4	1993	The remaining native disulfide bonds in the two partially reduced derivatives of alpha-lactalbumin are stable only when the proteins are in a Ca(2+)-bound state.	Disulfides	21-30	lactalbumin alpha	Bos taurus	81-98
8325249-4	1993	Similarly, the 140 kilodalton (kDa) disulfide-linked homodimer of MIS is proteolytically cleaved to generate its active C-terminal fragments.	Disulfides	36-45	anti-Mullerian hormone	Homo sapiens	66-69
8454613-3	1993	CD experiments reveal that for both peptides, the ordering of the Cys1-Cys7 disulfide link and the alpha-helix formation can be distinguished.	Disulfides	76-85	cystin 1	Homo sapiens	66-70
8438588-6	1993	Gp160t, gp160t/sec, and gp120 formed oligomers which were stabilized by intermolecular disulfide bonds and/or noncovalent interactions and were also found to bind to soluble CD4.	Disulfides	87-96	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	24-29
8419481-1	1993	The B cell Ag receptor complex consists of at least two disulfide-linked, heterodimeric structures: the clonally restricted membrane Ig (mIg) molecule and the nonpolymorphic Ig-alpha:Ig-beta protein dimer.	Disulfides	56-65	chemokine (C-X-C motif) ligand 9	Mus musculus	133-135
8419481-1	1993	The B cell Ag receptor complex consists of at least two disulfide-linked, heterodimeric structures: the clonally restricted membrane Ig (mIg) molecule and the nonpolymorphic Ig-alpha:Ig-beta protein dimer.	Disulfides	56-65	chemokine (C-X-C motif) ligand 9	Mus musculus	137-140
8428583-4	1993	After photolysis to label their nearest neighbors and reduction of the disulfide bond between proOmpA-Dhfr and the cross-linker, radiolabeled cross-linker was selectively recovered with the SecA and SecY subunits of preprotein translocase.	Disulfides	71-80	Dihydrofolate reductase	Escherichia coli	102-106
1332947-1	1992	Thioredoxin, despite its function as an intracellular disulfide reducing enzyme and its lack of a signal sequence, has been found to play some roles extracellularly.	Disulfides	54-63	thioredoxin	Homo sapiens	0-11
1385533-1	1992	The T cell receptor (TcR) is an integral membrane protein occurring as a disulfide linked heterodimer, non-covalently associated with CD3 on the surface of T lymphocytes.	Disulfides	73-82	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	4-19
1385533-1	1992	The T cell receptor (TcR) is an integral membrane protein occurring as a disulfide linked heterodimer, non-covalently associated with CD3 on the surface of T lymphocytes.	Disulfides	73-82	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	21-24
1401917-8	1992	Thus, a product of the B29 gene is a component of the AgR complex in human and murine B cells, occurring as a disulfide linked dimer with product(s) of the mb-1 gene.	Disulfides	110-119	CD79b molecule	Homo sapiens	23-26
1384484-4	1992	The results showed that as few as N-terminal 142 but not 133 amino acid residues of mSCF remained biologically active in vitro, suggesting that the region of 9 amino acids from Asp134 to Ser142 containing a Cys138-mediated disulfide bond may contribute to the C-terminal end of the active subdomain of mSCF.	Disulfides	223-232	kit ligand	Mus musculus	84-88
1505516-11	1992	Expression of zeta mutants in zeta-deficient T cells revealed that the zeta transmembrane domain is also responsible for reconstituting transport of functional TCR complexes to the cell surface and differentiated the requirements for disulfide-linked dimerization per se from assembly of the TCR complex.	Disulfides	234-243	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	160-163
1356152-0	1992	Identification of the mixed disulfide of glutathione and cysteinylglycine in bile: dependence on gamma-glutamyl transferase and responsiveness to oxidative stress.	Disulfides	28-37	gamma-glutamyltransferase 1	Rattus norvegicus	97-123
1501277-4	1992	If this cysteine is lacking, the HBe protein, which is predominantly a monomer with only HBe antigenicity, is expressed as a disulfide-linked homodimer showing both HBe and HBc antigenicity.	Disulfides	125-134	keratin 88, pseudogene	Homo sapiens	173-176
1510657-3	1992	Furthermore, recombinant ADF/human thioredoxin was found to have protein-refolding activity for scrambled (mispaired disulfide-containing) RNase A.	Disulfides	117-126	thioredoxin	Homo sapiens	25-28
1510657-3	1992	Furthermore, recombinant ADF/human thioredoxin was found to have protein-refolding activity for scrambled (mispaired disulfide-containing) RNase A.	Disulfides	117-126	thioredoxin	Homo sapiens	35-46
1323144-1	1992	The zeta subunit of the T cell antigen receptor (TCR) exists primarily as a disulfide-linked homodimer.	Disulfides	76-85	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	24-47
1323144-1	1992	The zeta subunit of the T cell antigen receptor (TCR) exists primarily as a disulfide-linked homodimer.	Disulfides	76-85	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	49-52
1639774-1	1992	The 4F2 cell surface antigen is a disulfide-linked heterodimer induced during the process of cellular activation and expressed widely in mammalian tissues (Parmacek, M. S., Karpinski, B.	Disulfides	34-43	solute carrier family 3 (amino acid transporter heavy chain), member 2 L homeolog	Xenopus laevis	4-7
1321713-1	1992	The thioredoxin system, comprising NADPH, thioredoxin reductase and thioredoxin reduces protein disulfides via redox-active dithiols.	Disulfides	96-106	peroxiredoxin 5	Bos taurus	42-63
1377675-3	1992	Reduction of the PDGF.alpha 2M complex following denaturation dissociated the cytokine from alpha 2M by greater than 90%, suggesting covalent disulfide bond formation.	Disulfides	142-151	alpha-2-macroglobulin	Homo sapiens	22-30
1369490-7	1992	PDI, which catalyzes disulfide bridging of proteins, also stimulated reactivation of the immunotoxin.	Disulfides	21-30	protein-disulfide isomerase	Escherichia coli	0-3
1369490-8	1992	Under optimum conditions, reactivation yields in the presence of PDI were about twice that obtained with nonenzymatic disulfide bond formation.	Disulfides	118-127	protein-disulfide isomerase	Escherichia coli	65-68
1605862-1	1992	Protein disulfide isomerase (PDI), a luminal enzyme of the endoplasmic reticulum (ER), is thought to be involved in the process that assures that the correct disulfide bonds form as a newly synthesized protein folds into its appropriate three-dimensional structure (Freeman, 1984).	Disulfides	8-17	protein-disulfide isomerase	Escherichia coli	29-32
1283100-7	1992	Determination of the number of free-SH groups of IGFBP-1 and -3 has revealed that most likely all cysteine residues are involved in disulfide bond formation.	Disulfides	132-141	insulin like growth factor binding protein 1	Homo sapiens	49-63
1570358-9	1992	Insulin proteolysis was inhibited by specific insulin protease inhibitors and stimulated by disulfide reducing agents.	Disulfides	92-101	insulin	Bos taurus	0-7
1318718-4	1992	The reaction of PQQ with reduced thioredoxin brings about the oxidation of two thiol groups of the oxireductase, whereas the enzyme phosphoribulose kinase is inactivated at 25 degrees C. The oxidized disulfide bond of phosphoribulose kinase is reduced by dithiothreitol and the enzyme recovers catalytic activity.	Disulfides	200-209	thioredoxin	Homo sapiens	33-44
1560364-7	1992	In contrast, under disulfide forms, the above selective aminopeptidase N or endopeptidase 24.11 inhibitors are inactive after i.v.	Disulfides	19-28	alanyl (membrane) aminopeptidase	Mus musculus	56-72
1312714-4	1992	Several mutant forms of the EPO-R were analyzed; all constitutively active mutants form disulfide-linked homodimers, whereas EPO-responsive or inactive forms of the receptor do not.	Disulfides	88-97	erythropoietin receptor	Homo sapiens	28-33
1542117-2	1992	Unfolding of the small alpha-amylase inhibitor tendamistat (74 residues, 2 disulfide bridges) has been characterized thermodynamically by high sensitivity scanning microcalorimetry.	Disulfides	75-84	alpha amylase	Bos taurus	23-36
1375132-1	1992	Human recombinant granulocyte-colony stimulating factor (rhG-CSF) has one free cysteine at position 17 and has two disulfide bridges (Cys36-Cys42 and Cys64-Cys74).	Disulfides	115-124	colony stimulating factor 3	Homo sapiens	18-55
1329444-5	1992	On the other hand, thioredoxin contains a redox active disulfide and has a reducing activity in the presence of thioredoxin reductase and NADPH.	Disulfides	55-64	thioredoxin	Homo sapiens	19-30
1953706-5	1991	These results suggest that the carboxyl-terminal sequence at residues 32-37 of big ET-1 is important for conversion, whereas the amino-terminal disulfide loop structure appears to interfere with access of ECE to big ET-1.	Disulfides	144-153	endothelin converting enzyme 1	Homo sapiens	205-208
1837314-6	1991	In addition, they preferentially expressed the disulfide linked form of the TCR, except in progressive systemic sclerosis where the nondisulfide form was displayed.	Disulfides	47-56	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	76-79
1724736-3	1991	The CD3 complex of gamma, delta and epsilon and the zeta-family disulfide dimer comprise the invariant TCR chains.	Disulfides	64-73	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	103-106
1724736-8	1991	Mounting evidence indicates that the structural complexity of the TCR is further enhanced by the various zeta family disulfide dimer pairs that can associate with the other TCR chains.	Disulfides	117-126	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	66-69
1724736-8	1991	Mounting evidence indicates that the structural complexity of the TCR is further enhanced by the various zeta family disulfide dimer pairs that can associate with the other TCR chains.	Disulfides	117-126	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	173-176
1778302-2	1991	This assay reflects the recently recognized ability of thioredoxin to catalyze disulfide bond formation in proteins.	Disulfides	79-88	thioredoxin	Homo sapiens	55-66
2037582-3	1991	Mutant TF lacking either the amino (TFS49S57) or carboxyl (TFS186S209) disulfide bond were expressed on the surface of cells consistent with proper processing.	Disulfides	71-80	coagulation factor III, tissue factor	Homo sapiens	7-9
2037582-7	1991	These data suggest that the Cys186-Cys209 disulfide bond is required to maintain conformation and implicate the disulfide loop or adjacent structures in the carboxyl half of the surface domain of TF in receptor function.	Disulfides	42-51	coagulation factor III, tissue factor	Homo sapiens	196-198
2037582-7	1991	These data suggest that the Cys186-Cys209 disulfide bond is required to maintain conformation and implicate the disulfide loop or adjacent structures in the carboxyl half of the surface domain of TF in receptor function.	Disulfides	112-121	coagulation factor III, tissue factor	Homo sapiens	196-198
2033048-9	1991	P34H Trx may be useful as an analogue of PDI for disulfide formation in vivo and in vitro.	Disulfides	49-58	protein-disulfide isomerase	Escherichia coli	41-44
2014246-4	1991	The specificities of these mAbs have been mapped to sequences near the tip of the disulfide loop of the gp120 third variable domain, Lys-Arg-Ile-His-Ile and His-Ile-Gly-Pro-Gly-Arg, respectively.	Disulfides	82-91	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	104-109
1848998-4	1991	Air oxidation of P39 gave P78, a 78-residue covalent dimer having a disulfide bridge linking its C termini.	Disulfides	68-77	microspherule protein 1	Homo sapiens	26-29
1848998-7	1991	Its C-terminal disulfide bridge renders P78 significantly more stable than P39 to thermal denaturation or denaturation by urea.	Disulfides	15-24	microspherule protein 1	Homo sapiens	40-43
1712069-0	1991	Covalent disulfide binding of human IL-1 beta to alpha 2-macroglobulin: inhibition by D-penicillamine.	Disulfides	9-18	alpha-2-macroglobulin	Homo sapiens	49-70
1712069-4	1991	Thus, the possibility that IL-1 beta forms a disulfide bond with alpha 2M was investigated.	Disulfides	45-54	alpha-2-macroglobulin	Homo sapiens	65-73
1712069-11	1991	Thus, disulfide bonds were formed between the free SH groups on [125I]rIL-1 beta and those resulting from the cleavage of the internal thioester bonds of alpha 2M.	Disulfides	6-15	alpha-2-macroglobulin	Homo sapiens	154-162
2011576-6	1991	A 20-residue synthetic peptide (termed 2.1) from a non-Ca2(+)-binding, disulfide-rich domain of SPARC also exhibited a dose-dependent inhibition of [3H]thymidine uptake in endothelial cells within 24 hr after release from G0 phase.	Disulfides	71-80	secreted protein acidic and cysteine rich	Bos taurus	96-101
1998959-8	1991	RTA immunotoxins were constructed using human TF or RI7/217 and a disulfide linker.	Disulfides	66-75	MAS related GPR family member F	Homo sapiens	0-3
1676628-3	1991	A study was performed to determine whether the formation and later breakdown of a stable disulfide between D-PEN and plasma albumin could explain these aspects of D-PEN pharmacokinetics.	Disulfides	89-98	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	109-112
1676628-3	1991	A study was performed to determine whether the formation and later breakdown of a stable disulfide between D-PEN and plasma albumin could explain these aspects of D-PEN pharmacokinetics.	Disulfides	89-98	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	165-168
1903095-3	1991	Human serum carnosinase was found to be a glycoprotein with a pI of 4.4 and a subunit Mr of 75,000; the active enzyme was a dimer, the two subunits being connected by one or more disulfide bonds.	Disulfides	179-188	carnosine dipeptidase 1	Homo sapiens	6-23
1991104-2	1991	Sequential assignments for nearly all of the 32 spin systems have been obtained, and results indicate that the heptaresidue loop formed by the disulfide bond between Cys-1 and Cys-7 is followed by an alpha-helical segment from Val-8 through Tyr-22.	Disulfides	143-152	cystin 1	Homo sapiens	166-171
1992463-6	1991	Monoclonal antibodies were used with Western blot analysis to localize the wild-type mouse peripherin/rds protein to isolated mouse rod outer segments and to show that it, like bovine peripherin, exists as two subunits linked by one or more disulfide bonds.	Disulfides	241-250	peripherin	Mus musculus	91-101
1703490-4	1991	Analysis by NEPHGE and SDS-PAGE showed that at least some beta TCR exists on the surface as a large disulfide-linked complex with unknown acidic molecules.	Disulfides	100-109	T cell receptor alpha variable 6-3	Mus musculus	63-66
1707134-2	1991	The third chain, C8 gamma, is covalently linked to C8 alpha by a disulfide linkage; it is demonstrated that Cys40 of C8 gamma is linked to Cys164 of C8 alpha, a unique cysteine located in a loop located between the cysteine-rich LDL-receptor class A module and the membrane-inserting region of C8 alpha.	Disulfides	65-74	complement C8 alpha chain	Homo sapiens	51-59
1708670-11	1990	These data suggest that the predominant form of PAI-2 in placenta extract is heterogeneous and of high molecular mass, containing complexes in which vitronectin is covalently bound to PAI-2 by disulfide bridges.	Disulfides	193-202	serpin family B member 2	Homo sapiens	48-53
1708670-11	1990	These data suggest that the predominant form of PAI-2 in placenta extract is heterogeneous and of high molecular mass, containing complexes in which vitronectin is covalently bound to PAI-2 by disulfide bridges.	Disulfides	193-202	serpin family B member 2	Homo sapiens	184-189
2084958-6	1990	In addition, the disulfide bonds (between Cys-49 and Cys-57 and between Cys-186 and Cys-209) were demonstrated by FAB-MS analysis of cysteine-containing fragments obtained from the tryptic map.	Disulfides	17-26	FA complementation group B	Homo sapiens	114-117
2145276-0	1990	Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187.	Disulfides	44-53	rhodopsin	Bos taurus	23-32
2145276-14	1990	The C110-C187 disulfide bond is buried in rhodopsin because reactions with disulfide reducing agents and cyanide ion require prior treatment with denaturants.	Disulfides	14-23	rhodopsin	Bos taurus	42-51
2145276-14	1990	The C110-C187 disulfide bond is buried in rhodopsin because reactions with disulfide reducing agents and cyanide ion require prior treatment with denaturants.	Disulfides	75-84	rhodopsin	Bos taurus	42-51
2079029-0	1990	Two-dimensional electrophoresis of the fatty acid binding protein from human heart: evidence for a thiol group which can form an intermolecular disulfide bond.	Disulfides	144-153	glutamic-oxaloacetic transaminase 2	Homo sapiens	39-65
2079029-8	1990	This protein was identified as a dimer of FABP and evidence for the involvement of an intermolecular disulfide bond in this dimerization is presented.	Disulfides	101-110	glutamic-oxaloacetic transaminase 2	Homo sapiens	42-46
2144290-0	1990	A fraction of CD3 epsilon subunits exists as disulfide-linked dimers in both human and murine T lymphocytes.	Disulfides	45-54	CD3 epsilon subunit of T-cell receptor complex	Homo sapiens	14-25
1974563-1	1990	CD27 mAb recognize a disulfide-linked homodimer of 55 kDa present in the majority of T cells and in a minor subpopulation of thymocytes.	Disulfides	21-30	CD27 molecule	Homo sapiens	0-4
2144901-7	1990	Since CD3-epsilon was shown to form disulfide-linked homodimers both in human and murine T cells, the two CD3-epsilon subunits present in the TCR-CD3 complex were in direct contact with one another.	Disulfides	36-45	CD3 epsilon subunit of T-cell receptor complex	Homo sapiens	6-17
2144901-7	1990	Since CD3-epsilon was shown to form disulfide-linked homodimers both in human and murine T cells, the two CD3-epsilon subunits present in the TCR-CD3 complex were in direct contact with one another.	Disulfides	36-45	T cell receptor alpha variable 6-3	Mus musculus	142-145
457626-2	1979	The C1r thus purified had a molecular weight of 105,000, consisting of two polypeptide chains connected by disulfide bonds; the molecular weights of the chains were 60,000 and 45,000.	Disulfides	107-116	complement C1r subcomponent	Oryctolagus cuniculus	4-7
894033-6	1977	of 93,000, whereas the reduced protein demonstrated two bands of 55,000 and 42,000 m.w., thereby establishing a composition of two disulfide-linked polypeptide chains for C3bINA.	Disulfides	131-140	complement factor I	Homo sapiens	171-177
1017794-5	1976	The deprotection of the alpha-amino group by HCl/acetic acid of Boc-Ile-Cys(SiPr)-Gly-Lys(Z) was accompanied by a disulfide exchange at the cysteine residue.	Disulfides	114-123	BOC cell adhesion associated, oncogene regulated	Homo sapiens	64-67
22801966-3	2013	Human tissue factor disulfide mutants have been proposed as a model for encrypted tissue factor, but poor expression of these mutants hampers research into tissue factor decryption.	Disulfides	20-29	coagulation factor III, tissue factor	Homo sapiens	82-95
1141233-0	1975	Elongation of the interchain disulfide bridges of insulin.	Disulfides	29-38	LOC105613195	Ovis aries	50-57
22801966-3	2013	Human tissue factor disulfide mutants have been proposed as a model for encrypted tissue factor, but poor expression of these mutants hampers research into tissue factor decryption.	Disulfides	20-29	coagulation factor III, tissue factor	Homo sapiens	82-95
22801966-12	2013	The murine model of disulfide-mutated tissue factor is more suitable for studying tissue factor decryption than are human tissue factor mutants.	Disulfides	20-29	coagulation factor III, tissue factor	Homo sapiens	82-95
1141233-2	1975	The sythesis and isolation in purified form of an analog of insulin with the interchain disulfide bridges elongated by a methylene group is described.	Disulfides	88-97	LOC105613195	Ovis aries	60-67
1141233-3	1975	This analog differs from the parent molecule in that the cystein residues occupying positions A-7 and A-20 and involved in the formation of the two interchain disulfide bridges of insulin have been replaced by homocysteine residues.	Disulfides	159-168	LOC105613195	Ovis aries	180-187
22990208-4	2013	A disulfide-linked immunoconjugate of a 5-amino-modified 24 mer phosphorothioate anti-sense E2A-PBX1 oligonucleotide (AON) with a mAb specific for a CD19 receptor (alphaCD19-AON) was prepared as a CD19-directed and leukemia-specific biotherapeutic agent against E2A-PBX1(+) B-lineage ALL.	Disulfides	2-11	PBX homeobox 1	Homo sapiens	96-100
22990208-4	2013	A disulfide-linked immunoconjugate of a 5-amino-modified 24 mer phosphorothioate anti-sense E2A-PBX1 oligonucleotide (AON) with a mAb specific for a CD19 receptor (alphaCD19-AON) was prepared as a CD19-directed and leukemia-specific biotherapeutic agent against E2A-PBX1(+) B-lineage ALL.	Disulfides	2-11	PBX homeobox 1	Homo sapiens	266-270
23849862-4	2013	However, PKA and PKG can also be functionally modulated independently of cyclic nucleotide stimulation through direct cysteine thiol oxidation leading to intermolecular disulfide formation.	Disulfides	169-178	protein kinase cGMP-dependent 1	Homo sapiens	17-20
33245448-5	2021	To inhibit AGE formation, we developed a disulfide compound linking GSH diester and mercaptoethylguanidine, and we named it carboxitin.	Disulfides	41-50	renin binding protein	Mus musculus	11-14
33652022-13	2021	CONCLUSION: Txnip is a cysteine-containing redox protein that robustly regulates the thioredoxin system via a disulfide bond-switching mechanism in adult cardiomyocytes.	Disulfides	110-119	thioredoxin 1	Mus musculus	85-96
23849862-5	2013	In the case of PKG, the formation of an intermolecular disulfide between two parallel dimeric subunits leads to enhanced kinase affinity for substrate.	Disulfides	55-64	protein kinase cGMP-dependent 1	Homo sapiens	15-18
34055495-5	2021	We show that the disulfide-stabilized dimer is resistant to tumor necrosis factor-alpha-converting enzyme (TACE) cleavage, while the monomeric form is more susceptible than the predominantly dimeric wild type.	Disulfides	17-26	ADAM metallopeptidase domain 17	Homo sapiens	60-105
34055495-5	2021	We show that the disulfide-stabilized dimer is resistant to tumor necrosis factor-alpha-converting enzyme (TACE) cleavage, while the monomeric form is more susceptible than the predominantly dimeric wild type.	Disulfides	17-26	ADAM metallopeptidase domain 17	Homo sapiens	107-111
33985344-0	2021	Influenza A virus hemagglutinin is produced in different disulfide-bonded states.	Disulfides	57-66	hemagglutinin	None	18-31
23709032-1	2013	cGMP-dependent protein kinase, also known as protein kinase G (PKG), is activated independently of cGMP by a novel thiol-reactive mechanism involving the formation of an intermolecular disulfide.	Disulfides	185-194	protein kinase cGMP-dependent 1	Homo sapiens	45-61
23709032-1	2013	cGMP-dependent protein kinase, also known as protein kinase G (PKG), is activated independently of cGMP by a novel thiol-reactive mechanism involving the formation of an intermolecular disulfide.	Disulfides	185-194	protein kinase cGMP-dependent 1	Homo sapiens	63-66
23709032-3	2013	Here, we describe the proteomic approach that lead to PKG being identified as a kinase susceptible to oxidant-dependent disulfide dimer formation, these methods being applicable for the identification of other disulfide bound protein complexes.	Disulfides	120-129	protein kinase cGMP-dependent 1	Homo sapiens	54-57
33964423-8	2021	A recombinant A2M with a modified bait region was used to map the bait region"s position in native A2M by XL-MS. A second recombinant A2M introduced an inter-subunit disulfide into the LNK region, demonstrating the predicted interactions between these regions in native A2M.	Disulfides	166-175	SH2B adaptor protein 3	Homo sapiens	185-188
23709032-3	2013	Here, we describe the proteomic approach that lead to PKG being identified as a kinase susceptible to oxidant-dependent disulfide dimer formation, these methods being applicable for the identification of other disulfide bound protein complexes.	Disulfides	210-219	protein kinase cGMP-dependent 1	Homo sapiens	54-57
23296605-5	2013	Four out of ten cysteines in the recombinant S100A3 form two intramolecular disulfide bridges that modulate its Ca(2+)-affinity.	Disulfides	76-85	S100 calcium binding protein A3	Homo sapiens	45-51
33957490-2	2021	In this study, three disulfide-linked polycaprolactone-b-polyethylene glycol methyl ether methacrylate (PCL-SS-PPEGMA) were synthesized and confirmed by 1H NMR and GPC, and then used for doxorubicin (DOX) delivery.	Disulfides	21-30	glycophorin C (Gerbich blood group)	Homo sapiens	164-167
23592978-3	2013	In this study, we examined how the conserved gp120-gp41 association site, formed by the N- and C-terminal segments of gp120 and the disulfide-bonded region (DSR) of gp41, adapts to glycan changes that are linked to neutralization sensitivity.	Disulfides	132-141	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	45-50
33359632-0	2021	Divalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern.	Disulfides	92-101	S100 calcium binding protein A9 (calgranulin B)	Mus musculus	59-65
33359632-9	2021	They also unravel an intramolecular disulfide bridge that stabilizes the C-terminal tail in a rigid conformation, thus shaping a second Zn-binding site per S100A9 protomer.	Disulfides	36-45	S100 calcium binding protein A9 (calgranulin B)	Mus musculus	156-162
33359632-11	2021	Using mass spectrometry, we demonstrate that mS100A9 can form both non-covalent and covalent homodimers with distinct disulfide bond patterns.	Disulfides	118-127	S100 calcium binding protein A9 (calgranulin B)	Mus musculus	45-52
22943363-2	2012	Oxidative inhibition of the V-ATPase is ascribed to disulfide-bond formation between conserved cysteine residues at the catalytic site of subunit A. Subunits containing amino acid substitutions of one of three conserved cysteine residues of VHA-A were expressed in a vha-A null mutant background in Arabidopsis.	Disulfides	52-61	vacuolar ATP synthase subunit A	Arabidopsis thaliana	241-246
33416847-8	2021	Mass spectrometry-based peptide mapping analysis revealed that Cys152 and Cys157 are critical for the intramolecular disulfide bond formation in PFK5.	Disulfides	117-126	phosphofructokinase 5	Arabidopsis thaliana	145-149
23010496-3	2012	Human Trx1 contains the active-site cysteines, Cys32 and Cys35, and three additional structural cysteines, Cys62, Cys69, and Cys73, that regulate Trx1 structure and activity via a second disulfide formation, S-glutathionylation or S-nitrosylation.	Disulfides	187-196	thioredoxin	Homo sapiens	6-10
33057791-2	2020	Reelin exists as a homodimer with two chains linked by a disulfide bond at cysteine 2101, a feature that is vital to the protein"s function.	Disulfides	57-66	reelin	Homo sapiens	0-6
23010496-3	2012	Human Trx1 contains the active-site cysteines, Cys32 and Cys35, and three additional structural cysteines, Cys62, Cys69, and Cys73, that regulate Trx1 structure and activity via a second disulfide formation, S-glutathionylation or S-nitrosylation.	Disulfides	187-196	thioredoxin	Homo sapiens	146-150
23045530-0	2012	Engineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair.	Disulfides	11-20	mutS homolog 6	Homo sapiens	134-138
23045530-4	2012	An engineered disulfide bond within this region prevented the ATP-driven conformational change and resulted in an Msh2-Msh6 complex that bound mispaired bases but could not form sliding clamps or bind Mlh1-Pms1.	Disulfides	14-23	mutS homolog 6	Homo sapiens	119-123
33240264-8	2020	On the other hand, these residues can be completely exposed in the soluble HLA-G1 dimer, due to the free rotation of the disulfide bridge (Cys42/Cys42).	Disulfides	121-130	major histocompatibility complex, class I, G	Homo sapiens	75-81
23045530-4	2012	An engineered disulfide bond within this region prevented the ATP-driven conformational change and resulted in an Msh2-Msh6 complex that bound mispaired bases but could not form sliding clamps or bind Mlh1-Pms1.	Disulfides	14-23	PMS1 homolog 1, mismatch repair system component	Homo sapiens	206-210
23019327-4	2012	The CHCH domain proteins are traditionally imported and trapped in the IMS by using a disulfide relay system mediated by Mia40 and Erv1.	Disulfides	86-95	growth factor, augmenter of liver regeneration	Homo sapiens	131-135
33046554-8	2020	This leads to accumulative oxidative stress, which can be seen in CA1 via increased levels of oxidized, inactivated potassium channel Kv2.1, which undergoes disulfide bridge oligomerization.	Disulfides	157-166	carbonic anhydrase 1	Homo sapiens	66-69
22977247-10	2012	Monitoring the redox state of Trx1 shows that cell death occurs when Trx1 is oxidized, followed by general protein oxidation catalyzed by the disulfide form of thioredoxin.	Disulfides	142-151	thioredoxin	Homo sapiens	30-34
32702157-10	2020	This review updates recent findings in the field and addresses emerging evidence that thiol/disulfide-based reactions mediated by the prothrombotic secreted PDIs are balanced by the transmembrane member of this family, TMX1.	Disulfides	92-101	thioredoxin-related transmembrane protein 1	Mus musculus	219-223
22977247-10	2012	Monitoring the redox state of Trx1 shows that cell death occurs when Trx1 is oxidized, followed by general protein oxidation catalyzed by the disulfide form of thioredoxin.	Disulfides	142-151	thioredoxin	Homo sapiens	160-171
23006890-7	2012	TF-FVIIa coagulant activity at the cell surface is influenced not only by TF protein expression levels but also independently by a variety of mechanisms, including alterations in membrane phospholipid composition and cholesterol content, thiol-dependent modifications of TF allosteric disulfide bonds, and other post-translational modifications of TF.	Disulfides	285-294	coagulation factor III, tissue factor	Homo sapiens	0-2
33063476-7	2020	The homogeneous self-assembly and stability enhancement of SS2 VLPs can be attributed to the new disulfide bonds contributed by Cys102 and Cys300, which are identified by mass spectrometry and explored by molecular dynamics simulations.	Disulfides	97-106	butyrophilin like 2	Homo sapiens	59-62
32946768-0	2020	Disulfide Reduction Allosterically Destabilizes the beta-Ladder Subdomain Assembly within the NS1 Dimer of ZIKV.	Disulfides	0-9	influenza virus NS1A binding protein	Homo sapiens	94-97
22725132-0	2012	An intermolecular disulfide-based light switch for chloroplast psbD gene expression in Chlamydomonas reinhardtii.	Disulfides	18-27	photosystem II protein D2	Chlamydomonas reinhardtii	63-67
23025382-2	2012	In plants, this enzymatic activity is biochemically regulated through an intersubunit disulfide bond between Cys86 and Cys119 in the N-terminal loop of APSK.	Disulfides	86-95	3'-phosphoadenosine 5'-phosphosulfate synthase 2	Homo sapiens	152-156
33056994-5	2020	ERO1L was found to promote the secretion of IL6R by affecting the formation of disulfide bonds.	Disulfides	79-88	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	0-5
32737467-5	2020	Here we have designed mutations in S that allow the production of thermostable, disulfide-bonded S-protein trimers that are trapped in the closed, prefusion state.	Disulfides	80-89	vitronectin	Homo sapiens	97-106
23025382-5	2012	The photoinduced increase of dimeric APSK was strongly implicated to arise from the formation of the Cys86-Cys119 disulfide bond.	Disulfides	114-123	3'-phosphoadenosine 5'-phosphosulfate synthase 2	Homo sapiens	37-41
22910915-0	2012	Structure of yeast sulfhydryl oxidase erv1 reveals electron transfer of the disulfide relay system in the mitochondrial intermembrane space.	Disulfides	76-85	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	38-42
32912963-6	2020	However, as detailed here, the unique chemical properties of oxytocin, including active disulfide bonds, and its capacity to shift chemical forms and bind to other molecules make this molecule difficult to work with and to measure.	Disulfides	88-97	oxytocin/neurophysin I prepropeptide	Homo sapiens	61-69
32505675-10	2020	With the fusion tag, EGF27 was refolded to produce the correct disulfide bond arrangement, which was verified enzymatically with the glycosyltransferases, Protein O-fucosyltransferase 1 (POFUT1) and Lunatic Fringe (LFNG).	Disulfides	63-72	protein O-fucosyltransferase 1	Mus musculus	155-185
32505675-10	2020	With the fusion tag, EGF27 was refolded to produce the correct disulfide bond arrangement, which was verified enzymatically with the glycosyltransferases, Protein O-fucosyltransferase 1 (POFUT1) and Lunatic Fringe (LFNG).	Disulfides	63-72	protein O-fucosyltransferase 1	Mus musculus	187-193
33011677-8	2020	A mechanistic explanation that ADAM17cyto favors the monomeric, active state of Trx-1 is the formation of a disulfide bond between Cys824 at the C-terminal of ADAM17cyto with the Cys73 of Trx-1, which is involved in the dimerization site of Trx-1.	Disulfides	108-117	ADAM metallopeptidase domain 17	Homo sapiens	31-37
33011677-8	2020	A mechanistic explanation that ADAM17cyto favors the monomeric, active state of Trx-1 is the formation of a disulfide bond between Cys824 at the C-terminal of ADAM17cyto with the Cys73 of Trx-1, which is involved in the dimerization site of Trx-1.	Disulfides	108-117	ADAM metallopeptidase domain 17	Homo sapiens	159-165
23089196-4	2012	In addition, using conditions which preserve the tapasin-ERp57 disulfide-bonded conjugate, we demonstrated that beta 2-microglobulin increases tapasin-containing protein complexes, and reduces the level of MHC class I/ERp57 complexes lacking tapasin.	Disulfides	63-72	beta-2-microglobulin	Homo sapiens	112-132
22776295-6	2012	The folded hepcidin displayed a typical disulfide-constrained beta-sheet structure and could induce internalization of enhanced green fluorescent protein (EGFP) tagged ferroportin in transfected HEK293 cells.	Disulfides	40-49	hepcidin antimicrobial peptide	Homo sapiens	11-19
32719007-2	2020	Although the canonical disulfide bond formation pathway involving Ero1alpha and PDI has been well-studied so far, the physiological roles of the newly identified PDI oxidases, glutathione peroxidase-7 (GPx7) and -8 (GPx8), are only poorly understood.	Disulfides	23-32	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	66-75
32779864-3	2020	Here, we show that the CHCHD4/GFER disulfide relay system in the mitochondrial intermembrane space (IMS) is required for PINK1 stabilization when mitochondrial membrane potential is lost.	Disulfides	35-44	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	23-29
32779864-3	2020	Here, we show that the CHCHD4/GFER disulfide relay system in the mitochondrial intermembrane space (IMS) is required for PINK1 stabilization when mitochondrial membrane potential is lost.	Disulfides	35-44	PTEN induced kinase 1	Homo sapiens	121-126
22199235-8	2012	Based on a peptide structure model of the histone-fold-motifs, disulfide bonding among intramolecular conserved cysteine residues of NF-YB, which is responsible for the redox-regulated assembly of NF-YB and NF-YC in human and Aspergillus nidulans, can be excluded for Arabidopsis NF-YB.	Disulfides	63-72	nuclear transcription factor Y subunit beta	Homo sapiens	133-138
32908504-11	2020	In conclusion, this single disulfide bond loss mutation of a new TPO homozygous mutation, p.Cys655Phe, reduced TPO activity and caused congenital hypothyroidism without affecting subcellular localization of TPO proteins.	Disulfides	27-36	thyroid peroxidase	Homo sapiens	65-68
32908504-11	2020	In conclusion, this single disulfide bond loss mutation of a new TPO homozygous mutation, p.Cys655Phe, reduced TPO activity and caused congenital hypothyroidism without affecting subcellular localization of TPO proteins.	Disulfides	27-36	thyroid peroxidase	Homo sapiens	111-114
32908504-11	2020	In conclusion, this single disulfide bond loss mutation of a new TPO homozygous mutation, p.Cys655Phe, reduced TPO activity and caused congenital hypothyroidism without affecting subcellular localization of TPO proteins.	Disulfides	27-36	thyroid peroxidase	Homo sapiens	111-114
22199235-8	2012	Based on a peptide structure model of the histone-fold-motifs, disulfide bonding among intramolecular conserved cysteine residues of NF-YB, which is responsible for the redox-regulated assembly of NF-YB and NF-YC in human and Aspergillus nidulans, can be excluded for Arabidopsis NF-YB.	Disulfides	63-72	nuclear transcription factor Y subunit beta	Homo sapiens	197-202
32762682-3	2020	The mitochondrial oxidoreductase MIA40, which catalyzes disulfide formation in the IMS, is imported by the combined action of the protein AIFM1 and MIA40 itself.	Disulfides	56-65	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	33-38
32762682-3	2020	The mitochondrial oxidoreductase MIA40, which catalyzes disulfide formation in the IMS, is imported by the combined action of the protein AIFM1 and MIA40 itself.	Disulfides	56-65	apoptosis inducing factor mitochondria associated 1	Homo sapiens	138-143
2209681-0	1990	Disulfide bridge formation between C1q and IgG in vitro.	Disulfides	0-9	complement C1q A chain	Homo sapiens	35-38
22199235-8	2012	Based on a peptide structure model of the histone-fold-motifs, disulfide bonding among intramolecular conserved cysteine residues of NF-YB, which is responsible for the redox-regulated assembly of NF-YB and NF-YC in human and Aspergillus nidulans, can be excluded for Arabidopsis NF-YB.	Disulfides	63-72	nuclear transcription factor Y subunit gamma	Homo sapiens	207-212
2209681-3	1990	During iodination, I+ and I2 oxidize these sulfhydryls to produce disulfide-linked C1q aggregates.	Disulfides	66-75	complement C1q A chain	Homo sapiens	83-86
2209681-6	1990	Disulfide bridging between C1q and IgG in vitro suggests that this may be a normal physiological function of C1q for which the free cysteines of human, mouse and guinea pig C1q have been conserved.	Disulfides	0-9	complement C1q A chain	Homo sapiens	27-30
2209681-6	1990	Disulfide bridging between C1q and IgG in vitro suggests that this may be a normal physiological function of C1q for which the free cysteines of human, mouse and guinea pig C1q have been conserved.	Disulfides	0-9	complement C1q A chain	Homo sapiens	109-112
32762682-3	2020	The mitochondrial oxidoreductase MIA40, which catalyzes disulfide formation in the IMS, is imported by the combined action of the protein AIFM1 and MIA40 itself.	Disulfides	56-65	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	148-153
2209681-6	1990	Disulfide bridging between C1q and IgG in vitro suggests that this may be a normal physiological function of C1q for which the free cysteines of human, mouse and guinea pig C1q have been conserved.	Disulfides	0-9	complement C1q A chain	Homo sapiens	109-112
22199235-8	2012	Based on a peptide structure model of the histone-fold-motifs, disulfide bonding among intramolecular conserved cysteine residues of NF-YB, which is responsible for the redox-regulated assembly of NF-YB and NF-YC in human and Aspergillus nidulans, can be excluded for Arabidopsis NF-YB.	Disulfides	63-72	nuclear transcription factor Y subunit beta	Homo sapiens	197-202
22581768-0	2012	PEP-FOLD: an updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides.	Disulfides	77-86	progestagen associated endometrial protein	Homo sapiens	0-3
2397216-3	1990	To this amatoxin vehicle we attached a targeting molecule, human recombinant leucine-21 epidermal growth factor (hrEGFL), via a disulfide-containing linker moiety.	Disulfides	128-137	epidermal growth factor	Homo sapiens	88-111
32749217-4	2020	In the complex, the luminal surface of CLC-7 is entirely covered by a dimer of the heavily glycosylated and disulfide-bonded OSTM1, which serves to protect CLC-7 from the degradative environment of the lysosomal lumen.	Disulfides	108-117	chloride voltage-gated channel 7	Homo sapiens	39-44
32749217-4	2020	In the complex, the luminal surface of CLC-7 is entirely covered by a dimer of the heavily glycosylated and disulfide-bonded OSTM1, which serves to protect CLC-7 from the degradative environment of the lysosomal lumen.	Disulfides	108-117	chloride voltage-gated channel 7	Homo sapiens	156-161
22406430-5	2012	Addition of enzymatically favorable buffer containing zinc and DTT reduced the interchain disulfide bond releasing and activating the captured L-chain with subsequent specific cleavage of the SNAP25(1-206) substrate.	Disulfides	90-99	synaptosome associated protein 25	Homo sapiens	192-198
2358464-3	1990	The primary structure of royalisin was determined to consist of 51 residues, with three intramolecular disulfide linkages, having a calculated molecular mass of 5523 Da.	Disulfides	103-112	defensin-1	Apis mellifera	25-34
22489915-1	2012	BACKGROUND: Ligation of the platelet-specific collagen receptor, GPVI/FcRgamma, causes rapid, transient disulfide-dependent homodimerization, and the production of intracellular reactive oxygen species (ROS) generated by the NADPH oxidase, linked to GPVI via TRAF4.	Disulfides	104-113	glycoprotein VI platelet	Homo sapiens	65-69
22489915-1	2012	BACKGROUND: Ligation of the platelet-specific collagen receptor, GPVI/FcRgamma, causes rapid, transient disulfide-dependent homodimerization, and the production of intracellular reactive oxygen species (ROS) generated by the NADPH oxidase, linked to GPVI via TRAF4.	Disulfides	104-113	glycoprotein VI platelet	Homo sapiens	250-254
22496424-0	2012	Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum.	Disulfides	51-60	vitamin K epoxide reductase complex subunit 1	Homo sapiens	0-27
2367520-11	1990	We conclude that the first step in the assembly of the rhodopsin molecule is the formation of a three-dimensional structure in the intradiscal domain involving the bulk of the out-of-the-membrane polypeptide segments followed by the linkage of Cys-110 and Cys-187 through a disulfide bond.	Disulfides	274-283	rhodopsin	Bos taurus	55-64
22496424-8	2012	These findings establish VKOR as a significant contributor to disulfide bond formation within the ER.	Disulfides	62-71	vitamin K epoxide reductase complex subunit 1	Homo sapiens	25-29
22593945-0	2004	(64)Cu-Labeled NOTA-conjugated anti-CD105 (endoglin) chimeric monoclonal antibody linked to near-infrared dye IRDye 800CW The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	184-193	endoglin	Homo sapiens	126-139
2113054-9	1990	The disulfide bonds of sCD4 were determined to be within domains 1, 2, and 4 and isolation of glycopeptides showed that both N-linked sites were glycosylated.	Disulfides	4-13	stearoyl-coenzyme A desaturase 4	Rattus norvegicus	23-27
22593945-0	2004	(64)Cu-Labeled NOTA-conjugated anti-CD105 (endoglin) chimeric monoclonal antibody linked to near-infrared dye IRDye 800CW The CD105 antigen (endoglin) is a hypoxia-inducible, 180-kDa, disulfide-linked homodimeric transmembrane glycoprotein that is a co-receptor for the transforming growth factor beta (TGF-beta) (1).	Disulfides	184-193	endoglin	Homo sapiens	141-149
2111744-1	1990	Single-chain urokinase plasminogen activator (scu-PA) that had been modified with N-succinimidyl-3-(2-pyridyldithio)propionate was covalently linked by disulfide bonds to the Fab" of a monoclonal antibody specific for the beta-chain of fibrin (antibody 59D8).	Disulfides	152-161	FA complementation group B	Homo sapiens	175-178
22334508-2	2012	In the presence of the dyad, the 1:1 association of a disulfide-bridged myoglobin dimer (green) with streptavidin (gray) afforded a submicrometer-sized fibrous alternating copolymer.	Disulfides	54-63	myoglobin	Homo sapiens	72-81
22181833-1	2012	The LRP (low-density lipoprotein receptor-related protein) can bind a wide range of structurally diverse ligands to regions composed of clusters of ~40 residue Ca2+-dependent, disulfide-rich, CRs (complement-like repeats).	Disulfides	176-185	low density lipoprotein receptor	Homo sapiens	9-41
1691174-3	1990	Characterization of this glycoprotein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, reverse-phase HPLC, amino acid analysis and partial NH2-terminal sequence analysis indicated that GPIII was a disulfide-linked heterodimer with 37-kDa subunits.	Disulfides	210-219	clusterin	Bos taurus	198-203
22362842-6	2012	In addition, we investigated the significance of the electrochemical proton gradient in reducing the gamma subunit by the reduced form of thioredoxin in chloroplasts, providing strong insights into the molecular mechanisms underlying the formation and reduction of the disulfide bond on the gamma subunit in vivo.	Disulfides	269-278	thioredoxin	Homo sapiens	138-149
2185957-3	1990	Sequence analysis of cystine-containing peptides in a thermolysin digest of this EH established the locations of 3 disulfide bonds in the molecule.	Disulfides	115-124	eclosion hormone	Bombyx mori	81-83
22834075-3	2012	We have recently developed bioreducible disulfide-based polyethylenimine (SSPEI) for potent in vitro and in vivo delivery of siRNA targeting human telomerase reverse transcriptase (hTERT).	Disulfides	40-49	telomerase reverse transcriptase	Homo sapiens	147-179
22834075-3	2012	We have recently developed bioreducible disulfide-based polyethylenimine (SSPEI) for potent in vitro and in vivo delivery of siRNA targeting human telomerase reverse transcriptase (hTERT).	Disulfides	40-49	telomerase reverse transcriptase	Homo sapiens	181-186
2342486-2	1990	The interaction between C1q and IgG was disrupted by varying the pH, modifying essential residues in the IgG binding site of C1q and by reducing the interchain disulfides of IgG.	Disulfides	160-170	complement C1q A chain	Homo sapiens	24-27
2342486-4	1990	SDS-PAGE analysis of the crosslinked material showed a 210 kDa band consistent with one IgG crosslinked to two disulfide linked C1q chains.	Disulfides	111-120	complement C1q A chain	Homo sapiens	128-131
22053845-1	2012	SIGNIFICANCE: In photosynthetic organisms, besides the well-established disulfide/dithiol exchange reactions specifically controlled by thioredoxins (TRXs), protein S-glutathionylation is emerging as an alternative redox modification occurring under stress conditions.	Disulfides	72-81	thioredoxin	Homo sapiens	136-148
2297728-1	1990	A site-specific labeling method was developed in which sulfhydryl groups of a murine IgG2a anti-ovarian monoclonal antibody, 5G6.4, were biotinylated with N-iodoacetyl-N"-biotinylhexylenediamine (Compound 1) following partial reduction of disulfide bonds with dithiothreitol.	Disulfides	239-248	immunoglobulin heavy variable V1-9	Mus musculus	85-90
22053845-2	2012	This modification, consisting of the formation of a mixed disulfide between glutathione and a protein cysteine residue, can not only protect specific cysteines from irreversible oxidation but also modulate protein activities and appears to be specifically controlled by small disulfide oxidoreductases of the TRX superfamily named glutaredoxins (GRXs).	Disulfides	58-67	thioredoxin	Homo sapiens	309-312
22230366-0	2012	Thioredoxin-1 and protein disulfide isomerase catalyze the reduction of similar disulfides in HIV gp120.	Disulfides	80-90	thioredoxin	Homo sapiens	0-13
22230366-0	2012	Thioredoxin-1 and protein disulfide isomerase catalyze the reduction of similar disulfides in HIV gp120.	Disulfides	80-90	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	98-103
22230366-2	2012	For entry, gp120 undergoes conformational changes that depend on the reduction of one or more disulfides.	Disulfides	94-104	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	11-16
22230366-3	2012	Previous studies indicate that protein disulfide isomerase (PDI), thioredoxin-1 (Trx1), and glutaredoxin-1 (Grx1) catalyze gp120 reduction, but their specific disulfide targets are not known.	Disulfides	39-48	thioredoxin	Homo sapiens	81-85
2153824-0	1990	Synthesis and biological activity of atrial natriuretic factor analogues: effect of modifications to the disulfide bridge.	Disulfides	105-114	natriuretic peptide A	Bos taurus	37-62
22230366-3	2012	Previous studies indicate that protein disulfide isomerase (PDI), thioredoxin-1 (Trx1), and glutaredoxin-1 (Grx1) catalyze gp120 reduction, but their specific disulfide targets are not known.	Disulfides	39-48	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	123-128
2153824-1	1990	A series of atrial natriuretic factor (ANF) analogues with modifications to the disulfide bridge and lacking the exocyclic N-terminal sequence was synthesized.	Disulfides	80-89	natriuretic peptide A	Bos taurus	12-37
22189830-0	2012	Characterization of an alternative low energy fold for bovine alpha-lactalbumin formed by disulfide bond shuffling.	Disulfides	90-99	lactalbumin alpha	Bos taurus	62-79
2153824-1	1990	A series of atrial natriuretic factor (ANF) analogues with modifications to the disulfide bridge and lacking the exocyclic N-terminal sequence was synthesized.	Disulfides	80-89	natriuretic peptide A	Bos taurus	39-42
2153824-5	1990	The compounds retained high affinity for ANF receptors in bovine adrenal zona glomerulosa cells and were found to be potent antihypertensive and diuretic agents, indicating that the native disulfide bridge can be mimicked by isosteric spanning residues.	Disulfides	189-198	natriuretic peptide A	Bos taurus	41-44
1698402-4	1990	Further digestion of this "tryptic core" with S. aureus V8 protease produced a unique immunoreactive hGM-CSF product comprising two peptides, residues 86-93 and 112-127, linked by a disulfide bond between residues 88 and 121.	Disulfides	182-191	colony stimulating factor 2	Homo sapiens	101-108
22189830-1	2012	Bovine alpha-lactalbumin (alphaLA) forms a misfolded disulfide bond shuffled isomer, X-alphaLA.	Disulfides	53-62	lactalbumin alpha	Bos taurus	7-24
22189830-1	2012	Bovine alpha-lactalbumin (alphaLA) forms a misfolded disulfide bond shuffled isomer, X-alphaLA.	Disulfides	53-62	lactalbumin alpha	Bos taurus	26-33
22189830-1	2012	Bovine alpha-lactalbumin (alphaLA) forms a misfolded disulfide bond shuffled isomer, X-alphaLA.	Disulfides	53-62	lactalbumin alpha	Bos taurus	87-94
22189830-2	2012	This X-alphaLA isomer contains two native disulfide bridges (Cys 6-Cys 120 and Cys 28-Cys 111) and two non-native disulfide bridges (Cys 61-Cys 73 and Cys 77-Cys 91).	Disulfides	42-51	lactalbumin alpha	Bos taurus	7-14
2182738-4	1990	In an attempt to further understand the interaction between GM-CSF and its cell surface receptor, we have constructed models of the tertiary structure of human GM-CSF using the known disulfide bonding pattern, predictions of the secondary structure of the growth factor and a model based on conformational homologies among cytokines (Parry et al., J Mol Recognition 1988;1:107-110).	Disulfides	183-192	colony stimulating factor 2	Homo sapiens	60-66
2182738-4	1990	In an attempt to further understand the interaction between GM-CSF and its cell surface receptor, we have constructed models of the tertiary structure of human GM-CSF using the known disulfide bonding pattern, predictions of the secondary structure of the growth factor and a model based on conformational homologies among cytokines (Parry et al., J Mol Recognition 1988;1:107-110).	Disulfides	183-192	colony stimulating factor 2	Homo sapiens	160-166
22189830-2	2012	This X-alphaLA isomer contains two native disulfide bridges (Cys 6-Cys 120 and Cys 28-Cys 111) and two non-native disulfide bridges (Cys 61-Cys 73 and Cys 77-Cys 91).	Disulfides	114-123	lactalbumin alpha	Bos taurus	7-14
22189830-3	2012	MD simulations have been used to characterize the X-alphaLA isomer and its formation via disulfide bond shuffling and to compare it with the native fold of alphaLA.	Disulfides	89-98	lactalbumin alpha	Bos taurus	52-59
22189830-8	2012	Calcium binding to native alphaLA is shown to help preserve the structure of the beta-domain of the protein limiting possibilities for disulfide bond shuffling.	Disulfides	135-144	lactalbumin alpha	Bos taurus	26-33
22210900-3	2012	According to this view, under oxidizing conditions occurring during the night the two AGP small subunits (APS1) are covalently linked via an intermolecular disulfide bridge that inactivates the protein, whereas under reducing conditions occurring during the day NADP-thioredoxin reductase C (NTRC)-dependent reductive monomerization of APS1 activates the enzyme.	Disulfides	156-165	ADP-glucose pyrophosphorylase small subunit 2	Arabidopsis thaliana	86-89
2955517-3	1987	The expression of a disulfide-linked and a nondisulfide-linked form of TCR gamma correlates with the use of the C gamma 1 and C gamma 2 constant-region gene segments, respectively.	Disulfides	20-29	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	71-74
33813822-4	2021	Novel Pluronic-based micelles are designed with the pendant pyridyl disulfide group, which are used to conjugate TF-targeting siRNA by the thiol-exchange reaction.	Disulfides	68-77	coagulation factor III, tissue factor	Homo sapiens	113-115
23234010-4	2012	Human epididimis protein 4 (HE4) belongs to a group with four disulfide core proteins.	Disulfides	62-71	WAP four-disulfide core domain 2	Homo sapiens	28-31
33971209-1	2021	Being essential for oxidative protein folding in the mitochondrial intermembrane space, the mitochondrial disulfide relay relies on the electron transfer (ET) from the sulfhydryl oxidase Erv1 to cytochrome c (Cc).	Disulfides	106-115	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	187-191
22054663-8	2012	Furthermore, co-expression of mutant forms of alpha(2)delta-1 Cys404Ser and Cys1047Ser with recombinant neuronal N-type (Ca(V)2.2alpha(1)/beta(3)) channels, showed decreased whole-cell patch-clamp currents indicating that the disulfide bond between these residues is required for alpha(2)delta-1 function.	Disulfides	226-235	caveolin 2	Homo sapiens	104-127
32955262-8	2020	However, PNGase H+ provides broader specificity and greater tolerance to the disulfide-bond reducing agent TCEP, while PNGase A offers advantages in terms of commercial availability and purity.	Disulfides	77-86	N-glycanase 1	Homo sapiens	9-15
32955262-9	2020	Overall, our findings demonstrate the unique features of PNGase H+ for improving conformational analysis of glycoproteins by HDX-MS, in particular, challenging glycoproteins containing both glycosylations and disulfide-bonds.	Disulfides	209-218	N-glycanase 1	Homo sapiens	57-63
22119849-0	2012	Stabilization of vimentin coil2 fragment via an engineered disulfide.	Disulfides	59-68	vimentin	Homo sapiens	17-25
21199936-3	2011	We show that the oxidation state of disulfide groups in the cuticle is tightly regulated during the molting cycle, and that when trxr-1 and gsr-1 function is reduced, disulfide groups in the cuticle remain oxidized.	Disulfides	36-45	Glutathione reductase, mitochondrial	Caenorhabditis elegans	140-145
21199936-3	2011	We show that the oxidation state of disulfide groups in the cuticle is tightly regulated during the molting cycle, and that when trxr-1 and gsr-1 function is reduced, disulfide groups in the cuticle remain oxidized.	Disulfides	167-176	Glutathione reductase, mitochondrial	Caenorhabditis elegans	140-145
22645657-4	2012	The Cys(183)-Cys(232) disulfide bond in mouse CD132 is susceptible to reduction by enzymes such as thioredoxin (TRX), gamma interferon-inducible lysosomal thiolreductase and protein disulfide isomerase, which are commonly secreted during immune activation.	Disulfides	22-31	interferon gamma inducible protein 30	Mus musculus	118-169
22645657-6	2012	Conditions that lead to the reduction of the Cys(183)-Cys(232) disulfide bond in CD132 inhibit proliferation of an IL-2-dependent T cell clone and concomitant inhibition of the STAT-5 signalling pathway.	Disulfides	63-72	signal transducer and activator of transcription 5A	Homo sapiens	177-183
16500675-5	2006	A unique disulfide bond links the alpha1 helix to the beta-sheet floor, explaining the known thermal stability of m144.	Disulfides	9-18	adrenoceptor alpha 1D	Homo sapiens	34-40
23139753-2	2012	HE-4, an epididymal protein, is a member of whey acidic protein four-disulfide core (WFDC) family with no known function.	Disulfides	69-78	WAP four-disulfide core domain 2	Homo sapiens	0-4
7688724-1	1993	Bovine seminal ribonuclease (BS-RNase), a homolog of bovine pancreatic ribonuclease (RNase A), is isolated as a dimer in which the subunits are cross-linked by two disulfide bonds.	Disulfides	164-173	seminal ribonuclease	Bos taurus	7-27
34767654-0	2022	Low light-regulated intramolecular disulfide fine-tunes Arabidopsis PTOX role.	Disulfides	35-44	Alternative oxidase family protein	Arabidopsis thaliana	68-72
23139753-5	2012	Here, we show that HE-4 is secreted in the human seminal fluid as a disulfide-bonded homo-trimer and is a cross-class protease inhibitor inhibits some of the serine, aspartyl and cysteine proteases tested using hemoglobin as a substrate.	Disulfides	68-77	WAP four-disulfide core domain 2	Homo sapiens	19-23
22081312-1	2012	We purified to homogeneity and characterized a heat stable thioredoxin which catalyzes thiol/disulfide exchange reaction, for the first time from dromedary pancreas.	Disulfides	93-102	thioredoxin	Camelus dromedarius	59-70
34952470-4	2022	As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5.	Disulfides	26-35	thioredoxin family protein	Arabidopsis thaliana	75-82
34952470-5	2022	However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown.	Disulfides	85-94	thioredoxin family protein	Arabidopsis thaliana	17-24
34698634-2	2021	We previously showed that EDEM2 stably disulfide-bonded to the thioredoxin domain-containing protein TXNDC11 is responsible for the first step (George et al., 2020).	Disulfides	39-48	thioredoxin domain containing 11	Homo sapiens	101-108
22025616-3	2011	To challenge this proposition, we redesigned the uPAR structure to limit its inherent conformational flexibility by covalently tethering domains DI and DIII via a non-natural interdomain disulfide bond (uPAR(H47C-N259C)).	Disulfides	187-196	plasminogen activator, urokinase receptor	Homo sapiens	49-53
34216797-5	2021	It contains an intramolecular disulfide bond and is thermally stable up to 70  C. NMR resonance assignment of reduced and oxidized SelW1 showed that SelW1 adopts a thioredoxin fold.	Disulfides	30-39	uncharacterized protein	Chlamydomonas reinhardtii	149-154
22025616-3	2011	To challenge this proposition, we redesigned the uPAR structure to limit its inherent conformational flexibility by covalently tethering domains DI and DIII via a non-natural interdomain disulfide bond (uPAR(H47C-N259C)).	Disulfides	187-196	plasminogen activator, urokinase receptor	Homo sapiens	203-207
22050912-9	2011	These results suggest that the HMP is a disulfide-linked protein complex involving mtMGST1, ANT, CypD and function as a MPT pore in PON-induced swelling, in which the Ca(2+) released by PON might play an important role in the complex formation.	Disulfides	40-49	solute carrier family 25 member 6	Homo sapiens	92-95
34473496-3	2021	hBD-3 has six cysteine residues, which form three pairs of disulfide bonds, and those bonds break in the reducing condition.	Disulfides	59-68	defensin beta 103B	Homo sapiens	0-5
21945374-2	2011	However, its 10 disulfide bond forming cysteines have hampered the efficient production of recombinant GLuc and thus limited its use in bio-imaging application.	Disulfides	16-25	glucosylceramidase beta	Homo sapiens	103-107
34573130-6	2021	On the contrary, H2O2 inactivates LasR via producing a disulfide bond between Cys201 and Cys203.	Disulfides	55-64	transcriptional regulator LasR	Pseudomonas aeruginosa PAO1	34-38
21945374-5	2011	Reversed phase HPLC indicated that the GLuc-C9D variant folded with a single disulfide bond pattern after proper oxidization.	Disulfides	77-86	glucosylceramidase beta	Homo sapiens	39-47
21671135-7	2011	RESULTS: Two Fabs move towards Fc asymmetrically repeatedly leading to spatial proximity of LC.Cys214 and HC.Cys128 residues in one Fab with Cys residues in the upper hinge region, which could initiate disulfide scrambling.	Disulfides	202-211	FA complementation group B	Homo sapiens	13-16
34469718-3	2021	First, the signal peptide improves folding fidelity by enhancing conformational plasticity of gp120 by driving disulfide isomerization through a redox-active cysteine.	Disulfides	111-120	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	94-99
34197876-3	2021	Previous studies have shown that beta2GPI adopts two interconvertible biochemical conformations, oxidized and reduced, depending on the integrity of the disulfide bonds.	Disulfides	153-162	apolipoprotein H	Homo sapiens	33-41
32724477-1	2020	Rationale: Endoplasmic reticulum oxidoreductase 1 alpha (ERO1L) is an endoplasmic reticulum (ER) luminal glycoprotein that has a role in the formation of disulfide bonds of secreted proteins and membrane proteins.	Disulfides	154-163	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	11-55
32724477-1	2020	Rationale: Endoplasmic reticulum oxidoreductase 1 alpha (ERO1L) is an endoplasmic reticulum (ER) luminal glycoprotein that has a role in the formation of disulfide bonds of secreted proteins and membrane proteins.	Disulfides	154-163	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	57-62
34197876-4	2021	However, the precise contribution of the disulfide bonds to beta2GPI structure and function is unknown.	Disulfides	41-50	apolipoprotein H	Homo sapiens	60-68
34197876-5	2021	Here, we substituted cysteine residues with serine to investigate how the disulfide bonds C32-C60 in domain I (DI) and C288-C326 in domain V (DV) regulate beta2GPI"s structure and function.	Disulfides	74-83	apolipoprotein H	Homo sapiens	155-163
34197876-9	2021	We conclude that the disulfide bond C288-C326 operates as a molecular switch capable of regulating beta2GPI"s physiological functions in a redox-dependent manner.	Disulfides	21-30	apolipoprotein H	Homo sapiens	99-107
32750885-4	2021	We proposed a GPCR-specified energy function composed of four novel empirical potential energy terms: a two-dimensional contact energy force field, knowledge-based helix pair connection distance energy term, knowledge-based helix pair angle restraint energy term and a disulfide bond energy term.	Disulfides	269-278	vomeronasal 1 receptor 17 pseudogene	Homo sapiens	14-18
21453190-6	2011	The dramatic progress in redox proteomics techniques has enabled the identification of an increasing number of proteins, including peroxiredoxin 1, whose disulfide bond formation and nitrosylation status are regulated by Trx1.	Disulfides	154-163	peroxiredoxin 1	Homo sapiens	131-146
34269678-5	2021	Multiple interaction types are responsible for A2AR oligomerization, including disulfide linkages, hydrogen bonds, electrostatic interactions, and hydrophobic interactions.	Disulfides	79-88	adenosine A2a receptor	Homo sapiens	47-51
21453190-6	2011	The dramatic progress in redox proteomics techniques has enabled the identification of an increasing number of proteins, including peroxiredoxin 1, whose disulfide bond formation and nitrosylation status are regulated by Trx1.	Disulfides	154-163	thioredoxin	Homo sapiens	221-225
22645650-4	2011	These labile disulfide bonds are common, with several classes of proteins being identified and around 30 membrane proteins regularly identified under different reducing conditions including using enzymes such as thioredoxin.	Disulfides	13-22	thioredoxin	Homo sapiens	212-223
34405003-7	2021	Human epididymis protein 4 (HE4) in the whey/four-disulfide core (WFDC) proteins family shows satisfactory sensitivity in the early diagnosis of ovary cancer.	Disulfides	50-59	WAP four-disulfide core domain 2	Homo sapiens	0-26
34405003-7	2021	Human epididymis protein 4 (HE4) in the whey/four-disulfide core (WFDC) proteins family shows satisfactory sensitivity in the early diagnosis of ovary cancer.	Disulfides	50-59	WAP four-disulfide core domain 2	Homo sapiens	28-31
32602810-5	2021	rBAT (heavy subunit; SLC3A1) and catalytic b0,+AT (light subunit; SLC7A9), linked by single disulfide bond, mediate renal reabsorption of cystine and dibasic amino acids in Na+ independent manner.	Disulfides	92-101	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	0-4
32602810-5	2021	rBAT (heavy subunit; SLC3A1) and catalytic b0,+AT (light subunit; SLC7A9), linked by single disulfide bond, mediate renal reabsorption of cystine and dibasic amino acids in Na+ independent manner.	Disulfides	92-101	solute carrier family 7 member 9	Homo sapiens	43-49
32602810-5	2021	rBAT (heavy subunit; SLC3A1) and catalytic b0,+AT (light subunit; SLC7A9), linked by single disulfide bond, mediate renal reabsorption of cystine and dibasic amino acids in Na+ independent manner.	Disulfides	92-101	solute carrier family 7 member 9	Homo sapiens	66-72
21816778-13	2011	Our results highlight the crucial role of C65-C89 disulfide bond in LPL binding by GPIHBP1 Ly6 domain.	Disulfides	50-59	lipoprotein lipase	Homo sapiens	68-71
32606784-1	2020	Background: Quiescin sulfhydryl oxidase 1 (QSOX1) involves in the formation of disulfide bonds and participates in the protein folding process.	Disulfides	79-88	quiescin sulfhydryl oxidase 1	Homo sapiens	12-41
32606784-1	2020	Background: Quiescin sulfhydryl oxidase 1 (QSOX1) involves in the formation of disulfide bonds and participates in the protein folding process.	Disulfides	79-88	quiescin sulfhydryl oxidase 1	Homo sapiens	43-48
34187511-4	2021	Here, we engineered a series of interchain disulfide bonds in the Fab region of IgG-svFv BsAbs and evaluated its biophysical and biological properties.	Disulfides	43-52	FA complementation group B	Homo sapiens	66-69
21844193-7	2011	H(2)O(2) exposure triggers formation of a dual disulfide bonded Yap1 that is catalyzed by the presence of Gpx3 and Ybp1.	Disulfides	47-56	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	106-110
34194623-1	2021	L-type amino acid transporter 1 (LAT1)/SLC7A5 is the first identified CD98 light chain disulfide linked to the CD98 heavy chain (CD98hc/SLC3A2).	Disulfides	87-96	solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2	Mus musculus	70-74
34194623-1	2021	L-type amino acid transporter 1 (LAT1)/SLC7A5 is the first identified CD98 light chain disulfide linked to the CD98 heavy chain (CD98hc/SLC3A2).	Disulfides	87-96	solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2	Mus musculus	111-115
32338875-3	2020	Here, we designed and prepared A6 peptide (sequence: KPSSPPEE)-tagged core-disulfide-crosslinked biodegradable micelles (A6-PMs) for targeted CFZ therapy of CD44-overexpressing LP-1 human MM in vivo.	Disulfides	75-84	CD44 antigen	Mus musculus	157-161
32338875-9	2020	These A6-tagged core-disulfide-crosslinked micelles appear interesting for targeted delivery of proteasome inhibitors to CD44+ MM.	Disulfides	21-30	CD44 antigen	Mus musculus	121-125
34155225-0	2021	A comprehensive analysis of novel disulfide bond introduction site into the constant domain of human Fab.	Disulfides	34-43	FA complementation group B	Homo sapiens	101-104
21844193-7	2011	H(2)O(2) exposure triggers formation of a dual disulfide bonded Yap1 that is catalyzed by the presence of Gpx3 and Ybp1.	Disulfides	47-56	Ybp1p	Saccharomyces cerevisiae S288C	115-119
34155225-2	2021	To identify sites where intermolecular disulfide bond can be introduced into the Fab"s constant domain of the therapeutic IgG, Fab mutants were predicted using the MOE software, a molecular simulator, and expressed in Pichia pastoris.	Disulfides	39-48	FA complementation group B	Homo sapiens	81-84
21940832-0	2011	Complete abolishment of coagulant activity in monomeric disulfide-deficient tissue factor.	Disulfides	56-65	coagulation factor III, tissue factor	Homo sapiens	76-89
34155225-2	2021	To identify sites where intermolecular disulfide bond can be introduced into the Fab"s constant domain of the therapeutic IgG, Fab mutants were predicted using the MOE software, a molecular simulator, and expressed in Pichia pastoris.	Disulfides	39-48	FA complementation group B	Homo sapiens	127-130
34155225-4	2021	All these mutants showed increased thermal stability compared to that of Fab without intermolecular disulfide bond.	Disulfides	100-109	FA complementation group B	Homo sapiens	73-76
34155225-6	2021	Thus, our comprehensive analysis reveals that the introduction of intermolecular disulfide bond in the Fab"s constant domain is possible at various locations.	Disulfides	81-90	FA complementation group B	Homo sapiens	103-106
31989750-4	2020	Similar to insulin and relaxin, INSL5 consists of A and B peptide chains linked by three disulfide bonds, two between the chains and one intrinsic to the A chain.	Disulfides	89-98	insulin-like 5	Mus musculus	32-37
21910912-6	2011	TRX activity was assayed by the insulin disulfide-reducing assay.	Disulfides	40-49	thioredoxin	Homo sapiens	0-3
31760526-2	2020	CRP dissociates into subunits at inflammatory loci forming monomeric CRP (mCRP) with substantially enhanced activities, which can be further activated by reducing the intra-subunit disulfide bond.	Disulfides	181-190	C-reactive protein, pentraxin-related	Mus musculus	74-78
21742866-4	2011	Here we demonstrate that trbB can partially restore transfer of a variant of the distantly related R27 plasmid when both chromosomal and plasmid genes encoding disulfide bond isomerases have been disrupted.	Disulfides	160-169	F pilus assembly periplasmic protein TrbB	Escherichia coli	25-29
32214110-10	2020	Protein Disulfide Isomerase (PDI) mediated inhibition of MIC-A/B surface expression was observed in LMP2A expressing cells.	Disulfides	8-17	mic-a/b	None	57-64
32214110-10	2020	Protein Disulfide Isomerase (PDI) mediated inhibition of MIC-A/B surface expression was observed in LMP2A expressing cells.	Disulfides	8-17	lmp2a	None	100-105
31971218-2	2020	Herein, we report the design and synthesis of a tetrazine-based disulfide rebridging reagent, which allows the site-selective installation of a tetrazine group into disulfide-containing peptides and proteins such as the hormone somatostatin (SST) and the antigen binding fragment (Fab) of human immunoglobulin G (IgG).	Disulfides	64-73	somatostatin	Homo sapiens	228-240
31971218-2	2020	Herein, we report the design and synthesis of a tetrazine-based disulfide rebridging reagent, which allows the site-selective installation of a tetrazine group into disulfide-containing peptides and proteins such as the hormone somatostatin (SST) and the antigen binding fragment (Fab) of human immunoglobulin G (IgG).	Disulfides	64-73	somatostatin	Homo sapiens	242-245
34133931-5	2021	ANAC089 truncated mutants exhibit higher NO and lower ROS and ABA endogenous levels, alongside an altered thiol and disulfide homeostasis.	Disulfides	116-125	NAC domain containing protein 89	Arabidopsis thaliana	0-7
34072343-5	2021	Such structures can act as "seeds" of functionally active PML bodies, providing the necessary concentration of PML isoforms for the formation of intermolecular disulfide bonds between PML monomers.	Disulfides	160-169	PML nuclear body scaffold	Homo sapiens	58-61
34072343-5	2021	Such structures can act as "seeds" of functionally active PML bodies, providing the necessary concentration of PML isoforms for the formation of intermolecular disulfide bonds between PML monomers.	Disulfides	160-169	PML nuclear body scaffold	Homo sapiens	111-114
34072343-5	2021	Such structures can act as "seeds" of functionally active PML bodies, providing the necessary concentration of PML isoforms for the formation of intermolecular disulfide bonds between PML monomers.	Disulfides	160-169	PML nuclear body scaffold	Homo sapiens	184-187
35247515-0	2022	Inhibitors of ERp44, PDIA1, and AGR2 induce disulfide-mediated oligomerization of Death Receptors 4 and 5 and cancer cell death.	Disulfides	44-53	anterior gradient 2, protein disulphide isomerase family member	Homo sapiens	32-36
21742866-5	2011	In addition, we show that TrbB displays both disulfide bond isomerase and reductase activities on substrates not involved in the conjugative process.	Disulfides	45-54	F pilus assembly periplasmic protein TrbB	Escherichia coli	26-30
21742866-6	2011	Unlike canonical members of the disulfide bond isomerase family, secondary structure predictions suggest that TrbB lacks both an N-terminal dimerization domain and an alpha-helical domain found in other disulfide bond isomerases.	Disulfides	32-41	F pilus assembly periplasmic protein TrbB	Escherichia coli	110-114
21742866-8	2011	Interestingly, although TrbB diverges structurally from other disulfide bond isomerases, we show that like those isomerases, TrbB relies on DsbD from E. coli for maintenance of its C-X-X-C redox active site motif.	Disulfides	62-71	F pilus assembly periplasmic protein TrbB	Escherichia coli	125-129
35636326-2	2022	In this study, mineralization-stimulative and antibacterial networking nanostructures are assembled via amyloid-like aggregation of lactoferrin (LF) triggered by reducing the intramolecular disulfide bonds.	Disulfides	190-199	lactotransferrin	Mus musculus	132-143
31971218-2	2020	Herein, we report the design and synthesis of a tetrazine-based disulfide rebridging reagent, which allows the site-selective installation of a tetrazine group into disulfide-containing peptides and proteins such as the hormone somatostatin (SST) and the antigen binding fragment (Fab) of human immunoglobulin G (IgG).	Disulfides	165-174	somatostatin	Homo sapiens	228-240
31971218-2	2020	Herein, we report the design and synthesis of a tetrazine-based disulfide rebridging reagent, which allows the site-selective installation of a tetrazine group into disulfide-containing peptides and proteins such as the hormone somatostatin (SST) and the antigen binding fragment (Fab) of human immunoglobulin G (IgG).	Disulfides	165-174	somatostatin	Homo sapiens	242-245
35636326-2	2022	In this study, mineralization-stimulative and antibacterial networking nanostructures are assembled via amyloid-like aggregation of lactoferrin (LF) triggered by reducing the intramolecular disulfide bonds.	Disulfides	190-199	lactotransferrin	Mus musculus	145-147
21755988-0	2011	Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft.	Disulfides	128-137	thioredoxin	Homo sapiens	101-112
32110281-1	2020	The sequence asparagine-glycine arginine (NGR), flanked by Cysteine (Cys) residues so as to form a disulfide-bridge (CNGRC), has previously been found to target and bind specifically to aminopeptidase N (APN), which is highly expressed on the surface of tumor cells.	Disulfides	99-108	reticulon 4 receptor	Homo sapiens	42-45
21755988-6	2011	Previous work has shown that apo-nNOS can be activated by thiol-disulfide exchange, and we show substantial activation with a small molecule dithiol modeled on the active motifs of thioredoxin and protein disulfide isomerase.	Disulfides	64-73	thioredoxin	Homo sapiens	181-192
21595632-0	2011	Redox properties of the tissue factor Cys186-Cys209 disulfide bond.	Disulfides	52-61	coagulation factor III, tissue factor	Homo sapiens	24-37
31584064-0	2020	Galectin-13/placental protein 13: redox-active disulfides as switches for regulating structure, function and cellular distribution.	Disulfides	47-57	galectin 13	Homo sapiens	0-11
31584064-0	2020	Galectin-13/placental protein 13: redox-active disulfides as switches for regulating structure, function and cellular distribution.	Disulfides	47-57	galectin 13	Homo sapiens	12-32
31584064-3	2020	The previous crystal structure and gel filtration data show that Gal-13 dimerizes via formation of two disulfide bonds formed by Cys136 and Cys138.	Disulfides	103-112	galectin 13	Homo sapiens	65-71
35514997-6	2022	Our analysis of 8 possible dimerization models, suggested that the most likely ERAP1/ERAP2 heterodimerization topology involves the exon 10 loop, a non-conserved loop previously implicated in interactions between ERAP1 and the disulfide-bond shuffling chaperone ERp44.	Disulfides	227-236	endoplasmic reticulum aminopeptidase 1	Homo sapiens	79-84
35091368-5	2022	Conformations of the disulfide/selenosulfide/diselenide were identified using the side-chain torsional angle chi1, chi2, chi3, chi2", chi1" and mapped to one of the possible 32 conformations of the cysteine disulfide.	Disulfides	21-30	chitinase 1	Homo sapiens	121-125
21595632-4	2011	A standard redox potential of -278 mV was determined for the Cys(186)-Cys(209) disulfide of recombinant soluble TF.	Disulfides	79-88	coagulation factor III, tissue factor	Homo sapiens	112-114
20849374-3	2011	Pathways that form disulfide bonds have now been unraveled in the bacterial periplasm (disulfide bond protein A [DsbA], DsbB, DsbC, DsbG, and DsbD), the endoplasmic reticulum (protein disulfide isomerase and Ero1), and the mitochondrial intermembrane space (Mia40 and Erv1).	Disulfides	19-28	growth factor, augmenter of liver regeneration	Homo sapiens	268-272
31790574-1	2020	Disulfide-rich animal venom peptides targeting either the voltage-sensing domain or the pore domain of voltage-gated sodium channel 1.7 (NaV1.7) have been widely studied as drug leads and pharmacological probes for the treatment of chronic pain.	Disulfides	0-9	sodium voltage-gated channel alpha subunit 9	Homo sapiens	137-143
35352250-3	2022	The association of the minor allele rs1046495-C with type 2 diabetes mellitus can be explained by its more pronounced effect on the expression of the GFER enzyme that through glutathionation maintains the ROS level for optimal functioning of complexes III and IV of the electron transport chain and promotes the formation of disulfide bonds in the CHCHD4 chaperone molecule.	Disulfides	325-334	growth factor, augmenter of liver regeneration	Homo sapiens	150-154
21975240-2	2011	The more reactive conformation is the homocysteine thiolactone (HcyT), product to the nonspecific action of methionyl-tRNA synthetase, which is incorporated into proteins by disulfide bonds (S-homocysteinilation) or amide bonds (N-homocysteinilation) affecting protein structure and function leading to cell toxicity, autoimmune responses and atherogenesis.	Disulfides	174-183	methionyl-tRNA synthetase 1	Homo sapiens	108-133
35107099-4	2022	Here we find that TRFS-green, a disulfide containing fluorescent probe which was used to detect thioredoxin reductase (TrxR) in mammalian cells, is a substrate of bacterial Trxs and Grxs, but not a substrate of bacterial TrxR and GSH.	Disulfides	32-41	peroxiredoxin 5	Homo sapiens	96-117
35107099-4	2022	Here we find that TRFS-green, a disulfide containing fluorescent probe which was used to detect thioredoxin reductase (TrxR) in mammalian cells, is a substrate of bacterial Trxs and Grxs, but not a substrate of bacterial TrxR and GSH.	Disulfides	32-41	peroxiredoxin 5	Homo sapiens	119-123
35107099-4	2022	Here we find that TRFS-green, a disulfide containing fluorescent probe which was used to detect thioredoxin reductase (TrxR) in mammalian cells, is a substrate of bacterial Trxs and Grxs, but not a substrate of bacterial TrxR and GSH.	Disulfides	32-41	peroxiredoxin 5	Homo sapiens	221-225
31914632-2	2020	The majority of Prph2 mutations are located in the large intradiscal loop (D2), a region that contains seven cysteines involved in intra- and intermolecular disulfide bonding and protein folding.	Disulfides	157-166	peripherin 2	Homo sapiens	16-21
21337337-5	2011	We show how a fully bioactive protein produced by OCFS from optimized frozen extract can be purified directly using a streamlined purification process that yields a biologically active cytokine, human granulocyte-macrophage colony-stimulating factor, produced at titers of 700 mg/L in 10 h. These results represent a milestone for in vitro protein synthesis, with potential for the cGMP production of disulfide-bonded biotherapeutic proteins.	Disulfides	401-410	colony stimulating factor 2	Homo sapiens	201-249
33615311-6	2020	Besides aiding in protein folding of transmembrane and secretory proteins in conjunction with PDI, ERO1alpha is also known for formation of de novo disulfide bridges.	Disulfides	148-157	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	99-108
35204825-9	2022	Redox sensitivity of p53 functions is supported by (i) thioredoxin-dependent reduction of p53 disulfides, (ii) inhibition of the thioredoxin-dependent deoxyribonucleotide synthesis by p53 binding to RRM2B and (iii) changed intracellular distribution of p53 through its oxidation by CHCHD4 in the mitochondrial intermembrane space.	Disulfides	94-104	thioredoxin	Homo sapiens	55-66
35204259-5	2022	Here we investigated whether Fast-TRFS, a disulfide-containing fluorescent probe utilized in analysis of mammalian thioredoxin reductase, could be used to detect cellular disulfide reducibility in bacteria.	Disulfides	171-180	thioredoxin	Homo sapiens	115-126
35204259-9	2022	The Trx system was shown to be the predominant disulfide reductase for fast disulfide reduction rather than the Grx system.	Disulfides	76-85	thioredoxin	Homo sapiens	4-7
35204259-11	2022	It also indicated that cellular disulfide reduction could be classified into fast and slow reaction, which are predominantly catalyzed by E. coli Trx and Grx system, respectively.	Disulfides	32-41	thioredoxin	Homo sapiens	146-149
21568348-4	2011	This 6-TGNP in turn reacts with the Cys(20) side chain of the redox-sensitive GXXXCGK(S/T)C motif of RhoC to produce a 6-TGNP-RhoC disulfide adduct.	Disulfides	131-140	ras homolog family member C	Homo sapiens	101-105
35282008-4	2022	The analysis of the changes in the content of free SH group and glutenin macropolymer (GMP) demonstrated that the addition of CAS promoted protein disulfide cross-linking and decreased protein mobility during holding.	Disulfides	147-156	BCAR1 scaffold protein, Cas family member	Homo sapiens	126-129
35111980-0	2022	Sensitive and resistant of the homologous disulfide-bridged proteins alpha-lactalbumin and lysozyme to attack of hydrogen-atoms, dithiothreitol and trifluoroacetic acid, examined by matrix-assisted laser desorption/ionization mass spectrometry.	Disulfides	42-51	lactalbumin alpha	Bos taurus	69-86
31575656-2	2020	QSOX1 catalyzes the formation of disulfide bonds in proteins.	Disulfides	33-42	quiescin sulfhydryl oxidase 1	Homo sapiens	0-5
21568348-4	2011	This 6-TGNP in turn reacts with the Cys(20) side chain of the redox-sensitive GXXXCGK(S/T)C motif of RhoC to produce a 6-TGNP-RhoC disulfide adduct.	Disulfides	131-140	ras homolog family member C	Homo sapiens	126-130
31479652-9	2019	S-sulfonation of hTTR at the free cysteine residue in position 10 appears to be the result of a mixed disulfide exchange possibly with S-cysteinylated hTTR or S-cysteinylated HSA.	Disulfides	102-111	transthyretin	Homo sapiens	17-21
35162999-5	2022	We sought to determine whether PDIA3 is required for disulfide bonds of NA, its activity, and propagation of the virus.	Disulfides	53-62	protein disulfide isomerase associated 3	Mus musculus	31-36
21524995-0	2011	Cytosolic CD38 protein forms intact disulfides and is active in elevating intracellular cyclic ADP-ribose.	Disulfides	36-46	CD38 molecule	Homo sapiens	10-14
35162999-6	2022	Requirement of disulfides for NA oligomerization and activity were determined using biotin switch and redox assays in WT and PDIA3-/- in A549 cells.	Disulfides	15-25	protein disulfide isomerase associated 3	Mus musculus	125-130
21422471-5	2011	Arsenic-caused intermolecular disulfide formation in PML also contributes to PML-multimerization.	Disulfides	30-39	PML nuclear body scaffold	Homo sapiens	53-56
34978456-5	2022	Using this strategy, we completed the synthesis of correctly folded hepcidin, an iron-regulating hormone bearing four pairs of disulfide-bonds, and the first total synthesis of correctly folded interleukin-5 (IL-5), a 26 kDa homodimer cytokine responsible for eosinophil growth and differentiation.	Disulfides	127-136	hepcidin antimicrobial peptide	Homo sapiens	68-76
31681379-7	2019	Therefore, land plants evolved additional thiol/disulfide-modulating proteins, such as Low Quantum Yield of PSII 1 (LQY1), to aid in the repair and reassembly cycle of PSII.	Disulfides	48-57	DnaJ/Hsp40 cysteine-rich domain superfamily protein	Arabidopsis thaliana	116-120
31513391-3	2019	Here, we report on trastuzumab-decorated disulfide-cross-linked polymersomes (Tra-Ps) for specific delivery of epirubicin hydrochloride (EPI HCl) to HER2-positive SKOV-3 ovarian tumor.	Disulfides	41-50	T cell receptor alpha locus	Homo sapiens	78-81
21422471-5	2011	Arsenic-caused intermolecular disulfide formation in PML also contributes to PML-multimerization.	Disulfides	30-39	PML nuclear body scaffold	Homo sapiens	77-80
21334075-1	2011	Interferon-gamma-inducible-lysosomal thiol reductase (GILT) plays a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction.	Disulfides	166-175	gamma-interferon-inducible lysosomal thiol reductase	Ovis aries	0-52
31500118-2	2019	Under these conditions, the cytosolic copper chaperone Atox1, which delivers Cu(I) to the secretory pathway, gets oxidized, i.e., a disulfide bond is formed between the cysteine residues of the Cu(I)-binding CxxC motif.	Disulfides	132-141	antioxidant 1 copper chaperone	Homo sapiens	55-60
31299423-7	2019	In addition to the disulfide bond between the Cys10 and Cys13 of SELENOW, a second disulfide bond was formed between Cys33 and Cys87 under oxidative stress conditions.	Disulfides	19-28	selenoprotein W	Mus musculus	65-72
21334075-1	2011	Interferon-gamma-inducible-lysosomal thiol reductase (GILT) plays a key role in the processing and presentation of MHC class II-restricted antigen (Ag) by catalyzing disulfide bond reduction.	Disulfides	166-175	gamma-interferon-inducible lysosomal thiol reductase	Ovis aries	54-58
21371427-1	2011	L-type amino-acid transporter 1 (LAT1) is the first identified light chain of CD98 molecule, disulfide-linked to a heavy chain of CD98.	Disulfides	93-102	solute carrier family 7 member 5	Homo sapiens	33-37
31299423-7	2019	In addition to the disulfide bond between the Cys10 and Cys13 of SELENOW, a second disulfide bond was formed between Cys33 and Cys87 under oxidative stress conditions.	Disulfides	83-92	selenoprotein W	Mus musculus	65-72
21111739-9	2011	Moreover, ethanol feeding induced oxidation of PDI, which might compromise PDI-mediated disulfide bond formation during ER protein folding.	Disulfides	88-97	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	47-50
31299423-8	2019	The second disulfide bond was reduced by Trx1, but the disulfide bond between Cys10 and Cys13 was not.	Disulfides	11-20	thioredoxin 1	Mus musculus	41-45
31299423-10	2019	The second disulfide bond of the mutant SELENOW, in which Cys37 was replaced with Ser, was formed at a much lower concentration of hydrogen peroxide than the wild type.	Disulfides	11-20	selenoprotein W	Mus musculus	40-47
31299423-12	2019	Furthermore, the SELENOW (C33, 87S) mutant, which could not form the second disulfide bond, also showed antioxidant activity.	Disulfides	76-85	selenoprotein W	Mus musculus	17-24
31299423-13	2019	Taken together, these results indicate that GSTpi-mediated S-glutathionylation of mouse SELENOW at Cys33 is required for the protection of cells in conditions of oxidative stress, through inhibition of the formation of the second disulfide bond.	Disulfides	230-239	selenoprotein W	Mus musculus	88-95
21111739-9	2011	Moreover, ethanol feeding induced oxidation of PDI, which might compromise PDI-mediated disulfide bond formation during ER protein folding.	Disulfides	88-97	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	75-78
21132260-7	2011	Furthermore, a glutathione (GSH) bead pull-down assay revealed that the intramolecular disulfide-bonded maspin lost its binding activity to endogenous GST, indicating that intramolecular disulfide-bonded maspin might have some distinct properties under oxidative stress, although the precise biological significance of this modification remains elusive.	Disulfides	87-96	serpin family B member 5	Homo sapiens	104-110
31306516-2	2019	Owing to its lack of disulfides and the calcium-independent activity, APEX2 can be applied intracellularly for targeted electron microscopy imaging or interactome mapping when fusing to a protein of interest.	Disulfides	21-31	apurinic/apyrimidinic endodeoxyribonuclease 2	Homo sapiens	70-75
31306516-10	2019	Overall, we believe APEX2C32S is a superior fusion tag to APEX2 for proximity labeling applications, especially when mismatched disulfide bonding or poor expression is a concern.	Disulfides	128-137	apurinic/apyrimidinic endodeoxyribonuclease 2	Homo sapiens	20-25
21132260-7	2011	Furthermore, a glutathione (GSH) bead pull-down assay revealed that the intramolecular disulfide-bonded maspin lost its binding activity to endogenous GST, indicating that intramolecular disulfide-bonded maspin might have some distinct properties under oxidative stress, although the precise biological significance of this modification remains elusive.	Disulfides	87-96	serpin family B member 5	Homo sapiens	204-210
21132260-7	2011	Furthermore, a glutathione (GSH) bead pull-down assay revealed that the intramolecular disulfide-bonded maspin lost its binding activity to endogenous GST, indicating that intramolecular disulfide-bonded maspin might have some distinct properties under oxidative stress, although the precise biological significance of this modification remains elusive.	Disulfides	187-196	serpin family B member 5	Homo sapiens	104-110
31117394-4	2019	In-cell acylation by this catalyst system is challenging, however, mainly due to the low cell permeability of acyl-CoA and the propensity of DSH to form inactive disulfide.	Disulfides	162-171	dishevelled segment polarity protein 1 pseudogene 1	Homo sapiens	141-144
21132260-7	2011	Furthermore, a glutathione (GSH) bead pull-down assay revealed that the intramolecular disulfide-bonded maspin lost its binding activity to endogenous GST, indicating that intramolecular disulfide-bonded maspin might have some distinct properties under oxidative stress, although the precise biological significance of this modification remains elusive.	Disulfides	187-196	serpin family B member 5	Homo sapiens	204-210
21152909-5	2011	We investigate the interactions between the KCNE1 loop (positions 36-47) and KCNQ1 S1-S2 linker (positions 140-148) by means of disulfide trapping and voltage clamp techniques.	Disulfides	128-137	potassium voltage-gated channel subfamily Q member 1	Homo sapiens	77-82
30971427-3	2019	Because oxidation of cell-surface thiols also alters protein functionality, we hypothesized that increasing the levels of thioredoxin (Trx), an antioxidant molecule facilitating reduction of proteins through cysteine thiol-disulfide exchange, in T cells will promote their sustained antitumor function.	Disulfides	223-232	thioredoxin 1	Mus musculus	122-133
30971427-3	2019	Because oxidation of cell-surface thiols also alters protein functionality, we hypothesized that increasing the levels of thioredoxin (Trx), an antioxidant molecule facilitating reduction of proteins through cysteine thiol-disulfide exchange, in T cells will promote their sustained antitumor function.	Disulfides	223-232	thioredoxin 1	Mus musculus	135-138
30959459-3	2019	This redox state change was accompanied by loss of two surface-exposed disulfide bonds in the catalytic domain of the alpha-2,6-sialyltransferase (ST6Gal-I) and its ability to functionally interact with B4GalT-I, an enzyme adding the preceding galactose to complex N-glycans.	Disulfides	71-80	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	147-155
21029046-8	2011	Apo-GLRX5 reduced glutathione mixed disulfides with a rate 100 times lower than did GLRX2 and was active as a glutathione-dependent electron donor for mammalian ribonucleotide reductase.	Disulfides	36-46	aminopeptidase O (putative)	Homo sapiens	0-9
30668888-0	2019	The N-terminal p.(Ser38Cys) TIMP3 mutation underlying Sorsby fundus dystrophy is a founder mutation disrupting an intramolecular disulfide bond.	Disulfides	129-138	TIMP metallopeptidase inhibitor 3	Homo sapiens	28-33
21150130-6	2011	The resulting ATF6(C)-TAP translocated into the ER, where it was glycosylated and disulfide bonded.	Disulfides	82-91	activating transcription factor 6	Homo sapiens	14-18
30668888-9	2019	In conclusion, we propose a novel pathogenetic mechanism underlying the p.(Ser38Cys) TIMP3 founder mutation involving intramolecular disulfide bonding.	Disulfides	133-142	TIMP metallopeptidase inhibitor 3	Homo sapiens	85-90
21099205-11	2011	These findings suggest that Crp4 has selective bactericidal activities against intestinal microbiota and that the activities are dependent on the disulfide bonds.	Disulfides	146-155	defensin, alpha, 20	Mus musculus	28-32
30850396-7	2019	We applied iTORC to a mouse hepatocyte lysate to identify known sulfenylated and disulfide-bonded proteins, including elongation factor 1-alpha1 and mouse serum albumin, and found that iTORC reliably detected their expected oxidation status.	Disulfides	81-90	eukaryotic translation elongation factor 1 alpha 1	Mus musculus	118-144
30850265-2	2019	The flavin adenosine dinucleotide (FAD) containing endoplasmic reticulum oxidoreductin enzyme (Ero1L) catalyzes de-novo disulfide bridge formation of ER resident proteins and contributes to proper protein folding.	Disulfides	120-129	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	95-100
21062891-4	2011	Here we report a structural model of the p14   bulged duplex interaction based on a combination of X-ray crystallography of an adenine p14/SF3b155 peptide complex, biochemical comparison of a panel of disulfide cross-linked protein-RNA complexes, and small-angle X-ray scattering (SAXS).	Disulfides	201-210	splicing factor 3b subunit 6	Homo sapiens	41-44
20840079-5	2010	Reactions were followed by measuring the accumulation of disulfide-linked Prx dimers, via non-reducing SDS/PAGE, or the loss of the corresponding hydroperoxide, using quench-flow and LC (liquid chromatography)/MS.	Disulfides	57-66	periaxin	Homo sapiens	74-77
20946172-0	2010	Disulfide bond reduction of von Willebrand factor by ADAMTS-13.	Disulfides	0-9	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	53-62
20946172-4	2010	OBJECTIVES: We tested a hypothesis that ADAMTS-13 has a disulfide bond reducing activity that regulates shear-induced thiol-disulfide exchange of VWF.	Disulfides	56-65	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	40-49
30414947-6	2019	Based on these methods, we obtained the structure of Nkrp1b ectodomain in its monomeric and dimeric conformations, identified the dimerization interface, and determined disulfide connections within the molecule.	Disulfides	169-178	killer cell lectin-like receptor subfamily B member 1B	Mus musculus	53-59
20946172-4	2010	OBJECTIVES: We tested a hypothesis that ADAMTS-13 has a disulfide bond reducing activity that regulates shear-induced thiol-disulfide exchange of VWF.	Disulfides	124-133	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	40-49
20946172-6	2010	RESULTS: ADAMTS-13 contains a disulfide bond reducing activity that primarily targets disulfide bonds in plasma-type VWF multimers induced by high shear stress or formed with thiol beads, but not disulfide bonds in native multimeric structures.	Disulfides	30-39	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	9-18
20946172-6	2010	RESULTS: ADAMTS-13 contains a disulfide bond reducing activity that primarily targets disulfide bonds in plasma-type VWF multimers induced by high shear stress or formed with thiol beads, but not disulfide bonds in native multimeric structures.	Disulfides	86-95	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	9-18
30867731-1	2019	Neuron-derived neurotrophic factor (NDNF) is a glycosylated, disulfide-bonded secretory protein that contains a fibronectin type III domain.	Disulfides	61-70	neuron derived neurotrophic factor	Homo sapiens	0-34
20946172-6	2010	RESULTS: ADAMTS-13 contains a disulfide bond reducing activity that primarily targets disulfide bonds in plasma-type VWF multimers induced by high shear stress or formed with thiol beads, but not disulfide bonds in native multimeric structures.	Disulfides	86-95	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	9-18
30867731-1	2019	Neuron-derived neurotrophic factor (NDNF) is a glycosylated, disulfide-bonded secretory protein that contains a fibronectin type III domain.	Disulfides	61-70	neuron derived neurotrophic factor	Homo sapiens	36-40
20946172-11	2010	CONCLUSIONS: This novel disulfide-bond-reducing activity of ADAMTS-13 may prevent covalent lateral association and increased platelet adherence of plasma-type VWF multimers induced by high fluid shear stress.	Disulfides	24-33	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	60-69
20668226-1	2010	Protein disulfide isomerase (PDI) catalyzes the oxidation reduction and isomerization of disulfide bonds.	Disulfides	8-17	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	29-32
30030721-3	2019	This study aimed to evaluate the effect of reduction of disulfide bonds of BLG with different rice thioredoxins (Trxs) on its digestibility and allergenicity.	Disulfides	56-65	beta-lactoglobulin	Bos taurus	75-78
30030721-5	2019	Based on SDS-PAGE, HPLC analysis, and competitive ELISA, the reduction of disulfide bonds of BLG with OsNTRB/OsTrx23, OsNTRB/OsTrx1, GSH/OsTrx1, or GSH/OsTrx20 increased its trypsin digestibility and reduced its immunoreactivity.	Disulfides	74-83	beta-lactoglobulin	Bos taurus	93-96
20831872-7	2010	Further analysis of binding and functional data suggests that the ASIP C-terminal loop (a six-amino-acid segment closed by the final disulfide bond) is essential for high-affinity MC1R binding and inverse agonism.	Disulfides	133-142	melanocortin 1 receptor	Homo sapiens	180-184
30650365-5	2019	We demonstrate that unfolded reduced proteins, upon translocation into the IMS, initiate formation of a metastable disulfide-linked complex with CHCHD4.	Disulfides	115-124	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	145-151
20136511-6	2010	After disulfide transfer from Tim40/Mia40 to substrate proteins, Tim40/Mia40 is reoxidized again by Erv1, which is then oxidized by electron transfer to either cytochrome c or molecular oxygen.	Disulfides	6-15	growth factor, augmenter of liver regeneration	Homo sapiens	100-104
21076498-3	2010	Covalent binding of these molecules slightly decreases the disulfide-reducing activity of recombinant TRX1, when compared with the effect of strong thioalkylating agents such as N-ethylmaleimide.	Disulfides	59-68	thioredoxin	Homo sapiens	102-106
29577955-1	2019	Adrenomedullin (AM), a peptide isolated from an extract of human pheochromocytoma, comprises 52 amino acids with an intramolecular disulfide bond and amidation at the carboxy-terminus.	Disulfides	131-140	adrenomedullin	Homo sapiens	16-18
30367560-3	2019	Quiescin sulfhydryl oxidase 1 (QSOX1), a catalyst of disulfide bond formation secreted by fibroblasts, is a multi-domain thioredoxin superfamily enzyme with certain similarities to the protein disulfide isomerase (PDI) enzymes.	Disulfides	53-62	quiescin sulfhydryl oxidase 1	Homo sapiens	0-29
30367560-3	2019	Quiescin sulfhydryl oxidase 1 (QSOX1), a catalyst of disulfide bond formation secreted by fibroblasts, is a multi-domain thioredoxin superfamily enzyme with certain similarities to the protein disulfide isomerase (PDI) enzymes.	Disulfides	53-62	quiescin sulfhydryl oxidase 1	Homo sapiens	31-36
30367560-10	2019	IMPACT STATEMENT: We show that mutation of a conserved cis-proline amino acid, analogous to a mutation used to trap substrates of a bacterial disulfide catalyst, has a dramatic effect on the physiological function of the mammalian disulfide catalyst QSOX1.	Disulfides	142-151	quiescin sulfhydryl oxidase 1	Homo sapiens	250-255
30367560-10	2019	IMPACT STATEMENT: We show that mutation of a conserved cis-proline amino acid, analogous to a mutation used to trap substrates of a bacterial disulfide catalyst, has a dramatic effect on the physiological function of the mammalian disulfide catalyst QSOX1.	Disulfides	231-240	quiescin sulfhydryl oxidase 1	Homo sapiens	250-255
20969804-4	2010	RESULTS: NDNF is a glycosylated, disulfide-bonded secretory protein that contains a fibronectin type III domain.	Disulfides	33-42	neuron-derived neurotrophic factor	Mus musculus	9-13
30100456-6	2018	Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation.	Disulfides	45-54	beta-lactoglobulin	Bos taurus	163-166
20981267-6	2010	In addition to the identified candidate nsSNPs for increased or reduced arsenic responsiveness, we observed i) a nsSNP that results in the breakage of a disulfide bond, as candidate marker for reduced arsenic responsiveness of KLK7, a secreted serine protease participate in normal shedding of the skin; and ii) 6 pairs of vicinal cysteines in KLK7 protein that could be binding sites for arsenic.	Disulfides	153-162	kallikrein related peptidase 7	Homo sapiens	227-231
30524244-2	2018	Recently, we have reported that protein disulfide isomerase (PDI) reduces disulfide bond (S-S) to free thiol (-SH) on NMDAR.	Disulfides	40-49	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	61-64
20981267-6	2010	In addition to the identified candidate nsSNPs for increased or reduced arsenic responsiveness, we observed i) a nsSNP that results in the breakage of a disulfide bond, as candidate marker for reduced arsenic responsiveness of KLK7, a secreted serine protease participate in normal shedding of the skin; and ii) 6 pairs of vicinal cysteines in KLK7 protein that could be binding sites for arsenic.	Disulfides	153-162	kallikrein related peptidase 7	Homo sapiens	344-348
20621156-12	2010	GSH should combine with the hAS3MT after the methylation to reduce the disulfide bond formed during the catalytic cycle in the hAS3MT to resume the active form of the enzyme.	Disulfides	71-80	PDS5 cohesin associated factor B	Homo sapiens	28-32
20506311-4	2010	Endoplasmic reticulum oxidoreductase (ERO1L) maintains PDI in an oxidized state so that disulfide bond formation occurs.	Disulfides	88-97	endoplasmic reticulum oxidoreductase 1 alpha	Rattus norvegicus	38-43
30346167-5	2018	Molecular docking of peptide ensembles from NMR into a homology model-derived NaV1.7 structure supported prioritization of key residues clustered on a hydrophobic face of the disulfide-rich folded peptide for derivatization.	Disulfides	175-184	sodium voltage-gated channel alpha subunit 9	Homo sapiens	78-84
30464464-10	2018	Intracellular trafficking and in vitro expression study indicated that the DHP nanocomplex escaped from lysosomes and the disulfide bonds between PAMAM and PEG cleaved due to the high concentration of GSH in the cytoplasm, pDNA consequently became exclusively located in the nucleus under the guidance of HMGB1, thereby promoting the red fluorescence protein (RFP) expression.	Disulfides	122-131	tripartite motif containing 27	Homo sapiens	360-363
20506311-5	2010	Here, PDI and its helper protein, ERO1L were overexpressed in rCHO cells producing an Ab in an attempt to ease the bottleneck in disulfide bond formation, and hence, Ab folding and secretion.	Disulfides	129-138	endoplasmic reticulum oxidoreductase 1 alpha	Rattus norvegicus	34-39
20540164-5	2010	The MALDI-MS analysis of Glu-C digested, purified intermediates indicated that an intra-A-chain disulfide bond formed first among A6, A7, and A11.	Disulfides	96-105	DXS435E	Homo sapiens	142-145
30076903-0	2018	Cysteine mediated disulfide bond formation in RAGE V domain facilitates its functionally relevant dimerization.	Disulfides	18-27	advanced glycosylation end-product specific receptor	Homo sapiens	46-50
20540164-6	2010	Various non-native intra-A (A20 with A6, A7, or A11), intra-B (between B7 and B19), and inter-A-B disulfide bonds were observed in the intermediates with two disulfide bonds.	Disulfides	158-167	DXS435E	Homo sapiens	48-51
30011082-0	2018	Binding of p67phox to Nox2 is stabilized by disulfide bonds between cysteines in the 369 Cys-Gly-Cys371 triad in Nox2 and in p67phox.	Disulfides	44-53	cytochrome b-245 beta chain	Homo sapiens	22-26
30011082-0	2018	Binding of p67phox to Nox2 is stabilized by disulfide bonds between cysteines in the 369 Cys-Gly-Cys371 triad in Nox2 and in p67phox.	Disulfides	44-53	cytochrome b-245 beta chain	Homo sapiens	113-117
20570702-0	2010	Role of the intra-A-chain disulfide bond of insulin-like peptide 3 in binding and activation of its receptor, RXFP2.	Disulfides	26-35	relaxin family peptide receptor 2	Homo sapiens	110-115
30011082-6	2018	Results show that the primary interaction of p67phox with Nox2 is followed by a stabilizing step, based on the establishment of disulfide bonds between cysteine(s) in the 369 Cys-Gly-Cys371 triad and cysteine(s) in p67phox .	Disulfides	128-137	cytochrome b-245 beta chain	Homo sapiens	58-62
20550946-6	2010	Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER).	Disulfides	8-17	thioredoxin	Homo sapiens	53-64
20550946-6	2010	Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER).	Disulfides	8-17	thioredoxin	Homo sapiens	66-68
20550946-6	2010	Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER).	Disulfides	127-136	thioredoxin	Homo sapiens	53-64
30138703-1	2018	A carrier-free and reduction-degradable Janus prodrug, termed as CPT-SS-GEM, was fabricated by redox-sensitive disulfide bond linked gemcitabine and camptothecin.	Disulfides	111-120	choline phosphotransferase 1	Homo sapiens	65-68
20550946-6	2010	Protein disulfide isomerase (PDI) is a member of the thioredoxin (TX) superfamily and is believed to accelerate the folding of disulfide-bonded proteins by catalyzing the disulfide interchange reaction, which is the rate-limiting step during protein folding in the luminal space of the endoplasmic reticulum (ER).	Disulfides	127-136	thioredoxin	Homo sapiens	66-68
19958171-6	2010	Oxidized protein repair systems, thioredoxin/thioredoxin reductase or glutaredoxin/glutathione/glutathione reductase that catalytically reduce disulfide bridges or sulfenic acids, and methionine sulfoxide reductase that reverses methionine sulfoxide back to methionine within proteins, are present in the mitochondrial matrix.	Disulfides	143-152	thioredoxin	Homo sapiens	33-44
30052299-6	2018	Using mass spectrometry analyses of recombinant dUTPase constructs, we have discovered an intermolecular disulfide bridge between cysteine-3 of each nDut monomer.	Disulfides	105-114	Deoxyuridine triphosphatase	Drosophila melanogaster	48-55
19958171-6	2010	Oxidized protein repair systems, thioredoxin/thioredoxin reductase or glutaredoxin/glutathione/glutathione reductase that catalytically reduce disulfide bridges or sulfenic acids, and methionine sulfoxide reductase that reverses methionine sulfoxide back to methionine within proteins, are present in the mitochondrial matrix.	Disulfides	143-152	peroxiredoxin 5	Homo sapiens	45-66
20448108-3	2010	Recently, the protein disulfide isomerase (PDI) has been hypothesized to regulate TF decryption through the redox switch of an exposed disulfide in TF extracellular domain.	Disulfides	22-31	coagulation factor III, tissue factor	Homo sapiens	82-84
20448108-3	2010	Recently, the protein disulfide isomerase (PDI) has been hypothesized to regulate TF decryption through the redox switch of an exposed disulfide in TF extracellular domain.	Disulfides	22-31	coagulation factor III, tissue factor	Homo sapiens	148-150
29995353-5	2018	Meanwhile, the Qu released concomitantly with the breakdown of disulfide bonds combines with P-gp and inhibits the drug efflux triggered by P-gp.	Disulfides	63-72	phosphoglycolate phosphatase	Mus musculus	93-97
20572017-0	2010	Probing local structural fluctuations in myoglobin by size-dependent thiol-disulfide exchange.	Disulfides	75-84	myoglobin	Homo sapiens	41-50
29995353-5	2018	Meanwhile, the Qu released concomitantly with the breakdown of disulfide bonds combines with P-gp and inhibits the drug efflux triggered by P-gp.	Disulfides	63-72	phosphoglycolate phosphatase	Mus musculus	140-144
20651086-0	2010	Tissue factor mutated at the allosteric Cys186-Cys209 disulfide bond is severely impaired in decrypted procoagulant activity.	Disulfides	54-63	coagulation factor III, tissue factor	Homo sapiens	0-13
29949057-1	2018	Reduced Oxytocin: Influence of Disulfide Bridges on CID and Vacuum UV Photo-Fragmentation.	Disulfides	31-40	oxytocin/neurophysin I prepropeptide	Homo sapiens	8-16
29949057-3	2018	In particular, the effect of the presence (or absence in reduced OT) of oxytocin"s internal disulfide bridge is evaluated in terms of photo-fragmentation yield and nature of the photo-fragments.	Disulfides	92-101	oxytocin/neurophysin I prepropeptide	Homo sapiens	72-80
20053169-2	2010	It is composed of a specific light chain, xCT, and a heavy chain, 4F2, linked by a disulfide bridge.	Disulfides	83-92	solute carrier family 3 member 2	Homo sapiens	66-69
20426484-4	2010	Here we show that the Cys residues in the CPC motif of the PICK1 PDZ domain forms reversible, intermolecular disulfide bonds under mild oxidation conditions.	Disulfides	109-118	protein interacting with PRKCA 1	Homo sapiens	59-64
30135511-5	2018	MRJP1 has a unique six-bladed beta-propeller fold with three disulfide bonds, and it interacts with apisimin mainly by hydrophobic interaction.	Disulfides	61-70	major royal jelly protein 1	Apis mellifera	0-5
29999306-3	2018	Currently, the disulfide bond between the two conserved cysteines in the ECL2 and TM3 is considered to be a basic GPCR structural feature.	Disulfides	15-24	tropomyosin 3	Homo sapiens	82-85
20426484-5	2010	Importantly, formation of the disulfide-mediated dimer abolishes the lipid membrane binding capacity of the PICK1 PDZ domain and thereby is expected to alter the cellular functions of PICK1.	Disulfides	30-39	protein interacting with PRKCA 1	Homo sapiens	108-113
20426484-5	2010	Importantly, formation of the disulfide-mediated dimer abolishes the lipid membrane binding capacity of the PICK1 PDZ domain and thereby is expected to alter the cellular functions of PICK1.	Disulfides	30-39	protein interacting with PRKCA 1	Homo sapiens	184-189
20426484-6	2010	The structures of the PDZ dimers provide atomic-scale pictures of disulfide-mediated PICK1 dimer formation and a molecular explanation of the oxidation-induced dissociation of PICK1 from membranes.	Disulfides	66-75	protein interacting with PRKCA 1	Homo sapiens	85-90
29789425-3	2018	The aim of the present work was to characterize their circulating forms to better understand how their activities are regulated in vivo First, by cotransfecting BMP9 and BMP10, we found that both can form a disulfide-bonded heterodimer in vitro and that this heterodimer is functional on endothelial cells via ALK1.	Disulfides	207-216	growth differentiation factor 2	Mus musculus	161-165
20426484-6	2010	The structures of the PDZ dimers provide atomic-scale pictures of disulfide-mediated PICK1 dimer formation and a molecular explanation of the oxidation-induced dissociation of PICK1 from membranes.	Disulfides	66-75	protein interacting with PRKCA 1	Homo sapiens	176-181
29789425-3	2018	The aim of the present work was to characterize their circulating forms to better understand how their activities are regulated in vivo First, by cotransfecting BMP9 and BMP10, we found that both can form a disulfide-bonded heterodimer in vitro and that this heterodimer is functional on endothelial cells via ALK1.	Disulfides	207-216	bone morphogenetic protein 10	Mus musculus	170-175
20306235-16	2010	Recent evidence suggests selenoprotein W and the six other small thioredoxin-like mammalian selenoproteins may serve to transduce hydrogen peroxide signals into regulatory disulfide bonds in specific target proteins.	Disulfides	172-181	thioredoxin	Homo sapiens	65-76
32254339-9	2018	These hyaluronic acid-shelled and disulfide-crosslinked micelles with great simplicity and selectivity are highly promising for treating various CD44-overexpressing cancers.	Disulfides	34-43	CD44 antigen	Mus musculus	145-149
20235151-2	2010	Arsenic activated c-RET kinase with promotion of disulfide bond-mediated dimerization of c-RET protein.	Disulfides	49-58	ret proto-oncogene	Homo sapiens	91-94
20454679-10	2010	Inhibition of Glo1 by chemical reaction with its co-factor and the role of its intramolecular disulfides are expected to be important factors within the context of redox-dependent regulation of glucose metabolism in cells.	Disulfides	94-104	glyoxalase I	Homo sapiens	14-18
29596046-5	2018	Furthermore, our insulin-bound IDE structures explain how IDE processively degrades insulin by stochastically cutting either chain without breaking disulfide bonds.	Disulfides	148-157	insulin degrading enzyme	Homo sapiens	31-34
29596046-5	2018	Furthermore, our insulin-bound IDE structures explain how IDE processively degrades insulin by stochastically cutting either chain without breaking disulfide bonds.	Disulfides	148-157	insulin degrading enzyme	Homo sapiens	58-61
20219472-13	2010	Our data indicate that in vitro, HuR RRM1 and RRM1,2 homodimerization involves a disulfide bond at cysteine 13.	Disulfides	81-90	ELAV like RNA binding protein 1	Homo sapiens	33-36
29288085-12	2018	Disulfide bonds in PAG enables a rapid disassembly of PAG micelles in response to reducing agents and to release all loaded drugs (DTX, GA and MMP-9 shRNA) at tumor sites.	Disulfides	0-9	phosphoprotein membrane anchor with glycosphingolipid microdomains 1	Homo sapiens	19-22
20108326-4	2010	Extraction of Spetex-1 from spermatozoa by SDS or urea required dithiothreitol, suggesting crosslinking by disulfide bond is involved in the assembly of satellite fibrils containing Spetex-1.	Disulfides	107-116	spermatogenesis associated 18	Homo sapiens	182-190
29288085-12	2018	Disulfide bonds in PAG enables a rapid disassembly of PAG micelles in response to reducing agents and to release all loaded drugs (DTX, GA and MMP-9 shRNA) at tumor sites.	Disulfides	0-9	phosphoprotein membrane anchor with glycosphingolipid microdomains 1	Homo sapiens	54-57
29288085-12	2018	Disulfide bonds in PAG enables a rapid disassembly of PAG micelles in response to reducing agents and to release all loaded drugs (DTX, GA and MMP-9 shRNA) at tumor sites.	Disulfides	0-9	matrix metallopeptidase 9	Homo sapiens	143-148
20163832-4	2010	Experimental evidence debate the disulfide switch model of TF decryption and its regulation by PDI.	Disulfides	33-42	coagulation factor III, tissue factor	Homo sapiens	59-61
29463024-8	2018	The analysis of sera of patients provided these major findings: the circulating VTN fragment (i) is overexpressed in NASH patients and positively correlates with the NASH activity score (NAS); (ii) originates from the disulfide bond reduction between the V10 and the V65 subunits.	Disulfides	218-227	vitronectin	Homo sapiens	80-83
20056998-1	2010	In the endoplasmic reticulum (ER), a number of thioredoxin (Trx) superfamily proteins are present to enable correct disulfide bond formation of secretory and membrane proteins via Trx-like domains.	Disulfides	116-125	thioredoxin	Homo sapiens	47-58
29307194-5	2018	The derivative TP-disulfide-CR7 (TP-S-S-CR7) containing a disulfide linkage between TP and R7 possesses less toxicity at various concentrations on the immortal human keratinocyte (HaCaT) cell line by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay compared with free TP.	Disulfides	18-27	teratocarcinoma-derived growth factor 1 pseudogene 7	Homo sapiens	28-31
29307194-5	2018	The derivative TP-disulfide-CR7 (TP-S-S-CR7) containing a disulfide linkage between TP and R7 possesses less toxicity at various concentrations on the immortal human keratinocyte (HaCaT) cell line by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay compared with free TP.	Disulfides	18-27	teratocarcinoma-derived growth factor 1 pseudogene 7	Homo sapiens	40-43
20056998-1	2010	In the endoplasmic reticulum (ER), a number of thioredoxin (Trx) superfamily proteins are present to enable correct disulfide bond formation of secretory and membrane proteins via Trx-like domains.	Disulfides	116-125	thioredoxin	Homo sapiens	60-63
20056998-1	2010	In the endoplasmic reticulum (ER), a number of thioredoxin (Trx) superfamily proteins are present to enable correct disulfide bond formation of secretory and membrane proteins via Trx-like domains.	Disulfides	116-125	thioredoxin	Homo sapiens	180-183
29348576-0	2018	Redundancy of protein disulfide isomerases in the catalysis of the inactivating disulfide switch in A Disintegrin and Metalloprotease 17.	Disulfides	22-31	ADAM metallopeptidase domain 17	Homo sapiens	100-136
20097862-2	2010	ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation.	Disulfides	172-181	hypothetical protein	Escherichia coli	0-4
20039682-0	2010	Determination of Fab-hinge disulfide connectivity in structural isoforms of a recombinant human immunoglobulin G2 antibody.	Disulfides	27-36	FA complementation group B	Homo sapiens	17-20
28801097-5	2018	Moreover, the films processed by compression moulding showed enhanced tensile strength, which increased with the incorporation of hydrolyzed keratin due to the formation of disulfide bonds.	Disulfides	173-182	keratin	Gallus gallus	141-148
19731375-8	2010	The approach correctly predicted the system of disulfide bridges between the EC loops in A2AR and elucidated the probable pathways for forming this system.	Disulfides	47-56	adenosine A2a receptor	Homo sapiens	89-93
29478057-5	2018	RESULTS AND CONCLUSIONS: Significant blood-brain barrier disruption appeared 24 h after injection of lipopolysaccharide, disulfide HMGB1, or fully reduced HMGB1 compared to controls, as assessed in post-gadolinium T1-weighted MRI images and confirmed by increased uptake of FITC-conjugated dextran.	Disulfides	121-130	high mobility group box 1	Rattus norvegicus	131-136
29478057-7	2018	Additionally, disulfide HMGB1 increased major histocompatibility complex class II expression and apoptosis.	Disulfides	14-23	high mobility group box 1	Rattus norvegicus	24-29
29127146-2	2017	In this study, we investigated a major immunogenic peptide in glucose-6-phosphate isomerase (G6PI), a potential autoantigen in rheumatoid arthritis, which can form internal disulfide bonds.	Disulfides	173-182	glucosamine-6-phosphate deaminase 1	Mus musculus	62-91
29127146-2	2017	In this study, we investigated a major immunogenic peptide in glucose-6-phosphate isomerase (G6PI), a potential autoantigen in rheumatoid arthritis, which can form internal disulfide bonds.	Disulfides	173-182	glucosamine-6-phosphate deaminase 1	Mus musculus	93-97
20018758-2	2010	Bacterial homologs of VKOR were recently found to participate in a pathway leading to disulfide bond formation in secreted proteins of many bacteria.	Disulfides	86-95	vitamin K epoxide reductase complex subunit 1	Homo sapiens	22-26
29270408-6	2017	Most IMS proteins lack presequences and instead utilize the IMS receptor Mia40, which facilitates their translocation across the outer membrane in a reaction that is coupled to the formation of disulfide bonds within the protein.	Disulfides	194-203	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	73-78
29270408-8	2017	Mia40 fulfills two roles: First, it acts as a holdase, which is crucial in the import of IMS proteins and second, it functions as a foldase, introducing disulfide bonds into newly imported proteins, which induces and stabilizes their natively folded state.	Disulfides	153-162	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
20018758-6	2010	We present a simple assay in Escherichia coli, based on a disulfide-sensitive beta-galactosidase, which can be used to screen for stronger inhibitors of the M. tuberculosis VKOR homolog.	Disulfides	58-67	vitamin K epoxide reductase complex subunit 1	Homo sapiens	173-177
20609916-5	2010	The active site of Trx contains two cysteine residues that undergo reversible oxidation to form a disulfide bond with each other, so that the conformation of Trx is changed by intracellular redox conditions.	Disulfides	98-107	thioredoxin	Homo sapiens	19-22
20609916-5	2010	The active site of Trx contains two cysteine residues that undergo reversible oxidation to form a disulfide bond with each other, so that the conformation of Trx is changed by intracellular redox conditions.	Disulfides	98-107	thioredoxin	Homo sapiens	158-161
19852990-5	2010	Circular dichroism spectroscopy and nuclear magnetic resonance analyses showed that the structure of the recombinant peptide was identical to that of the chemically synthesized and oxidized LEAP-2, with two disulfide bonds between Cys residues in relative 1-3 and 2-4 positions.	Disulfides	207-216	liver enriched antimicrobial peptide 2	Homo sapiens	190-196
19852990-12	2010	The DNA-binding efficacy of linear LEAP-2 was three times higher than that of the peptide-containing disulfide bridges.	Disulfides	101-110	liver enriched antimicrobial peptide 2	Homo sapiens	35-41
19376195-8	2009	Beyond, the degenerate GSH specificity of GPx-4 allows selenylation and oxidation to disulfides of protein thiols.	Disulfides	85-95	glutathione peroxidase 4	Homo sapiens	42-47
19734147-0	2009	Structural mapping of post-translational modifications in human interleukin-24: role of N-linked glycosylation and disulfide bonds in secretion and activity.	Disulfides	115-124	interleukin 24	Homo sapiens	64-78
19734147-2	2009	The primary sequence of human IL-24 differs from homologous cytokines, because it possesses three consensus N-linked glycosylation sites and the potential for a single disulfide bond.	Disulfides	168-177	interleukin 24	Homo sapiens	30-35
19734147-8	2009	These structure-function relationships show that, although IL-24 is a member of the IL-19 subfamily of IL-10-like cytokines by sequence similarity, its surface properties and its distinctive disulfide arrangement make it unique.	Disulfides	191-200	interleukin 24	Homo sapiens	59-64
19703468-1	2009	The Mia40-Erv1 disulfide relay system is of high importance for mitochondrial biogenesis.	Disulfides	15-24	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	10-14
19703468-6	2009	Among these, three represent novel proteins, which we named Cmc2 to 4 (for Cx(9)C motif-containing protein) and which we demonstrated to be dependent for import on the Mia40-Erv1 disulfide relay.	Disulfides	179-188	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	174-178
19766572-5	2009	Prdx1 activates GDE2 through reduction of an intramolecular disulfide bond that bridges its intracellular N- and C-terminal domains.	Disulfides	60-69	peroxiredoxin 1	Homo sapiens	0-5
19674100-7	2009	CD spectroscopic analysis and peptide mapping showed that the refolded INSL3 possessed an insulin-like fold with the expected disulfide linkages.	Disulfides	126-135	insulin like 3	Homo sapiens	71-76
19581399-5	2009	HNP-1 required intact disulfide bonds to prevent toxin-mediated hemolysis.	Disulfides	22-31	HNP1	Homo sapiens	0-5
19588976-5	2009	MS-based structural insights evidenced that heterogeneous disulfide bridge pairings of recombinant JAM-A alter neither its native structure nor mAbs 6F4 recognition properties.	Disulfides	58-67	F11 receptor	Mus musculus	99-104
19583593-1	2009	Protein disulfide isomerase (PDI) and other PDI family proteins are members of the thioredoxin superfamily and are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum (ER).	Disulfides	8-17	protein disulfide-isomerase	Glycine max	29-32
19583593-1	2009	Protein disulfide isomerase (PDI) and other PDI family proteins are members of the thioredoxin superfamily and are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum (ER).	Disulfides	8-17	protein disulfide-isomerase	Glycine max	44-47
19570911-5	2009	First, in H(2)O(2)-treated cells, Trx1 reduces the various disulfide bonds generated between cysteines of ASK1 by a rapid and transient action.	Disulfides	59-68	thioredoxin	Homo sapiens	34-38
19570911-5	2009	First, in H(2)O(2)-treated cells, Trx1 reduces the various disulfide bonds generated between cysteines of ASK1 by a rapid and transient action.	Disulfides	59-68	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	106-110
19432421-1	2009	Urotensin II (U-II) is a disulfide bridged peptide hormone identified as the ligand of a G protein-coupled receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	0-12
19432421-1	2009	Urotensin II (U-II) is a disulfide bridged peptide hormone identified as the ligand of a G protein-coupled receptor.	Disulfides	25-34	urotensin 2	Homo sapiens	14-18
26609860-2	2009	The three disulfide bonds -CH2-S-S-CH2- were simultaneously described at the MP2/6-31+G**(S),6-31G*(C,H) level of theory, and the remaining of the 29 residues of kalata B1 were described by the CHARMM27 force field.	Disulfides	10-19	tryptase pseudogene 1	Homo sapiens	77-85
19364476-3	2009	Mammalian thioredoxin reductases are selenium-containing flavoprotein oxidoreductases, dependent upon a selenocysteine residue for reduction of the active site disulfide in thioredoxins.	Disulfides	160-169	thioredoxin	Homo sapiens	10-21
19636948-4	2009	Like other PTPases, PRL-1 is inhibited by oxidation at its active site Cys, however, disulfide bond formation occurs unusually readily in wild-type PRL-1.	Disulfides	85-94	protein tyrosine phosphatase 4A1	Homo sapiens	20-25
19636948-4	2009	Like other PTPases, PRL-1 is inhibited by oxidation at its active site Cys, however, disulfide bond formation occurs unusually readily in wild-type PRL-1.	Disulfides	85-94	protein tyrosine phosphatase 4A1	Homo sapiens	148-153
19038358-6	2009	Grx1 catalyzes the reduction of two disulfide bridges in gp120 in a similar manner as PDI.	Disulfides	36-45	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	57-62
19341304-3	2009	PRL-1 activity is inhibited by disulfide bond formation at the active site in vitro, suggesting PRL-1 may be susceptible to redox regulation in vivo.	Disulfides	31-40	protein tyrosine phosphatase 4A1	Homo sapiens	0-5
19341304-3	2009	PRL-1 activity is inhibited by disulfide bond formation at the active site in vitro, suggesting PRL-1 may be susceptible to redox regulation in vivo.	Disulfides	31-40	protein tyrosine phosphatase 4A1	Homo sapiens	96-101
19341304-4	2009	Because PRL-1 has been observed to localize to several different subcellular locations and cellular redox conditions vary with tissue type, age, stage of cell cycle, and subcellular location, we determined the reduction potential of the active site disulfide bond that controls phosphatase activity to improve our understanding of the function of PRL-1 in various cellular environments.	Disulfides	249-258	protein tyrosine phosphatase 4A1	Homo sapiens	8-13
19341304-4	2009	Because PRL-1 has been observed to localize to several different subcellular locations and cellular redox conditions vary with tissue type, age, stage of cell cycle, and subcellular location, we determined the reduction potential of the active site disulfide bond that controls phosphatase activity to improve our understanding of the function of PRL-1 in various cellular environments.	Disulfides	249-258	protein tyrosine phosphatase 4A1	Homo sapiens	347-352
19293155-7	2009	DJ-1 was apparently recruited into the ASK1 signalosome via Cys-106-linked mixed disulfides.	Disulfides	81-91	Parkinson disease (autosomal recessive, early onset) 7	Mus musculus	0-4
19293155-7	2009	DJ-1 was apparently recruited into the ASK1 signalosome via Cys-106-linked mixed disulfides.	Disulfides	81-91	mitogen-activated protein kinase kinase kinase 5	Mus musculus	39-43
19409522-1	2009	A disulfide relay system (DRS) was recently identified in the yeast mitochondrial intermembrane space (IMS) that consists of two essential components: the sulfhydryl oxidase Erv1 and the redox-regulated import receptor Mia40.	Disulfides	2-11	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	174-178
19261614-8	2009	We generated disulfide-bonded MPL(W515L) homodimers by the S402C substitution, both in the normal and KDEL context.	Disulfides	13-22	myeloproliferative leukemia virus oncogene	Mus musculus	30-33
19279007-0	2009	Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradation.	Disulfides	17-26	alpha-1,2-mannosidase MNL1	Saccharomyces cerevisiae S288C	80-85
19279007-5	2009	Analyses of a series of Mnl1p mutants revealed that interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI.	Disulfides	145-154	alpha-1,2-mannosidase MNL1	Saccharomyces cerevisiae S288C	24-29
19279007-5	2009	Analyses of a series of Mnl1p mutants revealed that interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI.	Disulfides	145-154	alpha-1,2-mannosidase MNL1	Saccharomyces cerevisiae S288C	98-103
19279007-5	2009	Analyses of a series of Mnl1p mutants revealed that interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI.	Disulfides	145-154	alpha-1,2-mannosidase MNL1	Saccharomyces cerevisiae S288C	98-103
19279007-5	2009	Analyses of a series of Mnl1p mutants revealed that interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI.	Disulfides	208-217	alpha-1,2-mannosidase MNL1	Saccharomyces cerevisiae S288C	24-29
19279007-5	2009	Analyses of a series of Mnl1p mutants revealed that interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI.	Disulfides	208-217	alpha-1,2-mannosidase MNL1	Saccharomyces cerevisiae S288C	98-103
19279007-5	2009	Analyses of a series of Mnl1p mutants revealed that interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI.	Disulfides	208-217	alpha-1,2-mannosidase MNL1	Saccharomyces cerevisiae S288C	98-103
19279007-6	2009	This disulfide bond is essential for the ERAD activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p.	Disulfides	5-14	alpha-1,2-mannosidase MNL1	Saccharomyces cerevisiae S288C	58-63
19279007-6	2009	This disulfide bond is essential for the ERAD activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p.	Disulfides	5-14	alpha-1,2-mannosidase MNL1	Saccharomyces cerevisiae S288C	125-130
19116168-7	2009	Formation of various hCD83ext multimeric forms, including dimer, trimer, and tetramer, via intermolecular disulfide bonds was observed.	Disulfides	106-115	CD83 molecule	Homo sapiens	21-26
19170994-0	2009	Reduction of disulfide bonds within anti-D results in enhanced Fcgamma receptor blockade.	Disulfides	13-22	Fc gamma receptor Ia	Homo sapiens	63-79
19170994-1	2009	BACKGROUND: We have investigated whether chemicals known to disrupt disulfide bonds are capable of altering immunoglobulin anti-D structure resulting in an increased efficacy of the chemically modified anti-D to inhibit Fcgamma receptor (FcgammaR)-mediated phagocytosis.	Disulfides	68-77	Fc gamma receptor Ia	Homo sapiens	220-236
19385090-3	2009	In addition to its anti-oxidative effect by dithiol-disulfide exchange in its active site, Trx 1 has anti-apoptotic and anti-inflammatory effects.	Disulfides	52-61	thioredoxin	Homo sapiens	91-96
19222191-8	2009	On the basis of this result, an engineered disulfide bond was designed to constrain the alpha5 helix of Galpha(i1) into its EPR-measured receptor-associated conformation through the introduction of cysteines at position 56 in the alpha1 helix and position 333 in the alpha5 helix (I56C/Q333C Galpha(i1)).	Disulfides	43-52	nischarin	Homo sapiens	104-113
19222191-8	2009	On the basis of this result, an engineered disulfide bond was designed to constrain the alpha5 helix of Galpha(i1) into its EPR-measured receptor-associated conformation through the introduction of cysteines at position 56 in the alpha1 helix and position 333 in the alpha5 helix (I56C/Q333C Galpha(i1)).	Disulfides	43-52	nischarin	Homo sapiens	104-114
19230834-4	2009	Mitochondrial peroxiredoxin 3 underwent significant oxidation to its disulfide-linked dimer during ischemia.	Disulfides	69-78	peroxiredoxin 3	Mus musculus	14-29
19136576-4	2009	Digestion of purified VEGF(165) with NE generated a partially degraded disulfide-linked fragment of VEGF.	Disulfides	71-80	elastase, neutrophil expressed	Mus musculus	37-39
19178278-2	2009	This strategy utilized homogeneous enzymatic reactions to generate molecular beacon-structured allele-specific products that could be cooperatively annealed to capture probes stably immobilized on the surface via disulfide anchors, thus allowing ultrasensitive surface hybridization detection of the allele-specific products through redox tags in close proximity to the electrode.	Disulfides	213-222	ubiquitin like 5	Homo sapiens	77-83
19106090-3	2009	Gpx3 (glutathione peroxidase-like protein 3) acts as a receptor for H(2)O(2), and Ybp1 (Yap1-binding protein 1) is crucial for Gpx3-dependent disulfide bond formation in Yap1.	Disulfides	142-151	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	0-4
19106090-3	2009	Gpx3 (glutathione peroxidase-like protein 3) acts as a receptor for H(2)O(2), and Ybp1 (Yap1-binding protein 1) is crucial for Gpx3-dependent disulfide bond formation in Yap1.	Disulfides	142-151	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	6-43
19106090-3	2009	Gpx3 (glutathione peroxidase-like protein 3) acts as a receptor for H(2)O(2), and Ybp1 (Yap1-binding protein 1) is crucial for Gpx3-dependent disulfide bond formation in Yap1.	Disulfides	142-151	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	127-131
19106090-5	2009	In the present study, we show that Tsa1 can interact with Yap1 via disulfide linkages and induce the formation of intramolecular disulfide bonds in Yap1 in ybp1-1 cells.	Disulfides	67-76	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	35-39
19011240-2	2009	This import pathway employs a disulfide relay system whose key components are the redox-regulated import receptor Mia40 and the thiol oxidase Erv1.	Disulfides	30-39	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	142-146
19011240-7	2009	It is required for the interaction of Mia40 with Erv1 in a disulfide intermediate and forms a redox-sensitive disulfide bond with the first cysteine residue.	Disulfides	59-68	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	49-53
19011240-7	2009	It is required for the interaction of Mia40 with Erv1 in a disulfide intermediate and forms a redox-sensitive disulfide bond with the first cysteine residue.	Disulfides	110-119	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	49-53
19011240-13	2009	Furthermore, the disulfide bond in the CPC segment mediates the redox reactions with the thiol oxidase Erv1 and substrate proteins in mitochondria.	Disulfides	17-26	flavin-linked sulfhydryl oxidase	Saccharomyces cerevisiae S288C	103-107
19301948-9	2009	In conclusion, the disulfide bridges disrupted in all the tested mutants appear essential for the cell fusion, while only the disulfide bridge C(5)-C(8) seems to be crucial for the transport of E1 and E2 in the cell.	Disulfides	126-135	small nucleolar RNA, H/ACA box 73A	Homo sapiens	194-202
18796561-0	2009	Oxidative, multistep activation of the noncanonical NF-kappaB pathway via disulfide Bcl-3/p50 complex.	Disulfides	74-83	BCL3 transcription coactivator	Homo sapiens	84-89
18796561-4	2009	The early phase, coinciding with substantial thiol depletion, produces a cytosolic preparative complex, consisting of p50 and its interactor Bcl-3 linked by interprotein disulfide bridges.	Disulfides	170-179	BCL3 transcription coactivator	Homo sapiens	141-146
18951873-3	2008	The monkey group 1 CD1 isoforms contained amino acid residues and motifs known to be critical for intramolecular disulfide bond formation, N-linked glycosylation, and endosomal trafficking as in human group 1 CD1 molecules.	Disulfides	113-122	CD1b molecule	Homo sapiens	19-22
28935607-11	2017	The mixed disulfide and the C150-C154 disulfide bond protect GAPDH from irreversible oxidation and can be reduced in the excess of thiols.	Disulfides	38-47	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	61-66
18940237-5	2008	The DYT1 mutation also triggers the formation of abnormal intermolecular disulfide bonds in torsinA, although the significance of this finding is unclear.	Disulfides	73-82	torsin family 1 member A	Homo sapiens	4-8
29101848-5	2017	We found that panitumumab and denosumab samples enriched for the more flexible A disulfide isoform bound FCRL5 with two-fold and 82-fold higher apparent affinity, respectively, than the B isoform.	Disulfides	81-90	Fc receptor like 5	Homo sapiens	105-110
18940237-5	2008	The DYT1 mutation also triggers the formation of abnormal intermolecular disulfide bonds in torsinA, although the significance of this finding is unclear.	Disulfides	73-82	torsin family 1 member A	Homo sapiens	92-99
29101848-11	2017	Statistical analyses of kinetic parameters and similarity scores obtained from sensogram comparisons indicated that IgG2 disulfide isoforms, heat stressed and deamidated samples each bind FCRL5 differently.	Disulfides	121-130	Fc receptor like 5	Homo sapiens	188-193
29101848-12	2017	We conclude that based on FCRL5 binding, we can discern distinct changes in the IgG2 molecule, including the disulfide isoform structure and charge variants related to deamidation.	Disulfides	109-118	Fc receptor like 5	Homo sapiens	26-31
18940237-8	2008	Subsequently, we determined that the abnormal disulfide bond-dependent oligomerization of mutant torsinA is not a result of its redistribution to the nuclear envelope, but a direct consequence of the mutation.	Disulfides	46-55	torsin family 1 member A	Homo sapiens	97-104
29101848-13	2017	Since both IgG2 deamidation and conversion of disulfide isoforms occur in vivo, these findings elucidate the biological FCRL5 ligand.	Disulfides	46-55	Fc receptor like 5	Homo sapiens	120-125
18940237-9	2008	Finally, we established that the presence of disulfide links in mutant torsinA oligomers interfere with their degradation by the proteasome, thus relying on autophagy as the main pathway for clearance.	Disulfides	45-54	torsin family 1 member A	Homo sapiens	71-78
19216714-1	2008	Among the key antioxidant enzymes, thioredoxin and glutaredoxin systems play an important role in cell defense against oxidative stress and maintenance of redox homeostasis owing to the regulation of thiol-disulfide exchange.	Disulfides	206-215	thioredoxin	Homo sapiens	35-46
19216714-2	2008	The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite.	Disulfides	116-125	thioredoxin	Homo sapiens	4-15
19216714-2	2008	The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite.	Disulfides	116-125	thioredoxin	Homo sapiens	25-29
28899696-1	2017	The serotonin 2A (5-HT2A) receptor is a G-protein coupled receptor (GPCR) with a conserved disulfide bridge formed by Cys148 (transmembrane helix 3, TM3) and Cys227 (extracellular loop 2, ECL-2).	Disulfides	91-100	tropomyosin 3	Homo sapiens	149-152
28899696-8	2017	Our findings suggest that the decrease of efficacy may be due to disruption of disulfide bridge between TM3 and ECL-2.	Disulfides	79-88	tropomyosin 3	Homo sapiens	104-107
19216714-2	2008	The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite.	Disulfides	116-125	thioredoxin 2	Homo sapiens	53-57
18663433-7	2008	Disulfide bridge-containing peptides obtained from proteolytic digests were submitted to low-energy nanoESI CID using a quadrupole time-of-flight (Q-TOF) instrument as a mass analyser.	Disulfides	0-9	FEZ family zinc finger 2	Homo sapiens	149-152
18725202-0	2008	The significance of disulfide bonding in biological activity of HB-EGF, a mutagenesis approach.	Disulfides	20-29	heparin-binding EGF-like growth factor	Mus musculus	64-70
18725202-1	2008	A site-directed mutagenesis approach was taken to disrupt each of 3 disulfide bonds within human HB-EGF by substituting serine for both cysteine residues that contribute to disulfide bonding.	Disulfides	68-77	heparin binding EGF like growth factor	Homo sapiens	97-103
28837266-7	2017	Wild-type ILEI monomers, but not C185A mutants, could be converted into covalent dimers extracellularly upon overexpression by intramolecular-to-intermolecular disulfide bond isomerization.	Disulfides	160-169	FAM3 metabolism regulating signaling molecule C	Mus musculus	10-14
18725202-1	2008	A site-directed mutagenesis approach was taken to disrupt each of 3 disulfide bonds within human HB-EGF by substituting serine for both cysteine residues that contribute to disulfide bonding.	Disulfides	173-182	heparin binding EGF like growth factor	Homo sapiens	97-103
28849192-1	2017	High molecular weight (HMW) adiponectin (APN) is closely correlated with the development of fatty liver and is modulated by the Akt/forkhead box protein O1 (FOXO1) pathway through disulfide-bond A oxidoreductase-like protein (DsbA-L).	Disulfides	180-189	adiponectin, C1Q and collagen domain containing	Rattus norvegicus	28-39
18725202-2	2008	Each HB-EGF disulfide analogue (HB-EGF-Cys/Ser(108/121), HB-EGF-Cys/Ser(116/132), and HB-EGF-Cys/Ser(134/143)) was cloned under the regulation of the mouse metallothionein (MT) promoter and stably expressed in mouse fibroblasts.	Disulfides	12-21	heparin-binding EGF-like growth factor	Mus musculus	5-11
28849192-1	2017	High molecular weight (HMW) adiponectin (APN) is closely correlated with the development of fatty liver and is modulated by the Akt/forkhead box protein O1 (FOXO1) pathway through disulfide-bond A oxidoreductase-like protein (DsbA-L).	Disulfides	180-189	adiponectin, C1Q and collagen domain containing	Rattus norvegicus	41-44
18692066-1	2008	Proteins of the thioredoxin (Trx) superfamily catalyze disulfide-bond formation, reduction and isomerization in substrate proteins both in prokaryotic and in eukaryotic cells.	Disulfides	55-64	thioredoxin	Homo sapiens	16-27
28391181-7	2017	Both Cys87 and Cys154 were essential to the peroxidase activity, since single mutants for each Cys residue presented no activity and no formation of intramolecular disulfide bond upon treatment with hydroperoxides.	Disulfides	164-173	peroxidase 24	Musa acuminata	44-54
18692066-1	2008	Proteins of the thioredoxin (Trx) superfamily catalyze disulfide-bond formation, reduction and isomerization in substrate proteins both in prokaryotic and in eukaryotic cells.	Disulfides	55-64	thioredoxin	Homo sapiens	29-32
18544525-2	2008	The active site of reduced Trx comprises Cys(32)-Gly-Pro-Cys(35) thiols that catalyze target disulfide reduction, generating a disulfide.	Disulfides	93-102	thioredoxin	Homo sapiens	27-30
28533135-1	2017	Mutation of the cysteines forming the disulfide loop of the platelet GPIbalpha adhesive A1 domain of von Willebrand factor (VWF) causes quantitative VWF deficiencies in the blood and von Willebrand disease.	Disulfides	38-47	glycoprotein Ib platelet subunit alpha	Homo sapiens	69-78
28533135-6	2017	Less restrained through mutation, loss of the disulfide preferentially diverts binding through an induced-fit disease pathway enabling high-affinity GPIbalpha binding and firm platelet adhesion to a partially disordered A1 domain.	Disulfides	46-55	glycoprotein Ib platelet subunit alpha	Homo sapiens	149-158
18544525-2	2008	The active site of reduced Trx comprises Cys(32)-Gly-Pro-Cys(35) thiols that catalyze target disulfide reduction, generating a disulfide.	Disulfides	127-136	thioredoxin	Homo sapiens	27-30
18544525-3	2008	Human Trx1 has also three structural Cys residues in positions 62, 69, and 73 that upon diamide oxidation induce a second Cys(62)-Cys(69) disulfide as well as dimers and multimers.	Disulfides	138-147	thioredoxin	Homo sapiens	6-10
18544525-4	2008	We have discovered that after incubation with H(2)O(2) only monomeric two-disulfide molecules are generated, and they are inactive but able to regain full activity in an autocatalytic process in the presence of NADPH and TrxR.	Disulfides	74-83	peroxiredoxin 5	Homo sapiens	221-225
28325840-5	2017	Within the native IL-12 heterodimer, composed of IL-12alpha and IL-12beta, IL-12alpha possesses three intramolecular and one intermolecular disulfide bridges.	Disulfides	140-149	interleukin 12A	Homo sapiens	75-85
28325840-6	2017	We show that, in isolation, IL-12alpha fails to form its native structure but, instead, misfolds, forming incorrect disulfide bonds.	Disulfides	116-125	interleukin 12A	Homo sapiens	28-38
18544525-7	2008	Starting from fully reduced human Trx, both Cys(69) and Cys(73) were nitrosylated, and the active site formed a disulfide; the nitrosylated Trx was not a substrate for TrxR but regained activity after a lag phase consistent with autoactivation.	Disulfides	112-121	thioredoxin	Homo sapiens	34-37
28325840-8	2017	On the basis of these findings, we identified the disulfide bonds in IL-12alpha that are critical for assembly-induced secretion and biological activity of IL-12 versus misfolding and degradation of IL-12alpha.	Disulfides	50-59	interleukin 12A	Homo sapiens	69-79
28325840-9	2017	Surprisingly, two of the three disulfide bridges in IL-12alpha are dispensable for IL-12 secretion, stability, and biological activity.	Disulfides	31-40	interleukin 12A	Homo sapiens	52-62
18544525-7	2008	Starting from fully reduced human Trx, both Cys(69) and Cys(73) were nitrosylated, and the active site formed a disulfide; the nitrosylated Trx was not a substrate for TrxR but regained activity after a lag phase consistent with autoactivation.	Disulfides	112-121	thioredoxin	Homo sapiens	140-143
18641333-8	2008	Further investigation revealed two invariant disulfide bonds were important for activity of PAP2 while the disulfide bond that is observed in long-form C-type lectin proteins was not essential for activity.	Disulfides	45-54	regenerating islet-derived 3 alpha	Rattus norvegicus	92-96
28515726-9	2017	For instance, all 20 cysteine residues involved in disulfide bonds in the human 4-1BB molecule were also present in devil 4-1BB.	Disulfides	51-60	TNF receptor superfamily member 9	Homo sapiens	80-85
28515726-9	2017	For instance, all 20 cysteine residues involved in disulfide bonds in the human 4-1BB molecule were also present in devil 4-1BB.	Disulfides	51-60	TNF receptor superfamily member 9	Homo sapiens	122-127
18756111-0	2008	Disulfide bond bridged divalent antibody-toxin, (Fab-PE38fl)2, with the toxin PE38 fused to the light chain.	Disulfides	0-9	FA complementation group B	Homo sapiens	49-52
28274878-5	2017	Moreover, structural superpositions suggest that dimerization of UBXD7UBX via an intermolecular disulfide bond could interfere with the formation of the p97NTD-UBXD7UBX complex.	Disulfides	96-105	UBX domain protein 7	Homo sapiens	65-73
28274878-5	2017	Moreover, structural superpositions suggest that dimerization of UBXD7UBX via an intermolecular disulfide bond could interfere with the formation of the p97NTD-UBXD7UBX complex.	Disulfides	96-105	UBX domain protein 7	Homo sapiens	65-70
18361921-7	2008	Moreover, we observed that full-length mCLEC-2 could be cleaved probably by proteases sensitive to aprotinin and PMSF into a soluble form that partially existed as a disulfide-linked homodimer.	Disulfides	166-175	C-type lectin domain family 1, member b	Mus musculus	39-46
28159752-1	2017	The house mouse Androgen-binding protein (Abp) gene family is comprised of 64 paralogs, 30 Abpa and 34 Abpbg, encoding the alpha (ABPA) and beta-gamma (ABPBG) protein subunits that are disulfide-bridged to form dimers in secretions.	Disulfides	185-194	secretoglobin, family 1B, member 27	Mus musculus	16-40
28159752-1	2017	The house mouse Androgen-binding protein (Abp) gene family is comprised of 64 paralogs, 30 Abpa and 34 Abpbg, encoding the alpha (ABPA) and beta-gamma (ABPBG) protein subunits that are disulfide-bridged to form dimers in secretions.	Disulfides	185-194	secretoglobin, family 1B, member 27	Mus musculus	42-45
28159752-1	2017	The house mouse Androgen-binding protein (Abp) gene family is comprised of 64 paralogs, 30 Abpa and 34 Abpbg, encoding the alpha (ABPA) and beta-gamma (ABPBG) protein subunits that are disulfide-bridged to form dimers in secretions.	Disulfides	185-194	secretoglobin, family 1B, member 27	Mus musculus	130-134
18318660-3	2008	We thereby isolated several murine uPA-binding peptide sequences, the predominant of which was the disulfide-bridged constrained sequence CPAYSRYLDC, which we will refer to as mupain-1.	Disulfides	99-108	plasminogen activator, urokinase	Mus musculus	35-38
18035847-1	2008	Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is similar in structure and mechanism to glutathione reductase except for a C-terminal 16-amino acid extension containing a rare vicinal selenylsulfide bond.	Disulfides	81-90	peroxiredoxin 5	Homo sapiens	10-31
18035847-1	2008	Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is similar in structure and mechanism to glutathione reductase except for a C-terminal 16-amino acid extension containing a rare vicinal selenylsulfide bond.	Disulfides	81-90	peroxiredoxin 5	Homo sapiens	33-35
18035847-1	2008	Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is similar in structure and mechanism to glutathione reductase except for a C-terminal 16-amino acid extension containing a rare vicinal selenylsulfide bond.	Disulfides	81-90	thioredoxin	Homo sapiens	10-21
18035847-1	2008	Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is similar in structure and mechanism to glutathione reductase except for a C-terminal 16-amino acid extension containing a rare vicinal selenylsulfide bond.	Disulfides	81-90	thioredoxin	Homo sapiens	112-115
17931747-5	2008	Structure-activity relationship studies have shown that the minimal sequence required to retain full biological activity is the conserved U-II(4-11) domain, in particular the Cys5 and Cys10 residues involved in the disulfide bridge, and the Phe6, Lys8 and Tyr9 residues.	Disulfides	215-224	urotensin 2	Homo sapiens	138-142
2592414-9	1989	These and other results indicate that (a) specific neurite extension activity and neuronal survival activity are two related activities inherent to the S100 beta molecule; (b) a disulfide-linked form of S100 beta is required for full biological activity, and (c) the relative position of the cysteines can be modified.	Disulfides	178-187	S100 calcium binding protein B	Bos taurus	152-161
2592414-9	1989	These and other results indicate that (a) specific neurite extension activity and neuronal survival activity are two related activities inherent to the S100 beta molecule; (b) a disulfide-linked form of S100 beta is required for full biological activity, and (c) the relative position of the cysteines can be modified.	Disulfides	178-187	S100 calcium binding protein B	Bos taurus	203-212
28100779-3	2017	We further show that Astn2 undergoes proteolytic cleavage in the second transmembrane domain (TM2) and that a disulfide bond holds the resulting two fragments together.	Disulfides	110-119	astrotactin 2	Mus musculus	21-26
18643017-0	2008	Two-pathway four-state kinetic model of thioredoxin-catalyzed reduction of single forced disulfide bonds.	Disulfides	89-98	thioredoxin	Homo sapiens	40-51
28218242-2	2017	Using PDI variants that form mixed disulfide complexes with their substrates, we identify by kinetic trapping multiple substrate proteins, including vitronectin.	Disulfides	35-44	vitronectin	Mus musculus	149-160
28218242-4	2017	The released PDI reduces disulfide bonds on plasma vitronectin, enabling vitronectin to bind to alphaVbeta3 and alphaIIbbeta3.	Disulfides	25-34	vitronectin	Mus musculus	51-62
28218242-4	2017	The released PDI reduces disulfide bonds on plasma vitronectin, enabling vitronectin to bind to alphaVbeta3 and alphaIIbbeta3.	Disulfides	25-34	vitronectin	Mus musculus	73-84
2483052-6	1989	The helicity developed in TFE by RCM-hCG beta appears much greater than that which occurs in the native, disulfide-intact form, thus suggesting that the disulfides prevent expression of helicity in regions with alpha-helix potential.	Disulfides	153-163	chorionic gonadotropin subunit beta 3	Homo sapiens	37-45
2478557-0	1989	Elimination of disulfide bonds affects assembly and secretion of the human chorionic gonadotropin beta subunit.	Disulfides	15-24	chorionic gonadotropin subunit beta 3	Homo sapiens	75-110
2478557-10	1989	Thus, interruption of any disulfide bond in the hCG beta subunit alters the structure sufficiently to block dimer formation and in some cases slow secretion, although the stability for most of the mutant hCG beta subunits is not greatly affected.	Disulfides	26-35	chorionic gonadotropin subunit beta 3	Homo sapiens	48-56
18643017-1	2008	Recent single-molecule experiments found that the thioredoxin-catalyzed reduction of individual disulfide bonds placed under a stretching mechanical force has distinct characteristics: the reduction rate of human thioredoxin monotonically decreases with the force, while the rate of E. coli thioredoxin first decreases and then increases as the force goes beyond a certain threshold.	Disulfides	96-105	thioredoxin	Homo sapiens	50-61
18643017-1	2008	Recent single-molecule experiments found that the thioredoxin-catalyzed reduction of individual disulfide bonds placed under a stretching mechanical force has distinct characteristics: the reduction rate of human thioredoxin monotonically decreases with the force, while the rate of E. coli thioredoxin first decreases and then increases as the force goes beyond a certain threshold.	Disulfides	96-105	thioredoxin	Homo sapiens	213-224
2474534-6	1989	8, 4162-4168) with purified recombinant TGF-beta 1 (rTGF-beta 1) precursor produced by Chinese hamster ovary (CHO) cells revealed that Cys-33 can form a disulfide bond with at least 1 cysteine residue in mature TGF-beta 1, contributing to the formation of a 90-110-kDa protein.	Disulfides	153-162	transforming growth factor beta-1 proprotein	Cricetulus griseus	40-50
18643017-1	2008	Recent single-molecule experiments found that the thioredoxin-catalyzed reduction of individual disulfide bonds placed under a stretching mechanical force has distinct characteristics: the reduction rate of human thioredoxin monotonically decreases with the force, while the rate of E. coli thioredoxin first decreases and then increases as the force goes beyond a certain threshold.	Disulfides	96-105	thioredoxin	Homo sapiens	213-224
2474534-6	1989	8, 4162-4168) with purified recombinant TGF-beta 1 (rTGF-beta 1) precursor produced by Chinese hamster ovary (CHO) cells revealed that Cys-33 can form a disulfide bond with at least 1 cysteine residue in mature TGF-beta 1, contributing to the formation of a 90-110-kDa protein.	Disulfides	153-162	transforming growth factor beta-1 proprotein	Cricetulus griseus	53-63
27733423-2	2017	In a previous study, we found that immunization with a recombinant disulfide-bridged dimeric form of OspC (D-OspC) stimulates increased antibody responses relative to immunization with commonly employed monomeric OspC.	Disulfides	67-76	OspC	Borreliella burgdorferi	101-105
27733423-2	2017	In a previous study, we found that immunization with a recombinant disulfide-bridged dimeric form of OspC (D-OspC) stimulates increased antibody responses relative to immunization with commonly employed monomeric OspC.	Disulfides	67-76	OspC	Borreliella burgdorferi	109-113
18463717-1	2008	The objective of this study was to pursue the techniques involving the screening of the human antibody Fab fragment against hepatitis B virus surface antigen (HBsAg) and the construction of its disulfide-stabilized Fv fragment (dsFv).	Disulfides	194-203	FA complementation group B	Homo sapiens	103-106
27771573-0	2017	Disulfide bond characterization of human factor Xa by mass spectrometry through protein-level partial reduction.	Disulfides	0-9	coagulation factor X	Homo sapiens	41-50
27771573-2	2017	Human Factor Xa containing twelve disulfide bonds was selected as a model protein to demonstrate this methodology.	Disulfides	34-43	coagulation factor X	Homo sapiens	6-15
2525380-4	1989	Iso-rANP has a single disulfide bond between residues 23-39 and this portion of the peptide shows substantial homology to rANP and to porcine brain natriuretic peptide (BNP).	Disulfides	22-31	natriuretic peptide A	Rattus norvegicus	4-8
18413607-4	2008	Here, we show that the p66(Shc) N terminus forms a redox module responsible for apoptosis initiation, and that this module can be activated through reversible tetramerization by forming two disulfide bonds.	Disulfides	190-199	DNA polymerase delta 3, accessory subunit	Homo sapiens	23-26
2713490-1	1989	Platelet membrane GPIIb is comprised of a disulfide-linked heavy chain (GPIIb(H)) and light chain (GPIIb(L)).	Disulfides	42-51	integrin subunit alpha 2b	Homo sapiens	18-23
2713490-1	1989	Platelet membrane GPIIb is comprised of a disulfide-linked heavy chain (GPIIb(H)) and light chain (GPIIb(L)).	Disulfides	42-51	integrin subunit alpha 2b	Homo sapiens	72-77
2713490-1	1989	Platelet membrane GPIIb is comprised of a disulfide-linked heavy chain (GPIIb(H)) and light chain (GPIIb(L)).	Disulfides	42-51	integrin subunit alpha 2b	Homo sapiens	72-77
2713490-3	1989	Lysates of surface radioiodinated platelets were treated with 1% 2-mercaptoethanol for 18 hours at 4 degrees C. Reduction of the interchain disulfide in GPIIb was followed by immunoprecipitation with antipeptide antibodies specific for GPIIb(H) or GPIIb(L).	Disulfides	140-149	integrin subunit alpha 2b	Homo sapiens	153-158
27770625-1	2017	Previously, we have shown that flies under-expressing the two mitochondrial peroxiredoxins (Prxs), dPrx3 and dPrx5, display increases in tissue-specific apoptosis and dramatically shortened life span, associated with a redox crisis, manifested as changes in GSH:GSSG and accumulation of protein mixed disulfides.	Disulfides	301-311	Peroxiredoxin 5	Drosophila melanogaster	109-114
27683014-5	2016	Discrete mutations proximal to a conserved ECL2-TM3 disulfide bond selectively affected orthosteric ligand affinity, whereas a cluster of five residues near the TM4-ECL2 juncture influenced orthosteric agonist efficacy.	Disulfides	52-61	tropomyosin 3	Homo sapiens	48-51
18179776-3	2008	Recently, a disulfide relay system in the IMS has been identified which consists of two essential components, the sulfhydryl oxidase Erv1 and the redox-regulated import receptor Mia40/Tim40.	Disulfides	12-21	growth factor, augmenter of liver regeneration	Homo sapiens	133-137
2523415-4	1989	After SDS-PAGE of N-glycanase-treated FcR III under nonreducing conditions, the apparent Mr of each structural type was decreased, suggesting the presence of intramolecular disulfide bonds.	Disulfides	173-182	Fc gamma receptor IIIa	Homo sapiens	38-45
18179776-5	2008	In order to enable Mia40 to perform the oxidation of substrate proteins, the sulfhydryl oxidase Erv1 mediates the oxidation of Mia40 in a disulfide transfer reaction.	Disulfides	138-147	growth factor, augmenter of liver regeneration	Homo sapiens	96-100
18179776-6	2008	To recycle Erv1 into its oxidized form, electrons are transferred to cytochrome c connecting the disulfide relay system to the electron transport chain of mitochondria.	Disulfides	97-106	growth factor, augmenter of liver regeneration	Homo sapiens	11-15
27634040-0	2016	Activity-dependent Regulation of Histone Lysine Demethylase KDM1A by a Putative Thiol/Disulfide Switch.	Disulfides	86-95	lysine demethylase 1A	Homo sapiens	60-65
27634040-6	2016	MALDI-TOF mass spectrometry indicates that hydrogen peroxide blocks labeling of cysteine 600, which we propose forms an intramolecular disulfide with cysteine 618 to negatively regulate the catalytic activity of KDM1A.	Disulfides	135-144	lysine demethylase 1A	Homo sapiens	212-217
2542756-6	1989	The ANF-R2 receptor, which is expressed selectively by the fibroblast cell line NIH-3T3, is a 130-kDa protein composed of two disulfide-linked subunits of 64-kDa.	Disulfides	126-135	natriuretic peptide A	Rattus norvegicus	4-7
18255328-8	2008	The AbTRx-2 mRNA was up-regulated in gill and digestive tract tissues initially at 3 h post-injection of H(2)O(2) and maintained higher level at 6 h. Our results suggest that abalone TRx-2 may play an important role in regulating oxidative stress in mitochondria by catalyzing protein disulfide reduction, scavenging of ROS, and minimizing the DNA damage.	Disulfides	285-294	thioredoxin 2	Homo sapiens	6-11
2651524-1	1989	Activation of the Hageman factor-dependent pathways in human plasma leads to the cleavage of high molecular weight kininogen (HMWK) into a disulfide-linked two-chain (heavy and light chain) molecule and release of bradykinin, a vasoactive peptide.	Disulfides	139-148	coagulation factor XII	Homo sapiens	18-32
27754694-0	2016	Synthetic Route to Human Relaxin-2 via Iodine-Free Sequential Disulfide Bond Formation.	Disulfides	62-71	relaxin 2	Homo sapiens	25-34
18322016-6	2008	Based on our data, we propose a model for thioredoxin f-mediated activation of PRK and GAPDH by two mechanisms: directly through reduction of disulfide bonds within these enzymes and indirectly by mediating the breakdown of the complex in response to changes in light intensity.	Disulfides	142-151	thioredoxin	Homo sapiens	42-53
27754694-1	2016	A new synthetic route to human relaxin-2 has been established through a sequential disulfide bond formation process in the absence of iodine.	Disulfides	83-92	relaxin 2	Homo sapiens	31-40
2468506-2	1989	Insulin-immune T cells require intact conformation of the interchain disulfide bond that forms the A chain loop but do not require the B chain.	Disulfides	69-78	insulin	Cavia porcellus	0-7
18292814-1	2008	Thiol isomerases, including protein disulfide isomerase (PDI), catalyze disulfide oxidation, reduction, and isomerization, thereby playing an important role in protein synthesis.	Disulfides	36-45	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	57-60
2466936-7	1989	Evidence is presented that demonstrates that Blast-1 and LFA-3 possess a disulfide-bonded second domain.	Disulfides	73-82	CD48 molecule	Homo sapiens	45-52
27569046-5	2016	The p24beta1 and p24delta1 GOLD domains share a common beta-sandwich fold with a characteristic intrasheet disulfide bond.	Disulfides	107-116	transmembrane p24 trafficking protein 10	Homo sapiens	17-26
27609313-4	2016	TGFBIp contains 11 cysteine residues and is thus able to form five intramolecule disulfide bonds, leaving a single cysteine residue available for the collagen cross-link.	Disulfides	81-90	transforming growth factor beta induced	Homo sapiens	0-6
27609313-6	2016	We here present the disulfide bridge pattern of TGFBIp, which was determined by generating specific peptides.	Disulfides	20-29	transforming growth factor beta induced	Homo sapiens	48-54
27609313-13	2016	The interdomain disulfide bonds indicate that the NH2 terminus of TGFBIp (CRD, FAS1-1, and FAS1-2) adopts a compact globular fold, leaving FAS1-3 and FAS1-4 exposed.	Disulfides	16-25	transforming growth factor beta induced	Homo sapiens	66-72
3266557-7	1988	The NMR data, combined with known disulfide linkages and a small number of critical long-range NOEs, provide the global folding pattern of C3a in solution.	Disulfides	34-43	complement C3	Homo sapiens	139-142
18313382-2	2008	Here, specificity-transplant and disulfide-crosslinking experiments reveal that the ssrA tag interacts with different loops that form the top, middle, and lower portions of the central channel of the ClpX hexamer.	Disulfides	33-42	caseinolytic mitochondrial matrix peptidase chaperone subunit X	Homo sapiens	200-204
2848681-10	1988	Reduction of receptor disulfide bonds with dithiothreitol and beta-mercaptoethanol released a low Mr (less than or equal to 14K) labeled PTH receptor component, similar treatment of renal membranes abolished specific PTH binding, indicating that an intact disulfide bond(s) is essential for receptor function.	Disulfides	22-31	parathyroid hormone	Bos taurus	137-140
2848681-10	1988	Reduction of receptor disulfide bonds with dithiothreitol and beta-mercaptoethanol released a low Mr (less than or equal to 14K) labeled PTH receptor component, similar treatment of renal membranes abolished specific PTH binding, indicating that an intact disulfide bond(s) is essential for receptor function.	Disulfides	256-265	parathyroid hormone	Bos taurus	137-140
27402851-5	2016	The use of a polarized electrode to efficiently interconvert the ferric (Fe(3+)) and ferrous (Fe(2+)) forms of an immobilized NGB showed that the disulfide bridge both defines the kinetics of NO dioxygenase activity and regulates appearance of the free ferrous deoxy-NGB, which is the redox active form of the protein in contrast to oxy-NGB.	Disulfides	146-155	neuroglobin	Homo sapiens	126-129
27402851-5	2016	The use of a polarized electrode to efficiently interconvert the ferric (Fe(3+)) and ferrous (Fe(2+)) forms of an immobilized NGB showed that the disulfide bridge both defines the kinetics of NO dioxygenase activity and regulates appearance of the free ferrous deoxy-NGB, which is the redox active form of the protein in contrast to oxy-NGB.	Disulfides	146-155	neuroglobin	Homo sapiens	267-270
27402851-5	2016	The use of a polarized electrode to efficiently interconvert the ferric (Fe(3+)) and ferrous (Fe(2+)) forms of an immobilized NGB showed that the disulfide bridge both defines the kinetics of NO dioxygenase activity and regulates appearance of the free ferrous deoxy-NGB, which is the redox active form of the protein in contrast to oxy-NGB.	Disulfides	146-155	neuroglobin	Homo sapiens	267-270
3264320-1	1988	Human CD8 has been thought to consist of disulfide-linked homodimers and homomultimers of a single polypeptide chain homologous to mouse and rat CD8 alpha.	Disulfides	41-50	CD8a molecule	Homo sapiens	6-9
18237398-5	2008	However, its removal improved folding of a gp120 variant lacking the 385-418 disulfide bond, suggesting that it plays an auxiliary role in protein folding in the presence of this disulfide bond.	Disulfides	77-86	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	43-48
3264320-2	1988	In contrast, mouse and rat CD8 are composed of disulfide-linked heterodimers of alpha and beta chains.	Disulfides	47-56	CD8a molecule	Homo sapiens	27-30
27566173-0	2016	(13)C-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI).	Disulfides	21-30	spleen trypsin inhibitor I	Bos taurus	53-88
27566173-0	2016	(13)C-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI).	Disulfides	21-30	spleen trypsin inhibitor I	Bos taurus	90-94
27566173-3	2016	We explored the disulfide conformational isomerization of the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor (BPTI), by performing an NMR line-shape analysis of its Cys carbon peaks.	Disulfides	16-25	spleen trypsin inhibitor I	Bos taurus	129-133
18237398-5	2008	However, its removal improved folding of a gp120 variant lacking the 385-418 disulfide bond, suggesting that it plays an auxiliary role in protein folding in the presence of this disulfide bond.	Disulfides	179-188	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	43-48
27566173-3	2016	We explored the disulfide conformational isomerization of the Cys14-Cys38 disulfide bond in bovine pancreatic trypsin inhibitor (BPTI), by performing an NMR line-shape analysis of its Cys carbon peaks.	Disulfides	74-83	spleen trypsin inhibitor I	Bos taurus	129-133
3192937-6	1988	The predominant localization of PDI on the intracisternal surface of the ER and nuclear envelope supports a potential role of PDI in the formation of disulfide bonds of nascent polypeptides, thus accelerating formation of the higher-order structure of secretory and membrane proteins and rendering the translocation process irreversible.	Disulfides	150-159	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	32-35
3192937-6	1988	The predominant localization of PDI on the intracisternal surface of the ER and nuclear envelope supports a potential role of PDI in the formation of disulfide bonds of nascent polypeptides, thus accelerating formation of the higher-order structure of secretory and membrane proteins and rendering the translocation process irreversible.	Disulfides	150-159	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	126-129
18759962-2	2008	Disulfide-linked HLA-B27 heavy-chain homodimers have been implicated as novel structures involved in the aetiology of AS.	Disulfides	0-9	major histocompatibility complex, class I, B	Homo sapiens	17-24
3410841-0	1988	Thiol/disulfide exchange between 3-hydroxy-3-methylglutaryl-CoA reductase and glutathione.	Disulfides	6-15	3-hydroxy-3-methylglutaryl-CoA reductase	Rattus norvegicus	33-73
27549196-12	2016	CONCLUSION: The results indicate that PDI8 is a type I transmembrane protein with its catalytic domain facing the lumen of the ER and functions in the oxidation of cysteines to produce disulfide bonds.	Disulfides	185-194	PDI-like 5-2	Arabidopsis thaliana	38-42
27502485-0	2016	A disulfide bond in the TIM23 complex is crucial for voltage gating and mitochondrial protein import.	Disulfides	2-11	translocase of inner mitochondrial membrane 23	Homo sapiens	24-29
18071941-3	2008	The situation gets more complex for Fab fragments and full-sized antibodies: while the disulfide-linked C(L)/C(H) heterodimer shows very limited thermodynamic stability, its unfolding kinetics are very slow.	Disulfides	87-96	FA complementation group B	Homo sapiens	36-39
27502485-3	2016	This disulfide bond is critical for efficient protein translocation through the TIM23 complex and for dynamic gating of its preprotein-conducting channel.	Disulfides	5-14	translocase of inner mitochondrial membrane 23	Homo sapiens	80-85
27502488-6	2016	http://dx.doi.org/10.1083/jcb.201602074) show that the TIM23 subunit Tim17 contains a disulfide bond that is crucial for protein translocation and channel gating.	Disulfides	86-95	translocase of inner mitochondrial membrane 23	Homo sapiens	55-60
3413110-3	1988	AR is a single-chain extremely hydrophilic glycoprotein containing cysteines in disulfide linkage(s) that are essential for biological activity; it is stable between pH 2 and pH 12 and after heating for 30 min at 56 degrees C but unstable at 100 degrees C. The apparent molecular weights of AR and N-Glycanase-treated AR are 14,000 and 15,000, respectively, as assessed by gel chromatography, and approximately 22,500 and approximately 14,000, respectively, as determined by polyacrylamide gel electrophoresis.	Disulfides	80-89	amphiregulin	Homo sapiens	0-2
3136022-1	1988	The cysteine at position 575 of the immunoglobulin mu heavy chain is thought to provide the only disulfide bonds joining the monomer subunits of mouse polymeric IgM.	Disulfides	97-106	immunoglobulin heavy constant mu	Mus musculus	161-164
3136022-3	1988	Thirty percent of the secreted mutant IgM was covalently assembled polymer implying that cysteines other than Cys575 can form inter-subunit disulfide bonds.	Disulfides	140-149	immunoglobulin heavy constant mu	Mus musculus	38-41
3042032-0	1988	Purification of the guinea pig sperm PH-20 antigen and detection of a site-specific endoproteolytic activity in sperm preparations that cleaves PH-20 into two disulfide-linked fragments.	Disulfides	159-168	hyaluronidase PH-20	Cavia porcellus	144-149
27259101-1	2016	Human insulin-like peptide-6 (INSL-6) belongs to the insulin superfamily and shares the distinctive disulfide bond configuration of human insulin.	Disulfides	100-109	insulin like 6	Homo sapiens	6-28
27259101-1	2016	Human insulin-like peptide-6 (INSL-6) belongs to the insulin superfamily and shares the distinctive disulfide bond configuration of human insulin.	Disulfides	100-109	insulin like 6	Homo sapiens	30-36
27259101-2	2016	In this report we present the first chemical synthesis of INSL-6 utilizing fluorenylmethyloxycarbonyl-based (Fmoc) solid-phase peptide chemistry and regioselective disulfide bond construction protocols.	Disulfides	164-173	insulin like 6	Homo sapiens	58-64
27259101-5	2016	The methodologies presented here offer an efficient synthetic route to INSL-6 and will further improve synthetic access to other multiple-disulfide-containing peptides with oxidation-sensitive residues.	Disulfides	138-147	insulin like 6	Homo sapiens	71-77
18374192-5	2008	VKOR uses two sulfhydryl groups for the catalytic reaction and these two sulfhydryl groups are oxidized back to a disulfide bond during each catalytic cycle.	Disulfides	114-123	vitamin K epoxide reductase complex subunit 1	Homo sapiens	0-4
3339349-3	1988	Both S100b subtypes appeared highly purified and differed only by their oxidation state: all four cysteinyl sulfhydryl groups were free in reduced S100b protein whereas two of them gave disulfide bridges in oxidized S100b protein.	Disulfides	186-195	S100 calcium binding protein B	Bos taurus	5-10
3693398-7	1987	After intracellular cleavage of the 80-kD protein, the 35-45-kD subunits are secreted as an 80-kD glycoprotein complex (gp 80) linked together by disulfide bonds.	Disulfides	146-155	clusterin	Canis lupus familiaris	120-125
17959605-2	2007	We have characterized the redox behavior of Mia40p and reconstituted the disulfide transfer system of Mia40p by using recombinant functional C-terminal fragment of Mia40p, Mia40C, and Erv1p.	Disulfides	73-82	growth factor, augmenter of liver regeneration	Homo sapiens	184-189
2959961-9	1987	Affinity crosslinking of 125I-IGF-II to the Sephadex G-200 void volume material demonstrated a specific band at 210 kDa without reduction and at 240 kDa after reduction of disulfide bonds.	Disulfides	172-181	insulin-like growth factor 2	Rattus norvegicus	30-36
27345325-2	2016	Adrenomedullin is composed of 52 amino acids, has an internal molecular ring composed by 6 amino acids and a disulfide bond, and shares structural similarities with calcitonin gene-related peptide, amylin, and intermedin.	Disulfides	109-118	adrenomedullin	Homo sapiens	0-14
27020146-4	2016	Immunoglobulin G (IgG)-stimulated reactive oxygen species (ROS) production and the inhibition of phagosomal proteolysis and disulfide reduction were dependent on NOX2, FcgammaR and protein kinase C (PKC)/spleen tyrosine kinase (Syk) signaling.	Disulfides	124-133	spleen tyrosine kinase	Mus musculus	228-231
17959605-8	2007	In the course of this reaction, mixed disulfides of Mia40C and Erv1p were formed.	Disulfides	38-48	growth factor, augmenter of liver regeneration	Homo sapiens	63-68
2962707-2	1987	Acid extraction and purification of atrial natriuretic factor resulted initially in the purification of a low molecular weight peptide containing a disulfide bond.	Disulfides	148-157	natriuretic peptide A	Rattus norvegicus	36-61
17959605-11	2007	In the reconstituted system the thiol oxidase Erv1p was sufficient to transfer disulfide bonds to Mia40C, which then could oxidize the variant of Mia40C.	Disulfides	79-88	growth factor, augmenter of liver regeneration	Homo sapiens	46-51
27355203-0	2016	Identification of a Disulfide Bridge in Sodium-Coupled Neutral Amino Acid Transporter 2(SNAT2) by Chemical Modification.	Disulfides	20-29	solute carrier family 38 member 2	Homo sapiens	40-87
17959605-12	2007	In summary, we reconstituted a disulfide relay system consisting of Mia40C and Erv1p.	Disulfides	31-40	growth factor, augmenter of liver regeneration	Homo sapiens	79-84
27355203-0	2016	Identification of a Disulfide Bridge in Sodium-Coupled Neutral Amino Acid Transporter 2(SNAT2) by Chemical Modification.	Disulfides	20-29	solute carrier family 38 member 2	Homo sapiens	88-93
18020379-7	2007	The adsorption of alpha-lipoic acid to CdS in the presence of light proceeds with photo-oxidation of the CdS surface and reductive cleavage of the disulfide bond of alpha-lipoic acid to produce some adsorbed dihydrolipoic acid and thiosulfate.	Disulfides	147-156	CDP-diacylglycerol synthase 1	Homo sapiens	39-42
27355203-3	2016	To better define the potential of intrinsic cysteines to form disulfide bonds in SNAT2, mutagenesis experiments and thiol-specific chemical modifications by N-ethylmaleimide (NEM) and methoxy-polyethylene glycol maleimide (mPEG-Mal, MW 5000) were performed, with or without the reducing regent dithiothreitol (DTT) treatment.	Disulfides	62-71	solute carrier family 38 member 2	Homo sapiens	81-86
2440681-7	1987	alpha 2-Antiplasmin contains two disulfide bridges (Cys64-Cys104 and Cys31-Cys113) and four glucosamine-based carbohydrate chains attached to Asn87, Asn256, Asn270 and Asn277.	Disulfides	33-42	serpin family F member 2	Homo sapiens	0-19
18020379-8	2007	The adsorption of alpha-lipoic acid to CdS in the absence of visible light shows no photo-oxidation and suggests that adsorption occurs via retention of the disulfide bond.	Disulfides	157-166	CDP-diacylglycerol synthase 1	Homo sapiens	39-42
3614558-5	1987	This suggests that the AII binding unit may contain essential disulfide bonds close to the AII binding site.	Disulfides	62-71	arginase type II	Mus musculus	23-26
3614558-5	1987	This suggests that the AII binding unit may contain essential disulfide bonds close to the AII binding site.	Disulfides	62-71	arginase type II	Mus musculus	91-94
27660688-3	2016	We previously identified the cyclic peptide APY-d2 (APYCVYRbetaASWSC-nh2, containing a disulfide bond) as a potent and selective EphA4 antagonist.	Disulfides	87-96	EPH receptor A4	Homo sapiens	129-134
17726162-9	2007	Overall, the present data undermine the recently proposed hypothesis that PDI-mediated disulfide exchange plays a role in regulating TF procoagulant and cell signaling functions.	Disulfides	87-96	coagulation factor III, tissue factor	Homo sapiens	133-135
27067900-8	2016	The affinity binding constants KD towards the antibodies were determined using a surface acoustic wave (SAW) biosensor, and showed the highest affinity with a KD of approximately 40 nM to the HD6 antibody for the (203-219)-SS-(257-273) mixed disulfide epitope.	Disulfides	242-251	defensin alpha 6	Homo sapiens	192-195
17703232-5	2007	Notably, disulfide-bonded fusion proteins of the THD of mTRAIL and mCD95L with a subdomain of the tenascin-C (TNC) oligomerization domain, which still assembled into trimers, efficiently interacted with their cognate cellular receptors and robustly stimulated CD95 and TRAILR2 signaling after secondary cross-linking.	Disulfides	9-18	Fas cell surface death receptor	Homo sapiens	68-72
26854372-6	2016	All these data strongly indicated that the recombinant SN-1 peptide had a folding with six disulfide bonds that was identical to the native SN-1.	Disulfides	91-100	STSN1	Solanum tuberosum	55-59
2875734-1	1986	Under very mild oxidizing conditions the delta subunit of the F1-ATPase of Escherichia coli can be crosslinked by a disulfide linkage to one of the alpha subunits of the enzyme.	Disulfides	116-125	ATPase	Escherichia coli	65-71
17703232-5	2007	Notably, disulfide-bonded fusion proteins of the THD of mTRAIL and mCD95L with a subdomain of the tenascin-C (TNC) oligomerization domain, which still assembled into trimers, efficiently interacted with their cognate cellular receptors and robustly stimulated CD95 and TRAILR2 signaling after secondary cross-linking.	Disulfides	9-18	TNF receptor superfamily member 10b	Homo sapiens	269-276
2428504-4	1986	This newly defined polypeptide, p21, is specifically immunoprecipitated with the antigen receptor complex, is endoglycosaminidase F-resistant, and is itself part of a disulfide-linked molecule.	Disulfides	167-176	cyclin-dependent kinase inhibitor 1A (P21)	Mus musculus	32-35
26898501-4	2016	The activity also utilizes the FAD and the N-terminal redox active disulfide/dithiol motif of TrxR1.	Disulfides	67-76	thioredoxin reductase 1	Homo sapiens	94-99
17945253-3	2007	In contrast to the previously characterized CLIC1 protein, which forms a possibly functionally important disulfide-induced dimer under oxidizing conditions, we show that CLIC2 possesses an intramolecular disulfide and that the protein remains monomeric irrespective of redox conditions.	Disulfides	204-213	chloride intracellular channel 2	Homo sapiens	170-175
17688903-8	2007	The crystal structure of the complex between Fab-7D11 and L1 reveals the basis for the conformation-specific binding as recognition of a discontinuous epitope containing two loops that are held together by a disulfide bond.	Disulfides	208-217	FA complementation group B	Homo sapiens	45-48
26923188-2	2016	Our previous work on the structure of the RANK-RANKL complex revealed that Loop3 of RANK, specifically the non-canonical disulfide bond at the tip, performs a crucial role in specific recognition of RANKL.	Disulfides	121-130	TNF superfamily member 11	Homo sapiens	47-52
26923188-2	2016	Our previous work on the structure of the RANK-RANKL complex revealed that Loop3 of RANK, specifically the non-canonical disulfide bond at the tip, performs a crucial role in specific recognition of RANKL.	Disulfides	121-130	TNF superfamily member 11	Homo sapiens	199-204
26923188-5	2016	The kinetic analysis and osteoclast differentiation assay showed that in addition to the sharp turn induced by the disulfide bond, two consecutive arginine residues were also important for binding to RANKL and inhibiting osteoclastogenesis.	Disulfides	115-124	TNF superfamily member 11	Homo sapiens	200-205
3771096-0	1986	Preparation of Boc-[S-(3-nitro-2-pyridinesulfenyl)]-cysteine and its use for unsymmetrical disulfide bond formation.	Disulfides	91-100	BOC cell adhesion associated, oncogene regulated	Homo sapiens	15-18
3016176-0	1986	Disulfide bond formation between nerve growth factor and the nerve growth factor receptor from embryonic sensory neurons.	Disulfides	0-9	nerve growth factor receptor	Gallus gallus	61-89
17947653-2	2007	Recent studies showed that the expression and function of human TCR was improved by the introduction of an additional disulfide bond between the alpha- and beta-chains or by the exchange of the human constant region for murine sequences.	Disulfides	118-127	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	64-67
3523209-1	1986	A two-chain polypeptide, which corresponds to amino acid residues 115-143 and 144-184(185) of bovine serum albumin, connected to each other by a disulfide bridge, potentiated the effects of insulin on glucose transport and glucose metabolism in isolated rat adipocytes.	Disulfides	145-154	albumin	Rattus norvegicus	101-114
17720812-2	2007	Upon exposure to H(2)O(2) Orp1(Cys36) forms a disulfide-bonded complex with the C-terminal domain of the Yap1 protein (Yap1-cCRD).	Disulfides	46-55	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	26-30
3005648-3	1986	These two glycoproteins have been shown to exist as a disulfide-linked complex (gp55-116) within the envelope of mature virions.	Disulfides	54-63	neuroplastin	Homo sapiens	80-84
27098205-1	2016	Members of the lymphocyte antigen-6 (Ly6)/urokinase-type plasminogen activator receptor (uPAR) superfamily of proteins are cysteine-rich proteins characterized by a distinct disulfide bridge pattern that creates the three-finger Ly6/uPAR (LU) domain.	Disulfides	174-183	lymphocyte antigen 6 complex	Mus musculus	37-40
27098205-1	2016	Members of the lymphocyte antigen-6 (Ly6)/urokinase-type plasminogen activator receptor (uPAR) superfamily of proteins are cysteine-rich proteins characterized by a distinct disulfide bridge pattern that creates the three-finger Ly6/uPAR (LU) domain.	Disulfides	174-183	lymphocyte antigen 6 complex	Mus musculus	229-232
17716625-1	2007	Thioredoxin-1 (Trx) becomes inactive when cysteine-73 forms a mixed disulfide with glutathione.	Disulfides	68-77	thioredoxin	Homo sapiens	0-13
26948310-5	2016	CCl4 affected the formation of disulfide bonds through excessive hyper-oxidation of protein disulfide isomerase (PDI).	Disulfides	31-40	chemokine (C-C motif) ligand 4	Mus musculus	0-4
27054568-5	2016	Prerequisites postulated for physiological GARP function include membrane anchorage of GARP, disulfide bridges between the propeptide of TGFbeta and GARP and connection of this propeptide to alphavbeta6 or alphavbeta8 integrins of target cells during mechanical TGFbeta release.	Disulfides	93-102	leucine rich repeat containing 32	Homo sapiens	43-47
3006053-2	1986	GPIIb is a two-chain protein containing disulfide-linked alpha and beta subunits.	Disulfides	40-49	integrin subunit alpha 2b	Homo sapiens	0-5
2939067-2	1986	We found here that alpha-thrombin also rapidly converted single-chain bovine protein S to a nicked form, which consisted of the NH2-terminal segment containing gamma-carboxyglutamic acid and the COOH-terminal large segment bridged by a disulfide linkage(s).	Disulfides	236-245	coagulation factor II, thrombin	Bos taurus	25-33
17716625-1	2007	Thioredoxin-1 (Trx) becomes inactive when cysteine-73 forms a mixed disulfide with glutathione.	Disulfides	68-77	thioredoxin	Homo sapiens	15-18
17627859-4	2007	The P60 protein was a protein complex composed of several subunits with disulfide bridges.	Disulfides	72-81	plasma protein 1	Mus musculus	4-7
3940901-3	1986	The lobe of the S-protein part of the molecule, which lacks one disulfide bridge and has two shortened loops in turtle ribonuclease, has the lowest percentage of invariant residues, although the active-site residue His 119 is located in this part.	Disulfides	64-73	vitronectin	Homo sapiens	16-25
26799472-2	2016	Unlike its ligand TSH, whose subunits are encoded by two genes, the TSHR is expressed as a single polypeptide that subsequently undergoes intramolecular cleavage into disulfide-linked subunits.	Disulfides	167-176	thyroid stimulating hormone receptor	Homo sapiens	68-72
17652454-0	2007	Disulfide Bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis.	Disulfides	0-9	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	43-47
26609561-1	2016	Endoplasmic reticulum (ER) oxidoreductin 1alpha (Ero1alpha) is a disulfide producer in the ER of mammalian cells.	Disulfides	65-74	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	49-58
26609561-4	2016	Accordingly, disulfide production by Ero1alpha is accelerated by reducing conditions, which minimize the formation of inhibitory disulfides, or by mutations of regulatory cysteines.	Disulfides	13-22	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	37-46
26609561-4	2016	Accordingly, disulfide production by Ero1alpha is accelerated by reducing conditions, which minimize the formation of inhibitory disulfides, or by mutations of regulatory cysteines.	Disulfides	129-139	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	37-46
26609561-8	2016	In agreement, we identify a reciprocal crosstalk between the stabilities of the Cys(208)-Cys(241) disulfide and the inhibitory disulfide bonds involving Cys(104) and Cys(131), which also controls the recruitment of the H2O2 scavenger GPx8 to Ero1alpha.	Disulfides	98-107	glutathione peroxidase 8 (putative)	Homo sapiens	234-238
26609561-8	2016	In agreement, we identify a reciprocal crosstalk between the stabilities of the Cys(208)-Cys(241) disulfide and the inhibitory disulfide bonds involving Cys(104) and Cys(131), which also controls the recruitment of the H2O2 scavenger GPx8 to Ero1alpha.	Disulfides	98-107	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	242-251
26609561-8	2016	In agreement, we identify a reciprocal crosstalk between the stabilities of the Cys(208)-Cys(241) disulfide and the inhibitory disulfide bonds involving Cys(104) and Cys(131), which also controls the recruitment of the H2O2 scavenger GPx8 to Ero1alpha.	Disulfides	127-136	glutathione peroxidase 8 (putative)	Homo sapiens	234-238
26609561-8	2016	In agreement, we identify a reciprocal crosstalk between the stabilities of the Cys(208)-Cys(241) disulfide and the inhibitory disulfide bonds involving Cys(104) and Cys(131), which also controls the recruitment of the H2O2 scavenger GPx8 to Ero1alpha.	Disulfides	127-136	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	242-251
3161885-7	1985	Platelet GP IIb and GP IIIa and the related membrane proteins on both HUVE and BAE cells showed similar changes in electrophoretic mobility upon disulfide reduction.	Disulfides	145-154	integrin subunit alpha 2b	Homo sapiens	9-15
6515735-0	1984	[Transketolase inhibitors based on disulfide derivatives of oxythiamine with branched hydrocarbon chains].	Disulfides	35-44	transketolase	Mus musculus	1-14
17652454-2	2007	We found that cell exposure to H(2)O(2) caused the rapid oxidation of Ask1, leading to its multimerization through the formation of interchain disulfide bonds.	Disulfides	143-152	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	70-74
17678622-4	2007	We have developed a truncated version of RAP d3 in which these scaffolding regions are excised and replaced with a single, intramolecular disulfide bond.	Disulfides	138-147	LDL receptor related protein associated protein 1	Homo sapiens	41-44
6468376-0	1984	Location of the sulfhydryl groups involved in disulfide interaction between the neighboring proteins L6 and L29 in mammalian ribosomes.	Disulfides	46-55	ribosomal protein L29	Homo sapiens	108-111
6468376-2	1984	Proteins L6 and L29 occupy closely adjacent sites in mammalian 60-S ribosomal subparticles and are easily cross-linked by intermolecular disulfide bond formation.	Disulfides	137-146	ribosomal protein L29	Homo sapiens	16-19
6468376-3	1984	For locating the interacting thiols within the polypeptide chains the dissociated proteins L6 and L29 obtained from the isolated disulfide complex were subjected to S-cleavage following [14C]cyanylation of the two cysteine residues.	Disulfides	129-138	ribosomal protein L29	Homo sapiens	98-101
17698234-4	2007	Site-directed mutagenesis revealed that the heterogeneity and instability of HSA-IFN-alpha2b was caused by the incomplete disulfide bridge formation between Cys1 and Cys98 of IFN-alpha2b.	Disulfides	122-131	cystin 1	Homo sapiens	157-161
6329286-0	1984	Importance of disulfide bonds in receptors for vasoactive intestinal peptide and secretin in rat pancreatic plasma membranes.	Disulfides	14-23	secretin	Rattus norvegicus	81-89
26823467-8	2016	H2O2 inhibited Panx1 function temporarily by formation of disulfide bonds at the thiol group of its terminal cysteine.	Disulfides	58-67	pannexin 1	Homo sapiens	15-20
26886339-4	2016	Transferrin (Tf), a targeting protein, was mixed with 2-mercaptoethanol to break disulfide bonds.	Disulfides	81-90	transferrin	Mus musculus	0-11
26886339-4	2016	Transferrin (Tf), a targeting protein, was mixed with 2-mercaptoethanol to break disulfide bonds.	Disulfides	81-90	transferrin	Mus musculus	13-15
17692543-1	2007	Oxytocin (OT; Cys-Tyr-Ile-Gln-Asn-Cys-Pro-leu-Gly), a posterior pituitary peptide hormone, is characterized by a Cys1-Cys6 disulfide bond in its stable, isolated state.	Disulfides	123-132	cystin 1	Homo sapiens	113-117
26515416-9	2015	The specific HMGB1 isoform known to activate TLR4 signaling (disulfide HMGB1) stimulates smooth muscle cell to migrate and produce monocyte chemotactic protein 1/CCL2) via TLR4.	Disulfides	61-70	chemokine (C-C motif) ligand 2	Mus musculus	131-161
26515416-9	2015	The specific HMGB1 isoform known to activate TLR4 signaling (disulfide HMGB1) stimulates smooth muscle cell to migrate and produce monocyte chemotactic protein 1/CCL2) via TLR4.	Disulfides	61-70	chemokine (C-C motif) ligand 2	Mus musculus	162-166
26515416-10	2015	Macrophages produce smooth muscle cell mitogens in response to disulfide HMGB1 also in a TLR4/myeloid differentiation primary response gene (88)/Trif-dependent manner.	Disulfides	63-72	toll-like receptor adaptor molecule 2	Mus musculus	145-149
6538787-0	1984	Rat atrial natriuretic factor: complete amino acid sequence and disulfide linkage essential for biological activity.	Disulfides	64-73	natriuretic peptide A	Rattus norvegicus	4-29
17546662-1	2007	Glutaredoxins (Grxs) are glutathione-dependent oxidoreductases that belong to the thioredoxin superfamily catalyzing thiol-disulfide exchange reactions via active site cysteine residues.	Disulfides	123-132	thioredoxin	Homo sapiens	82-93
6667025-1	1983	Inactive NADP-malate dehydrogenase (disulfide form) from chloroplasts of Zea mays is activated by reduced thioredoxin while the active enzyme (dithiol form) is inactivated by incubation with oxidized thioredoxin.	Disulfides	36-45	LOC101027257	Zea mays	106-117
6667025-1	1983	Inactive NADP-malate dehydrogenase (disulfide form) from chloroplasts of Zea mays is activated by reduced thioredoxin while the active enzyme (dithiol form) is inactivated by incubation with oxidized thioredoxin.	Disulfides	36-45	LOC101027257	Zea mays	200-211
26422261-2	2015	The molecular structure of human SSADH revealed the intrinsic regulatory mechanism--redox-switch modulation--by which large conformational changes are brought about in the catalytic loop through disulfide bonding.	Disulfides	195-204	aldehyde dehydrogenase 5 family member A1	Homo sapiens	33-38
17676769-0	2007	Heat treatment of bovine alpha-lactalbumin results in partially folded, disulfide bond shuffled states with enhanced surface activity.	Disulfides	72-81	lactalbumin alpha	Bos taurus	25-42
26368576-6	2015	We used this approach for the replacement of the A-chain intramolecular disulfide bond of human relaxin 2 (H2 relaxin), an insulin-like peptide that has important regulatory roles in cardiovascular and connective tissue homeostasis that has led to successful Phase IIIa clinical trials for the treatment of acute heart failure.	Disulfides	72-81	relaxin 2	Homo sapiens	96-105
17661444-1	2007	High-molecular weight thioredoxin reductases (TRs) catalyze the reduction of the redox-active disulfide bond of thioredoxin, but an important difference in the TR family is the sequence of the C-terminal redox-active tetrapeptide that interacts directly with thioredoxin, especially the presence or absence of a selenocysteine (Sec) residue in this tetrapeptide.	Disulfides	94-103	thioredoxin	Homo sapiens	22-33
26302233-2	2015	CTB-FIX (~1 mg/g) in lyophilized cells was stable with proper folding, disulfide bonds and pentamer assembly when stored ~2 years at ambient temperature.	Disulfides	71-80	phosphate cytidylyltransferase 1B, choline	Homo sapiens	0-3
6132923-1	1983	The polypeptide hormone insulin and the binding unit of cholera toxin (CTB) were coupled via a disulfide bond.	Disulfides	95-104	phosphate cytidylyltransferase 1B, choline	Rattus norvegicus	71-74
17661444-1	2007	High-molecular weight thioredoxin reductases (TRs) catalyze the reduction of the redox-active disulfide bond of thioredoxin, but an important difference in the TR family is the sequence of the C-terminal redox-active tetrapeptide that interacts directly with thioredoxin, especially the presence or absence of a selenocysteine (Sec) residue in this tetrapeptide.	Disulfides	94-103	thioredoxin	Homo sapiens	112-123
6856484-3	1983	PP13 appears to be composed of two identical subunits which are held together by disulfide bonds.	Disulfides	81-90	galectin 13	Homo sapiens	0-4
6815193-2	1982	Two forms of kallikrein were generated that were each composed of two disulfide-linked polypeptide chains: a heavy chain of apparent Mr = 43,000 and a light chain of apparent Mr = either 36,000 or 33,000.	Disulfides	70-79	kallikrein related peptidase 4	Homo sapiens	13-23
26504166-1	2015	The endoplasmic reticulum (ER)-localized peroxiredoxin 4 (PRDX4) supports disulfide bond formation in eukaryotic cells lacking endoplasmic reticulum oxidase 1 (ERO1).	Disulfides	74-83	peroxiredoxin 4	Homo sapiens	41-56
26504166-1	2015	The endoplasmic reticulum (ER)-localized peroxiredoxin 4 (PRDX4) supports disulfide bond formation in eukaryotic cells lacking endoplasmic reticulum oxidase 1 (ERO1).	Disulfides	74-83	peroxiredoxin 4	Homo sapiens	58-63
17661444-1	2007	High-molecular weight thioredoxin reductases (TRs) catalyze the reduction of the redox-active disulfide bond of thioredoxin, but an important difference in the TR family is the sequence of the C-terminal redox-active tetrapeptide that interacts directly with thioredoxin, especially the presence or absence of a selenocysteine (Sec) residue in this tetrapeptide.	Disulfides	94-103	thioredoxin	Homo sapiens	112-123
17641688-6	2007	Fourth, mixed disulfide complexes, apparent intermediates in the electron transfer process, are detected between DsbDbeta and thioredoxin molecules on each side of the membrane.	Disulfides	14-23	thioredoxin	Homo sapiens	126-137
26504166-2	2015	The source of peroxide that fuels PRDX4-mediated disulfide bond formation has remained a mystery, because ERO1 is believed to be a major producer of hydrogen peroxide (H2O2) in the ER lumen.	Disulfides	49-58	peroxiredoxin 4	Homo sapiens	34-39
26504166-4	2015	Furthermore, expression of an ER-adapted catalase to degrade lumenal H2O2 attenuated PRDX4-mediated disulfide bond formation in cells lacking ERO1, whereas depletion of H2O2 in the cytosol or mitochondria had no similar effect.	Disulfides	100-109	peroxiredoxin 4	Homo sapiens	85-90
6292294-4	1982	The PC-1 antigen is therefore similar to the transferrin receptor in Mr, charge, subunit composition, disulfide bonding, and developmental regulation.	Disulfides	102-111	minisatellite 6 hypermutable	Mus musculus	4-8
7150622-0	1982	Thiol-disulfide-dependent interconversion of active and latent forms of rat hepatic 3-hydroxy-3-methylglutaryl-coenzyme A reductase.	Disulfides	6-15	3-hydroxy-3-methylglutaryl-CoA reductase	Rattus norvegicus	84-131
17557078-4	2007	Using a mechanism-based kinetic trapping technique to identify disulfide exchange interactions on the intact surface of living lymphocytes, we found that Trx1 catalytically interacts with a single principal target protein.	Disulfides	63-72	thioredoxin	Homo sapiens	154-158
6191201-4	1982	Monoclonal antibody to Lyt-2 or Lyt-3 (which are linked to one another by disulfide bonds) gave a uniform distribution of fluorescence and was mobile on the cell surface.	Disulfides	74-83	CD8 antigen, beta chain 1	Mus musculus	32-37
6896234-0	1982	Mouse whey acidic protein is a novel member of the family of "four-disulfide core" proteins.	Disulfides	67-76	whey acidic protein	Mus musculus	6-25
26468675-2	2015	Quiescin sulfhydryl oxidase (QSOX) is a multidomain catalyst of disulfide-bond formation that relays electrons from substrate cysteines through two redox-active sites to molecular oxygen.	Disulfides	64-73	quiescin sulfhydryl oxidase 1	Homo sapiens	0-27
26468675-2	2015	Quiescin sulfhydryl oxidase (QSOX) is a multidomain catalyst of disulfide-bond formation that relays electrons from substrate cysteines through two redox-active sites to molecular oxygen.	Disulfides	64-73	quiescin sulfhydryl oxidase 1	Homo sapiens	29-33
17591922-1	2007	Fibronectin (FN) is secreted as a disulfide-bonded FN dimer.	Disulfides	34-43	fibronectin 1	Mus musculus	0-11
26358741-4	2015	The synthetic human beta-defensin-2 carrying MeOGly at its N-terminus or the side chain amino group of Lys(10) reacted with phenylisothiocyanate or fluorescein isothiocyanate also at the N-methoxyamino group under the same conditions, demonstrating that this method is generally useful for the site-specific labeling of linear synthetic peptides as well as disulfide-containing peptides.	Disulfides	357-366	defensin beta 4B	Homo sapiens	20-35
26629401-6	2015	RESULTS: Adiporedoxin functions via a CXXC active site, and is upstream of protein disulfide isomerase whose direct function is disulfide bond formation, and ultimately protein secretion.	Disulfides	83-92	peroxiredoxin like 2A	Mus musculus	9-21
26629401-7	2015	Over and under expression of Adrx in vitro enhances and reduces, respectively, the secretion of the disulfide-bonded proteins including adiponectin and collagen isoforms.	Disulfides	100-109	peroxiredoxin like 2A	Mus musculus	29-33
6915937-2	1982	In each case, an initial cleavage is seen which produces HFa with Mr = 80,000 consisting of a heavy chain of Mr = 52,000 disulfide-linked to a light chain of Mr = 28,000.	Disulfides	121-130	coagulation factor XII	Homo sapiens	57-60
17591922-1	2007	Fibronectin (FN) is secreted as a disulfide-bonded FN dimer.	Disulfides	34-43	fibronectin 1	Mus musculus	13-15
17591922-1	2007	Fibronectin (FN) is secreted as a disulfide-bonded FN dimer.	Disulfides	34-43	fibronectin 1	Mus musculus	51-53
17549383-7	2007	Both VLHL PAI-1s convert into the latent form when treated with a reducing agent (DTT) that breaks disulfide bridges.	Disulfides	99-108	serpin family E member 1	Homo sapiens	10-15
7309367-0	1981	Synthesis of two analogs of a cyclic hexapeptide with disulfide bridge corresponding to bovine prothrombin precursor sequence 18-23.	Disulfides	54-63	coagulation factor II, thrombin	Bos taurus	95-106
738998-1	1978	The formation of interchain disulfide bonds from partially reduced Bence Jones protein (Nag, type lambda) and Fab(t) fragments of IgG1 myeloma proteins was studied in the presence of various disulfide reagents.	Disulfides	28-37	NBAS subunit of NRZ tethering complex	Homo sapiens	88-91
738998-7	1978	The fraction of intermediate having the ability to form the inter L-L disulfide bond was estimated to be 72% of the total Nag protein and was the same irrespective of the kind of disulfide reagent examined.	Disulfides	70-79	NBAS subunit of NRZ tethering complex	Homo sapiens	122-125
26297249-9	2015	Disulfide bond formation between Cys residues not present in the native state are relevant only on the time scale of collapse of BPTI.	Disulfides	0-9	spleen trypsin inhibitor I	Bos taurus	129-133
17503775-7	2007	By analogy to thioredoxin, Rdx proteins can use catalytic cysteine (or Sec) to form transient mixed disulfides with substrate proteins.	Disulfides	100-110	thioredoxin	Homo sapiens	14-25
26077311-8	2015	Thus inactivated FGE accumulates in which the cysteine pair Cys336/Cys341 in the catalytic site is oxidized to form disulfide bridges between either Cys336 and Cys341 or Cys341 and the CxPxR cysteine of the sulfatase.	Disulfides	116-125	sulfatase modifying factor 1	Homo sapiens	17-20
26077311-10	2015	The available data characterize eukaryotic FGE as a monooxygenase, in which Cys336/Cys341 disulfide bridge formation donates the electrons required to reduce one oxygen atom of O2 to water while the other oxygen atom oxidizes the CxPxR cysteine to FGly.	Disulfides	90-99	sulfatase modifying factor 1	Homo sapiens	43-46
26085103-2	2015	Mia40 is the oxidoreductase that inserts two disulfide bonds into the substrate simultaneously.	Disulfides	45-54	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
26085103-2	2015	Mia40 is the oxidoreductase that inserts two disulfide bonds into the substrate simultaneously.	Disulfides	45-54	thioredoxin reductase 1	Homo sapiens	13-27
26085103-6	2015	In addition, a ternary complex consisting of Erv1, Mia40, and substrate, linked by disulfide bonds, was not detected in vitro.	Disulfides	83-92	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	51-56
26085103-9	2015	Therefore, these studies support that Mia40 functions as an electron sink to facilitate the insertion of two disulfide bonds into substrates.	Disulfides	109-118	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	38-43
26075496-10	2015	This highly conserved pseudogene-derived variant in the TNX fibrinogen-like domain is predicted to be deleterious and disulfide bonded, results in reduced dermal elastin and fibrillin-1 staining and altered TGF-beta1 binding, and represents a novel TNXA/TNXB chimera.	Disulfides	118-127	elastin	Homo sapiens	162-169
410030-3	1977	The two intrachain disulfide bridges are separated by a stretch of amino acids containing an acid-labile aspartyl-prolHLA-2, A28, and AW25 contain this acid-labile peptide bond in their larger subunit.	Disulfides	19-28	immunoglobulin kappa variable 2-19 (pseudogene)	Homo sapiens	125-128
956663-9	1976	Maintenance of three interconnected disulfide linkages helps to explain a near identity between the secondary structures of human and porcine C3a as indicated by circular dichroism measurements.	Disulfides	36-45	complement C3	Homo sapiens	142-145
17555594-9	2007	TRX activity was assayed by the insulin disulfide reducing assay.	Disulfides	40-49	thioredoxin	Homo sapiens	0-3
17452033-2	2007	It contains three subunits (C8alpha, C8beta, C8gamma) arranged as a disulfide-linked C8alpha-gamma heterodimer that is noncovalently associated with C8beta.	Disulfides	68-77	complement C8 alpha chain	Homo sapiens	28-35
947897-2	1976	The catalysis of reoxidation of reduced bovine serum albumin by glutathione and a disulfide interchange enzyme.	Disulfides	82-91	albumin	Rattus norvegicus	47-60
26075496-10	2015	This highly conserved pseudogene-derived variant in the TNX fibrinogen-like domain is predicted to be deleterious and disulfide bonded, results in reduced dermal elastin and fibrillin-1 staining and altered TGF-beta1 binding, and represents a novel TNXA/TNXB chimera.	Disulfides	118-127	tenascin XA (pseudogene)	Homo sapiens	249-253
17452033-2	2007	It contains three subunits (C8alpha, C8beta, C8gamma) arranged as a disulfide-linked C8alpha-gamma heterodimer that is noncovalently associated with C8beta.	Disulfides	68-77	complement C8 alpha chain	Homo sapiens	85-92
25956655-3	2015	Recent data demonstrate that APE1 interacts with the mitochondrial import and assembly protein Mia40 suggesting the involvement of a redox-assisted mechanism, dependent on the disulfide transfer system, to be responsible of APE1 trafficking into the mitochondria.	Disulfides	176-185	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	95-100
25956655-5	2015	It is composed by two main proteins: Mia40 is the oxidoreductase that catalyzes the formation of the disulfide bonds in the substrate, while ALR reoxidizes Mia40 after the import.	Disulfides	101-110	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	37-42
947897-5	1976	Using this technique, we have shown that the rate of refolding of reduced bovine serum albumin catalyzed by either glutathione or rat liver disulfide interchange enzyme is greater than the rate of air reoxidation of albumin.	Disulfides	140-149	albumin	Rattus norvegicus	81-94
25956655-5	2015	It is composed by two main proteins: Mia40 is the oxidoreductase that catalyzes the formation of the disulfide bonds in the substrate, while ALR reoxidizes Mia40 after the import.	Disulfides	101-110	thioredoxin reductase 1	Homo sapiens	50-64
17437522-3	2007	SDS/PAGE, under nonreducing conditions, and a systematic substitution analysis of all six Cys residues of Nogo-A indicated that this domain forms two structural disulfide bonds among Cys residues 424, 464, 559 and 597, whereas the Cys residues at positions 699 and 912 seem to be dispensable for folding.	Disulfides	161-170	reticulon 4	Homo sapiens	106-112
25956655-6	2015	In this study, we demonstrated that: (i) APE1 and Mia40 interact through disulfide bond formation; and (ii) Mia40 expression levels directly affect APE1"s mitochondrial translocation and, consequently, play a role in the maintenance of mitochondrial DNA integrity.	Disulfides	73-82	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	50-55
25956655-6	2015	In this study, we demonstrated that: (i) APE1 and Mia40 interact through disulfide bond formation; and (ii) Mia40 expression levels directly affect APE1"s mitochondrial translocation and, consequently, play a role in the maintenance of mitochondrial DNA integrity.	Disulfides	73-82	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	108-113
943182-2	1976	Accurate delineation of the reactive site around the disulfide 6-127 by immunochemical study of beta-propiolactone lysozyme derivative and of synthetic disulfide peptides.	Disulfides	53-62	lysozyme C, milk isozyme	Capra hircus	115-123
17437523-3	2007	Recently, two M-1 branch conotoxins (mr3e and tx3a) have been reported to possess a new disulfide bond arrangement between Cys1 and Cys5, Cys2 and Cys4, and Cys3 and Cys6, which is different from those seen in the M-2 and M-4 branches.	Disulfides	88-97	cystin 1	Homo sapiens	123-127
1238393-12	1975	The 6 half-cystine residues in C3a are all interconnected through three disulfide linkages intersecting in a disulfide knot.	Disulfides	72-81	complement C3	Homo sapiens	31-34
1238393-12	1975	The 6 half-cystine residues in C3a are all interconnected through three disulfide linkages intersecting in a disulfide knot.	Disulfides	109-118	complement C3	Homo sapiens	31-34
25903127-8	2015	Mass spectrometry studies revealed that STZ oxidizes TRPA1 cysteines to disulfides and sulfenic acids.	Disulfides	72-82	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	53-58
25903135-0	2015	Olfactomedin-1 Has a V-shaped Disulfide-linked Tetrameric Structure.	Disulfides	30-39	olfactomedin 1	Homo sapiens	0-14
17448992-1	2007	Introduction of disulfide bonds into proteins entering the secretory pathway is catalyzed by Ero1p, which generates disulfide bonds de novo, and Pdi1p, which transfers disulfides to substrate proteins.	Disulfides	16-25	peptidyl arginine deiminase 1	Homo sapiens	145-150
25903135-3	2015	Using a combined approach of x-ray crystallography, solution scattering, analytical ultracentrifugation, and electron microscopy we determined that full-length Olfm1 forms disulfide-linked tetramers with a distinctive V-shaped architecture.	Disulfides	172-181	olfactomedin 1	Homo sapiens	160-165
25903135-6	2015	This agrees with our crystal structure of a C-terminal coiled-coil segment and beta-propeller combination (Olfm1(coil-Olf)) that reveals a disulfide-linked dimeric arrangement with the beta-propeller top faces in an outward exposed orientation.	Disulfides	139-148	olfactomedin 1	Homo sapiens	107-112
25697776-3	2015	We report that additional mutation of the Cys(208)-Cys(241) disulfide in hyperactive Ero1alpha (Ero1alpha-C104A/C131A) potentiates H2O2 production, ER oxidation, and cell toxicity.	Disulfides	60-69	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	85-94
25697776-3	2015	We report that additional mutation of the Cys(208)-Cys(241) disulfide in hyperactive Ero1alpha (Ero1alpha-C104A/C131A) potentiates H2O2 production, ER oxidation, and cell toxicity.	Disulfides	60-69	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	96-105
25697776-5	2015	Through its carboxyterminal active site, PDI unlocks this seal by forming a Cys(208)/Cys(241)-dependent mixed-disulfide complex with Ero1alpha.	Disulfides	110-119	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	133-142
1164027-0	1975	Cooperative calcium binding by the phospholipid binding region of bovine prothrombin: a requirement for intact disulfide bridges.	Disulfides	111-120	coagulation factor II, thrombin	Bos taurus	73-84
17448992-1	2007	Introduction of disulfide bonds into proteins entering the secretory pathway is catalyzed by Ero1p, which generates disulfide bonds de novo, and Pdi1p, which transfers disulfides to substrate proteins.	Disulfides	168-178	peptidyl arginine deiminase 1	Homo sapiens	145-150
1236742-0	1975	Chemical and physical properties of the disulfides of bovine neurophysin-II.	Disulfides	40-50	arginine vasopressin	Bos taurus	61-75
25731082-2	2015	We have reported that P5 has insulin reductase activity and inhibits lysozyme refolding by formation of lysozyme multimers with hypermolecular mass inactivated by intermolecular disulfides (hyLYS) in oxidative refolding of reduced denatured lysozyme.	Disulfides	178-188	protein disulfide isomerase family A member 6	Homo sapiens	22-24
17192269-6	2007	Domain cC2 also contains two cysteines on neighboring strands F and G, which would be able to form a disulfide bridge in a similar position as in telokin.	Disulfides	101-110	myosin light chain kinase	Homo sapiens	146-153
25560178-9	2015	Moreover, in vitro analyses show that the disulfide bond linking the resolving and peroxidatic cysteines protects the latter from overoxidation, thus explaining the dominant role of NTRC on the level of 2-Cys Prx overoxidation in vivo.	Disulfides	42-51	NADPH-dependent thioredoxin reductase C	Arabidopsis thaliana	182-186
235996-1	1975	Trinitroglycerin oxidizes the essential sulfhydryl group, Cys-149, of pig muscle glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate : NAD+ oxidoreductase(phosphorylating) EC 1.2.1.12) TO A SLUFENIC ACID, NOT TO A DISULFIDE.	Disulfides	233-242	glyceraldehyde-3-phosphate dehydrogenase	Sus scrofa	81-121
4577790-1	1973	Protein Hal is a human gamma4 heavy-chain disease protein whose molecular weight is reduced from 55,000 to 25,000 in 6 M guanidine due to the lack of disulfide bonds between heavy chains.	Disulfides	150-159	histidine ammonia-lyase	Homo sapiens	8-11
17329830-6	2007	Pulse chase labeling and surface labeling experiments of this cell line indicate that the protein synthesis of LAT1 and 4F2hc is slow, however, the heterodimeric complex assembled in the cells is very stable, and that the disulfide bond between the LAT1 and 4F2hc is not directly involved in the stability of the heterodimer.	Disulfides	222-231	solute carrier family 7 member 5	Homo sapiens	111-115
4564211-0	1972	Covalent structure of bovine neurophysin-II: localization of the disulfide bonds.	Disulfides	65-74	arginine vasopressin	Bos taurus	29-43
4564211-1	1972	The completed amino-acid sequence of bovine neurophysin-II, a major neurohypophyseal hormone-binding protein in the hypothalamo-neurohypophyseal complex of cows, set the stage for the localization of the disulfide bonds of this sulfur-rich molecule.	Disulfides	204-213	arginine vasopressin	Bos taurus	44-58
4564211-5	1972	Our assignment of the seven disulfide bridges present in neurophysin-II is as follows: Cys(10)-Cys(93); Cys(13)-Cys(95); Cys(21)-Cys(27); Cys(28)-Cys(44); Cys(54)-Cys(61); Cys(67)-Cys(73); Cys(74)-Cys(79).	Disulfides	28-37	arginine vasopressin	Bos taurus	57-71
4100047-1	1971	A gamma1 protein, designated CRA, found in heavy chain disease contains three inter-heavy disulfide bridges instead of the two normally found in gamma1 immunoglobulin heavy chains.	Disulfides	90-99	myotubularin related protein 11	Homo sapiens	29-32
25811377-3	2015	Moreover, ER function depends on proper disulfide bond formation--a partially oxygen-dependent process mediated by protein disulfide isomerase (PDI) and ER oxidoreductases.	Disulfides	40-49	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	115-142
25811377-3	2015	Moreover, ER function depends on proper disulfide bond formation--a partially oxygen-dependent process mediated by protein disulfide isomerase (PDI) and ER oxidoreductases.	Disulfides	40-49	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	144-147
25811377-9	2015	Decreased expression of PDI and QSOX1 (p&lt;0.05) reveal an impaired disulfide bond formation pathway, which may underlie nicotine-induced ER stress.	Disulfides	69-78	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	24-27
25811377-9	2015	Decreased expression of PDI and QSOX1 (p&lt;0.05) reveal an impaired disulfide bond formation pathway, which may underlie nicotine-induced ER stress.	Disulfides	69-78	quiescin sulfhydryl oxidase 1	Rattus norvegicus	32-37
25811377-10	2015	Finally, elevated expression of Hif1alpha and GCN2 (p&lt;0.05) indicate hypoxia and amino acid deprivation in nicotine-exposed placentas, respectively, which may also cause impaired disulfide bond formation and augmented ER stress.	Disulfides	182-191	hypoxia inducible factor 1 subunit alpha	Rattus norvegicus	32-41
17329830-6	2007	Pulse chase labeling and surface labeling experiments of this cell line indicate that the protein synthesis of LAT1 and 4F2hc is slow, however, the heterodimeric complex assembled in the cells is very stable, and that the disulfide bond between the LAT1 and 4F2hc is not directly involved in the stability of the heterodimer.	Disulfides	222-231	solute carrier family 7 member 5	Homo sapiens	249-253
17329830-6	2007	Pulse chase labeling and surface labeling experiments of this cell line indicate that the protein synthesis of LAT1 and 4F2hc is slow, however, the heterodimeric complex assembled in the cells is very stable, and that the disulfide bond between the LAT1 and 4F2hc is not directly involved in the stability of the heterodimer.	Disulfides	222-231	solute carrier family 3 member 2	Homo sapiens	120-125
17269658-1	2007	Bovine seminal ribonuclease (BS-RNase) is made up of two identical subunits bridged through two disulfide bonds.	Disulfides	96-105	seminal ribonuclease	Bos taurus	7-27
25740509-4	2015	Multistate structural modeling revealed that the R201 residue in Kv7.2, corresponding to R230 in Kv7.3, stabilized the resting and nearby voltage-sensing domain states by forming an intricate network of electrostatic interactions with neighboring negatively charged residues, a result also confirmed by disulfide trapping experiments.	Disulfides	303-312	potassium voltage-gated channel subfamily Q member 2	Homo sapiens	65-70
33479819-4	2021	OXT possesses the particular analytical measurement challenge of a disulfide bond.	Disulfides	67-76	oxytocin/neurophysin I prepropeptide	Homo sapiens	0-3
26028988-5	2015	With charge enhancement upon the addition of sulfolane to the analyte solution, improved protein fragmentation and disulfide bond cleavage efficiency was observed for proteins including bovine beta-lactoglobulin, soybean trypsin inhibitor, human proinsulin, and chicken lysozyme.	Disulfides	115-124	beta-lactoglobulin	Bos taurus	193-211
17259326-4	2007	Cystamine, which inactivates TG2 activity by forming a mixed disulfide, may interfere with and inhibit other thiol-dependent enzymes such as caspases.	Disulfides	61-70	transglutaminase 2, C polypeptide	Mus musculus	29-32
25568124-10	2015	Intracerebral disulfide HMGB-1 mimicked the effect of the stressor, because microglia isolated from HMGB-1-treated rats expressed exaggerated NLRP3 and proinflammatory cytokine expression after LPS treatment, whereas fully reduced HMGB-1 had no effect.	Disulfides	14-23	high mobility group box 1	Rattus norvegicus	24-30
25568124-10	2015	Intracerebral disulfide HMGB-1 mimicked the effect of the stressor, because microglia isolated from HMGB-1-treated rats expressed exaggerated NLRP3 and proinflammatory cytokine expression after LPS treatment, whereas fully reduced HMGB-1 had no effect.	Disulfides	14-23	high mobility group box 1	Rattus norvegicus	100-106
25568124-10	2015	Intracerebral disulfide HMGB-1 mimicked the effect of the stressor, because microglia isolated from HMGB-1-treated rats expressed exaggerated NLRP3 and proinflammatory cytokine expression after LPS treatment, whereas fully reduced HMGB-1 had no effect.	Disulfides	14-23	high mobility group box 1	Rattus norvegicus	100-106
33616882-11	2021	Interestingly, cases of FJHN with c744C > G (p.Cys248Trp) mutations also exhibit a high incidence of juvenile onset, and identical disulfide bridges are considered responsible for the accumulation of mutant UMOD in the endoplasmic reticulum.	Disulfides	131-140	uromodulin	Homo sapiens	207-211
33539081-2	2021	With an additional disulfide bond to enhance the protein stability, human A15C neuroglobin (Ngb) is an ideal protein scaffold for heme enzyme design.	Disulfides	19-28	neuroglobin	Homo sapiens	92-95
33348174-6	2021	We propose that the formation of an intramolecular disulfide bond within ICP6 triggers the formation of amyloid assemblies that are distinct from previously characterised viral amyloids M45 and ORF20.	Disulfides	51-60	M-phase specific PLK1 interacting protein	Homo sapiens	194-199
17102135-12	2007	Furthermore, the present data demonstrate that the mitochondrial dithiol compound dihydrolipoic acid restores mitochondrial aldehyde dehydrogenase activity via reduction of a disulfide at the active site and thereby improves nitrate tolerance.	Disulfides	175-184	aldehyde dehydrogenase 2 family member	Rattus norvegicus	110-146
33552266-2	2021	It exists as a monomer of 25 kDa, a homodimer of 45 kDa or a heterodimer of 135 kDa (disulfide bound to latent matrix metalloproteinase-9).	Disulfides	85-94	matrix metallopeptidase 9	Homo sapiens	111-137
17127392-2	2007	The complex structural paradigm of these channels is now known to include a pore-forming alpha1 subunit(s) whose electrophysiological properties are modulated by an intracellular beta subunit, a disulfide-linked complex of a membrane-spanning delta subunit with an extracellular alpha2 subunit, and a transmembrane gamma subunit.	Disulfides	195-204	adrenoceptor alpha 1D	Homo sapiens	89-95
33257569-5	2020	R2 is flanked by two cysteines that form a disulfide bridge in FGF23-WT; disulfide bridge formation in FGF23-WT is dispensable for KLA binding and for cell signaling via FGFRs.	Disulfides	43-52	fibroblast growth factor 23	Homo sapiens	63-68
33257569-5	2020	R2 is flanked by two cysteines that form a disulfide bridge in FGF23-WT; disulfide bridge formation in FGF23-WT is dispensable for KLA binding and for cell signaling via FGFRs.	Disulfides	73-82	fibroblast growth factor 23	Homo sapiens	103-108
25359430-2	2015	The peptide hormone somatostatin (SST) served as model compound for intercalation into the available disulfide functionalization schemes starting from the intercalator or the reactive SST precursor before or after bioconjugation.	Disulfides	101-110	somatostatin	Homo sapiens	20-32
25205713-6	2015	Fetuin-A is a liver-derived plasma protein with multiple functions, which is proteolytically processed to yield a disulfide-linked two-chain form.	Disulfides	114-123	alpha-2-HS-glycoprotein	Mus musculus	0-8
17154358-9	2007	In contrast, for thioredoxin a bonding of As that depended on the concentration of the disulfide-reducing agent tris(2-carboxyethyl) phosphine was demonstrated.	Disulfides	87-96	thioredoxin	Homo sapiens	17-28
25451030-1	2014	Mia40 (a mitochondrial import and assembly protein) catalyzes disulfide bond formation in proteins in the mitochondrial intermembrane space.	Disulfides	62-71	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
25451030-2	2014	By using Cox17 (a mitochondrial copper-binding protein) as a natural substrate, we discovered that, in the presence of Mia40, the formation of native disulfides is strongly favored.	Disulfides	150-160	cytochrome c oxidase copper chaperone COX17	Homo sapiens	9-14
25451030-2	2014	By using Cox17 (a mitochondrial copper-binding protein) as a natural substrate, we discovered that, in the presence of Mia40, the formation of native disulfides is strongly favored.	Disulfides	150-160	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	119-124
32861757-4	2020	METHODS: We designed and synthesized a set of mono and bicyclic AIF(370-394) analogs containing both disulfide and 1,2,3-triazole bridges, in the attempt to both stabilize the peptide conformation and improve its binding affinity to CypA.	Disulfides	101-110	apoptosis inducing factor mitochondria associated 1	Homo sapiens	64-67
17178406-3	2006	Here we show that stabilization of the binding domain dimer by the generation of intermolecular disulfide bonds apparently blocked desensitization of the kainate receptor GluR6.	Disulfides	96-105	glutamate ionotropic receptor kainate type subunit 2	Homo sapiens	171-176
32524995-5	2020	The native 23-residue peptide, stabilised by two disulfide bonds, has been reported to inhibit rat NaV1.8 and mouse NaV1.9 with low micromolar activity, and may therefore represent a scaffold for development of novel modulators with activity at human tetrodotoxin-resistant NaV isoforms.	Disulfides	49-58	sodium channel, voltage-gated, type XI, alpha	Mus musculus	116-122
25451030-3	2014	The catalytic mechanism of Mia40 involves a functional interplay between the chaperone site and the catalytic disulfide.	Disulfides	110-119	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	27-32
25451030-4	2014	Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide.	Disulfides	30-39	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
25451030-4	2014	Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide.	Disulfides	30-39	cytochrome c oxidase copper chaperone COX17	Homo sapiens	43-48
25451030-4	2014	Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide.	Disulfides	78-88	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
25451030-4	2014	Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide.	Disulfides	78-88	cytochrome c oxidase copper chaperone COX17	Homo sapiens	43-48
25451030-4	2014	Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide.	Disulfides	78-87	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
25451030-4	2014	Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide.	Disulfides	78-87	cytochrome c oxidase copper chaperone COX17	Homo sapiens	43-48
25451030-6	2014	We found that species with inadvertently formed incorrect disulfides are rebound by Mia40 and reshuffled, revealing a proofreading mechanism that is steered by the conformational folding of the substrate protein.	Disulfides	58-68	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	84-89
32791141-0	2020	Oxidation of apoptosis-inducing factor (AIF) to disulfide-linked conjugates.	Disulfides	48-57	apoptosis inducing factor mitochondria associated 1	Homo sapiens	13-38
32791141-0	2020	Oxidation of apoptosis-inducing factor (AIF) to disulfide-linked conjugates.	Disulfides	48-57	apoptosis inducing factor mitochondria associated 1	Homo sapiens	40-43
17068840-1	2006	The Plasmodium falciparum merozoite surface protein-1 19 kDa fragment (MSP-1(19)) comprises two closely packed EGF-like domains (EGF=epidermal growth factor), each stabilized by three disulfide bonds.	Disulfides	184-193	salivary protein electrophoretic 1, regulator	Mus musculus	71-76
32791141-5	2020	Our data showed that endogenous AIF could be oxidized to disulfide-linked conjugates (DLC).	Disulfides	57-66	apoptosis inducing factor mitochondria associated 1	Homo sapiens	32-35
32517586-9	2020	INNOVATION: This study reveals a mechanism to shuttle oxidizing equivalents from the primary MsrB3 active site toward the enzyme surface, where they would be available for further dithiol-disulfide exchange reactions.	Disulfides	188-197	methionine sulfoxide reductase B3	Homo sapiens	93-98
32517586-10	2020	CONCLUSION: Conformational changes must occur during the MsrB3 catalytic cycle to transfer oxidizing equivalents from the active site to the amino-terminal redox-active disulfide.	Disulfides	169-178	methionine sulfoxide reductase B3	Homo sapiens	57-62
32517586-11	2020	The accessibility of this exposed disulfide may help couple MsrB3 activity to other dithiol/disulfide redox events in the secretory pathway.	Disulfides	34-43	methionine sulfoxide reductase B3	Homo sapiens	60-65
32517586-11	2020	The accessibility of this exposed disulfide may help couple MsrB3 activity to other dithiol/disulfide redox events in the secretory pathway.	Disulfides	92-101	methionine sulfoxide reductase B3	Homo sapiens	60-65
25269953-6	2014	S100A4 was readily oxidized and formed disulfide-linked dimers and oligomers.	Disulfides	39-48	S100 calcium binding protein A4	Homo sapiens	0-6
24684506-7	2014	Some disulfide bonds in EGFR intracellular kinase domain were susceptible to H2S-induced cleavage.	Disulfides	5-14	epidermal growth factor receptor	Rattus norvegicus	24-28
16935838-4	2006	The unique gene structure, the conservation of both cysteines that form leptin"s single disulfide bridge, and stable clustering in phylogenetic analyses substantiate the unambiguous orthology of mammalian and carp leptins, despite low amino acid identity.	Disulfides	88-97	leptin	Homo sapiens	72-78
32771683-6	2020	High Mobility Group Box 1 (HMGB1) is a mediator of lethality in trauma and sepsis and our mechanistic studies revealed that disulfide and oxidized forms of HMGB1 bind to the gp91phox subunit of NOX2, and thus decrease the neutrophil respiratory burst and bacterial killing.	Disulfides	124-133	cytochrome b-245 beta chain	Homo sapiens	174-182
32771683-6	2020	High Mobility Group Box 1 (HMGB1) is a mediator of lethality in trauma and sepsis and our mechanistic studies revealed that disulfide and oxidized forms of HMGB1 bind to the gp91phox subunit of NOX2, and thus decrease the neutrophil respiratory burst and bacterial killing.	Disulfides	124-133	cytochrome b-245 beta chain	Homo sapiens	194-198
17002656-4	2006	Tissue factor (TF) was the first hemostasis protein shown to be controlled by an allosteric disulfide bond, the Cys186-Cys209 bond in the membrane-proximal fibronectin type III domain.	Disulfides	92-101	coagulation factor III, tissue factor	Homo sapiens	0-13
32603023-0	2020	Disulfide bond replacement with 1,4- and 1,5-disubstituted [1,2,3]-triazole on C-X-C chemokine receptor type 4 (CXCR4) peptide ligands: small changes that make big differences.	Disulfides	0-9	C-X-C motif chemokine receptor 4	Homo sapiens	79-110
32603023-0	2020	Disulfide bond replacement with 1,4- and 1,5-disubstituted [1,2,3]-triazole on C-X-C chemokine receptor type 4 (CXCR4) peptide ligands: small changes that make big differences.	Disulfides	0-9	C-X-C motif chemokine receptor 4	Homo sapiens	112-117
32603023-1	2020	Here we investigate the structural and biological effects ensuing form the disulfide bond replacement of a potent and selective C-X-C chemokine receptor type 4 (CXCR4) peptide antagonist, with 1,4- and 1,5- disubstituted 1,2,3-triazole moieties.	Disulfides	75-84	C-X-C motif chemokine receptor 4	Homo sapiens	128-159
32603023-1	2020	Here we investigate the structural and biological effects ensuing form the disulfide bond replacement of a potent and selective C-X-C chemokine receptor type 4 (CXCR4) peptide antagonist, with 1,4- and 1,5- disubstituted 1,2,3-triazole moieties.	Disulfides	75-84	C-X-C motif chemokine receptor 4	Homo sapiens	161-166
24684506-11	2014	INNOVATION AND CONCLUSION: H2S directly targets some disulfide bonds in EGFR, which activates the EGFR/gab1/PI3K/Akt pathway and subsequent Na(+)/K(+)-ATPase endocytosis and inhibition in renal tubular epithelial cells.	Disulfides	53-62	epidermal growth factor receptor	Rattus norvegicus	72-76
24684506-11	2014	INNOVATION AND CONCLUSION: H2S directly targets some disulfide bonds in EGFR, which activates the EGFR/gab1/PI3K/Akt pathway and subsequent Na(+)/K(+)-ATPase endocytosis and inhibition in renal tubular epithelial cells.	Disulfides	53-62	epidermal growth factor receptor	Rattus norvegicus	98-102
25123642-8	2014	Western blot analysis, using monoclonal antibodies, demonstrated that the crucial inter-subunit disulfide bond linking the p35 and p40 subunits is intact in the purified hIL-12.	Disulfides	96-105	interleukin 12A	Homo sapiens	123-126
25259790-6	2014	p35 and p40 but not p35 and EBI3 form an inter-chain disulfide bridge.	Disulfides	53-62	interleukin 12b	Mus musculus	8-11
17002656-4	2006	Tissue factor (TF) was the first hemostasis protein shown to be controlled by an allosteric disulfide bond, the Cys186-Cys209 bond in the membrane-proximal fibronectin type III domain.	Disulfides	92-101	coagulation factor III, tissue factor	Homo sapiens	15-17
31584633-1	2020	AIMS: Thioredoxin 1 (Trx1) is an evolutionarily conserved oxidoreductase that cleaves disulfide bonds in oxidized substrate proteins such as mechanistic target of rapamycin (mTOR) and maintains nuclear-encoded mitochondrial gene expression.	Disulfides	86-95	thioredoxin 1	Mus musculus	6-19
31584633-1	2020	AIMS: Thioredoxin 1 (Trx1) is an evolutionarily conserved oxidoreductase that cleaves disulfide bonds in oxidized substrate proteins such as mechanistic target of rapamycin (mTOR) and maintains nuclear-encoded mitochondrial gene expression.	Disulfides	86-95	thioredoxin 1	Mus musculus	21-25
17002656-6	2006	Reduction and oxidation of the Cys186-Cys209 disulfide bond is central to the transition between the three forms of TF.	Disulfides	45-54	coagulation factor III, tissue factor	Homo sapiens	116-118
24827137-1	2014	We have synthesized a new macromolecular architecture, (PAMAM)-CD8 , which consists of eight beta-cyclodextrin units (beta-CD) attached to a generation 1 poly(amidoamine) (PAMAM) dendrimer through a disulfide bond, which can be cleaved under reducing conditions.	Disulfides	199-208	CD8a molecule	Homo sapiens	63-66
17029235-1	2006	AtFKBP13, an immunophilin in the chloroplast thylakoid lumen, participates in redox-regulatory processes via a pair of conserved disulfide bonds that are present at the N- and C-termini of the protein.	Disulfides	129-138	FK506-binding protein 12	Arabidopsis thaliana	13-25
25137134-3	2014	In Prx4-mediated oxidative protein folding we discovered a new reaction that the sulfenic acid form of Prx4 can directly react with thiols in folding substrates, resulting in non-native disulfide cross-linking and aggregation.	Disulfides	186-195	peroxiredoxin 4	Homo sapiens	3-7
25137134-3	2014	In Prx4-mediated oxidative protein folding we discovered a new reaction that the sulfenic acid form of Prx4 can directly react with thiols in folding substrates, resulting in non-native disulfide cross-linking and aggregation.	Disulfides	186-195	peroxiredoxin 4	Homo sapiens	103-107
32436653-5	2020	METHODS AND RESULTS: Non-conserved amino acids within the beta1 ECII loop (compared with the amino acids constituting the ECII loop of the beta2 -adrenoceptor) were one by one replaced with alanine; potential intra-loop disulfide bridges were probed by cysteine-serine exchanges.	Disulfides	220-229	adrenoceptor beta 2	Homo sapiens	139-158
17021858-0	2006	Aberrant expression of HLA-B*3565Q is associated with a disrupted disulfide bond.	Disulfides	66-75	major histocompatibility complex, class I, B	Homo sapiens	23-28
32626998-1	2020	Endoplasmic reticulum (ER) oxidase 1alpha (ERO1alpha) is a glycosylated flavoenzyme that is located on the luminal side of the ER membrane, which serves an important role in catalyzing the formation of protein disulfide bonds and ER redox homeostasis.	Disulfides	210-219	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	43-52
32269095-2	2020	In peripheral APCs, gamma-IFN-inducible lysosomal thiol reductase (GILT) is critical for MHC class II-restricted presentation of disulfide bond-containing proteins, including the self-antigen and melanoma Ag tyrosinase-related protein 1 (TRP1).	Disulfides	129-138	tyrosinase-related protein 1	Mus musculus	238-242
32204567-3	2020	Apamin accounts for about 2%-3% dry weight of bee venom and is a peptide neurotoxin that contains 18 amino acid residues that are tightly crosslinked by two disulfide bonds.	Disulfides	157-166	apamin	Apis mellifera	0-6
25109971-4	2014	NMR studies demonstrate that ESP1 adopts a compact structure with a helical fold stabilized by an intramolecular disulfide bridge.	Disulfides	113-122	exocrine gland secreted peptide 1	Mus musculus	29-33
24888638-3	2014	The flavoenzyme quiescin sulfhydryl oxidase (QSOX), a catalyst of disulfide bond formation with an interdomain electron transfer step in its catalytic cycle, provides a unique opportunity for exploring the structural environment of enzymatic dithiol/disulfide exchange.	Disulfides	250-259	quiescin sulfhydryl oxidase 1	Homo sapiens	45-49
16899458-9	2006	A disulfide bridge holds the C-b2/C-b3 portions in close positions.	Disulfides	2-11	cannabinoid receptor 2	Homo sapiens	29-33
32197489-4	2020	However, the involvement of PDI in disulfide bond formation/S-nitrosylation of PSD95 and its role in epilepsy are still unknown.	Disulfides	35-44	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	28-31
32197489-9	2020	These findings indicate that PDI-mediated reduction of disulfide-bond formations may facilitate the NR2A-PSD95 binding and contribute to spontaneous seizure generation in epileptic animals.	Disulfides	55-64	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	29-32
16930550-3	2006	Four of the proteins were found to belong to the Kazal protease inhibitor family and were named SPINK8, SPINK10, SPINK11, and SPINK12, whereas one of the proteins, WFDC10, contained the WAP four-disulfide core domain structure.	Disulfides	195-204	WAP four-disulfide core domain 10	Mus musculus	164-170
32564733-7	2020	We found that formation of the disulfide bond between Cys12 and Cys20 residues as a result of XRCC1 oxidation (previously shown to modulate the protein affinity for Polbeta), affects the yield of the final product of SP BER and of non-ligated DNA intermediates (substrates of long-patch BER).	Disulfides	31-40	X-ray repair cross complementing 1	Homo sapiens	94-99
17041149-0	2006	Retention of a bean phaseolin/maize gamma-Zein fusion in the endoplasmic reticulum depends on disulfide bond formation.	Disulfides	94-103	prolamin 50 kDa gamma zein	Zea mays	36-46
31793782-0	2020	Disulfide-driven cyclic peptide synthesis of human endothelin-2 with a solid-supported Npys-Cl.	Disulfides	0-9	endothelin 2	Homo sapiens	51-63
31793782-1	2020	We report here the synthesis of human endothelin-2, a peptide of 21 amino acid residues with two disulfide bonds, based on a novel idea, a disulfide-driven cyclic peptide synthesis (DdCPS).	Disulfides	97-106	endothelin 2	Homo sapiens	38-50
31793782-1	2020	We report here the synthesis of human endothelin-2, a peptide of 21 amino acid residues with two disulfide bonds, based on a novel idea, a disulfide-driven cyclic peptide synthesis (DdCPS).	Disulfides	139-148	endothelin 2	Homo sapiens	38-50
25988148-6	2014	We suggest that in addition to their general ability to target misfolded polypeptide substrates to the Hsp70/Hsp110 chaperone machinery, Type I J-proteins carry an ancillary protein dithiol-isomerase function that can synergize the unfolding action of the chaperone, in the particular case of substrates that are further stabilized by non-native disulfide bonds.	Disulfides	346-355	heat shock protein family A (Hsp70) member 4	Homo sapiens	103-108
24983674-1	2014	Mal d 2 is a minor allergen from apple which shows a high conformational stability due to its eight conserved disulfide bridges.	Disulfides	110-119	mal d 2	Malus domestica	0-7
16808898-6	2006	Gpx3 can interact with Mxr1 through the formation of an intermolecular disulfide bond.	Disulfides	71-80	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	0-4
24782311-0	2014	Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretion.	Disulfides	24-33	somatostatin	Homo sapiens	88-103
31805285-1	2020	A relaxin-like gonad-stimulating peptide (RGP), comprising two peptide chains (A- and B-chains) linked by two interchain bonds and one intrachain disulfide bond, acts as a gonadotropin in starfish.	Disulfides	146-155	gonad-stimulating substance-like	Asterias rubens	2-40
16893552-0	2006	Gain of function in an ERV/ALR sulfhydryl oxidase by molecular engineering of the shuttle disulfide.	Disulfides	90-99	growth factor, augmenter of liver regeneration	Homo sapiens	27-30
31906511-3	2020	These polymers were then self-assembled and air-oxidised to form disulfide cross-linked nanoparticles (MP1-5) under sonication.	Disulfides	65-74	late endosomal/lysosomal adaptor, MAPK and MTOR activator 3	Homo sapiens	103-108
24912152-7	2014	Finally, disulfide cross-linking revealed interactions between the donor Ub-bound Cdc34 acidic loop and the Ub K48 site, as well as residues within the Y59-E51 loop, suggesting a mechanism in which the Ub Y59-E51 loop helps recruit the E2 acidic loop that aligns the receptor Ub K48 to the donor Ub for catalysis.	Disulfides	9-18	cell division cycle 34, ubiqiutin conjugating enzyme	Homo sapiens	82-87
16893552-1	2006	The ERV/ALR sulfhydryl oxidase domain is a versatile module adapted for catalysis of disulfide bond formation in various organelles and biological settings.	Disulfides	85-94	growth factor, augmenter of liver regeneration	Homo sapiens	8-11
16893552-5	2006	We have determined by X-ray crystallography the structure of AtErv1, an ERV/ALR enzyme that contains a Cys-X4-Cys shuttle disulfide and oxidizes thioredoxin in vitro, and compared it to ScErv2, which has a Cys-X-Cys shuttle and does not oxidize thioredoxin at an appreciable rate.	Disulfides	122-131	growth factor, augmenter of liver regeneration	Homo sapiens	76-79
24778189-7	2014	Moreover, these analyses revealed reversible homotypic interactions of NT5B at low pH and in high calcium, between disulfide-linked NT5B dimers, but not monomers.	Disulfides	115-124	5'-nucleotidase, cytosolic II	Homo sapiens	71-75
24778189-7	2014	Moreover, these analyses revealed reversible homotypic interactions of NT5B at low pH and in high calcium, between disulfide-linked NT5B dimers, but not monomers.	Disulfides	115-124	5'-nucleotidase, cytosolic II	Homo sapiens	132-136
16893552-5	2006	We have determined by X-ray crystallography the structure of AtErv1, an ERV/ALR enzyme that contains a Cys-X4-Cys shuttle disulfide and oxidizes thioredoxin in vitro, and compared it to ScErv2, which has a Cys-X-Cys shuttle and does not oxidize thioredoxin at an appreciable rate.	Disulfides	122-131	thioredoxin	Homo sapiens	145-156
32060887-4	2020	The IL-17 family itself comprises at least six members, IL-17A, IL-17B, IL-17C, IL-17D, IL-17E (also called IL-25), and IL-17F, all of which are known to be secreted as disulfide-linked homo- or heterodimers.	Disulfides	169-178	interleukin 17A	Homo sapiens	4-9
16893552-9	2006	We found that the AtErv1 shuttle disulfide region could indeed confer thioredoxin oxidase activity on the ScErv2 core.	Disulfides	33-42	thioredoxin	Homo sapiens	70-81
16766796-5	2006	We explored the mechanism of the Txnip-thioredoxin interaction and present evidence that Txnip and thioredoxin form a stable disulfide-linked complex.	Disulfides	125-134	thioredoxin	Homo sapiens	39-50
31889463-1	2020	A previous study showed that introducing an Arabidopsis thaliana thiol/disulfide-modulating protein, Low Quantum Yield of Photosystem II 1 (LQY1), into the cyanobacterium Synechocystis sp.	Disulfides	71-80	DnaJ/Hsp40 cysteine-rich domain superfamily protein	Arabidopsis thaliana	140-144
24881000-3	2014	The inhibitory action of 1,2,4-thiadiazole (TDZ) derivatives has been associated in the literature with their ability to form disulfide bridges with the catalytic cysteine of CatB.	Disulfides	126-135	cathepsin B	Homo sapiens	175-179
16766796-5	2006	We explored the mechanism of the Txnip-thioredoxin interaction and present evidence that Txnip and thioredoxin form a stable disulfide-linked complex.	Disulfides	125-134	thioredoxin	Homo sapiens	99-110
16766796-6	2006	We identified two Txnip cysteines that are important for thioredoxin binding and showed that this interaction is consistent with a disulfide exchange reaction between oxidized Txnip and reduced thioredoxin.	Disulfides	131-140	thioredoxin	Homo sapiens	57-68
31779209-7	2019	The disulfide-linker HLA-G1 dimer further exhibited significant avidity effects.	Disulfides	4-13	major histocompatibility complex, class I, G	Homo sapiens	21-27
16766796-6	2006	We identified two Txnip cysteines that are important for thioredoxin binding and showed that this interaction is consistent with a disulfide exchange reaction between oxidized Txnip and reduced thioredoxin.	Disulfides	131-140	thioredoxin	Homo sapiens	194-205
24700462-4	2014	MetAP2, but not MetAP1, contains a single Cys(228)-Cys(448) disulfide bond that has an -RHStaple configuration and links two beta-loop structures, which are hallmarks of allosteric disulfide bonds.	Disulfides	60-69	methionyl aminopeptidase 2	Homo sapiens	0-6
16870748-3	2006	Although CAP11 has a unique homodimeric structure with a disulfide bridge, the biological activities of dimeric and monomeric forms of CAP11 were almost the same.	Disulfides	57-66	cathelicidin antimicrobial peptide	Cavia porcellus	9-14
24700462-4	2014	MetAP2, but not MetAP1, contains a single Cys(228)-Cys(448) disulfide bond that has an -RHStaple configuration and links two beta-loop structures, which are hallmarks of allosteric disulfide bonds.	Disulfides	181-190	methionyl aminopeptidase 2	Homo sapiens	0-6
24700462-7	2014	The MetAP2 disulfide bond also exists in oxidized and reduced states in glioblastoma tumor cells, and stressing the cells by oxygen or glucose deprivation results in more oxidized enzyme.	Disulfides	11-20	methionyl aminopeptidase 2	Homo sapiens	4-10
24700462-10	2014	These findings indicate that MetAP2 is post-translationally regulated by an allosteric disulfide bond, which controls substrate specificity and catalytic efficiency.	Disulfides	87-96	methionyl aminopeptidase 2	Homo sapiens	29-35
31726976-2	2019	Structural studies showed that the long Olfm1 isoform BMZ forms a disulfide-linked tetramer with a V-shaped architecture.	Disulfides	66-75	olfactomedin 1	Homo sapiens	40-45
31726976-8	2019	The shorter Olfactomedin-1 isoform BMY is a disulfide-linked tetramer with a shape similar to the corresponding region in the longer BMZ isoform.	Disulfides	44-53	olfactomedin 1	Homo sapiens	12-26
16774767-2	2006	Insulin is a small, predominantly alpha-helical protein consisting of 51 residues in two disulfide-linked polypeptide chains that readily assembles into amyloid fibrils under conditions of low pH and elevated temperature.	Disulfides	89-98	insulin	Bos taurus	0-7
31513374-9	2019	The disulfide bridge used as a linker in the most active conjugate (III) upon incubation with S. aureus cells is reduced releasing constituent peptide and CIP-Cys.	Disulfides	4-13	muscular LMNA interacting protein	Homo sapiens	155-158
31085544-6	2019	For a diverse set of drug-linker conjugates, we determined that TRX in the presence of TRX-reductase and NADPH generated the cleaved products that are consistent with catalytic disulfide cleavage and linker immolation.	Disulfides	177-186	2,4-dienoyl-CoA reductase 1	Homo sapiens	105-110
31500118-6	2019	With the aim to investigate the interaction of cisplatin with the disulfide form of the protein, we performed a structural characterization in solution and in the solid state of oxidized human Atox1 and explored its ability to bind cisplatin under conditions mimicking an oxidizing environment.	Disulfides	66-75	antioxidant 1 copper chaperone	Homo sapiens	193-198
31417095-5	2019	Unlike previously reported semaphorin structures, Sema1a, Sema2a and Sema2b show stabilisation of sema domain dimer formation via a disulfide bond.	Disulfides	132-141	Semaphorin 1a	Drosophila melanogaster	50-56
24563467-5	2014	Reducing agent treatment decreased the cell adhesion activity of full-length NELL1 but not of its C-terminal fragments, suggesting that the intramolecular disulfide bonds within this region are not functionally necessary but that other disulfide linkages in the N-terminal region of NELL1 may be involved in cell adhesion activity.	Disulfides	155-164	NEL-like 1	Mus musculus	77-82
24563467-5	2014	Reducing agent treatment decreased the cell adhesion activity of full-length NELL1 but not of its C-terminal fragments, suggesting that the intramolecular disulfide bonds within this region are not functionally necessary but that other disulfide linkages in the N-terminal region of NELL1 may be involved in cell adhesion activity.	Disulfides	236-245	NEL-like 1	Mus musculus	77-82
27919037-1	2014	In the ER (endoplasmic reticulum) of human cells, disulfide bonds are predominantly generated by the two isoforms of Ero1 (ER oxidoreductin-1): Ero1alpha and Ero1beta.	Disulfides	50-59	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	144-153
27919037-2	2014	The activity of Ero1alpha is tightly regulated through the formation of intramolecular disulfide bonds to help ensure balanced ER redox conditions.	Disulfides	87-96	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	16-25
16507315-5	2006	We evaluated one such candidate, thioredoxin, a PDI family member reported to reduce a labile disulfide bond in CD4.	Disulfides	94-103	thioredoxin	Homo sapiens	33-44
27919037-4	2014	Ero1beta contains an additional cysteine residue (Cys262), which has been suggested to engage in an isoform-specific regulatory disulfide bond with Cys100 However, we show that the two regulatory disulfide bonds in Ero1alpha are likely conserved in Ero1beta (Cys90-Cys130 and Cys95-Cys100).	Disulfides	128-137	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	215-224
27919037-4	2014	Ero1beta contains an additional cysteine residue (Cys262), which has been suggested to engage in an isoform-specific regulatory disulfide bond with Cys100 However, we show that the two regulatory disulfide bonds in Ero1alpha are likely conserved in Ero1beta (Cys90-Cys130 and Cys95-Cys100).	Disulfides	196-205	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	215-224
31417599-12	2019	The activity of oxidized AtAMY3 was completely restored by simultaneous reduction by both glutaredoxin (specific for the removal of glutathione-mixed disulfide) and thioredoxin (specific for the reduction of protein disulfide), supporting a possible liaison between both redox modifications.	Disulfides	150-159	CAX interacting protein 1	Arabidopsis thaliana	90-102
31417599-12	2019	The activity of oxidized AtAMY3 was completely restored by simultaneous reduction by both glutaredoxin (specific for the removal of glutathione-mixed disulfide) and thioredoxin (specific for the reduction of protein disulfide), supporting a possible liaison between both redox modifications.	Disulfides	216-225	CAX interacting protein 1	Arabidopsis thaliana	90-102
24522867-7	2014	These differences may be attributed primarily to the very low pKa of Cys23 in hGrx1 and allow rationalisation of conclusion (ii) above: hGrx1 may catalyse the oxidation of Atox1(dithiol) by GSSG, but not the complementary reduction of the oxidised Atox1(disulfide) by GSH unless Cu(aq)(+) is present at a concentration that allows binding of Cu(I) to reduced Atox1 but not to hGrx1.	Disulfides	254-263	antioxidant 1 copper chaperone	Homo sapiens	172-177
30996299-6	2019	The p.C356W mutation may damage the predicted protein stability of ANO5 by altering the structure of several extracellular loops of ANO5 and affecting the formation of the disulfide bond, thereby disrupting the correct folding of ANO5 protein.	Disulfides	172-181	anoctamin 5	Homo sapiens	67-71
16507315-6	2006	We found that the ability of thioredoxin to reduce the disulfide bond in CD4 is enhanced in the presence of HIV-1 Env gp120 and that thioredoxin also reduces disulfide bonds in gp120 directly in the absence of CD4.	Disulfides	55-64	thioredoxin	Homo sapiens	29-40
16756322-5	2006	This is consistent with a restriction of possible conformations in the disulfide-containing mutant and a reduction of average water-exposed nonpolar surface area in the free state, resulting in a smaller conformational entropy penalty, but also a smaller change in surface area, for binding of mutant compared to wild-type Z(SPA)(-)(1).	Disulfides	71-80	signal-induced proliferation-associated 1	Homo sapiens	323-335
31177989-7	2019	Both the all-thiol and disulfide types of HMGB1 induced CitH3 via their specific receptors, CXCR4 and TLR4, respectively.	Disulfides	23-32	high mobility group box 1	Rattus norvegicus	42-47
31177989-7	2019	Both the all-thiol and disulfide types of HMGB1 induced CitH3 via their specific receptors, CXCR4 and TLR4, respectively.	Disulfides	23-32	C-X-C motif chemokine receptor 4	Rattus norvegicus	92-97
16771672-5	2006	A redox pathway (Mia40p and Erv1p) mediates the import of intermembrane space proteins such as the small Tim proteins, Cox17p, and Cox19p, which have disulfide bonds.	Disulfides	150-159	growth factor, augmenter of liver regeneration	Homo sapiens	28-33
30919383-5	2019	The crystal structure of FXa shows that this disulfide bond is solvent accessible, indicating that its stability might be subject to the oxidation/reduction balance.	Disulfides	45-54	coagulation factor X	Homo sapiens	25-28
24532791-8	2014	Intermediate disulfide trapping results confirmed an intra-molecular electron transfer pathway for VKORC1L1"s active site reduction.	Disulfides	13-22	vitamin K epoxide reductase complex subunit 1 like 1	Homo sapiens	99-107
24532791-9	2014	Our results allow us to propose a concerted action of the four conserved cysteines of VKORC1L1 for active site regeneration; the second loop cysteine, Cys-58, attacks the active site disulfide, forming an intermediate disulfide with Cys-139; the first loop cysteine, Cys-50, attacks the intermediate disulfide resulting in active site reduction.	Disulfides	183-192	vitamin K epoxide reductase complex subunit 1 like 1	Homo sapiens	86-94
16618117-2	2006	It contains three subunits (C8alpha, C8beta, C8gamma) arranged as a disulfide-linked C8alpha-gamma dimer that is noncovalently associated with C8beta.	Disulfides	68-77	complement C8 alpha chain	Homo sapiens	28-35
24532791-9	2014	Our results allow us to propose a concerted action of the four conserved cysteines of VKORC1L1 for active site regeneration; the second loop cysteine, Cys-58, attacks the active site disulfide, forming an intermediate disulfide with Cys-139; the first loop cysteine, Cys-50, attacks the intermediate disulfide resulting in active site reduction.	Disulfides	218-227	vitamin K epoxide reductase complex subunit 1 like 1	Homo sapiens	86-94
24532791-9	2014	Our results allow us to propose a concerted action of the four conserved cysteines of VKORC1L1 for active site regeneration; the second loop cysteine, Cys-58, attacks the active site disulfide, forming an intermediate disulfide with Cys-139; the first loop cysteine, Cys-50, attacks the intermediate disulfide resulting in active site reduction.	Disulfides	218-227	vitamin K epoxide reductase complex subunit 1 like 1	Homo sapiens	86-94
16618117-2	2006	It contains three subunits (C8alpha, C8beta, C8gamma) arranged as a disulfide-linked C8alpha-gamma dimer that is noncovalently associated with C8beta.	Disulfides	68-77	complement C8 alpha chain	Homo sapiens	85-92
30944182-0	2019	Effects of the SOS (A501C/T605C) and DS (I201C/A433C) Disulfide Bonds on HIV-1 Membrane Envelope Glycoprotein Conformation and Function.	Disulfides	54-63	endogenous retrovirus group K member 20	Homo sapiens	88-109
24563858-4	2014	We will describe here three redox sensors, the transcription factors OxyR, Yap1 and Pap1, which respond by disulfide bond formation to hydrogen peroxide stress, focusing specially on the differences among the three peroxide-sensing mechanisms.	Disulfides	107-116	RP9 pre-mRNA splicing factor	Homo sapiens	84-88
30944182-2	2019	Here we examine two previously reported Env mutants designed to be stabilized in this conformation by the introduction of artificial disulfide bonds: A501C/T605C (called SOS) and I201C/A433C (called DS).	Disulfides	133-142	endogenous retrovirus group K member 20	Homo sapiens	40-43
16481328-7	2006	The corresponding reaction with reduced Escherichia coli Trx was also negligible, but MGd was a better substrate (kcat/Km of 2.23 x 10(5) M(-1) s(-1)) for TrxR from E. coli and a strong inhibitor of Trx-dependent protein disulfide reduction.	Disulfides	221-230	peroxiredoxin 5	Homo sapiens	155-159
31459939-3	2019	This model is the first one to recapitulate all known biochemical features of LOX, namely, the coordination of the copper ion and the formation of the lysine tyrosylquinone cofactor and the disulfide bridges.	Disulfides	190-199	lysyl oxidase	Homo sapiens	78-81
23919619-11	2014	Thus, the Ero1alpha/GPx7/PDI triad generates two disulfide bonds and two H2O molecules at the expense of a single O2 molecule.	Disulfides	49-58	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	10-19
16481328-7	2006	The corresponding reaction with reduced Escherichia coli Trx was also negligible, but MGd was a better substrate (kcat/Km of 2.23 x 10(5) M(-1) s(-1)) for TrxR from E. coli and a strong inhibitor of Trx-dependent protein disulfide reduction.	Disulfides	221-230	thioredoxin	Homo sapiens	155-158
24332979-2	2014	In particular, selenoprotein M (SelM) may function as thiol disulfide oxidoreductase that participates in the formation of disulfide bonds, and can be implicated in calcium responses.	Disulfides	60-69	selenoprotein M	Homo sapiens	15-30
16231315-9	2006	TRP-1 has a thioredoxin activity, which was detected using the insulin disulfide reduction assay.	Disulfides	71-80	tRNA-Pro (anticodon AGG) 2-5	Homo sapiens	0-5
24332979-2	2014	In particular, selenoprotein M (SelM) may function as thiol disulfide oxidoreductase that participates in the formation of disulfide bonds, and can be implicated in calcium responses.	Disulfides	60-69	selenoprotein M	Homo sapiens	32-36
30578712-3	2019	Here, we show that a single proteolytic cleavage in the Stx2a A-subunit, resulting into two fragments (A1 and A2) linked by a disulfide bridge (cleaved Stx2a), dictates different binding abilities.	Disulfides	126-135	syntaxin 2	Homo sapiens	56-61
30578712-3	2019	Here, we show that a single proteolytic cleavage in the Stx2a A-subunit, resulting into two fragments (A1 and A2) linked by a disulfide bridge (cleaved Stx2a), dictates different binding abilities.	Disulfides	126-135	syntaxin 2	Homo sapiens	152-157
16231315-9	2006	TRP-1 has a thioredoxin activity, which was detected using the insulin disulfide reduction assay.	Disulfides	71-80	thioredoxin	Homo sapiens	12-23
24450625-6	2014	We have been studying how the H2O2 produced during disulfide formation in the ER (endoplasmic reticulum) is metabolized and have shown that ER-resident peroxiredoxin IV not only can remove H2O2, but also contributes to de novo disulfide formation.	Disulfides	51-60	peroxiredoxin 4	Homo sapiens	152-168
16425180-6	2006	The presence of a calcium-binding site comprising one glutamyl and three aspartyl residues in both the LDLR repeats and in the linkers supports the suggestion that calcium is required for the folding and disulfide connectivity of the linkers as in the LDLR repeats.	Disulfides	204-213	low density lipoprotein receptor	Homo sapiens	103-107
24450625-6	2014	We have been studying how the H2O2 produced during disulfide formation in the ER (endoplasmic reticulum) is metabolized and have shown that ER-resident peroxiredoxin IV not only can remove H2O2, but also contributes to de novo disulfide formation.	Disulfides	227-236	peroxiredoxin 4	Homo sapiens	152-168
24345576-0	2014	The role of interchain disulfide bond in a recombinant human interleukin-17A variant.	Disulfides	23-32	interleukin 17A	Homo sapiens	61-76
30966750-2	2019	To reduce allergenicity to arginine kinase (AK), site-directed mutagenesis was used to destroy disulfide bonds or mutate critical amino acids of conformational epitopes.	Disulfides	95-104	potassium voltage-gated channel subfamily A member 2	Rattus norvegicus	44-46
30668797-4	2019	Here we tested whether the enzymes Erv1 and Mia40 of the yeast mitochondrial disulfide relay could be functionally replaced by corresponding components of other compartments.	Disulfides	77-86	Mia40p	Saccharomyces cerevisiae S288C	44-49
30867432-7	2019	Importantly, we highlight a widespread PERK-dependent repression program, consisting of ER targeted proteins, including transmembrane proteins, glycoproteins, and proteins with disulfide bonds.	Disulfides	177-186	eukaryotic translation initiation factor 2 alpha kinase 3	Mus musculus	39-43
16425180-6	2006	The presence of a calcium-binding site comprising one glutamyl and three aspartyl residues in both the LDLR repeats and in the linkers supports the suggestion that calcium is required for the folding and disulfide connectivity of the linkers as in the LDLR repeats.	Disulfides	204-213	low density lipoprotein receptor	Homo sapiens	252-256
16414957-7	2006	These data suggest that activation of dimeric EpoR by Epo binding is achieved by reorienting the EpoR transmembrane and the connected cytosolic domains and that certain disulfide-bonded dimers represent the activated dimeric conformation of the EpoR, constitutively activating downstream signaling.	Disulfides	169-178	erythropoietin receptor	Mus musculus	46-50
30659052-4	2019	We hypothesized that a mechanism of T-cell-intrinsic energy consumption was the process of oxidative protein folding and disulfide bond formation that takes place in the endoplasmic reticulum (ER) guided by protein kinase R-like endoplasmic reticulum kinase (PERK) and downstream PERK axis target ER oxidoreductase 1 (ERO1alpha).	Disulfides	121-130	eukaryotic translation initiation factor 2 alpha kinase 3	Mus musculus	207-257
30659052-4	2019	We hypothesized that a mechanism of T-cell-intrinsic energy consumption was the process of oxidative protein folding and disulfide bond formation that takes place in the endoplasmic reticulum (ER) guided by protein kinase R-like endoplasmic reticulum kinase (PERK) and downstream PERK axis target ER oxidoreductase 1 (ERO1alpha).	Disulfides	121-130	eukaryotic translation initiation factor 2 alpha kinase 3	Mus musculus	259-263
30659052-4	2019	We hypothesized that a mechanism of T-cell-intrinsic energy consumption was the process of oxidative protein folding and disulfide bond formation that takes place in the endoplasmic reticulum (ER) guided by protein kinase R-like endoplasmic reticulum kinase (PERK) and downstream PERK axis target ER oxidoreductase 1 (ERO1alpha).	Disulfides	121-130	eukaryotic translation initiation factor 2 alpha kinase 3	Mus musculus	280-284
16414957-7	2006	These data suggest that activation of dimeric EpoR by Epo binding is achieved by reorienting the EpoR transmembrane and the connected cytosolic domains and that certain disulfide-bonded dimers represent the activated dimeric conformation of the EpoR, constitutively activating downstream signaling.	Disulfides	169-178	erythropoietin	Mus musculus	46-49
24080471-2	2014	Other therapeutic uses of NAC have also emerged, including the alleviation of clinical symptoms of cystic fibrosis through cysteine-mediated disruption of disulfide cross-bridges in the glycoprotein matrix in mucus.	Disulfides	155-164	X-linked Kx blood group	Homo sapiens	26-29
16519524-2	2006	A number of published structural and biochemical studies show conflicting results for the disulfide bonding pattern and the overall fold of the SMB domain, possibly because this domain may undergo disulfide shuffling and/or conformational changes during handling.	Disulfides	197-206	small nuclear ribonucleoprotein polypeptides B and B1	Rattus norvegicus	144-147
24346086-2	2014	In the present study, we synthesized a ternary copolymer mPEG-b-PLL-g-(ss-lPEI), denoted as PLI, by introducing disulfide bond linkages to graft low molecular weight linear polyethylenimine (lPEI) to the block copolymer of poly(L-lysine) (PLL) and poly(ethylene glycol) (PEG) for siRNA delivery.	Disulfides	112-121	serpin family F member 2	Homo sapiens	92-95
30478816-2	2019	Here, we report analysis of disulfide linkages in insulin variant, endothelin 3, and relaxin 2 by in-source dissociation (ISD) during LC-MS. A duplet insulin peptide from Glu-C digestion that contains peptides p1 and p2 (from chains A and B, respectively) was selected as a model peptide.	Disulfides	28-37	endothelin 3	Homo sapiens	67-79
30478816-2	2019	Here, we report analysis of disulfide linkages in insulin variant, endothelin 3, and relaxin 2 by in-source dissociation (ISD) during LC-MS. A duplet insulin peptide from Glu-C digestion that contains peptides p1 and p2 (from chains A and B, respectively) was selected as a model peptide.	Disulfides	28-37	relaxin 2	Homo sapiens	85-94
30478816-9	2019	ISD was also successfully applied to determine double disulfide linkages in endothelin 3 and relaxin 2 peptides.	Disulfides	54-63	endothelin 3	Homo sapiens	76-88
30478816-9	2019	ISD was also successfully applied to determine double disulfide linkages in endothelin 3 and relaxin 2 peptides.	Disulfides	54-63	relaxin 2	Homo sapiens	93-102
30580571-0	2019	Redox Activation of Nox1 (NADPH Oxidase 1) Involves an Intermolecular Disulfide Bond Between Protein Disulfide Isomerase and p47phox in Vascular Smooth Muscle Cells.	Disulfides	70-79	neutrophil cytosolic factor 1	Homo sapiens	125-132
30580571-4	2019	Mass spectrometry of crosslinked peptides confirmed redox-dependent disulfide bonds between cysteines of p47phox and PDI and an intramolecular bond between Cys 196 and 378 in p47phox.	Disulfides	68-77	neutrophil cytosolic factor 1	Homo sapiens	105-112
24427321-11	2014	Curcumin may suppress GSTM5 expression to enhance the lethal effect of irinotecan on LOVO cells, and maybe their combination via the affection of PDI and PRDX4 to disturb the formation and reduction of disulfides results in inducing apoptosis of LOVO cell.	Disulfides	202-212	peroxiredoxin 4	Homo sapiens	154-159
16354652-2	2006	We report that human peptidoglycan recognition proteins 3 and 4 (PGLYRP3 and PGLYRP4) are secreted as 89-115-kDa disulfide-linked homo- and heterodimers and are bactericidal against several pathogenic and nonpathogenic transient, but not normal flora, Gram-positive bacteria.	Disulfides	113-122	peptidoglycan recognition protein 3	Homo sapiens	21-63
24161674-3	2013	A disulfide dimer peptide of CXCL14(51-77) bound to CXCR4 with comparable affinity to full length CXCL14, and exhibited CXCL12 inhibitor activity.	Disulfides	2-11	C-X-C motif chemokine receptor 4	Homo sapiens	52-57
24062305-8	2013	Our results also showed that physiological concentrations of glutathione, NADPH, and glutathione reductase reduced the non-active site disulfide in vitro.	Disulfides	135-144	2,4-dienoyl-CoA reductase 1	Homo sapiens	74-79
30658470-4	2019	The developed MS-based platform was evaluated to analyze the disulfide bonds of structural isomers during the folding reaction of synthetic cardiotoxin A3 polypeptide (syn-CTX A3), an important medical component in cobra venom.	Disulfides	61-70	synemin	Homo sapiens	130-133
30658470-6	2019	Quantitative analysis of these disulfide-linked peptides showed the occurrence of a progressive disulfide rearrangement that generates a native disulfide bond pattern on syn-CTX A3 folded protein.	Disulfides	31-40	synemin	Homo sapiens	170-173
30658470-6	2019	Quantitative analysis of these disulfide-linked peptides showed the occurrence of a progressive disulfide rearrangement that generates a native disulfide bond pattern on syn-CTX A3 folded protein.	Disulfides	96-105	synemin	Homo sapiens	170-173
30658470-6	2019	Quantitative analysis of these disulfide-linked peptides showed the occurrence of a progressive disulfide rearrangement that generates a native disulfide bond pattern on syn-CTX A3 folded protein.	Disulfides	96-105	synemin	Homo sapiens	170-173
24101517-2	2013	Here we report that the mammalian homolog of the yeast mitochondrial disulfide relay protein Mia40 (CHCHD4) is necessary for the respiratory-dependent translocation of p53 into the mitochondria.	Disulfides	69-78	Mia40p	Saccharomyces cerevisiae S288C	93-98
30647152-2	2019	Different BILF1 homologs display highly conserved extracellular loops (ECLs) including the conserved cysteine residues involved in disulfide bridges present in class A GPCRs (GPCR bridge between transmembrane helix 3 [TM-3] and ECL-2) and in chemokine receptors (CKR bridge between the N terminus and ECL-3).	Disulfides	131-140	membrane protein BILF1	Human gammaherpesvirus 4	10-15
16354652-2	2006	We report that human peptidoglycan recognition proteins 3 and 4 (PGLYRP3 and PGLYRP4) are secreted as 89-115-kDa disulfide-linked homo- and heterodimers and are bactericidal against several pathogenic and nonpathogenic transient, but not normal flora, Gram-positive bacteria.	Disulfides	113-122	peptidoglycan recognition protein 3	Homo sapiens	65-72
16421453-4	2006	The cysteine residues in this motif form a redox-active disulfide necessary for thioredoxin activity.	Disulfides	56-65	thioredoxin	Homo sapiens	80-91
30243381-0	2018	Improved thermostability and catalytic efficiency of overexpressed catalase from B. pumilus ML 413 (KatX2) by introducing disulfide bond C286-C289.	Disulfides	122-131	AKO65_RS18850	Bacillus pumilus	67-75
30243381-4	2018	To satisfy requirements for this critical bottleneck, in this work, we improved the thermo-stability of a heme-catalase (KatX2) from a high oxidative stress resistance Bacillus pumilus ML413 through the construction of a disulfide bond between S286C and D289C.	Disulfides	221-230	AKO65_RS18850	Bacillus pumilus	111-119
30243381-5	2018	After the site-directed mutagenesis targeting the disulfide bond between S286C and D289C into the wild-type catalase, a potential improvement of thermo-stability half-life at 60  C was increased by 48 min compared to the wild-type half-life.	Disulfides	50-59	AKO65_RS18850	Bacillus pumilus	108-116
24101517-2	2013	Here we report that the mammalian homolog of the yeast mitochondrial disulfide relay protein Mia40 (CHCHD4) is necessary for the respiratory-dependent translocation of p53 into the mitochondria.	Disulfides	69-78	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	100-106
16269408-0	2006	Deficiency of disulfide bonds facilitating fibrillogenesis of endostatin.	Disulfides	14-23	collagen type XVIII alpha 1 chain	Homo sapiens	62-72
23249342-3	2013	TTR was selected due to its low molecular weight and the free cysteine residue in the polypeptide chain, which is known to be extensively modified by formation of mixed disulfides.	Disulfides	169-179	transthyretin	Homo sapiens	0-3
23834247-2	2013	Mia40 uses its redox active CPC motif to shuttle disulfides between its client proteins (newly imported proteins) and the thiol oxidase Erv1.	Disulfides	49-59	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
30351116-3	2018	Different preparations of FH can also reduce the disulfide bonds linking large Von Willebrand factor (VWF) multimers into smaller, less adhesive forms.	Disulfides	49-58	complement factor H	Homo sapiens	26-28
16269408-10	2006	Our present work not only elucidates the correlation between the existence of disulfide bonds and the fibril formation of endostatin but also may provide some insights into the structural and functional basis of endostatin in Alzheimer disease brains.	Disulfides	78-87	collagen type XVIII alpha 1 chain	Homo sapiens	122-132
24043701-1	2013	Ero1-alpha and endoplasmic reticulum (ER) oxidoreductases of the protein disulfide isomerase (PDI) family promote the efficient introduction of disulfide bonds into nascent polypeptides in the ER.	Disulfides	73-82	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	0-10
16343416-0	2006	Disulfide between Cys392 and Cys438 of human serum albumin is redox-active, which is responsible for the thioredoxin-supported lipid peroxidase activity.	Disulfides	0-9	thioredoxin	Homo sapiens	105-116
23403147-2	2013	In human neuroglobin, the presence of an internal disulfide bond in the CD loop (CD7-D5) is found to modulate the ligand binding through a change in the heme pocket structure.	Disulfides	50-59	neuroglobin	Homo sapiens	9-20
30374105-3	2018	Here we show that fixing loop TMH1-2ND3 to the nearby subunit PSST via a disulfide bridge introduced by site-directed mutagenesis reversibly disengages proton pumping without impairing ubiquinone reduction, inhibitor binding or the Active/Deactive transition.	Disulfides	73-82	NADH:ubiquinone oxidoreductase core subunit S7	Homo sapiens	62-66
16343416-3	2006	In this paper, we identified the redox-active disulfide, which can be specifically reduced by Trx, responsible for the Trx-dependent lipid peroxidase activity.	Disulfides	46-55	thioredoxin	Homo sapiens	94-97
16343416-3	2006	In this paper, we identified the redox-active disulfide, which can be specifically reduced by Trx, responsible for the Trx-dependent lipid peroxidase activity.	Disulfides	46-55	thioredoxin	Homo sapiens	119-122
30231474-2	2018	NGAL exists as a 25 kDa monomer, a 46 kDa homodimer (the most abundant form in healthy subjects) and a 130 kDa disulfide-linked heterodimer bound to latent matrix metalloproteinase-9.	Disulfides	111-120	lipocalin 2	Homo sapiens	0-4
16343416-7	2006	Taken together, these results suggested that HSA has a capability to reduce lipid hydroperoxide with the use of Trx as an in vivo electron donor, and that the redox-active disulfide between Cys392 and Cys438 acts as a primary site of the catalysis for the Trx-linked lipid peroxidase activity.	Disulfides	172-181	thioredoxin	Homo sapiens	256-259
23765404-0	2013	Extracellular disulfide bridges serve different purposes in two homologous chemokine receptors, CCR1 and CCR5.	Disulfides	14-23	C-C motif chemokine receptor 5	Homo sapiens	105-109
16303961-11	2005	All zeta-crystallin present in the nuclear WI fraction appeared to be there as a result of disulfide cross-linking.	Disulfides	91-100	quinone oxidoreductase	Cavia porcellus	4-19
23848407-0	2013	Beta-lactoglobulin self-assembly: structural changes in early stages and disulfide bonding in fibrils.	Disulfides	73-82	beta-lactoglobulin	Bos taurus	0-18
30150531-0	2018	Stabilization of the CD81 Large Extracellular Loop with De Novo Disulfide Bonds Improves Its Amenability for Peptide Grafting.	Disulfides	64-73	CD81 molecule	Homo sapiens	21-25
30150531-2	2018	To enhance the tolerance of a tetraspanin fold to modification, we achieved significant thermal stabilization of the human CD81 large extracellular loop (hCD81 LEL) via de novo disulfide bonds.	Disulfides	177-186	CD81 molecule	Homo sapiens	123-127
30150531-2	2018	To enhance the tolerance of a tetraspanin fold to modification, we achieved significant thermal stabilization of the human CD81 large extracellular loop (hCD81 LEL) via de novo disulfide bonds.	Disulfides	177-186	CD81 molecule	Homo sapiens	154-159
16159880-3	2005	The evidence for a functional association between PHGPx, SMCP, and keratins is further supported by the identification of a sequence motif of regularly spaced Cys-Cys doublets common to SMCP and high sulfur keratin-associated proteins, involved in bundling hair shaft keratin by disulfide cross-linking.	Disulfides	279-288	glutathione peroxidase 4	Homo sapiens	50-55
30150531-3	2018	The best mutants were shown to exhibit a positive shift in the melting temperature (Tm) of up to 25  C. The combination of two most potent disulfide bonds connecting different strands of the protein resulted in a mutant with a Tm of 109  C, 43  C over the Tm of the wild-type hCD81 LEL.	Disulfides	139-148	CD81 molecule	Homo sapiens	276-281
29757379-1	2018	Quiescin sulfhydryl oxidase 1 (QSOX1) catalyzes the formation of disulfide bonds in protein substrates.	Disulfides	65-74	quiescin sulfhydryl oxidase 1	Homo sapiens	0-29
29757379-1	2018	Quiescin sulfhydryl oxidase 1 (QSOX1) catalyzes the formation of disulfide bonds in protein substrates.	Disulfides	65-74	quiescin sulfhydryl oxidase 1	Homo sapiens	31-36
29845893-6	2018	Recently, intra- and intermolecular disulfide bridges were identified that are essential for the structure and the function of the DUOX2-DUOXA2 complex.	Disulfides	36-45	dual oxidase maturation factor 2	Homo sapiens	137-143
23199280-0	2013	VEGFR2 functions as an H2S-targeting receptor protein kinase with its novel Cys1045-Cys1024 disulfide bond serving as a specific molecular switch for hydrogen sulfide actions in vascular endothelial cells.	Disulfides	92-101	kinase insert domain receptor	Homo sapiens	0-6
23704371-2	2013	Quiescin sulfhydryl oxidase 1 (QSOX1) is an atypical disulfide catalyst, localized to the Golgi apparatus or secreted from cells.	Disulfides	53-62	quiescin sulfhydryl oxidase 1	Homo sapiens	9-29
16159880-3	2005	The evidence for a functional association between PHGPx, SMCP, and keratins is further supported by the identification of a sequence motif of regularly spaced Cys-Cys doublets common to SMCP and high sulfur keratin-associated proteins, involved in bundling hair shaft keratin by disulfide cross-linking.	Disulfides	279-288	sperm mitochondria associated cysteine rich protein	Homo sapiens	57-61
29858230-4	2018	We further show that ER oxidoreductin 1alpha (Ero1alpha), the pivotal sulfhydryl oxidase that catalyzes disulfide formation in the ER, is phosphorylated by Fam20C in the Golgi apparatus and retrograde-transported to the ER mediated by ERp44.	Disulfides	104-113	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	46-55
16159880-3	2005	The evidence for a functional association between PHGPx, SMCP, and keratins is further supported by the identification of a sequence motif of regularly spaced Cys-Cys doublets common to SMCP and high sulfur keratin-associated proteins, involved in bundling hair shaft keratin by disulfide cross-linking.	Disulfides	279-288	sperm mitochondria associated cysteine rich protein	Homo sapiens	186-190
16274250-13	2005	Stabilized isomers of EGF were further generated from denaturation of wild-type and mutant EGF via the method of disulfide scrambling.	Disulfides	113-122	epidermal growth factor	Homo sapiens	22-25
23704371-2	2013	Quiescin sulfhydryl oxidase 1 (QSOX1) is an atypical disulfide catalyst, localized to the Golgi apparatus or secreted from cells.	Disulfides	53-62	quiescin sulfhydryl oxidase 1	Homo sapiens	31-36
23704371-3	2013	We examined the physiological function for extracellular catalysis of de novo disulfide bond formation by QSOX1.	Disulfides	78-87	quiescin sulfhydryl oxidase 1	Homo sapiens	106-111
16274250-14	2005	Properties of these diverse isomers of EGF, including their isomerization, stability, unfolding, refolding, and disulfide structures, are described in this paper.	Disulfides	112-121	epidermal growth factor	Homo sapiens	39-42
30456358-5	2018	First, both human Ero1 isoforms exist in a dynamic mixed disulfide complex with protein disulfide isomerase, which involves cysteines (Cys166 in Ero1alpha and Cys165 in Ero1beta) that have previously been regarded as being nonfunctional.	Disulfides	57-66	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	145-154
16288040-6	2005	In this report, we first determined that PKCepsilon became resistant to inactivation by disulfides when Cys452 was replaced with alanine by site-specific mutagenesis of human PKCepsilon or a constitutively active PKCepsilon mutant.	Disulfides	88-98	protein kinase C epsilon	Homo sapiens	41-51
29932420-4	2018	Protein chemical studies show that ligand binding to extended alphaIIbbeta3 integrin renders the betaI-domain Cys177-Cys184 disulfide bond cleavable by ERp5.	Disulfides	124-133	protein disulfide isomerase family A member 6	Homo sapiens	152-156
23755192-5	2013	Molecular dynamics simulation suggested that AtEPF1/EPF2-like peptides form an additional disulfide bond in their loop regions and show greater flexibility in these regions than AtEPFL9/Stomagen-like peptides.	Disulfides	90-99	epidermal patterning factor 1	Arabidopsis thaliana	45-51
16288040-6	2005	In this report, we first determined that PKCepsilon became resistant to inactivation by disulfides when Cys452 was replaced with alanine by site-specific mutagenesis of human PKCepsilon or a constitutively active PKCepsilon mutant.	Disulfides	88-98	protein kinase C epsilon	Homo sapiens	175-185
23478141-6	2013	RESULTS: Disrupting the hGH C-terminal disulfide bridge significantly reduces binding affinity to GHR and GHBP.	Disulfides	39-48	growth hormone receptor	Homo sapiens	98-101
29778741-5	2018	Further co-relationship analysis of the gene expression level and content changes of primary metabolites indicated the following: the acyl-CoA dehydrogenase and fatty acid synthase genes were closely associated with lipid metabolism, and the hexokinase and the glycogen synthase gene expression levels were related to carbohydrate metabolism, while the aminopeptidase N and the protein disulfide isomerase gene expression levels were not correlated with protein metabolism.	Disulfides	386-395	fatty acid synthase	Homo sapiens	161-180
16288040-6	2005	In this report, we first determined that PKCepsilon became resistant to inactivation by disulfides when Cys452 was replaced with alanine by site-specific mutagenesis of human PKCepsilon or a constitutively active PKCepsilon mutant.	Disulfides	88-98	protein kinase C epsilon	Homo sapiens	175-185
23478141-6	2013	RESULTS: Disrupting the hGH C-terminal disulfide bridge significantly reduces binding affinity to GHR and GHBP.	Disulfides	39-48	growth hormone receptor	Homo sapiens	106-110
16288040-7	2005	These results showed that the disulfides inactivated PKCepsilon by thiol-disulfide exchange, either upon Cys452 S-thiolation or by rearrangement to an intra-protein disulfide.	Disulfides	30-40	protein kinase C epsilon	Homo sapiens	53-63
16288040-7	2005	These results showed that the disulfides inactivated PKCepsilon by thiol-disulfide exchange, either upon Cys452 S-thiolation or by rearrangement to an intra-protein disulfide.	Disulfides	30-39	protein kinase C epsilon	Homo sapiens	53-63
16288040-7	2005	These results showed that the disulfides inactivated PKCepsilon by thiol-disulfide exchange, either upon Cys452 S-thiolation or by rearrangement to an intra-protein disulfide.	Disulfides	73-82	protein kinase C epsilon	Homo sapiens	53-63
29111118-5	2018	The Thioredoxin-Thioredoxin Reductase system (Trx-TrxR) specifically reduces the interchain disulfide bond while the cytosolic chaperone protein Hsp90 mediates L refolding.	Disulfides	92-101	thioredoxin 1	Mus musculus	4-15
16262253-6	2005	We also found that the C-terminal penultimate selenocysteine was required for transfer of reducing equivalents from the thiol/disulfide active site of TGR to the glutaredoxin domain.	Disulfides	126-135	thioredoxin reductase 3	Homo sapiens	151-154
29111118-5	2018	The Thioredoxin-Thioredoxin Reductase system (Trx-TrxR) specifically reduces the interchain disulfide bond while the cytosolic chaperone protein Hsp90 mediates L refolding.	Disulfides	92-101	thioredoxin 1	Mus musculus	16-27
29111118-5	2018	The Thioredoxin-Thioredoxin Reductase system (Trx-TrxR) specifically reduces the interchain disulfide bond while the cytosolic chaperone protein Hsp90 mediates L refolding.	Disulfides	92-101	thioredoxin 1	Mus musculus	46-49
23532321-8	2013	The three cysteine residues of HSP60 exhibit different responses to gossypol treatment: an increase of thiol/disulfide ratio for the Cys447 residue due to a decrease of the cellular GSH level, and a decrease of thiol/disulfide ratios for Cys442 and Cys237 residues due to oxidation and sulfation.	Disulfides	109-118	heat shock protein family D (Hsp60) member 1	Homo sapiens	31-36
23532321-8	2013	The three cysteine residues of HSP60 exhibit different responses to gossypol treatment: an increase of thiol/disulfide ratio for the Cys447 residue due to a decrease of the cellular GSH level, and a decrease of thiol/disulfide ratios for Cys442 and Cys237 residues due to oxidation and sulfation.	Disulfides	217-226	heat shock protein family D (Hsp60) member 1	Homo sapiens	31-36
16217027-5	2005	Once activated, the C-terminal redox center reduces a disulfide bond within thioredoxin.	Disulfides	54-63	thioredoxin	Homo sapiens	76-87
23479674-10	2013	The latter, deprived of its disulfide bond by mutations, was predominantly unfolded at 20 C. These results will help better understand and design the properties of ED3 for its use as diagnostic, vaccine or therapeutic tools.	Disulfides	28-37	ectodysplasin A receptor	Homo sapiens	164-167
29703838-4	2018	Electrophilic ligands are able to activate TRPA1 channels by interacting with critical cysteine residues on the N terminus of the channels via covalent modification and/or disulfide bonds.	Disulfides	172-181	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	43-48
29524511-4	2018	Structural analyses and activity assays indicated that the Trx domain also contributes to the glutathione S-transferase activity of Grx3, via an inter-domain disulfide bond between Cys37 and Cys176.	Disulfides	158-167	monothiol glutaredoxin GRX3	Saccharomyces cerevisiae S288C	132-136
23479735-6	2013	This disulfide-linked CXCL1 dimer binds CXCR2 with nanomolar affinity and shows potent agonist activity in various cellular assays.	Disulfides	5-14	C-X-C motif chemokine ligand 1	Homo sapiens	22-27
16096271-10	2005	Furthermore, data were obtained demonstrating that homocysteine can covalently modify fibrillin-1 via disulfide bonds.	Disulfides	102-111	fibrillin 1	Homo sapiens	86-97
23337084-1	2013	Human leukocyte cell-derived chemotaxin 2 (LECT2) is a chemotactic factor for neutrophils and a 16-kDa secreted protein consisting of 133 amino acids with three intramolecular disulfide bonds.	Disulfides	176-185	leukocyte cell derived chemotaxin 2	Homo sapiens	6-41
29555931-6	2018	Profound aggravations of inflammation, deterioration of behavioral outcomes, and infarct expansion were observed in LPS-injected MCAO animals, in which serum HMGB1 surge, especially disulfide type, occurred immediately after LPS administration and aggravated brain and systemic inflammations probably by acting in synergy with LPS.	Disulfides	182-191	high mobility group box 1	Rattus norvegicus	158-163
23337084-1	2013	Human leukocyte cell-derived chemotaxin 2 (LECT2) is a chemotactic factor for neutrophils and a 16-kDa secreted protein consisting of 133 amino acids with three intramolecular disulfide bonds.	Disulfides	176-185	leukocyte cell derived chemotaxin 2	Homo sapiens	43-48
29222746-2	2018	In a survey of proteins that might undergo Cd2+-dependent disulfide crosslinking, we identified the adenylyl cyclase-associated protein, CAP1, as undergoing a dimerization in response to Cd2+ (5-40 microM) that was sensitive to disulfide reducing agents, was reproduced by the disulfide crosslinking agent diamide, and was shown by site-directed mutagenesis to involve the Cys29 residue of the protein.	Disulfides	58-67	Cd2 molecule	Rattus norvegicus	43-46
16125134-5	2005	LAT1 forms a heterodimer with the 4F2hc heavy chain, which are joined by a disulfide bond between Cys160 of LAT1 and Cys110 of 4F2hc.	Disulfides	75-84	solute carrier family 7 member 5	Homo sapiens	0-4
29222746-2	2018	In a survey of proteins that might undergo Cd2+-dependent disulfide crosslinking, we identified the adenylyl cyclase-associated protein, CAP1, as undergoing a dimerization in response to Cd2+ (5-40 microM) that was sensitive to disulfide reducing agents, was reproduced by the disulfide crosslinking agent diamide, and was shown by site-directed mutagenesis to involve the Cys29 residue of the protein.	Disulfides	58-67	Cd2 molecule	Rattus norvegicus	187-190
29222746-2	2018	In a survey of proteins that might undergo Cd2+-dependent disulfide crosslinking, we identified the adenylyl cyclase-associated protein, CAP1, as undergoing a dimerization in response to Cd2+ (5-40 microM) that was sensitive to disulfide reducing agents, was reproduced by the disulfide crosslinking agent diamide, and was shown by site-directed mutagenesis to involve the Cys29 residue of the protein.	Disulfides	228-237	Cd2 molecule	Rattus norvegicus	187-190
29222746-2	2018	In a survey of proteins that might undergo Cd2+-dependent disulfide crosslinking, we identified the adenylyl cyclase-associated protein, CAP1, as undergoing a dimerization in response to Cd2+ (5-40 microM) that was sensitive to disulfide reducing agents, was reproduced by the disulfide crosslinking agent diamide, and was shown by site-directed mutagenesis to involve the Cys29 residue of the protein.	Disulfides	228-237	Cd2 molecule	Rattus norvegicus	187-190
22285006-2	2013	In urothelial carcinoma (UC), constitutive receptor activation occurs most commonly through substitution of a wild-type residue with cysteine in the extracellular domain of FGFR3, thereby resulting in dimerization (through disulfide bridge formation) and subsequent stimulation of tyrosine kinase activity.	Disulfides	223-232	fibroblast growth factor receptor 3	Homo sapiens	173-178
29215294-3	2018	LyP-1 is a short peptide cyclized with a disulfide bond.	Disulfides	41-50	protein tyrosine phosphatase non-receptor type 22	Homo sapiens	0-5
16125134-5	2005	LAT1 forms a heterodimer with the 4F2hc heavy chain, which are joined by a disulfide bond between Cys160 of LAT1 and Cys110 of 4F2hc.	Disulfides	75-84	solute carrier family 3 member 2	Homo sapiens	34-39
16125134-5	2005	LAT1 forms a heterodimer with the 4F2hc heavy chain, which are joined by a disulfide bond between Cys160 of LAT1 and Cys110 of 4F2hc.	Disulfides	75-84	solute carrier family 7 member 5	Homo sapiens	108-112
16125134-5	2005	LAT1 forms a heterodimer with the 4F2hc heavy chain, which are joined by a disulfide bond between Cys160 of LAT1 and Cys110 of 4F2hc.	Disulfides	75-84	solute carrier family 3 member 2	Homo sapiens	127-132
22633464-0	2013	Late-onset Charcot-Marie-Tooth disease type 1B due to a novel mutation in the extracellular disulfide bridge of MPZ gene.	Disulfides	92-101	myelin protein zero	Homo sapiens	112-115
16006626-4	2005	Its genome encodes two envelope proteins E1 and E2, which mature in the ER to form a noncovalently bound, native complex and disulfide aggregates and have previously been shown to induce expression of the molecular chaperone immunoglobulin heavy chain binding protein.	Disulfides	125-134	small nucleolar RNA, H/ACA box 73A	Homo sapiens	41-50
24008827-1	2013	BACKGROUND: Quiescin sulfhydryl oxidase 1 (QSOX1), which oxidizes sulfhydryl groups to form disulfide bonds in proteins, is found to be over-expressed in various pancreatic cancer cell lines and patients.	Disulfides	92-101	quiescin sulfhydryl oxidase 1	Homo sapiens	21-41
24008827-1	2013	BACKGROUND: Quiescin sulfhydryl oxidase 1 (QSOX1), which oxidizes sulfhydryl groups to form disulfide bonds in proteins, is found to be over-expressed in various pancreatic cancer cell lines and patients.	Disulfides	92-101	quiescin sulfhydryl oxidase 1	Homo sapiens	43-48
29102725-5	2018	In this respect, we proposed a cyclization strategy to improve enzyme-peptide binding affinity by, instead of traditionally maximizing enthalpy contribution, minimizing entropy cost of the binding, where a disulfide bond was added across the two terminal residues of linear peptides, resulting in a number of TIMP3-derived cyclic peptides.	Disulfides	206-215	TIMP metallopeptidase inhibitor 3	Homo sapiens	309-314
29277598-8	2018	CONCLUSIONS: The capacity of thioredoxin 1 and glutaredoxin 1 to reduce intra-protein disulfide bridges is weakened in Rap1 deficient mice, resulting in hyper-activation of NADPH oxidase and greater reactive oxygen species generation.	Disulfides	86-95	thioredoxin 1	Mus musculus	29-42
29343868-0	2018	Galectin-13, a different prototype galectin, does not bind beta-galacto-sides and forms dimers via intermolecular disulfide bridges between Cys-136 and Cys-138.	Disulfides	114-123	galectin 13	Homo sapiens	0-11
24348563-2	2013	The main components of this disulfide relay machinery are the oxidoreductase Mia40 and the sulfhydryl oxidase Erv1/ALR.	Disulfides	28-37	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	77-82
29343868-2	2018	To understand galectin-13 function at the molecular level, we solved its crystal structure and discovered that its dimer is stabilized by two disulfide bridges between Cys136 and Cys138 and six hydrogen bonds involving Val135, Val137, and Gln139.	Disulfides	142-151	galectin 13	Homo sapiens	14-25
16103172-0	2005	Glycosylation, disulfide bond formation, and the presence of a WSXWS-like motif in the orf virus GIF protein are critical for maintaining the integrity of Binding to ovine granulocyte-macrophage colony-stimulating factor and interleukin-2.	Disulfides	15-24	cobalamin binding intrinsic factor	Homo sapiens	97-100
32254199-6	2018	Subsequently, ultra-sensitive redox responsiveness is realized since the abundant disulfide bonds of the micellar matrix can be cleaved by a high level of GSH, leading to a rapid intracellular release of encapsulated doxorubicin (DOX) and PLK1-specific shRNA.	Disulfides	82-91	polo like kinase 1	Mus musculus	239-243
28935607-0	2017	S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase induces formation of C150-C154 intrasubunit disulfide bond in the active site of the enzyme.	Disulfides	108-117	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	23-63
28935607-10	2017	CONCLUSIONS: The mixed disulfide between Cys150 and GSH is an intermediate product of S-glutathionylation: its subsequent reaction with Cys154 results in the intrasubunit disulfide bond in the active site of GAPDH.	Disulfides	23-32	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	208-213
28935607-10	2017	CONCLUSIONS: The mixed disulfide between Cys150 and GSH is an intermediate product of S-glutathionylation: its subsequent reaction with Cys154 results in the intrasubunit disulfide bond in the active site of GAPDH.	Disulfides	171-180	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	208-213
23515368-3	2013	In the current study, a tumor-targeting cyclic peptide screened by phage display, Lyp-1 (a peptide that specifically binds to tumor and endothelial cells of tumor lymphatics in certain tumors), was structurally modified by replacement of the original intramolecular disulfide bond with a diseleno bond.	Disulfides	266-275	protein tyrosine phosphatase non-receptor type 22	Homo sapiens	82-87
28935607-11	2017	The mixed disulfide and the C150-C154 disulfide bond protect GAPDH from irreversible oxidation and can be reduced in the excess of thiols.	Disulfides	10-19	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	61-66
16103172-4	2005	Site-directed mutagenesis of the GIF protein demonstrated, first, the importance of disulfide bonds, and second, that a sequence motif (WDPWV), related to the WSXWS motif of the type 1 cytokine receptor superfamily, was necessary for biological activity.	Disulfides	84-93	cobalamin binding intrinsic factor	Homo sapiens	33-36
15901730-7	2005	We found that TGR can catalyze isomerization of protein and interprotein disulfide bonds and localized this function to its thiol domain.	Disulfides	73-82	thioredoxin reductase 3	Homo sapiens	14-17
29101848-0	2017	Human Fc receptor-like 5 distinguishes IgG2 disulfide isoforms and deamidated charge variants.	Disulfides	44-53	Fc receptor like 5	Homo sapiens	6-24
29184062-9	2017	Chemical crosslinking in reducing conditions shows that disulfide bridges are involved in KCC2 dimerization.	Disulfides	56-65	solute carrier family 12 member 5	Homo sapiens	90-94
23277477-4	2013	Based on endogenous disulfide formation between engineered cysteines (Cys), we found that in beta2 and beta3, as in beta1 and beta4, TM1 is closest to alphaS1 and alphaS2 and TM2 is closest to alphaS0.	Disulfides	20-29	hemoglobin, beta adult minor chain	Mus musculus	93-108
23277477-5	2013	Mouse beta3 (mbeta3) has seven Cys in its loop, one of which is free, and this Cys readily forms disulfides with Cys substituted in the extracellular flanks of each of alphaS0-alphaS6.	Disulfides	97-107	tubulin, beta 3 class III	Mus musculus	0-19
23277477-11	2013	In mbeta3, the free Cys is at position 7; position 2 lacks a Cys present in all other beta2-beta4; and the disulfide pattern is 1-8, 3-4, and 5-6.	Disulfides	107-116	tubulin, beta 3 class III	Mus musculus	3-9
15901730-9	2005	Together, TGR and GPx4 can serve as a novel disulfide bond formation system.	Disulfides	44-53	thioredoxin reductase 3	Homo sapiens	10-13
15901730-9	2005	Together, TGR and GPx4 can serve as a novel disulfide bond formation system.	Disulfides	44-53	glutathione peroxidase 4	Homo sapiens	18-22
23174349-7	2013	The binding study revealed that out of all analogs tested, [Ala(68,86)]CART(61-102), which contains two disulfide bridges (positions 74-94 and 88-101), preserved a high affinity to both native PC12 cells and those that had been differentiated into neurons.	Disulfides	104-113	CART prepropeptide	Rattus norvegicus	71-75
15989955-3	2005	After passage through the TOM channel, these proteins are covalently trapped by Mia40 via disulfide bridges.	Disulfides	90-99	pre-mRNA processing factor 6	Homo sapiens	26-29
23174349-9	2013	Therefore, the disulfide bridge between cysteines 68 and 86 in CART(61-102) can be omitted without a loss of biological activity, but the preservation of two other disulfide bridges and the full-length peptide are essential for biological activity.	Disulfides	15-24	CART prepropeptide	Rattus norvegicus	63-67
23326313-1	2013	Gamma-interferon-inducible lysosomal thiol reductase (GILT) is known to reduce disulfide bonds present in proteins internalized by antigen presenting cells, facilitating optimal processing and presentation of peptides on Major Histocompatibility Complex class II molecules, as well as the subsequent activation of CD4-positive T lymphocytes.	Disulfides	79-88	CD4 antigen	Mus musculus	314-317
29023092-6	2017	A disulfide engineering mutant, N-MdmXC25-C110/C76-C88, which incorporated two staples to rigidify the ligand-binding pocket, allowed an affinity for nutlin-3a higher than that of wild-type N-MdmX (Kd ~ 0.48 vs Kd ~ 20.3 muM).	Disulfides	2-11	transformed mouse 3T3 cell double minute 4	Mus musculus	32-38
15989955-6	2005	We propose that Erv1 and Mia40 function as a disulfide relay system that catalyzes the import of proteins into the IMS by an oxidative folding mechanism.	Disulfides	45-54	growth factor, augmenter of liver regeneration	Homo sapiens	16-20
15844167-2	2005	We have identified the rtv gene, and using the new HHpred homology detection method, we show that the Rtv protein defines a new family of disulfide-rich proteins in insects that are related to vertebrate snake neurotoxin-like proteins, including CD59 and transforming growth factor-beta type II receptors.	Disulfides	138-147	retroactive	Drosophila melanogaster	23-26
29095159-0	2017	Nogo Receptor crystal structures with a native disulfide pattern suggest a novel mode of self-interaction.	Disulfides	47-56	reticulon 4 receptor	Homo sapiens	0-13
29095159-3	2017	The available structures of the NgR ligand-binding leucine-rich repeat (LRR) domain have an artificial disulfide pattern owing to truncated C-terminal construct boundaries.	Disulfides	103-112	reticulon 4 receptor	Homo sapiens	32-35
29095159-5	2017	Here, crystal structures of the NgR LRR with a longer C-terminal segment and a native disulfide pattern are presented.	Disulfides	86-95	reticulon 4 receptor	Homo sapiens	32-35
28949004-3	2017	ADAM17 exists in two conformations which differ in their disulfide connection in the membrane-proximal domain (MPD).	Disulfides	57-66	ADAM metallopeptidase domain 17	Homo sapiens	0-6
23069765-1	2013	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.	Disulfides	87-96	interleukin 17A	Homo sapiens	35-50
23069765-1	2013	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.	Disulfides	87-96	interleukin 17A	Homo sapiens	52-58
23949117-1	2013	The mammalian endoplasmic reticulum (ER) harbors disulfide bond-generating enzymes, including Ero1alpha and peroxiredoxin 4 (Prx4), and nearly 20 members of the protein disulfide isomerase family (PDIs), which together constitute a suitable environment for oxidative protein folding.	Disulfides	49-58	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	94-103
23949117-1	2013	The mammalian endoplasmic reticulum (ER) harbors disulfide bond-generating enzymes, including Ero1alpha and peroxiredoxin 4 (Prx4), and nearly 20 members of the protein disulfide isomerase family (PDIs), which together constitute a suitable environment for oxidative protein folding.	Disulfides	49-58	peroxiredoxin 4	Homo sapiens	108-123
23949117-1	2013	The mammalian endoplasmic reticulum (ER) harbors disulfide bond-generating enzymes, including Ero1alpha and peroxiredoxin 4 (Prx4), and nearly 20 members of the protein disulfide isomerase family (PDIs), which together constitute a suitable environment for oxidative protein folding.	Disulfides	49-58	peroxiredoxin 4	Homo sapiens	125-129
28949004-6	2017	Here, we show that the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD against PDI-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 inhibition.	Disulfides	113-122	ADAM metallopeptidase domain 17	Homo sapiens	193-199
15844167-2	2005	We have identified the rtv gene, and using the new HHpred homology detection method, we show that the Rtv protein defines a new family of disulfide-rich proteins in insects that are related to vertebrate snake neurotoxin-like proteins, including CD59 and transforming growth factor-beta type II receptors.	Disulfides	138-147	retroactive	Drosophila melanogaster	102-105
15863837-4	2005	Previously, we reported that Angptl4 exists as variable-sized oligomers that contain intermolecular disulfide bonds.	Disulfides	100-109	angiopoietin like 4	Homo sapiens	29-36
28899838-6	2017	Therefore, we combined the 17-membered, internal disulfide ring portion of CNP with the C-terminal portion of ghrelin.	Disulfides	49-58	natriuretic peptide type C	Mus musculus	75-78
28925709-3	2017	Here, shell-sheddable micelles formed by a series of disulfide-linked copolymer poly(ethylene glycol)-b-poly(epsilon-caprolactone) (PEG-SS-PCL) containing the same chain length of PEG but different chain lengths of hydrophobic block PCL were prepared and well characterized.	Disulfides	53-62	PHD finger protein 1	Homo sapiens	139-142
23949117-3	2013	Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides.	Disulfides	168-177	peroxiredoxin 4	Homo sapiens	70-74
23949117-3	2013	Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides.	Disulfides	238-248	peroxiredoxin 4	Homo sapiens	70-74
23949117-4	2013	Remarkably, the Prx4-dependent formation of native disulfide bonds was accelerated when PDI was combined with ERp46 or P5, suggesting that PDIs work synergistically to increase the rate and fidelity of oxidative protein folding.	Disulfides	51-60	peroxiredoxin 4	Homo sapiens	16-20
15806144-7	2005	L- and S-endoglin isoforms can form disulfide-linked heterodimers, as demonstrated by cotransfection of L- and S-endoglin constructs.	Disulfides	36-45	endoglin	Mus musculus	7-17
23205738-0	2012	Contributions of a disulfide bond and a reduced cysteine side chain to the intrinsic activity of the high-density lipoprotein receptor SR-BI.	Disulfides	19-28	scavenger receptor class B member 1	Homo sapiens	135-140
23205738-3	2012	We used mass spectrometry to assign the two disulfide bonds in SR-BI that connect cysteines within the conserved Cys(321)-Pro(322)-Cys(323) (CPC) motif and connect Cys(280) to Cys(334).	Disulfides	44-53	scavenger receptor class B member 1	Homo sapiens	63-68
23169667-6	2012	Finally, PQLC2 transports a lysine-like mixed disulfide that serves as a chemical intermediate in cysteamine therapy of cystinosis, and PQLC2 gene silencing trapped this intermediate in cystinotic cells.	Disulfides	46-55	solute carrier family 66 member 1	Homo sapiens	9-14
29030641-3	2017	Disulfide bound complexes of lubricin and cartilage oligomeric matrix protein (COMP) have recently been identified in arthritic synovial fluid suggesting they may be lost from the cartilage surface in osteoarthritis and inflammatory arthritis.	Disulfides	0-9	cartilage oligomeric matrix protein	Homo sapiens	42-77
29030641-3	2017	Disulfide bound complexes of lubricin and cartilage oligomeric matrix protein (COMP) have recently been identified in arthritic synovial fluid suggesting they may be lost from the cartilage surface in osteoarthritis and inflammatory arthritis.	Disulfides	0-9	cartilage oligomeric matrix protein	Homo sapiens	79-83
28709872-1	2017	The insulin-like growth factor 1 receptor (IGF-1R) is a disulfide-linked heterotetramer containing two alpha-subunits and two beta-subunits.	Disulfides	56-65	insulin like growth factor 1 receptor	Homo sapiens	4-41
28709872-1	2017	The insulin-like growth factor 1 receptor (IGF-1R) is a disulfide-linked heterotetramer containing two alpha-subunits and two beta-subunits.	Disulfides	56-65	insulin like growth factor 1 receptor	Homo sapiens	43-49
16019431-2	2005	A combination of one, two and three native disulfide pair analogues of an active truncated (4-48) form of mEGF have been synthesised by replacing specific cysteine residues with isosteric a-amino-n-butyric acid (Abu).	Disulfides	43-52	epidermal growth factor	Mus musculus	106-110
23143686-5	2012	GPIbalpha complexed with GPIbbeta by disulfide bonding was expressed on GPIXW127X platelets and stable CHO-K1 cells lacking GPIX but expressing GPIbalpha and GPIbbeta.	Disulfides	37-46	glycoprotein Ib platelet subunit alpha	Homo sapiens	0-9
23143686-5	2012	GPIbalpha complexed with GPIbbeta by disulfide bonding was expressed on GPIXW127X platelets and stable CHO-K1 cells lacking GPIX but expressing GPIbalpha and GPIbbeta.	Disulfides	37-46	glycoprotein Ib platelet subunit alpha	Homo sapiens	144-153
16019431-4	2005	The contribution of individual, or pairs of, disulfide bonds to EGF structure was evaluated by CD and (1)H-NMR spectroscopy.	Disulfides	45-54	epidermal growth factor	Mus musculus	64-67
15909993-0	2005	Site-directed disulfide mapping of residues contributing to the Ca2+ and K+ binding pocket of the NCKX2 Na+/Ca2+-K+ exchanger.	Disulfides	14-23	solute carrier family 24 member 1	Homo sapiens	104-125
22992729-8	2012	Taken together, our results demonstrate that alpha-beta2 covalent association via a single, extracellular disulfide bond is required for beta2 targeting to specialized neuronal subcellular domains and for beta2 association with the neuronal cytoskeleton within those domains.	Disulfides	106-115	hemoglobin, beta adult minor chain	Mus musculus	137-142
28880078-0	2017	The Role of Disulfide Bond Replacements in Analogues of the Tarantula Toxin ProTx-II and Their Effects on Inhibition of the Voltage-Gated Sodium Ion Channel Nav1.7.	Disulfides	12-21	sodium voltage-gated channel alpha subunit 9	Homo sapiens	157-163
15909993-5	2005	Here we used site-directed disulfide mapping to report that the alpha repeats are found in close proximity in three-dimensional space, bringing together key functional NCKX residues, e.g., the two critical acidic residues, Glu188 and Asp548.	Disulfides	27-36	solute carrier family 24 member 1	Homo sapiens	168-172
28806750-6	2017	Based on its crystal structure, PHL forms a seven-bladed beta-propeller assembling into a homo-dimer with an inter-subunit disulfide bridge.	Disulfides	123-132	BCR activator of RhoGEF and GTPase	Homo sapiens	32-35
15909993-6	2005	Glu188Cys in the alpha1 repeat could form a disulfide cross-link with Asp548Cys in the alpha2 repeat.	Disulfides	44-53	adrenoceptor alpha 1D	Homo sapiens	17-23
15909993-7	2005	Surprisingly, cysteine substitutions of Ser185 in the alpha1 repeat could form disulfide cross-links with cysteine substitutions of three residues in the alpha2 repeat (Ser545, Asp548, and Ser552), thought to cover close to two full turns of an alpha helix, implying an area of increased flexibility.	Disulfides	79-88	adrenoceptor alpha 1D	Homo sapiens	54-60
15806300-1	2005	Thioredoxin (TRX), which is a stress-inducible protein with redox-active disulfide structures, has various biological activities by regulating DNA binding of transcription factors in cells.	Disulfides	73-82	thioredoxin	Homo sapiens	0-11
28740232-6	2017	The binding of Nt-Arg and synthetic ligands to ZZ domain facilitates disulfide bond-linked aggregation of p62 and p62 interaction with LC3, leading to the delivery of p62 and its cargoes to the autophagosome.	Disulfides	69-78	sequestosome 1	Homo sapiens	106-109
28740232-6	2017	The binding of Nt-Arg and synthetic ligands to ZZ domain facilitates disulfide bond-linked aggregation of p62 and p62 interaction with LC3, leading to the delivery of p62 and its cargoes to the autophagosome.	Disulfides	69-78	sequestosome 1	Homo sapiens	114-117
28740232-6	2017	The binding of Nt-Arg and synthetic ligands to ZZ domain facilitates disulfide bond-linked aggregation of p62 and p62 interaction with LC3, leading to the delivery of p62 and its cargoes to the autophagosome.	Disulfides	69-78	microtubule associated protein 1 light chain 3 alpha	Homo sapiens	135-138
28740232-6	2017	The binding of Nt-Arg and synthetic ligands to ZZ domain facilitates disulfide bond-linked aggregation of p62 and p62 interaction with LC3, leading to the delivery of p62 and its cargoes to the autophagosome.	Disulfides	69-78	sequestosome 1	Homo sapiens	114-117
22955273-7	2012	As the second-order reactant, reductant reduces the disulfide bond, most likely between Cys-250 and another cysteine residue of hAS3MT, and exposes the active site cysteine residues for binding trivalent inorganic arsenic (iAs(3+)) to give monomethylarsonic dicysteine (MADC(3+)).	Disulfides	52-61	arsenite methyltransferase	Homo sapiens	128-134
15806300-1	2005	Thioredoxin (TRX), which is a stress-inducible protein with redox-active disulfide structures, has various biological activities by regulating DNA binding of transcription factors in cells.	Disulfides	73-82	thioredoxin	Homo sapiens	13-16
22949505-5	2012	Here we reveal that, in contrast to other ubiquitin pathway E2 enzymes, Cdc34 is particularly sensitive to oxidative inactivation, through sequestration of the catalytic cysteine in a disulfide complex with Uba1, by levels of oxidant that do not reduce global ubiquitinylation of proteins.	Disulfides	184-193	SCF E2 ubiquitin-protein ligase catalytic subunit CDC34	Saccharomyces cerevisiae S288C	72-77
15713716-7	2005	These results demonstrate that the absence of the disulfide bridge Cys-53 to Cys-165 affects the binding affinity of GH for the GHR and subsequently the potency of GH to activate the Jak2/Stat5 signaling pathway.	Disulfides	50-59	signal transducer and activator of transcription 5A	Homo sapiens	188-193
15634676-0	2005	Contributions of disulfide bonds in a nested pattern to the structure, stability, and biological functions of endostatin.	Disulfides	17-26	collagen type XVIII alpha 1 chain	Homo sapiens	110-120
22842048-6	2012	These results suggest a model where the molecular interactions guiding the protein recognition between Mia40 and the disulfide-reduced CHCHD5 and CHCHD7 substrates occurs in vivo when the latter proteins are partially embedded in the protein import pore of the outer membrane of mitochondria.	Disulfides	117-126	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	103-108
22918950-2	2012	The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins.	Disulfides	4-13	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	150-155
22918950-2	2012	The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins.	Disulfides	80-89	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	135-140
22918950-2	2012	The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins.	Disulfides	80-89	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	150-155
22918950-8	2012	Thus Mia40 in cooperation with Erv1 promotes the formation of two disulfide bonds in the substrate protein, ensuring the efficiency of oxidative folding in the intermembrane space of mitochondria.	Disulfides	66-75	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	5-10
28458053-5	2017	Cysteine 53 of GP1, which forms a disulfide bond with GP2, was mutated to serine to avoid potential disulfide bond mispairing.	Disulfides	34-43	GTP binding protein 1	Homo sapiens	15-18
28458053-5	2017	Cysteine 53 of GP1, which forms a disulfide bond with GP2, was mutated to serine to avoid potential disulfide bond mispairing.	Disulfides	100-109	GTP binding protein 1	Homo sapiens	15-18
28658624-2	2017	NADPH-dependent reduction of thioredoxin-1 (Trx1) disulfide and glutathione disulfide by thioredoxin reductase-1 (TrxR1) and glutathione reductase (Gsr), respectively, fuels antioxidant systems and deoxyribonucleotide synthesis.	Disulfides	50-59	thioredoxin 1	Mus musculus	29-42
28658624-2	2017	NADPH-dependent reduction of thioredoxin-1 (Trx1) disulfide and glutathione disulfide by thioredoxin reductase-1 (TrxR1) and glutathione reductase (Gsr), respectively, fuels antioxidant systems and deoxyribonucleotide synthesis.	Disulfides	50-59	thioredoxin 1	Mus musculus	44-48
28658624-2	2017	NADPH-dependent reduction of thioredoxin-1 (Trx1) disulfide and glutathione disulfide by thioredoxin reductase-1 (TrxR1) and glutathione reductase (Gsr), respectively, fuels antioxidant systems and deoxyribonucleotide synthesis.	Disulfides	50-59	thioredoxin reductase 1	Mus musculus	89-112
28658624-2	2017	NADPH-dependent reduction of thioredoxin-1 (Trx1) disulfide and glutathione disulfide by thioredoxin reductase-1 (TrxR1) and glutathione reductase (Gsr), respectively, fuels antioxidant systems and deoxyribonucleotide synthesis.	Disulfides	50-59	thioredoxin reductase 1	Mus musculus	114-119
22684915-4	2012	Biochemical analyses further showed that mKLRG1 formed monomers and disulfide-linked dimers, trimers, and tetramers whereas hKLRG1 was exclusively present as disulfide-linked dimer.	Disulfides	158-167	killer cell lectin like receptor G1	Homo sapiens	124-130
15634676-8	2005	Our studies provide a structural basis for the two disulfide bonds on the biological functions of endostatin.	Disulfides	51-60	collagen type XVIII alpha 1 chain	Homo sapiens	98-108
28658624-6	2017	Also, Trx1 in the absence of TrxR1 provides a survival advantage to cells under hyperglycemic stress, suggesting that glutathione, likely via glutaredoxins, can reduce Trx1 disulfide in vivo.	Disulfides	173-182	thioredoxin 1	Mus musculus	6-10
28658624-6	2017	Also, Trx1 in the absence of TrxR1 provides a survival advantage to cells under hyperglycemic stress, suggesting that glutathione, likely via glutaredoxins, can reduce Trx1 disulfide in vivo.	Disulfides	173-182	thioredoxin 1	Mus musculus	168-172
22789714-1	2012	Thioredoxin domain-containing protein 12 (Txndc12) belongs to the thioredoxin superfamily, and has roles in redox regulation, defense against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors.	Disulfides	173-182	thioredoxin 1	Mus musculus	0-11
15766269-3	2005	This beta(2)m variant, DeltaK58-beta(2)m, is a disulfide-linked two-chain molecule consisting of amino acid residues 1-57 and 59-99 of intact beta(2)m, and we here demonstrate and characterize its decreased conformational stability as compared to wild-type (wt) beta(2)m.	Disulfides	47-56	beta-2-microglobulin	Homo sapiens	5-13
22789714-1	2012	Thioredoxin domain-containing protein 12 (Txndc12) belongs to the thioredoxin superfamily, and has roles in redox regulation, defense against oxidative stress, refolding of disulfide-containing proteins, and regulation of transcription factors.	Disulfides	173-182	thioredoxin 1	Mus musculus	66-77
22706041-2	2012	Cyclopeptide C*HSDGIC* (CHC), which results from the cyclization of PACAP (1-5) with disulfide, has been demonstrated to represent a potent agonist for the PACAP-specific receptor PAC1 which mediates the majority of PACAP"s effects.	Disulfides	85-94	adenylate cyclase activating polypeptide 1 receptor 1	Mus musculus	180-184
28438540-6	2017	This led us to obtain a new OTR-selective analog by comprehensive amino acid substitutions of OT and replacement of the disulfide bond.	Disulfides	120-129	oxytocin/neurophysin I prepropeptide	Homo sapiens	28-30
15766269-3	2005	This beta(2)m variant, DeltaK58-beta(2)m, is a disulfide-linked two-chain molecule consisting of amino acid residues 1-57 and 59-99 of intact beta(2)m, and we here demonstrate and characterize its decreased conformational stability as compared to wild-type (wt) beta(2)m.	Disulfides	47-56	beta-2-microglobulin	Homo sapiens	32-40
28224255-1	2017	Bovine lens aldose reductase is susceptible to a copper-mediated oxidation, leading to the generation of a disulfide bridge with the concomitant incorporation of two equivalents of the metal and inactivation of the enzyme.	Disulfides	107-116	aldose reductase	Bos taurus	12-28
15766269-3	2005	This beta(2)m variant, DeltaK58-beta(2)m, is a disulfide-linked two-chain molecule consisting of amino acid residues 1-57 and 59-99 of intact beta(2)m, and we here demonstrate and characterize its decreased conformational stability as compared to wild-type (wt) beta(2)m.	Disulfides	47-56	beta-2-microglobulin	Homo sapiens	32-40
15766269-3	2005	This beta(2)m variant, DeltaK58-beta(2)m, is a disulfide-linked two-chain molecule consisting of amino acid residues 1-57 and 59-99 of intact beta(2)m, and we here demonstrate and characterize its decreased conformational stability as compared to wild-type (wt) beta(2)m.	Disulfides	47-56	beta-2-microglobulin	Homo sapiens	32-40
15772339-0	2005	The disulfide isomerase Grp58 is a protective factor against prion neurotoxicity.	Disulfides	4-13	protein disulfide isomerase associated 3	Mus musculus	24-29
28363871-0	2017	Impact of antibody subclass and disulfide isoform differences on the biological activity of CD200R and betaklotho agonist antibodies.	Disulfides	32-41	klotho beta	Homo sapiens	103-113
22542816-1	2012	We attempted to generate a physicochemically stable cholera toxin B subunit (CTB) by de novo-introduction of intersubunit disulfide bonds between adjacent subunits.	Disulfides	122-131	phosphate cytidylyltransferase 1, choline, beta isoform	Mus musculus	77-80
22542816-4	2012	However, when the mutant CTB was heat-treated in the presence of a reducing agent, the thermostable phenotype was abolished, indicating the observed phenotype is due to the introduction of intersubunit disulfide bonds.	Disulfides	202-211	phosphate cytidylyltransferase 1, choline, beta isoform	Mus musculus	25-28
15762561-1	2005	A novel disulfide, which carried two pepstatin fragments at both ends, was prepared by the coupling of 11,11"-dithiobisundecanoic acid (DTUA) with a fragment (Val-Val-Sta) carrying a n-hexyl end (Pepsta(h)).	Disulfides	8-17	GCY	Homo sapiens	167-170
22514092-4	2012	The reversal of ZmC(4)-NADP-ME oxidation by chemical reductants suggests the presence of thiol groups able to form disulfide bonds.	Disulfides	115-124	NADP-dependent malic enzyme, chloroplastic	Zea mays	23-30
22582951-1	2012	This work explores the substrate specificity of the quiescin sulfhydryl oxidase (QSOX) family of disulfide-generating flavoenzymes to provide enzymological context for investigation of the physiological roles of these facile catalysts of oxidative protein folding.	Disulfides	97-106	quiescin sulfhydryl oxidase 1	Homo sapiens	52-79
22582951-1	2012	This work explores the substrate specificity of the quiescin sulfhydryl oxidase (QSOX) family of disulfide-generating flavoenzymes to provide enzymological context for investigation of the physiological roles of these facile catalysts of oxidative protein folding.	Disulfides	97-106	quiescin sulfhydryl oxidase 1	Homo sapiens	81-85
22582951-2	2012	QSOX enzymes are generally unable to form disulfide bonds within well-structured proteins.	Disulfides	42-51	quiescin sulfhydryl oxidase 1	Homo sapiens	0-4
22582951-4	2012	Fusion of Ubc4" with the more stable glutathione-S-transferase domain demonstrates that QSOX can selectively introduce disulfides into the less stable domain of the fusion protein.	Disulfides	119-129	quiescin sulfhydryl oxidase 1	Homo sapiens	88-92
28370139-5	2017	The present work describes two novel human G6PDH mutants, one that creates four disulfide bonds among apposing dimers, resulting in a "cross-linked" tetramer, and another that prevents the dimer to dimer association.	Disulfides	80-89	glucose-6-phosphate dehydrogenase	Homo sapiens	43-48
22582951-7	2012	Steady- and pre-steady-state kinetic experiments, combined with static fluorescence approaches, indicate that while QSOX is an efficient catalyst for disulfide bond formation between mobile elements of structure, it does not appear to have a significant binding site for unfolded proteins.	Disulfides	150-159	quiescin sulfhydryl oxidase 1	Homo sapiens	116-120
15546886-2	2005	This 21-amino acid peptide has 8 cysteines engaged in 4 disulfide bonds and is very similar to human hepcidin, an antimicrobial peptide with iron regulatory properties.	Disulfides	56-65	hepcidin antimicrobial peptide	Homo sapiens	101-109
22582951-8	2012	These aspects of protein substrate discrimination by QSOX family members are rationalized in terms of the stringent steric requirements for disulfide exchange reactions.	Disulfides	140-149	quiescin sulfhydryl oxidase 1	Homo sapiens	53-57
28083716-3	2017	Impairment in Disulfide bond A-like protein (DsbA-L) is associated with low adiponectin levels and diabetes.	Disulfides	14-23	adiponectin, C1Q and collagen domain containing	Rattus norvegicus	76-87
28275193-3	2017	We previously identified a disulfide bond, I201C-A433C (DS), which stabilizes Env in the vaccine-desired prefusion-closed state.	Disulfides	27-36	endogenous retrovirus group K member 20	Homo sapiens	78-81
15546886-4	2005	Its structure is very similar to that of human hepcidin, including the presence of an antiparallel beta-sheet, a conserved disulfide-bonding pattern, and a rare vicinal disulfide bond.	Disulfides	123-132	hepcidin antimicrobial peptide	Homo sapiens	47-55
28374821-3	2017	We found that the N-terminal caspase-like domain of Gpi8 forms a disulfide-linked dimer, which is strengthened by N-glycosylation.	Disulfides	65-74	GPI-anchor transamidase	Saccharomyces cerevisiae S288C	52-56
28374821-5	2017	In contrast to the previously reported disulfide linkage between Gpi8 and Gpi16 in human and trypanosome GPIT, our data show that the luminal domains of S. cerevisiae Gpi8 and S. cerevisiae Gpi16 do not interact directly, nor do they form a disulfide bond in the intact S. cerevisiae GPIT.	Disulfides	39-48	phosphatidylinositol glycan anchor biosynthesis class K	Homo sapiens	65-69
28374821-5	2017	In contrast to the previously reported disulfide linkage between Gpi8 and Gpi16 in human and trypanosome GPIT, our data show that the luminal domains of S. cerevisiae Gpi8 and S. cerevisiae Gpi16 do not interact directly, nor do they form a disulfide bond in the intact S. cerevisiae GPIT.	Disulfides	241-250	GPI-anchor transamidase	Saccharomyces cerevisiae S288C	167-171
22416136-3	2012	This leads to formation of a relatively stable complex of Cosmc and denatured T-synthase accompanied by formation of reactivated enzyme in an ATP-independent fashion that is not regulated by redox, calcium, pH, or intermolecular disulfide bond formation.	Disulfides	229-238	C1GALT1 specific chaperone 1	Homo sapiens	58-63
22296668-3	2012	The C-terminal FAD-binding domain of Erv1/ALR has an essential role in the import process by creating a transient  intermolecular disulfide bond with Mia40.	Disulfides	130-139	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	150-155
22296668-4	2012	The action of Mia40 is selective for the formation of both intra and intersubunit structural disulfide bonds of Erv1/ALR, but the complete maturation process requires additional binding of FAD.	Disulfides	93-102	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	14-19
15546886-4	2005	Its structure is very similar to that of human hepcidin, including the presence of an antiparallel beta-sheet, a conserved disulfide-bonding pattern, and a rare vicinal disulfide bond.	Disulfides	169-178	hepcidin antimicrobial peptide	Homo sapiens	47-55
15698950-11	2005	Following a differential peptide mass fingerprint approach by reflector mode MALDI-TOFMS, the disulfide patterns of these circulating restins were determined as Cys1-Cys4 and Cys2-Cys3.	Disulfides	94-103	cystin 1	Homo sapiens	161-165
28368308-6	2017	As characterizing the native heterodimer is challenging due to interference from monomers and homodimers, we engineered a "trapped" disulfide-linked CXCL7-CXCL1 heterodimer.	Disulfides	132-141	C-X-C motif chemokine ligand 1	Homo sapiens	155-160
28093500-0	2017	Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER.	Disulfides	58-67	thioredoxin reductase 1	Homo sapiens	10-33
28093500-4	2017	Here, we use a novel assay to demonstrate that the reduction in non-native disulfides requires NADPH as the ultimate electron donor, and a robust cytosolic thioredoxin system, driven by thioredoxin reductase 1 (TrxR1 or TXNRD1).	Disulfides	75-85	thioredoxin reductase 1	Homo sapiens	186-209
28093500-4	2017	Here, we use a novel assay to demonstrate that the reduction in non-native disulfides requires NADPH as the ultimate electron donor, and a robust cytosolic thioredoxin system, driven by thioredoxin reductase 1 (TrxR1 or TXNRD1).	Disulfides	75-85	thioredoxin reductase 1	Homo sapiens	211-216
28093500-4	2017	Here, we use a novel assay to demonstrate that the reduction in non-native disulfides requires NADPH as the ultimate electron donor, and a robust cytosolic thioredoxin system, driven by thioredoxin reductase 1 (TrxR1 or TXNRD1).	Disulfides	75-85	thioredoxin reductase 1	Homo sapiens	220-226
22505424-1	2012	Protein disulfide isomerase (PDI) is a multifunctional protein that catalyzes the formation of a disulfide bond in nascent and misfolded proteins and is also known to bind to the thyroid hormone triiodothyronine (T3).	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	29-32
15709754-0	2005	Agonist-induced conformational changes in thyrotropin-releasing hormone receptor type I: disulfide cross-linking and molecular modeling approaches.	Disulfides	89-98	thyrotropin releasing hormone receptor	Homo sapiens	42-80
15345746-11	2004	A Fab fragment of anti-GHR(ext-mAb) inhibited GH-induced GHR disulfide linkage and signaling, as well as phorbol ester-induced GHR proteolysis, in a fashion similar to the intact antibody.	Disulfides	61-70	FA complementation group B	Homo sapiens	2-5
22324914-5	2012	This observation in combination with the above findings indicated that human RNase kappa does not form homodimers through disulfide bridges, and cysteine residues are not implicated in RNA catalysis but participate in the formation of intramolecular disulfide bond(s) essential for its ribonucleolytic activity.	Disulfides	250-259	ribonuclease K	Homo sapiens	77-88
22105604-3	2012	HMGB1 contains three conserved redox-sensitive cysteine residues: C23 and C45 can form an intramolecular disulfide bond, whereas C106 is unpaired and is essential for the interaction with Toll-Like Receptor (TLR) 4.	Disulfides	105-114	nucleolin	Mus musculus	66-69
22105604-5	2012	Using tandem mass spectrometric analysis, we now have established that the C106 thiol and the C23-C45 disulfide bond are required for HMGB1 to induce nuclear NF-kappaB translocation and tumor necrosis factor (TNF) production in macrophages.	Disulfides	102-111	nucleolin	Mus musculus	94-97
28198441-2	2017	Protein disulfide isomerases (PDI), an endoplasmic reticulum (ER) chaperone, plays a crucial role in catalyzing disulfide bond formation, reduction, and isomerization.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	30-33
28198441-9	2017	These findings provide mechanistic insight into sulfhydration of disulfide bonds on NMDAR by PDI, and suggest that PDI may represent a target of potential therapeutics for epilepsy, which avoids a possible side effect on physiological receptor functionality.	Disulfides	65-74	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	93-96
28198441-9	2017	These findings provide mechanistic insight into sulfhydration of disulfide bonds on NMDAR by PDI, and suggest that PDI may represent a target of potential therapeutics for epilepsy, which avoids a possible side effect on physiological receptor functionality.	Disulfides	65-74	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	115-118
28003361-3	2017	Structural and biochemical analysis has led to the hypothesis that extracellular TG2 activation involves reduction of an allosteric disulfide bond by thioredoxin-1 (TRX), but cellular and in vivo evidence for this proposal is lacking.	Disulfides	132-141	thioredoxin 1	Mus musculus	150-163
22201216-4	2012	PDI is an isomerase enzyme in the endoplasmic reticulum and facilitates the formation or cleavage of disulfide bonds.	Disulfides	101-110	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	0-3
15313215-6	2004	Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain.	Disulfides	109-118	thioredoxin	Homo sapiens	78-83
21838701-0	2012	Synthesis and biological activity of mouse hepcidin peptide analogs containing three disulfide bridges: manual and microwave-assisted solid-phase peptide synthesis.	Disulfides	85-94	hepcidin antimicrobial peptide	Mus musculus	43-51
21838701-1	2012	Hepcidin, a 25 amino acid peptide hormone containing a complex network of four disulfide bonds is the hormone regulator of iron homeostasis.	Disulfides	79-88	hepcidin antimicrobial peptide	Mus musculus	0-8
28003361-3	2017	Structural and biochemical analysis has led to the hypothesis that extracellular TG2 activation involves reduction of an allosteric disulfide bond by thioredoxin-1 (TRX), but cellular and in vivo evidence for this proposal is lacking.	Disulfides	132-141	thioredoxin 1	Mus musculus	165-168
28003361-5	2017	By using the C35S mutant of TRX, which formed a metastable mixed disulfide bond with TG2, we demonstrated that these proteins specifically recognized each other in the extracellular matrix of fibroblasts.	Disulfides	65-74	thioredoxin 1	Mus musculus	28-31
27920204-9	2017	Homology-based structural modeling predicted a cysteine residue (Cys-298) in position to form a disulfide bridge between two Siglec-E polypeptides.	Disulfides	96-105	sialic acid binding Ig-like lectin E	Mus musculus	125-133
27869268-1	2016	A novel amphiphilic camptothecin prodrug, CPT-ss-Ir, consisting of CPT, Ir and a disulfide bond linker, was synthesized, and it could self-assemble into nanowires in aqueous solution.	Disulfides	81-90	choline phosphotransferase 1	Homo sapiens	42-45
15313215-6	2004	Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain.	Disulfides	109-118	phosphatase and tensin homolog	Homo sapiens	87-91
15313215-6	2004	Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain.	Disulfides	109-118	thioredoxin	Homo sapiens	159-164
15313215-6	2004	Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain.	Disulfides	109-118	phosphatase and tensin homolog	Homo sapiens	198-202
27879205-4	2016	The active site of POMK is established by residues located in non-canonical positions and is stabilized by a disulfide bridge.	Disulfides	109-118	protein O-mannose kinase	Homo sapiens	19-23
15313215-6	2004	Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain.	Disulfides	109-118	thioredoxin	Homo sapiens	159-164
22570527-1	2012	Agouti-related protein (AgRP) is a 4-kDa cystine-knot peptide of human origin with four disulfide bonds and four solvent-exposed loops.	Disulfides	88-97	agouti related neuropeptide	Homo sapiens	0-22
22570527-1	2012	Agouti-related protein (AgRP) is a 4-kDa cystine-knot peptide of human origin with four disulfide bonds and four solvent-exposed loops.	Disulfides	88-97	agouti related neuropeptide	Homo sapiens	24-28
15313215-6	2004	Molecular docking and site-specific mutation studies show that the binding of Trx-1 to PTEN occurs through a disulfide bond between the active site Cys(32) of Trx-1 and Cys(212) of the C2 domain of PTEN leading to steric interference by bound Trx-1 of the catalytic site of PTEN and of the C2 lipid membrane-binding domain.	Disulfides	109-118	phosphatase and tensin homolog	Homo sapiens	198-202
15252023-4	2004	A structure-based sequence alignment was performed that predicts that domain 5 contains the four conserved key residues (Gln, Arg, Glu, and Tyr) identified as essential for carbohydrate recognition by the CD-MPR and domains 3 and 9 of the CI-MPR, but lacks two cysteine residues predicted to form a disulfide bond within the binding pocket.	Disulfides	299-308	mannose-6-phosphate receptor, cation dependent	Homo sapiens	205-211
22327429-4	2012	All CD16 binding modules are disulfide-stabilized (ds).	Disulfides	29-38	Fc gamma receptor IIIa	Homo sapiens	4-8
15252023-4	2004	A structure-based sequence alignment was performed that predicts that domain 5 contains the four conserved key residues (Gln, Arg, Glu, and Tyr) identified as essential for carbohydrate recognition by the CD-MPR and domains 3 and 9 of the CI-MPR, but lacks two cysteine residues predicted to form a disulfide bond within the binding pocket.	Disulfides	299-308	insulin like growth factor 2 receptor	Homo sapiens	239-245
15358557-5	2004	We show that it is structured in solution, as suggested by circular dichroism and NMR spectroscopy, and displays an EGF-like disulfide bond topology, as determined by disulfide mapping.	Disulfides	125-134	epidermal growth factor	Homo sapiens	116-119
22916297-5	2012	We sequenced and recombinantly expressed two ~25 kDa polypeptides (BgAChBP1 and BgAChBP2) with a specific active site, N-glycan site and disulfide bridge variation.	Disulfides	137-146	acetylcholine-binding protein-like	Biomphalaria glabrata	80-88
22916297-7	2012	Recombinant BgAChBP1 formed pentamers and dodecahedra, recombinant BgAChBP2 formed pentamers and probably disulfide-bridged di-pentamers, but not dodecahedra.	Disulfides	106-115	acetylcholine-binding protein-like	Biomphalaria glabrata	67-75
15358557-5	2004	We show that it is structured in solution, as suggested by circular dichroism and NMR spectroscopy, and displays an EGF-like disulfide bond topology, as determined by disulfide mapping.	Disulfides	167-176	epidermal growth factor	Homo sapiens	116-119
15341514-0	2004	Molecular aging of tau: disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo.	Disulfides	24-33	microtubule associated protein tau	Homo sapiens	19-22
22927815-7	2012	YLDV-IL18BP forms a disulfide bonded homo-dimer engaging IL18 in a 2:2 stoichiometry, in contrast to the 1:1 complex of ectromelia virus (ECTV) IL18BP and IL18.	Disulfides	20-29	interleukin 18	Homo sapiens	5-9
15341729-4	2004	The redox potential of this disulfide bond is -251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins.	Disulfides	28-37	thioredoxin	Homo sapiens	103-114
15341729-4	2004	The redox potential of this disulfide bond is -251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins.	Disulfides	83-93	thioredoxin	Homo sapiens	103-114
15237985-1	2004	Heterodisulfide reductase (Hdr) from methanogenic archea is an iron-sulfur protein that catalyzes the reversible two-electron reduction of the mixed disulfide CoM-S-S-CoB to the thiol coenzymes, coenzyme M (CoM-SH) and coenzyme B (CoB-SH).	Disulfides	6-15	metabolism of cobalamin associated B	Homo sapiens	167-170
21994946-0	2011	Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle.	Disulfides	113-122	peroxiredoxin 4	Homo sapiens	45-61
21994946-4	2011	We show that PrxIV has a similar structure to other typical 2-Cys peroxiredoxins and undergoes a conformational change from a fully folded to a locally unfolded form following the formation of a disulfide between the peroxidatic and resolving cysteine residues.	Disulfides	195-204	peroxiredoxin 4	Homo sapiens	13-18
22069028-1	2011	Quiescin sulfhydryl oxidases (QSOXs) catalyze the formation of disulfide bonds in peptides and proteins, and in vertebrates comprise two proteins: QSOX1 and QSOX2.	Disulfides	63-72	quiescin sulfhydryl oxidase 1	Homo sapiens	147-152
15233797-3	2004	The NMR structure-based model reveals the structural features of the eLPs, in which the second extracellular loop (eLP(2)) and the disulfide bond between the first extracellular loop (eLP(1)) and eLP(2) play a major role in forming the ligand recognition pocket.	Disulfides	131-140	KDEL endoplasmic reticulum protein retention receptor 2	Homo sapiens	184-190
22099303-5	2011	Such VEGFR2 inactivation is due to the formation of intramolecular disulfide linkage between Cys1199 and Cys1206 in the C-terminal tail.	Disulfides	67-76	kinase insert domain receptor	Homo sapiens	5-11
15140129-0	2004	Mutations in the shutter region of antithrombin result in formation of disulfide-linked dimers and severe venous thrombosis.	Disulfides	71-80	serpin family C member 1	Homo sapiens	35-47
21835919-2	2011	In the case of Prx I-III, the disulfide is reduced by thioredoxin, thus enabling these proteins to function as peroxidases.	Disulfides	30-39	thioredoxin 1	Mus musculus	54-65
21862690-5	2011	Protein sequence comparison among zebrafish GPR81s, mammalian GPR81s, GPR109a, and GPR109b identified a common structure (six Cys residues at the extracellular domains that potentially form three disulfide bonds) in this subfamily of receptors.	Disulfides	196-205	hydroxycarboxylic acid receptor 1	Homo sapiens	44-49
21865601-3	2011	Its import into the IMS depends on the Mia40/Erv1 disulfide relay system, although Ccs1 is, in contrast to typical substrates, a multidomain protein and lacks twin Cx(n)C motifs.	Disulfides	50-59	Mia40p	Saccharomyces cerevisiae S288C	39-44
21865601-7	2011	Furthermore, C64 of Ccs1 is required for formation of a Ccs1 disulfide intermediate with Mia40.	Disulfides	61-70	Mia40p	Saccharomyces cerevisiae S288C	89-94
15140129-11	2004	The abnormal antithrombin purified from P80S carriers is an inactive disulfide-linked dimer of mutant antithrombin whose properties are consistent with head-to-head insertion of the reactive loop.	Disulfides	69-78	serpin family C member 1	Homo sapiens	13-25
15140129-11	2004	The abnormal antithrombin purified from P80S carriers is an inactive disulfide-linked dimer of mutant antithrombin whose properties are consistent with head-to-head insertion of the reactive loop.	Disulfides	69-78	serpin family C member 1	Homo sapiens	102-114
15246937-4	2004	Assuming the characteristic intramolecular disulfide bonds remain intact, an HLA class II binding motif can be modelled for HNP-1 and -2.	Disulfides	43-52	HNP1	Homo sapiens	124-136
21865601-8	2011	We conclude that the Mia40/Erv1 disulfide relay system introduces a structural disulfide bond in Ccs1 between the cysteine residues C27 and C64, thereby promoting mitochondrial import of this unconventional substrate.	Disulfides	32-41	Mia40p	Saccharomyces cerevisiae S288C	21-26
21865601-8	2011	We conclude that the Mia40/Erv1 disulfide relay system introduces a structural disulfide bond in Ccs1 between the cysteine residues C27 and C64, thereby promoting mitochondrial import of this unconventional substrate.	Disulfides	79-88	Mia40p	Saccharomyces cerevisiae S288C	21-26
15118998-1	2004	Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.	Disulfides	186-195	peroxiredoxin 5	Homo sapiens	0-21
21816817-0	2011	Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective.	Disulfides	36-45	cytochrome c oxidase copper chaperone COX17	Homo sapiens	61-66
21816817-3	2011	Here, the structures and the backbone mobilities of two Cox17 mutated forms with only one interhelical disulfide bond have been analyzed.	Disulfides	103-112	cytochrome c oxidase copper chaperone COX17	Homo sapiens	56-61
21816817-4	2011	It appears that the inner disulfide bond (formed by Cys-36 and Cys-45) stabilizes interhelical hydrophobic interactions, providing a structure with essentially the same structural dynamic properties of the mature Cox17 state.	Disulfides	26-35	cytochrome c oxidase copper chaperone COX17	Homo sapiens	213-218
15118998-1	2004	Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.	Disulfides	186-195	peroxiredoxin 5	Homo sapiens	23-27
15118998-1	2004	Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.	Disulfides	186-195	thioredoxin	Homo sapiens	49-60
21757736-4	2011	Among several possible disulfide bonds regulating ERO1alpha activity, Cys(94)-Cys(131) and Cys(99)-Cys(104) disulfide bonds are dominant regulators by excluding the involvement of the Cys(85)-Cys(391) disulfide in the regulation.	Disulfides	23-32	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	50-59
15118998-1	2004	Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.	Disulfides	186-195	thioredoxin	Homo sapiens	79-90
21757736-4	2011	Among several possible disulfide bonds regulating ERO1alpha activity, Cys(94)-Cys(131) and Cys(99)-Cys(104) disulfide bonds are dominant regulators by excluding the involvement of the Cys(85)-Cys(391) disulfide in the regulation.	Disulfides	108-117	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	50-59
21757736-4	2011	Among several possible disulfide bonds regulating ERO1alpha activity, Cys(94)-Cys(131) and Cys(99)-Cys(104) disulfide bonds are dominant regulators by excluding the involvement of the Cys(85)-Cys(391) disulfide in the regulation.	Disulfides	108-117	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	50-59
15118998-1	2004	Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.	Disulfides	186-195	thioredoxin	Homo sapiens	23-26
15118998-1	2004	Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.	Disulfides	186-195	thioredoxin	Homo sapiens	92-95
14747474-5	2004	Intriguingly, disulfide-bonded dimers of autoprocessed caspase-9 were generated in the mitochondria in the pre-apoptotic phase.	Disulfides	14-23	caspase 9	Homo sapiens	55-64
21778060-4	2011	It has recently been shown that peroxiredoxin 4 is involved in peroxide removal and disulfide formation.	Disulfides	84-93	peroxiredoxin 4	Homo sapiens	32-47
15046979-2	2004	Mammalian peroxiredoxin 5 has been recently classified as an atypical 2-Cys peroxiredoxin due to the presence of a conserved peroxidatic N-terminal cysteine (Cys47) and an unconserved resolving C-terminal cysteine residue (Cys151) forming an intramolecular disulfide intermediate in the oxidized enzyme.	Disulfides	257-266	peroxiredoxin 5	Homo sapiens	10-25
21631113-3	2011	LTP1 modifications analyzed by MS/MS revealed acylation, glycation, and disulfide bond breakage in both LH and HH malts.	Disulfides	72-81	non-specific lipid transport protein 1	Hordeum vulgare	0-4
14715928-4	2004	These mutations constitutively activate RET due to aberrant disulfide homodimerization and diminish the level of RET at the plasma membrane.	Disulfides	60-69	ret proto-oncogene	Homo sapiens	40-43
21525429-2	2011	Our data showed that disulfide bond formation mediated by Cys242 is critical for MG53-mediated translocation of intracellular vesicles toward the injury sites.	Disulfides	21-30	tripartite motif containing 72	Homo sapiens	81-85
14998722-10	2004	These results suggest that thiol antioxidant and reducing agents attenuate the expression of HO-1 induced by 15d-PGJ(2), and that the cellular thiol-disulfide redox status may be linked to HO-1 activation.	Disulfides	149-158	heme oxygenase 1	Homo sapiens	93-97
21600946-0	2011	Disulfide bond prolongs the half-life of therapeutic peptide-GLP-1.	Disulfides	0-9	glucagon	Rattus norvegicus	61-66
21600946-4	2011	In this study, we developed a cluster of GLP-1 homodimeric analogs, which fused the mutated GLP-1 monomer by an intra-disulfide bridge.	Disulfides	118-127	glucagon	Rattus norvegicus	41-46
21600946-4	2011	In this study, we developed a cluster of GLP-1 homodimeric analogs, which fused the mutated GLP-1 monomer by an intra-disulfide bridge.	Disulfides	118-127	glucagon	Rattus norvegicus	92-97
21689404-4	2011	We have previously stabilized soluble trimeric mimics of Env by introducing a disulfide bond between gp120 and gp41 and adding a trimer stabilizing mutation in gp41 (SOSIP.R6 gp140).	Disulfides	78-87	endogenous retrovirus group K member 20	Homo sapiens	57-60
14998722-10	2004	These results suggest that thiol antioxidant and reducing agents attenuate the expression of HO-1 induced by 15d-PGJ(2), and that the cellular thiol-disulfide redox status may be linked to HO-1 activation.	Disulfides	149-158	heme oxygenase 1	Homo sapiens	189-193
14697240-5	2004	Interestingly, dimerization of resistin appears to be mediated by both covalent (disulfide bond mediated) and non-covalent interactions as seen on reducing and non-reducing SDS-PAGE.	Disulfides	81-90	resistin	Homo sapiens	31-39
14704269-6	2004	The pattern of accessibility in E2 is consistent with a structure similar to that of bovine rhodopsin, in which the region C-terminal to the conserved disulfide bond is deeper in the binding-site crevice than is the N-terminal part of E2.	Disulfides	151-160	rhodopsin	Bos taurus	92-101
20354739-7	2011	It is concluded that redox-regulated PBGS activation via cleavage of disulfide bonds among Cys(122), Cys(124), and Cys(132) and coordination with zinc ion is closely linked to change in the oligomeric state.	Disulfides	69-78	aminolevulinate dehydratase	Homo sapiens	37-41
16328790-5	2004	Thioredoxins in turn reduce regulatory disulfides of various target enzymes.	Disulfides	39-49	thioredoxin	Homo sapiens	0-12
21525384-6	2011	Also, although the cAb H3 is much longer than classical H3 loops, it often contains common structural motifs and sometimes a disulfide bond to the H1.	Disulfides	125-134	neural proliferation, differentiation and control 1	Homo sapiens	19-22
16328791-0	2004	Ferredoxin:thioredoxin Reductase: Disulfide Reduction Catalyzed via Novel Site-specific [4Fe-4S] Cluster Chemistry.	Disulfides	34-43	peroxiredoxin 5	Homo sapiens	11-32
16328791-1	2004	Thioredoxin-mediated light regulation in plant chloroplasts involves a unique class of disulfide reductases that catalyze disulfide reduction in two one-electron steps using a [2Fe-2S] ferredoxin as the electron donor and an active site comprising a [4Fe-4S] cluster and a redox-active disulfide.	Disulfides	87-96	thioredoxin	Homo sapiens	0-11
16328791-1	2004	Thioredoxin-mediated light regulation in plant chloroplasts involves a unique class of disulfide reductases that catalyze disulfide reduction in two one-electron steps using a [2Fe-2S] ferredoxin as the electron donor and an active site comprising a [4Fe-4S] cluster and a redox-active disulfide.	Disulfides	122-131	thioredoxin	Homo sapiens	0-11
21524584-5	2011	A combination of both techniques yielded peptides with disulfide bonds, such as octreotide and polyphemusin II-derived CXCR4 antagonists.	Disulfides	55-64	C-X-C motif chemokine receptor 4	Homo sapiens	119-124
14657342-7	2003	NAC pretreatment augmented integrin alpha-4-dependent fibronectin adhesion and aggregation of Jurkat cells without changing its expression by fluorescence-activated cell sorter, suggesting that reduction of surface disulfides can affect proteins function.	Disulfides	215-225	integrin subunit alpha 4	Homo sapiens	27-43
21377473-4	2011	We identified two previously undocumented disulfide bridges in the crystal structure of properly folded S100A3: one disulfide bridge is between Cys30 in the N-terminal pseudo-EF-hand and Cys68 in the C-terminal EF-hand (SS1), and another disulfide bridge attaches Cys99 in the C-terminal coil structure to Cys81 in helix IV (SS2).	Disulfides	42-51	butyrophilin like 2	Homo sapiens	325-328
21521879-3	2011	Sema3A stimulation generated hydrogen peroxide (H2O2) through MICAL (molecule interacting with CasL) and oxidized CRMP2, enabling it to form a disulfide-linked homodimer through cysteine-504.	Disulfides	143-152	microtubule associated monooxygenase, calponin and LIM domain containing 1	Homo sapiens	62-67
21425467-5	2011	Using alkyne-azide click chemistry, PEG(Alk)/PMA multilayers are crosslinked with a bisazide linker that contains a disulfide bond, rendering these films and capsules redox-responsive.	Disulfides	116-125	ALK receptor tyrosine kinase	Homo sapiens	40-43
14645556-6	2003	The GP(2b), GP(3), and GP(4) proteins occur as a heterotrimeric complex in which disulfide bonds play an important role.	Disulfides	81-90	CD36 molecule	Homo sapiens	23-28
14528315-3	2003	LAP provides for a disulfide-linked shell hindering interaction of the cytokine with its cellular receptors, conferring a very long half-life of 55 h in vivo.	Disulfides	19-28	LAP	Homo sapiens	0-3
21430264-2	2011	Here, we apply a site-directed technology, disulfide trapping, to interrogate structurally and functionally how an allosteric site on the Ser/Thr kinase, 3-phosphoinositide-dependent kinase 1 (PDK1)--the PDK1-interacting-fragment (PIF) pocket--is engaged by an activating peptide motif on downstream substrate kinases (PIFtides) and by small molecule fragments.	Disulfides	43-52	pyruvate dehydrogenase kinase 1	Homo sapiens	204-208
21430264-4	2011	We also discovered a variety of small molecule fragment disulfides (&lt; 300 Da) that could either activate or inhibit PDK1 by conjugation to the PIF pocket, thus displaying greater functional diversity than is displayed by PIFtides conjugated to the same sites.	Disulfides	56-66	pyruvate dehydrogenase kinase 1	Homo sapiens	119-123
20537978-4	2011	Mia40 is maintained in an oxidized, active conformation by the sulfhydryl oxidase Erv1, a homodimeric flavoenzyme, which can form disulfide bonds de novo.	Disulfides	130-139	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
14528315-4	2003	Mutations of the disulfide bonds in LAP abolish this latency.	Disulfides	17-26	LAP	Homo sapiens	36-39
21215271-6	2011	Hence, GPx7 and GPx8 may represent a novel route for the productive use of peroxide produced by Ero1alpha during disulfide bond formation.	Disulfides	113-122	glutathione peroxidase 8 (putative)	Homo sapiens	16-20
12923196-4	2003	We found that the gp120-gp41 association function of the disulfide-bonded region is conserved.	Disulfides	57-66	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	18-23
21215271-6	2011	Hence, GPx7 and GPx8 may represent a novel route for the productive use of peroxide produced by Ero1alpha during disulfide bond formation.	Disulfides	113-122	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	96-105
14556853-2	2003	Activation by H2O2 involves Yap1 Cys303-Cys598 intra-molecular disulfide bond formation directed by the H2O2 sensor Orp1/Gpx3.	Disulfides	63-72	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	116-120
21084286-5	2011	The 1.6-A crystal structure of the complete mouse BST-2 ectodomain reveals an ~145-A parallel dimer in an extended alpha-helix conformation that predominantly forms a coiled coil bridged by three intermolecular disulfides that are required for stability.	Disulfides	211-221	bone marrow stromal cell antigen 2	Mus musculus	50-55
14556853-2	2003	Activation by H2O2 involves Yap1 Cys303-Cys598 intra-molecular disulfide bond formation directed by the H2O2 sensor Orp1/Gpx3.	Disulfides	63-72	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	121-125
14555493-6	2003	Substitution of the Aga1p GPI signal domain with those of other GPI-anchored proteins, a single transmembrane domain, or a cysteine capable of forming a disulfide all produced functional adhesins.	Disulfides	153-162	Aga1p	Saccharomyces cerevisiae S288C	20-25
21133413-7	2011	The truncated (-5)IDH1/IDH2 and tetrameric enzymes were much more sensitive than the wild-type enzyme to inhibition by the oxidant diamide and concomitant formation of a disulfide bond between IDH2 Cys-150 residues.	Disulfides	170-179	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	23-27
21133413-7	2011	The truncated (-5)IDH1/IDH2 and tetrameric enzymes were much more sensitive than the wild-type enzyme to inhibition by the oxidant diamide and concomitant formation of a disulfide bond between IDH2 Cys-150 residues.	Disulfides	170-179	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	193-197
21133413-9	2011	These results suggest that the octameric structure of IDH has in part evolved for regulation of disulfide bond formation and activity by ensuring the proximity of the amino terminus of an IDH1 subunit of one tetramer to the IDH2 Cys-150 residues in the other tetramer.	Disulfides	96-105	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	224-228
20506028-2	2011	ChM-I comprises two domains: an N-terminal hydrophilic domain (domain 1) containing an N-linked glycosylation site and a C-terminal hydrophobic domain (domain 2) with all four disulfide bonds that are present in this protein.	Disulfides	176-185	chondromodulin	Homo sapiens	0-5
12845650-1	2003	Interleukin-12 (IL-12) is a disulfide-linked p40-p35 heterodimeric cytokine and plays a key role in linking innate cellular immunity to an adaptive Th1 response against pathogens and tumor cells and in counteracting a Th2 immune response.	Disulfides	28-37	heart and neural crest derivatives expressed 2	Mus musculus	218-221
12911302-4	2003	However, in contrast to a recent crystal structure, the NMR solution structure for the reduced form of hDim1(1)(-)(128) presented here, along with thermodynamic data, indicates that the presence of a disulfide bond between Cys38 and Cys79 is structurally and functionally unimportant.	Disulfides	200-209	thioredoxin like 4A	Homo sapiens	103-108
13678526-4	2003	Both Ero1-Lalpha and Ero1-Lbeta interact via disulfide bonds with PDI and support the oxidation of immunoglobulin light chains.	Disulfides	45-54	endoplasmic reticulum oxidoreductins 1	Arabidopsis thaliana	5-9
13678526-4	2003	Both Ero1-Lalpha and Ero1-Lbeta interact via disulfide bonds with PDI and support the oxidation of immunoglobulin light chains.	Disulfides	45-54	endoplasmic reticulum oxidoreductins 1	Arabidopsis thaliana	21-25
12840147-0	2003	Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human beta-defensin 3.	Disulfides	12-21	defensin beta 103B	Homo sapiens	91-106
22028881-0	2011	Progranulin, a glycoprotein deficient in frontotemporal dementia, is a novel substrate of several protein disulfide isomerase family proteins.	Disulfides	106-115	granulin	Mus musculus	0-11
12840147-4	2003	Structures of several beta-defensins have recently been characterized, confirming the disulfide connectivity conserved within the family, i.e., Cys1-Cys5, Cys2-Cys4, and Cys3-Cys6.	Disulfides	86-95	cystin 1	Homo sapiens	144-148
21886772-0	2011	Fukutin-related protein resides in the Golgi cisternae of skeletal muscle fibres and forms disulfide-linked homodimers via an N-terminal interaction.	Disulfides	91-100	fukutin related protein	Homo sapiens	0-23
21886772-7	2011	The FKRP homodimer is kept together by a disulfide bridge provided by the most N-terminal cysteine, Cys6.	Disulfides	41-50	fukutin related protein	Homo sapiens	4-8
20947114-0	2010	The inability of vaccinia virus A33R protein to form intermolecular disulfide-bonded homodimers does not affect the production of infectious extracellular virus.	Disulfides	68-77	EEV membrane phosphoglycoprotein	Vaccinia virus	32-36
12840147-6	2003	Using the orthogonal protection of Cys1-Cys5 and of Cys1-Cys6, we chemically synthesized six topological analogs of hBD3 with predefined disulfide connectivities, including the (presumably) native beta pairing.	Disulfides	137-146	defensin beta 103B	Homo sapiens	116-120
12840147-9	2003	Our findings demonstrate that disulfide bonding in hBD3, although required for binding and activation of receptors for chemotaxis, is fully dispensable for its antimicrobial function, thus shedding light on the mechanisms of action for human beta-defensins and the design of novel peptide antibiotics.	Disulfides	30-39	defensin beta 103B	Homo sapiens	51-55
12770499-6	2003	Incubation of non-native human epidermal growth factor (hEGF) containing incorrect disulfide bonds with B. choshinensis cells secreting CatA protein resulted in the stimulation of the conversion of non-native hEGF to the native form.	Disulfides	83-92	epidermal growth factor	Homo sapiens	31-54
20888817-0	2010	A disulfide linkage in a CCCH zinc finger motif of an Arabidopsis CPSF30 ortholog.	Disulfides	2-11	cleavage and polyadenylation specificity factor 30	Arabidopsis thaliana	66-72
20888817-3	2010	This analysis reveals that this disulfide bond involves a CCCH zinc finger motif, one that is associated with the endonuclease activity of AtCPSF30.	Disulfides	32-41	cleavage and polyadenylation specificity factor 30	Arabidopsis thaliana	139-147
20888817-4	2010	This finding raises the possibility that redox regulation of AtCPSF30 may occur through oxidation and reduction of the disulfide linkage.	Disulfides	119-128	cleavage and polyadenylation specificity factor 30	Arabidopsis thaliana	61-69
27639450-5	2016	In order to identify Trx1 targets in vivo, we generated a transgenic mouse with inducible expression of a mutant Trx1 transgene to stabilize intermolecular disulfides with protein substrates.	Disulfides	156-166	thioredoxin 1	Mus musculus	21-25
27639450-5	2016	In order to identify Trx1 targets in vivo, we generated a transgenic mouse with inducible expression of a mutant Trx1 transgene to stabilize intermolecular disulfides with protein substrates.	Disulfides	156-166	thioredoxin 1	Mus musculus	113-117
20367259-4	2010	IMS import of SOD1 involves its copper chaperone, CCS, whose mitochondrial distribution is regulated by the Mia40/Erv1 disulfide relay system in a redox-dependent manner: CCS promotes SOD1 maturation and retention in the IMS.	Disulfides	119-128	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	108-113
12770499-6	2003	Incubation of non-native human epidermal growth factor (hEGF) containing incorrect disulfide bonds with B. choshinensis cells secreting CatA protein resulted in the stimulation of the conversion of non-native hEGF to the native form.	Disulfides	83-92	epidermal growth factor	Homo sapiens	56-60
20367271-1	2010	Erv1 and Mia40 constitute the two important components of the disulfide relay system that mediates oxidative protein folding in the mitochondrial intermembrane space.	Disulfides	62-71	Mia40p	Saccharomyces cerevisiae S288C	9-14
12770499-6	2003	Incubation of non-native human epidermal growth factor (hEGF) containing incorrect disulfide bonds with B. choshinensis cells secreting CatA protein resulted in the stimulation of the conversion of non-native hEGF to the native form.	Disulfides	83-92	epidermal growth factor	Homo sapiens	209-213
20367271-2	2010	Mia40 is the import receptor that recognizes the substrates introducing disulfide bonds while it is reduced.	Disulfides	72-81	Mia40p	Saccharomyces cerevisiae S288C	0-5
12773488-5	2003	Removal of the leader peptide critically depends on formation of at least some disulfide bonds in subunit gp120 during folding.	Disulfides	79-88	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	106-111
20455033-4	2010	The correct folding of t-PA requires the correct pairing of 17 disulfide bridges in the molecule.	Disulfides	63-72	chromosome 20 open reading frame 181	Homo sapiens	23-27
27562645-1	2016	Drosomycin (DRS) is a strictly antifungal peptide in Drosophila melanogaster, which contains four disulfide bridges (DBs) with three buried in molecular interior and one exposed on molecular surface to tie the amino- and carboxyl-termini of the molecule together (called wrapper disulfide bridge, WDB).	Disulfides	98-107	Drosomycin	Drosophila melanogaster	0-10
27562645-1	2016	Drosomycin (DRS) is a strictly antifungal peptide in Drosophila melanogaster, which contains four disulfide bridges (DBs) with three buried in molecular interior and one exposed on molecular surface to tie the amino- and carboxyl-termini of the molecule together (called wrapper disulfide bridge, WDB).	Disulfides	279-288	Drosomycin	Drosophila melanogaster	0-10
12869529-0	2003	Conformational dynamics of beta(2)-microglobulin analyzed by reduction and reoxidation of the disulfide bond.	Disulfides	94-103	beta-2-microglobulin	Homo sapiens	27-48
27574429-1	2016	Guanidinylated poly(amido amine)s with multiple disulfide linkages (Gua-SS-PAAs) were designed and constructed as nonviral gene carriers.	Disulfides	48-57	DExD-box helicase 21	Homo sapiens	0-3
27107383-1	2016	In this paper, a CD44-targeted and redox-responsive drug delivery system based on mesoporous silica nanoparticles (MSNs) was synthesized by conjugating tumor-shedable hyaluronic acid (HA) on the surface of MSNs via disulfide bonds.	Disulfides	215-224	CD44 molecule (Indian blood group)	Homo sapiens	17-21
20703838-3	2010	The MUC2 mucin protein forms trimers by disulfide bonding in cysteine-rich amino terminal von Willebrand factor (vWF) domains, coupled with crosslinking provided by TFF and Fcgbp proteins with MUC2 vWF domains, resulting in a highly viscous extracellular layer.	Disulfides	40-49	mucin 2	Mus musculus	4-8
12639915-1	2003	Two unusual features of the TSH receptor (TSHR) ectodomain are its intramolecular cleavage at the cell surface into disulfide-linked subunits and its constraint of ligand-independent (constitutive) activity inherent to the serpentine region.	Disulfides	116-125	thyrotropin receptor	Cricetulus griseus	42-46
12639915-8	2003	Trypsin treatment of the same cells expressing the noncleaving TSHR also generated disulfide-linked A and B subunits but, in contrast to thrombin, enhanced TSHR constitutive activity.	Disulfides	83-92	thyrotropin receptor	Cricetulus griseus	63-67
20585806-8	2010	Thus, ACTH(1-39) and N-POMC(1-28) have similar actions suggesting that the disulfide bridges are important but not essential.	Disulfides	75-84	proopiomelanocortin	Rattus norvegicus	23-27
27393305-5	2016	Here, we directly imaged GroEL-GroES interaction in the presence of disulfide-reduced alpha-lactalbumin as a substrate protein using high-speed atomic force microscopy.	Disulfides	68-77	heat shock protein family D (Hsp60) member 1	Homo sapiens	25-30
12943190-7	2003	Disulfide bridge disruption or replacement of the cysteine residues by their D-enantiomers markedly reduced the vasoconstrictor effect of UII and its analogues.	Disulfides	0-9	urotensin 2	Homo sapiens	138-141
27355203-7	2016	The results suggest a disulfide bond between Cys245 and Cys279 in SNAT2 which has no effect on cell surface trafficking, as well as transporter function.	Disulfides	22-31	solute carrier family 38 member 2	Homo sapiens	66-71
27355203-8	2016	The proposed disulfide bond may be important to delineate proximity in the extracellular domain of SNAT2 and related proteins.	Disulfides	13-22	solute carrier family 38 member 2	Homo sapiens	99-104
20643048-1	2010	In this report, we demonstrate that the internal disulfide bridge in human neuroglobin modulates structural changes associated with ligand photo-dissociation from the heme active site.	Disulfides	49-58	neuroglobin	Homo sapiens	75-86
12468550-8	2003	Mass spectrometry demonstrates that the peptides bind through a disulfide bond to a cysteine residue of annexin A2, the same mechanism that has been suggested for the inhibition mediated by homocysteine.	Disulfides	64-73	annexin A2	Homo sapiens	104-114
20643048-3	2010	Reduction of the internal disulfide bond in human neuroglobin leads to conformational changes (reflected by DeltaV) nearly identical to those observed for rat Ngb.	Disulfides	26-35	neuroglobin	Homo sapiens	50-61
20643048-4	2010	Our data favor the hypothesis that the disulfide bond between Cys46 and Cys55 modulates the functioning of human neuroglobin.	Disulfides	39-48	neuroglobin	Homo sapiens	113-124
20642009-10	2004	Uroguanylin (NDDCELCVNVACTGCL) is a 16 amino acid peptide with two disulfide bonds and is less complex than STh, which contains three disulfide bonds.	Disulfides	67-76	guanylate cyclase activator 2B	Homo sapiens	0-11
27189938-3	2016	This study showed that a 6-thioguanosine triphosphate (6-TGTP), converted in T-cells from 6-TP, targets Rac1 to form a disulfide adduct between 6-TGTP and the redox-sensitive GXXXXGK(S/T)C motif of Rac1.	Disulfides	119-128	Rac family small GTPase 1	Homo sapiens	104-108
27189938-3	2016	This study showed that a 6-thioguanosine triphosphate (6-TGTP), converted in T-cells from 6-TP, targets Rac1 to form a disulfide adduct between 6-TGTP and the redox-sensitive GXXXXGK(S/T)C motif of Rac1.	Disulfides	119-128	Rac family small GTPase 1	Homo sapiens	198-202
20642009-10	2004	Uroguanylin (NDDCELCVNVACTGCL) is a 16 amino acid peptide with two disulfide bonds and is less complex than STh, which contains three disulfide bonds.	Disulfides	134-143	guanylate cyclase activator 2B	Homo sapiens	0-11
27129265-5	2016	Increased sensitivity of anionic trypsinogen to CTRC-mediated degradation was due to an additional cleavage site at Leu-148 in the autolysis loop and the lack of the conserved Cys-139-Cys-206 disulfide bond.	Disulfides	192-201	chymotrypsin C	Homo sapiens	48-52
12626117-6	2003	A fine-tuning redox-dependent regulatory loop inhibits the activation of the kinase via reduction of protein disulfide groups, possibly involving the thioredoxin complex.	Disulfides	109-118	thioredoxin	Homo sapiens	150-161
27265872-5	2016	Here, we present evidence of the high evolutionary conservation of disulfide bond formation in Tim17 and Tim22 among fungi and metazoa.	Disulfides	67-76	protein transporter TIM17	Saccharomyces cerevisiae S288C	95-100
27166796-5	2016	We report the successful expression of active human sialyltransferases ST3Gal1 and ST6Gal1 in commercial Escherichia coli strains designed for production of disulfide-containing proteins.	Disulfides	157-166	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	83-90
27054568-8	2016	Surprisingly, soluble GARP and TGFbeta formed stable non-covalent complexes in addition to disulfide-coupled complexes, depending on the redox conditions of the microenvironment.	Disulfides	91-100	leucine rich repeat containing 32	Homo sapiens	22-26
20642009-10	2004	Uroguanylin (NDDCELCVNVACTGCL) is a 16 amino acid peptide with two disulfide bonds and is less complex than STh, which contains three disulfide bonds.	Disulfides	134-143	saitohin	Homo sapiens	108-111
20202930-1	2010	The cell catalysts calnexin (CNX) and protein-disulfide isomerase (PDI) cooperate in establishing the disulfide bonding of the HIV envelope (Env) glycoprotein.	Disulfides	46-55	endogenous retrovirus group K member 20	Homo sapiens	141-144
12626118-3	2003	A central component of the redox cascade is a novel enzyme, the ferredoxin:thioredoxin reductase, which is capable of reducing a disulfide bridge with the help of an iron-sulfur cluster.	Disulfides	129-138	peroxiredoxin 5	Homo sapiens	75-96
12493837-4	2003	We identified several circulating forms of LEAP-2 differing in their amino-terminal length, all containing a core structure with two disulfide bonds formed by cysteine residues in relative 1-3 and 2-4 positions.	Disulfides	133-142	liver enriched antimicrobial peptide 2	Homo sapiens	43-49
20351257-2	2010	Two crystal forms of XRCC1-NTD complexed with Pol beta have been solved, revealing that the XRCC1-NTD is able to adopt a redox-dependent alternate fold, characterized by a disulfide bond, and substantial variations of secondary structure, folding topology, and electrostatic surface.	Disulfides	172-181	X-ray repair cross complementing 1	Homo sapiens	21-26
20351257-2	2010	Two crystal forms of XRCC1-NTD complexed with Pol beta have been solved, revealing that the XRCC1-NTD is able to adopt a redox-dependent alternate fold, characterized by a disulfide bond, and substantial variations of secondary structure, folding topology, and electrostatic surface.	Disulfides	172-181	X-ray repair cross complementing 1	Homo sapiens	92-97
20145245-0	2010	Peroxiredoxin Ahp1 acts as a receptor for alkylhydroperoxides to induce disulfide bond formation in the Cad1 transcription factor.	Disulfides	72-81	Cad1p	Saccharomyces cerevisiae S288C	104-108
20145245-5	2010	We demonstrate that Ahp1 is required for the formation of intermolecular Cad1 disulfide bond(s) in both an in vitro redox system and in cells treated with alkylhydroperoxide.	Disulfides	78-87	Cad1p	Saccharomyces cerevisiae S288C	73-77
20130111-6	2010	Moreover, treatment with sulfhydryl-modifying agents that oxidize SH-groups of cysteine residues to disulfide bonds abolished ATRA-mediated RARA nuclear localization, suggesting that the thiol oxidoreductase activity of GRp58 may be required for RARA nuclear import.	Disulfides	100-109	retinoic acid receptor, alpha	Mus musculus	140-144
26894959-5	2016	Further mutagenesis combined with the use of spider toxins reveals that (55)Cys forms a disulfide bond with (910)Cys in the Nav1.2 domain II pore loop, thereby suggesting a 1:1 stoichiometry.	Disulfides	88-97	sodium voltage-gated channel alpha subunit 2	Homo sapiens	124-130
26894959-6	2016	Our results also provide clues as to which disulfide bonds are formed between adjacent Nav1.2 (912/918)Cys residues.	Disulfides	43-52	sodium voltage-gated channel alpha subunit 2	Homo sapiens	87-93
26789136-0	2016	The Disulfide Bonds within BST-2 Enhance Tensile Strength during Viral Tethering.	Disulfides	4-13	bone marrow stromal cell antigen 2	Homo sapiens	27-32
26789136-2	2016	BST-2 has an alpha-helical ectodomain that forms disulfide-linked dimers between two monomers forming a coiled coil.	Disulfides	49-58	bone marrow stromal cell antigen 2	Homo sapiens	0-5
12493918-2	2002	Using a pulse-chase approach in intact cells, we found instead that newly synthesized LDL-R molecules folded by way of "collapsed" intermediates that contained non-native disulfide bonds between distant cysteines.	Disulfides	171-180	low density lipoprotein receptor	Homo sapiens	86-91
26789136-5	2016	We explored the role of the disulfides in the structure of BST-2 using experimental, biophysical methods.	Disulfides	28-38	bone marrow stromal cell antigen 2	Homo sapiens	59-64
26789136-7	2016	We find that the disulfides coordinate the unfolding of the BST-2 monomers, which adds tensile strength to the coiled coil.	Disulfides	17-27	bone marrow stromal cell antigen 2	Homo sapiens	60-65
12493918-4	2002	Thus, productive LDL-R folding in a cell is not vectorial but is mostly posttranslational, and involves transient long-range non-native disulfide bonds that are isomerized into native short-range cysteine pairs.	Disulfides	136-145	low density lipoprotein receptor	Homo sapiens	17-22
26789136-8	2016	Structural differences between oxidized and reduced BST-2 are apparent during unfolding, showing the monomers slide past each other in the absence of the disulfides.	Disulfides	154-164	bone marrow stromal cell antigen 2	Homo sapiens	52-57
12413830-1	2002	Human urotensin II (hU-II; H-Glu-Thr-Pro-Asp-cyclo[Cys-Phe-Trp-Lys-Tyr-Cys]-Val-OH) is a disulfide bridged undecapeptide recently identified as the ligand of an orphan G protein-coupled receptor.	Disulfides	89-98	urotensin 2	Homo sapiens	6-18
26629855-3	2016	Recently, disulfide libraries and targeted GDP-mimetics have been used to selectively label the G12C oncogenic mutation in KRAS.	Disulfides	10-19	KRAS proto-oncogene, GTPase	Homo sapiens	123-127
20174556-8	2010	The disulfide connectivity pattern, together with data on the CD81 binding site and reported E2 deletion mutants, enabled the threading of the E2e polypeptide chain onto the structural template of class II fusion proteins of related flavi- and alphaviruses.	Disulfides	4-13	CD81 molecule	Homo sapiens	62-66
20009579-5	2010	In chloroplasts, it becomes apparent that protein import is affected by redox signals on both the outer and inner envelope: at the level of the Toc complex (translocon at the outer envelope of chloroplasts), the formation/reduction of disulfide bridges between the Toc components has a strong influence on import yield.	Disulfides	235-244	rhomboid 5 homolog 2	Homo sapiens	144-147
20009579-5	2010	In chloroplasts, it becomes apparent that protein import is affected by redox signals on both the outer and inner envelope: at the level of the Toc complex (translocon at the outer envelope of chloroplasts), the formation/reduction of disulfide bridges between the Toc components has a strong influence on import yield.	Disulfides	235-244	rhomboid 5 homolog 2	Homo sapiens	265-268
27454362-2	2016	Unlike its ligand TSH, whose subunits are encoded by two genes, the TSHR is expressed as a single polypeptide that subsequently undergoes intramolecular cleavage into disulfide-linked subunits.	Disulfides	167-176	thyroid stimulating hormone receptor	Homo sapiens	68-72
12413830-1	2002	Human urotensin II (hU-II; H-Glu-Thr-Pro-Asp-cyclo[Cys-Phe-Trp-Lys-Tyr-Cys]-Val-OH) is a disulfide bridged undecapeptide recently identified as the ligand of an orphan G protein-coupled receptor.	Disulfides	89-98	urotensin 2	Homo sapiens	20-25
20068548-2	2010	KLRG1 exists both as a monomer and as a disulfide-linked homodimer.	Disulfides	40-49	killer cell lectin like receptor G1	Homo sapiens	0-5
12239218-0	2002	Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain.	Disulfides	47-56	CD1d molecule	Homo sapiens	81-85
12239218-7	2002	Complete disulfide bond formation in the CD1d heavy chain was substantially impaired if the chaperone interactions were blocked by the glucosidase inhibitors castanospermine or N-butyldeoxynojirimycin.	Disulfides	9-18	CD1d molecule	Homo sapiens	41-45
12437921-5	2002	When oxidized by H2O2, Gpx3 Cys36 bridges Yap1 Cys598 by a disulfide bond.	Disulfides	59-68	peroxiredoxin HYR1	Saccharomyces cerevisiae S288C	23-27
19845005-0	2009	An interdomain disulfide bridge links the NtA and first FS domain in agrin.	Disulfides	15-24	agrin	Homo sapiens	69-74
19845005-7	2009	These results suggest that the interdomain disulfide bond between the NtA and the first FS domain might be important for the proper folding of agrin.	Disulfides	43-52	agrin	Homo sapiens	143-148
28580037-3	2016	The autoantibodies only bind to the extracellular portion of PLA2R under the non-reducing condition, indicating that the epitope in PLA2R is conformational requiring specific disulfide bonds to maintain its structure.	Disulfides	175-184	phospholipase A2 receptor 1	Homo sapiens	61-66
28580037-3	2016	The autoantibodies only bind to the extracellular portion of PLA2R under the non-reducing condition, indicating that the epitope in PLA2R is conformational requiring specific disulfide bonds to maintain its structure.	Disulfides	175-184	phospholipase A2 receptor 1	Homo sapiens	132-137
12547227-3	2002	Hephaestin is homologous to the plasma copper-containing protein ceruloplasmin, and all residues involved in copper binding and disulfide bond formation in ceruloplasmin are conserved in hephaestin.	Disulfides	128-137	ceruloplasmin	Mus musculus	65-78
26566734-6	2016	NMR data showed that the three-disulfide theta-defensin and cyclotide scaffolds accommodated the LyP1 and RGDS epitopes but that scaffolds with fewer disulfide bonds were structurally compromised by inclusion of the LyP1 epitope.	Disulfides	31-40	protein tyrosine phosphatase non-receptor type 22	Homo sapiens	97-101
12547227-3	2002	Hephaestin is homologous to the plasma copper-containing protein ceruloplasmin, and all residues involved in copper binding and disulfide bond formation in ceruloplasmin are conserved in hephaestin.	Disulfides	128-137	ceruloplasmin	Mus musculus	156-169
12413696-2	2002	It is an oligomeric protein composed of a disulfide-linked C8 alpha-gamma heterodimer and a non-covalently associated C8 beta chain.	Disulfides	42-51	complement C8 alpha chain	Homo sapiens	59-67
27423861-5	2016	First, we describe a convergent strategy to site-specifically attach the small ubiquitin-like modifier-3 (SUMO-3) protein to the site of Lys12 in histone H4 by means of a disulfide linkage.	Disulfides	171-180	small ubiquitin like modifier 3	Homo sapiens	73-104
19782948-0	2009	Endothelial CD146 is required for in vitro tumor-induced angiogenesis: the role of a disulfide bond in signaling and dimerization.	Disulfides	85-94	melanoma cell adhesion molecule	Homo sapiens	12-17
19679655-8	2009	To understand the functional role of each disulfide, small molecules and the physiological substrate protein Mia40 were used as electron donors in oxygen consumption assays.	Disulfides	42-51	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	109-114
19708669-1	2009	V. The effect of the disulfide bridge on the structural features of the peptide hormone somatostatin-14.	Disulfides	21-30	somatostatin	Homo sapiens	88-103
27423861-5	2016	First, we describe a convergent strategy to site-specifically attach the small ubiquitin-like modifier-3 (SUMO-3) protein to the site of Lys12 in histone H4 by means of a disulfide linkage.	Disulfides	171-180	small ubiquitin like modifier 3	Homo sapiens	106-112
26449594-7	2015	Together with recent results obtained with BoNTs specific for SNAP25 and syntaxin, the present data demonstrate the essential role of the thioredoxin-thioredoxin reductase system in reducing the interchain disulfide during the nerve intoxication mechanism of all serotypes.	Disulfides	206-215	thioredoxin 1	Mus musculus	138-149
26449594-7	2015	Together with recent results obtained with BoNTs specific for SNAP25 and syntaxin, the present data demonstrate the essential role of the thioredoxin-thioredoxin reductase system in reducing the interchain disulfide during the nerve intoxication mechanism of all serotypes.	Disulfides	206-215	thioredoxin 1	Mus musculus	150-161
12369846-3	2002	S-(Carboxymethyl)-alpha-lactalbumin, a disordered form of the protein with three out of four disulfide bridges reduced, was even more susceptible to fibrillation.	Disulfides	93-102	lactalbumin alpha	Bos taurus	18-35
26529388-8	2015	Addition of chemical blockers indicated that hydrogen bondings and disulfide bridges were the main mechanisms of interactions with mucin.	Disulfides	67-76	solute carrier family 13 member 2	Rattus norvegicus	131-136
12380820-0	2002	Screening for disulfide bonds in proteins by MALDI in-source decay and LIFT-TOF/TOF-MS.	Disulfides	14-23	FEZ family zinc finger 2	Homo sapiens	71-86
26416881-8	2015	The form that contains an intramolecular disulfide bond is bound to Mic60 of the MICOS complex.	Disulfides	41-50	Mic60p	Saccharomyces cerevisiae S288C	68-73
19630027-2	2009	Most of the sequence of somatostatin-14 is present within a loop defined by the disulfide linkage between Cys-3 and Cys-14.	Disulfides	80-89	somatostatin	Homo sapiens	24-39
12380820-4	2002	Signals (peak C) from putatively disulfide-linked peptides were subjected to LIFT-TOF/TOF-MS to confirm the existence of a disulfide bond.	Disulfides	33-42	FEZ family zinc finger 2	Homo sapiens	77-92
12389098-5	2002	Here we further analyzed the two IgNAR types, "type 1" having one cysteine in CDR3 and "type 2" with an even number (two or four) of CDR3 cysteines, and discovered that placement of the disulfide bridges in the IgNAR V domain differentially influences the selection of mutations in CDR1 and CDR2.	Disulfides	186-195	cerebellar degeneration related protein 1	Homo sapiens	282-286
19544475-1	2009	Kell (ECE-3), a highly polymorphic blood group glycoprotein, displays more than 30 antigens that produce allo-antibodies and, on red blood cells (RBCs), is complexed through a single disulfide bond with the integral membrane protein, XK.	Disulfides	183-192	Kell blood group	Mus musculus	6-11
26254010-5	2015	Oxidation occurred on methionine and tryptophan residues, and on the unique cysteine residue, in position 42 in S100A8, and 3 in S100A9, that generated glutathionylated, cysteinylated, sulfinic, sulfonic, and disulfide dimeric forms.	Disulfides	209-218	S100 calcium binding protein A9	Homo sapiens	129-135
26424450-2	2015	Previous studies showed that the chloroplastic atypical thioredoxin ACHT1 is oxidized by 2-Cys peroxiredoxin (2-Cys Prx) in Arabidopsis plants illuminated with growth light and in turn transmits a disulfide-based signal via yet unknown target proteins in a feedback regulation of photosynthesis.	Disulfides	197-206	atypical CYS HIS rich thioredoxin 1	Arabidopsis thaliana	68-73
12238917-0	2002	A new, potent urotensin II receptor peptide agonist containing a Pen residue at the disulfide bridge.	Disulfides	84-93	urotensin 2 receptor	Homo sapiens	14-35
26424450-5	2015	ACHT4 further reacted uniquely with the small subunit (APS1) of ADP-glucose pyrophosphorylase (AGPase), the first committed enzyme of the starch synthesis pathway, suggesting that it transfers the disulfides it receives from 2-Cys Prx to APS1 and turns off AGPase.	Disulfides	197-207	ATP sulfurylase 1	Arabidopsis thaliana	55-59
26424450-5	2015	ACHT4 further reacted uniquely with the small subunit (APS1) of ADP-glucose pyrophosphorylase (AGPase), the first committed enzyme of the starch synthesis pathway, suggesting that it transfers the disulfides it receives from 2-Cys Prx to APS1 and turns off AGPase.	Disulfides	197-207	ATP sulfurylase 1	Arabidopsis thaliana	238-242
19194473-3	2009	Consequently, in this study, we analyzed the uptake of grass pollen allergens by epithelial cells: Phl p 1 was selected as a glycosylated allergen containing disulfide bridges whereas Phl p 6 lacks post-translational modifications.	Disulfides	158-167	crystallin gamma F, pseudogene	Homo sapiens	103-106
19477928-1	2009	Mia40 and Erv1 execute a disulfide relay to import the small Tim proteins into the mitochondrial intermembrane space.	Disulfides	25-34	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
26449534-7	2015	Based on disulfide crosslinking that detects cognate alpha3-Rpt6 tail and alpha2-Rpt3 tail interactions in the proteasome, decreased alpha3-Rpt6 tail interaction facilitates robust alpha2-Rpt3 tail interaction that is also strongly ATP-dependent.	Disulfides	9-18	proteasome 26S subunit, ATPase 4	Homo sapiens	81-85
12220191-2	2002	It is an oligomeric protein composed of a disulfide-linked C8alpha-gamma heterodimer and a noncovalently associated C8beta chain.	Disulfides	42-51	complement C8 alpha chain	Homo sapiens	59-66
26449534-7	2015	Based on disulfide crosslinking that detects cognate alpha3-Rpt6 tail and alpha2-Rpt3 tail interactions in the proteasome, decreased alpha3-Rpt6 tail interaction facilitates robust alpha2-Rpt3 tail interaction that is also strongly ATP-dependent.	Disulfides	9-18	proteasome 26S subunit, ATPase 4	Homo sapiens	188-192
26387864-1	2015	The essential oxidoreductase Mia40/CHCHD4 mediates disulfide bond formation and protein folding in the mitochondrial intermembrane space.	Disulfides	51-60	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	29-34
26387864-1	2015	The essential oxidoreductase Mia40/CHCHD4 mediates disulfide bond formation and protein folding in the mitochondrial intermembrane space.	Disulfides	51-60	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	35-41
26387864-4	2015	We examined the biogenesis of MICU1 and find that Mia40 introduces an intermolecular disulfide bond that links MICU1 and its inhibitory paralog MICU2 in a heterodimer.	Disulfides	85-94	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	50-55
19419965-4	2009	However, conflicting disulfide maps, inconsistent orientations of subdomains within FDs, and the presence of binding partners in all FD structures led us to determine the three-dimensional structure of C7-FIMs by NMR spectroscopy.	Disulfides	21-30	complement C7	Homo sapiens	202-209
19432394-6	2009	A major protein was the Muc2 mucin that by its net-like disulfide-bonded polymer structure builds the mucus.	Disulfides	56-65	mucin 2	Mus musculus	24-28
12221002-8	2002	Preliminary biochemical analysis of Emu1/2 confirmed that they are secreted glycoproteins which are attached to the extracellular matrix and capable of forming homo- and heteromers via disulfide bonding.	Disulfides	185-194	EMI domain containing 1	Mus musculus	36-42
19435374-0	2009	Effects of disulfide bond formation and protein helicity on the aggregation of activating transcription factor 5.	Disulfides	11-20	activating transcription factor 5	Homo sapiens	79-112
19459666-2	2009	Electron photodetachment experiments as a function of the laser wavelength were performed on the native disulfide-containing ring oxytocin, the reduced dithiol oxytocin, and the Cu(II)-oxytocin complex.	Disulfides	104-113	oxytocin/neurophysin I prepropeptide	Homo sapiens	130-138
26281711-2	2015	We tested the feasibility of the concept by fusing a 10-residue-long, disulfide-bond-constrained inhibitory peptide, randomized in selected positions, to the catalytic domain of the serine protease murine urokinase-type plasminogen activator.	Disulfides	70-79	complement component 1, s subcomponent 1	Mus musculus	182-197
12353082-7	2002	Patient 1 had a C506Y missense mutation resulting in the expression of an unpaired cysteine; we propose that the Mr approximately 260,000 band is a disulfide-bonded beta3 dimer.	Disulfides	148-157	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	165-170
26126825-3	2015	GARP forms disulfide bonds with proTGF-beta1, favors its cleavage into latent inactive TGF-beta1, induces the secretion and surface presentation of GARP latent TGF-beta1 complexes, and is required for activation of the cytokine in Tregs.	Disulfides	11-20	leucine rich repeat containing 32	Homo sapiens	0-4
12019263-1	2002	The NH(2)-terminal somatomedin B (SMB) domain (residues 1-44) of human vitronectin contains eight Cys residues organized into four disulfide bonds and is required for the binding of type 1 plasminogen activator inhibitor (PAI-1).	Disulfides	131-140	small nuclear ribonucleoprotein polypeptides B and B1	Rattus norvegicus	34-37
19349277-5	2009	Mutant Txnl1 with one active site cysteine replaced by serine formed disulfide bonds to eEF1A1, a substrate-recruiting factor of the 26 S proteasome.	Disulfides	69-78	thioredoxin like 1	Homo sapiens	7-12
12019263-7	2002	Selective reduction/S-alkylation of these two disulfide linkages caused the complete loss of PAI-1 binding activity.	Disulfides	46-55	serpin family E member 1	Homo sapiens	93-98
11943769-0	2002	Conformation of beta 2-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond.	Disulfides	82-91	beta-2-microglobulin	Homo sapiens	16-36
19321446-2	2009	IDE exhibits a remarkable specificity to degrade insulin without breaking the disulfide bonds that hold the insulin A and B chains together.	Disulfides	78-87	insulin degrading enzyme	Homo sapiens	0-3
19321446-5	2009	This ensures that IDE effectively splits insulin into inactive N- and C-terminal halves without breaking the disulfide bonds.	Disulfides	109-118	insulin degrading enzyme	Homo sapiens	18-21
11943769-1	2002	Beta2-microglobulin (beta2-m), a major component of dialysis-related amyloid fibrils, has an intrachain disulfide bond buried inside the native structure.	Disulfides	104-113	beta-2-microglobulin	Homo sapiens	0-19
19018666-2	2009	The first switch leads to formation of two disulfides and occurs upon transport of Cox17 into mitochondrial intermembrane space (IMS).	Disulfides	43-53	cytochrome c oxidase copper chaperone COX17	Homo sapiens	83-88
11877442-4	2002	In its disulfide form, the 13-kDa protein thioredoxin-2 is a substrate of thioredoxin reductase-1 (K(m) = 5.2 microm, k(cat) = 14.5 s(-1)) and in its dithiol form, an electron donor for TPx-1 (K(m) = 9 microm, k(cat) = 5.4 s(-1)).	Disulfides	7-16	thioredoxin 2	Homo sapiens	42-55
19063682-5	2009	In the presence of agonist, H420C and M425C in TM6 formed disulfide bonds with all and with most, respectively, of the substituted cysteines incorporated in TM5.	Disulfides	58-67	tropomyosin 3	Homo sapiens	157-160
19586601-1	2009	During hair coloring a number of disulfide bonds in cystine are oxidized (1) to create cysteic acid, forming binding sites for metal ions such as Ca(2+ )and Cu(2+ )from tap water (2).	Disulfides	33-42	nuclear RNA export factor 1	Homo sapiens	169-172
11870603-4	2002	Elevation of expression level by selection for increased drug resistance in Chinese hamster ovary cells stably expressing ATIII resulted in formation of disulfide-bonded aggregates of ATIII.	Disulfides	153-162	serpin family C member 1	Homo sapiens	122-127
19359471-5	2009	A cysteine residue within the AGR2 thioredoxin-like domain forms mixed disulfide bonds with MUC2, indicating a direct role for AGR2 in mucin processing.	Disulfides	71-80	mucin 2	Mus musculus	92-96
11870603-4	2002	Elevation of expression level by selection for increased drug resistance in Chinese hamster ovary cells stably expressing ATIII resulted in formation of disulfide-bonded aggregates of ATIII.	Disulfides	153-162	serpin family C member 1	Homo sapiens	184-189
12014016-2	2002	CC10/uteroglobin is a homodimer consisting of 70 amino acid subunits arranged in an antiparallel fashion and connected by two disulfide bonds.	Disulfides	126-135	secretoglobin family 1A member 1	Homo sapiens	0-4
19053947-3	2009	Core-glycosylated CFTR was labelled and pulled down on streptavidin beads after exposure to sulfo-NHS-SS-biotin [biotin attached to a reactive NHS (N-hydroxysuccinimide) ester with a disulfide spacer; molecular mass=606.7 Da]; however, intracellular proteins were also detected in the precipitates.	Disulfides	183-192	cystic fibrosis transmembrane conductance regulator	Mesocricetus auratus	18-22
19035567-9	2009	The NMR study shows that the h-CFC overall topology is determined by the presence of three disulfide bridges and that residues H120 and W124 are located between the first strand and the first loop with the side chains externally exposed.	Disulfides	91-100	tubulin folding cofactor C	Homo sapiens	31-34
19159616-6	2009	The highly homologous porcine pancreatic kallikrein (pK1) showed a completely different response: Even at 20 mM DDT, no inactivation was seen; and in this case, only one of the five disulfides (Cys 22-Cys 157) was opened.	Disulfides	182-192	prokineticin 1	Homo sapiens	53-56
19159616-8	2009	A structural basis for this interpretation is provided when the two homologous proteins were compared with respect to the threedimensional architecture around the crucial disulfide Cys 191-Cys 220 where in the case of PK1, but not in PSA, the phenylalanine-residue (Phe 149) is in an interfering position.	Disulfides	171-180	prokineticin 1	Homo sapiens	218-221
12014016-2	2002	CC10/uteroglobin is a homodimer consisting of 70 amino acid subunits arranged in an antiparallel fashion and connected by two disulfide bonds.	Disulfides	126-135	secretoglobin family 1A member 1	Homo sapiens	5-16
11851431-1	2002	Ricin is a heterodimeric protein toxin in which a catalytic polypeptide (the A-chain or RTA) is linked by a disulfide bond to a cell-binding polypeptide (the B-chain or RTB).	Disulfides	108-117	MAS related GPR family member F	Homo sapiens	88-91
19201900-9	2009	These findings suggest that thiol-disulfide conversion occurring in the extracellular region of ADAM17 may be involved in its activation.	Disulfides	34-43	ADAM metallopeptidase domain 17	Homo sapiens	96-102
11809854-0	2002	Conserved cysteine residues in the extracellular loop of the human P2X(1) receptor form disulfide bonds and are involved in receptor trafficking to the cell surface.	Disulfides	88-97	purinergic receptor P2X 1	Homo sapiens	67-82
19201900-10	2009	An analysis of ADAM17 revealed that within its disintegrin/cysteine-rich region are two highly conserved, vicinal cysteine sulfhydryl motifs (cysteine-X-X-cysteine), which are well-characterized targets for thiol-disulfide exchange in various other proteins.	Disulfides	213-222	ADAM metallopeptidase domain 17	Homo sapiens	15-21
19010334-7	2009	The IMS of mitochondria harbors a disulfide relay system consisting of the import receptor Mia40 and the thiol oxidase Erv1, which drives the import of substrates with conserved cysteine residues arranged in typical twin Cx(3)C and twin Cx(9)C motifs.	Disulfides	34-43	Mia40p	Saccharomyces cerevisiae S288C	91-96
19010334-11	2009	Mia40 forms mixed disulfides with Ccs1, suggesting a role of Mia40 for the generation of disulfide bonds in Ccs1.	Disulfides	18-28	Mia40p	Saccharomyces cerevisiae S288C	0-5
19010334-11	2009	Mia40 forms mixed disulfides with Ccs1, suggesting a role of Mia40 for the generation of disulfide bonds in Ccs1.	Disulfides	18-27	Mia40p	Saccharomyces cerevisiae S288C	0-5
19010334-11	2009	Mia40 forms mixed disulfides with Ccs1, suggesting a role of Mia40 for the generation of disulfide bonds in Ccs1.	Disulfides	18-27	Mia40p	Saccharomyces cerevisiae S288C	61-66
19010334-12	2009	We suggest that the disulfide relay system transfers disulfide bonds via Mia40 to Ccs1, which then shuttles disulfide bonds to Sod1.	Disulfides	20-29	Mia40p	Saccharomyces cerevisiae S288C	73-78
19010334-12	2009	We suggest that the disulfide relay system transfers disulfide bonds via Mia40 to Ccs1, which then shuttles disulfide bonds to Sod1.	Disulfides	53-62	Mia40p	Saccharomyces cerevisiae S288C	73-78
11809854-8	2002	Based on phenotypic comparisons of single and double cysteine mutants, we propose the following disulfide bond pairs in the human P2X(1) receptor: C117-C165, C126-C149, C132-C159, C217-C227, and C261-C270.	Disulfides	96-105	purinergic receptor P2X 1	Homo sapiens	130-145
11772026-0	2002	The primary structure and the disulfide links of the bovine relaxin-like factor (RLF).	Disulfides	30-39	insulin like 3	Bos taurus	60-79
19010334-12	2009	We suggest that the disulfide relay system transfers disulfide bonds via Mia40 to Ccs1, which then shuttles disulfide bonds to Sod1.	Disulfides	53-62	Mia40p	Saccharomyces cerevisiae S288C	73-78
18761382-5	2009	Substrates are imported via a disulfide exchange relay with two components Mia40 and Erv1.	Disulfides	30-39	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	75-80
11772026-0	2002	The primary structure and the disulfide links of the bovine relaxin-like factor (RLF).	Disulfides	30-39	insulin like 3	Bos taurus	81-84
11772026-5	2002	Sequence analysis in combination with mass spectrometry and tryptic peptide mapping showed unambiguously that RLF is larger than previously assumed and that it has the relaxin-type disulfide bond distribution that makes it a bona fide member of the relaxin family of hormones.	Disulfides	181-190	insulin like 3	Bos taurus	110-113
12110134-10	2002	We have recently demonstrated that HLA-B27 is capable of forming disulfide-bonded homodimers.	Disulfides	65-74	major histocompatibility complex, class I, B	Homo sapiens	35-42
20028322-5	2009	The sequence of the human A(3)AR contains only one cysteine residue (Cys166) in the second extracellular loop (EL2), which putatively forms a conserved disulfide bridge with the respective cysteine residues of TM3 (Cys83).	Disulfides	152-161	spectrin alpha, erythrocytic 1	Homo sapiens	111-114
11752136-0	2002	Vaccinia virus G4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assembly.	Disulfides	78-87	glutaredoxin-like protein	Vaccinia virus	15-18
18854167-0	2008	Denaturation and unfolding of human anaphylatoxin C3a: an unusually low covalent stability of its native disulfide bonds.	Disulfides	105-114	complement C3	Homo sapiens	50-53
11752136-2	2002	Repression of E10R prevented the formation of intramolecular disulfide bonds of the G4L glutaredoxin, the L1R membrane protein, and the structurally related F9L protein.	Disulfides	61-70	glutaredoxin-like protein	Vaccinia virus	84-87
18854167-3	2008	Structurally, C3a is a relatively small protein (77 amino acids) comprising a N-terminal domain connected by 3 native disulfide bonds and a helical C-terminal segment.	Disulfides	118-127	complement C3	Homo sapiens	14-17
18854167-4	2008	The structural stability of C3a has been investigated here using three different methods: Disulfide scrambling; Differential CD spectroscopy; and Reductive unfolding.	Disulfides	90-99	complement C3	Homo sapiens	28-31
11752136-4	2002	By reacting free thiols with 4-acetamido-4"-malemideylstilbene-2,2"-disulfonic acid, alkylated and nonalkylated disulfide-bonded forms of G4L could be resolved from each other by polyacrylamide gel electrophoresis.	Disulfides	112-121	glutaredoxin-like protein	Vaccinia virus	138-141
18854167-6	2008	(a) There is an unusual disconnection between the conformational stability of C3a and the covalent stability of its three native disulfide bonds that is not seen with other disulfide proteins.	Disulfides	129-138	complement C3	Homo sapiens	78-81
18854167-6	2008	(a) There is an unusual disconnection between the conformational stability of C3a and the covalent stability of its three native disulfide bonds that is not seen with other disulfide proteins.	Disulfides	173-182	complement C3	Homo sapiens	78-81
11752136-5	2002	The cysteines of intracellular G4L were in both disulfide and reduced forms, whereas those of E10R, L1R, and F9L and virion-associated G4L were mostly disulfide bonded.	Disulfides	48-57	glutaredoxin-like protein	Vaccinia virus	31-34
18854167-7	2008	As measured by both methods of disulfide scrambling and differential CD spectroscopy, the native C3a exhibits a global conformational stability that is comparable to numerous proteins with similar size and disulfide content, all with mid-point denaturation of [GdmCl](1/2) at 3.4-5M.	Disulfides	31-40	complement C3	Homo sapiens	97-100
18854167-7	2008	As measured by both methods of disulfide scrambling and differential CD spectroscopy, the native C3a exhibits a global conformational stability that is comparable to numerous proteins with similar size and disulfide content, all with mid-point denaturation of [GdmCl](1/2) at 3.4-5M.	Disulfides	206-215	complement C3	Homo sapiens	97-100
11752136-5	2002	The cysteines of intracellular G4L were in both disulfide and reduced forms, whereas those of E10R, L1R, and F9L and virion-associated G4L were mostly disulfide bonded.	Disulfides	151-160	glutaredoxin-like protein	Vaccinia virus	135-138
18854167-9	2008	However, the native disulfide bonds of C3a is 150-1000 fold less stable than those proteins as evaluated by the method of reductive unfolding.	Disulfides	20-29	complement C3	Homo sapiens	39-42
18854167-10	2008	The 3 native disulfide bonds of C3a can be collectively and quantitatively reduced with as low as 1mM of dithiothreitol within 5 min.	Disulfides	13-22	complement C3	Homo sapiens	32-35
11752136-6	2002	Repression of G4L expression prevented the formation of disulfide bonds in both L1R and F9L but not E10R.	Disulfides	56-65	glutaredoxin-like protein	Vaccinia virus	14-17
18854167-11	2008	The fragility of the native disulfide bonds of C3a has not yet been observed with other native disulfide proteins.	Disulfides	28-37	complement C3	Homo sapiens	47-50
11752136-7	2002	Both cysteines of G4L were required for L1R and F9L disulfide bond formation or for trans-complementation of virus infectivity when G4L expression was repressed.	Disulfides	52-61	glutaredoxin-like protein	Vaccinia virus	18-21
18854167-11	2008	The fragility of the native disulfide bonds of C3a has not yet been observed with other native disulfide proteins.	Disulfides	95-104	complement C3	Homo sapiens	47-50
18854167-12	2008	(b) Using the method of disulfide scrambling, denatured C3a was shown to consist of diverse isomers adopting varied extent of unfolding.	Disulfides	24-33	complement C3	Homo sapiens	56-59
12189047-3	2002	Thioredoxin (TRX), a small protein with redox-active dithiol/disulfide in the active site, is induced by a variety of oxidative stresses and secreted from the cells.	Disulfides	61-70	thioredoxin	Homo sapiens	0-11
18854167-13	2008	Among them, the most extensively unfolded isomer of denatured C3a is found to assume beads-form disulfide pattern, comprising Cys(36)-Cys(49) and two disulfide bonds formed by two pair of consecutive cysteines, Cys(22)-Cys(23) and Cys(56)-Cys(57), a unique disulfide structure of polypeptide that has not been documented previously.	Disulfides	96-105	complement C3	Homo sapiens	62-65
18854167-13	2008	Among them, the most extensively unfolded isomer of denatured C3a is found to assume beads-form disulfide pattern, comprising Cys(36)-Cys(49) and two disulfide bonds formed by two pair of consecutive cysteines, Cys(22)-Cys(23) and Cys(56)-Cys(57), a unique disulfide structure of polypeptide that has not been documented previously.	Disulfides	150-159	complement C3	Homo sapiens	62-65
18854167-13	2008	Among them, the most extensively unfolded isomer of denatured C3a is found to assume beads-form disulfide pattern, comprising Cys(36)-Cys(49) and two disulfide bonds formed by two pair of consecutive cysteines, Cys(22)-Cys(23) and Cys(56)-Cys(57), a unique disulfide structure of polypeptide that has not been documented previously.	Disulfides	150-159	complement C3	Homo sapiens	62-65
12189047-3	2002	Thioredoxin (TRX), a small protein with redox-active dithiol/disulfide in the active site, is induced by a variety of oxidative stresses and secreted from the cells.	Disulfides	61-70	thioredoxin	Homo sapiens	13-16
26014136-3	2015	Reduced pancreatic ribonuclease A (rRNase), avian lysozyme, and riboflavin binding protein are all competent substrates of the Mia40/lfALR system, although they lack those sequence features previously thought to direct disulfide bond formation in cognate IMS substrates.	Disulfides	219-228	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	127-132
11747437-6	2001	Homology modeling of the LDL-R EGF domain revealed that the third disulfide loop is larger and more flexible than the equivalent loop in the factor IX EGF domain.	Disulfides	66-75	low density lipoprotein receptor	Homo sapiens	25-30
11749971-1	2001	We determined the position of a disulfide bridge in ZmERabp1 by mass-spectrometric analysis.	Disulfides	32-41	auxin-binding protein 1	Zea mays	52-60
25998848-3	2015	In the present study, we analyzed the effects of the natural disulfide compound lipoic acid (LA) on MGMT in vitro and in colorectal cancer cells.	Disulfides	61-70	O-6-methylguanine-DNA methyltransferase	Homo sapiens	100-104
19076451-4	2008	Mia40 is a protein in the intermembrane space that directly binds newly imported proteins via disulfide bonds.	Disulfides	94-103	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
19076451-5	2008	By reorganization of these bonds, intramolecular disulfide bonds are formed in the imported proteins, which are thereby released from Mia40 into the intermembrane space.	Disulfides	49-58	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	134-139
11749971-4	2001	Due to the high homology among all characterized ABPs, the information on the disulfide bonds will be important for functional analysis of recombinantly expressed ABP1.	Disulfides	78-87	auxin-binding protein 1	Zea mays	163-167
11750057-7	2001	In addition, mutational analysis of His(6)-p15 demonstrated that both intramolecular disulfide bonds are essential for its biological activity.	Disulfides	85-94	cyclin-dependent kinase inhibitor 2B	Rattus norvegicus	43-46
25839391-3	2015	The liposomes form a disulfide bond with activated complement C3 after intravenous injection and are taken up by G-MDSCs, which express the receptor for activated C3.	Disulfides	21-30	complement C3	Homo sapiens	51-64
11705765-10	2001	Inhibition of disulfide bond formation by thioredoxin or thioredoxin reductase significantly decreased xanthine/xanthine oxidase-induced activation of renal 5"-ND.	Disulfides	14-23	thioredoxin	Homo sapiens	42-53
26158899-1	2015	Quiescin sulfhydryl oxidase 1 (QSOX1) is a highly conserved disulfide bond-generating enzyme that is overexpressed in diverse tumor types.	Disulfides	60-69	quiescin sulfhydryl oxidase 1	Homo sapiens	0-29
26158899-1	2015	Quiescin sulfhydryl oxidase 1 (QSOX1) is a highly conserved disulfide bond-generating enzyme that is overexpressed in diverse tumor types.	Disulfides	60-69	quiescin sulfhydryl oxidase 1	Homo sapiens	31-36
26132214-3	2015	The PKG Ialpha LZ contains C42 that is known to form a disulfide bond upon oxidation and to activate PKG Ialpha.	Disulfides	55-64	CDK5 regulatory subunit associated protein 1	Homo sapiens	27-30
26132214-4	2015	To understand the molecular details of the PKG Ialpha LZ and C42-C42" disulfide bond, we determined crystal structures of the PKG Ialpha wild-type (WT) LZ and C42L LZ.	Disulfides	70-79	CDK5 regulatory subunit associated protein 1	Homo sapiens	61-64
11705765-10	2001	Inhibition of disulfide bond formation by thioredoxin or thioredoxin reductase significantly decreased xanthine/xanthine oxidase-induced activation of renal 5"-ND.	Disulfides	14-23	thioredoxin	Homo sapiens	57-68
26132214-4	2015	To understand the molecular details of the PKG Ialpha LZ and C42-C42" disulfide bond, we determined crystal structures of the PKG Ialpha wild-type (WT) LZ and C42L LZ.	Disulfides	70-79	CDK5 regulatory subunit associated protein 1	Homo sapiens	65-68
26132214-5	2015	Our data demonstrate that the C42-C42" disulfide bond dramatically stabilizes PKG Ialpha and that the C42L mutant mimics the oxidized WT LZ structurally.	Disulfides	39-48	CDK5 regulatory subunit associated protein 1	Homo sapiens	30-33
11766986-4	2001	The members of heterodimeric amino acid transporter family are linked via a disulfide bond to single membrane spanning type II membrane glycoproteins such as 4F2hc (4F2 heavy chain) and rBAT (related to b(0,+)-amino acid transporter).	Disulfides	76-85	solute carrier family 3 member 2	Homo sapiens	158-163
26132214-5	2015	Our data demonstrate that the C42-C42" disulfide bond dramatically stabilizes PKG Ialpha and that the C42L mutant mimics the oxidized WT LZ structurally.	Disulfides	39-48	CDK5 regulatory subunit associated protein 1	Homo sapiens	34-37
11766986-4	2001	The members of heterodimeric amino acid transporter family are linked via a disulfide bond to single membrane spanning type II membrane glycoproteins such as 4F2hc (4F2 heavy chain) and rBAT (related to b(0,+)-amino acid transporter).	Disulfides	76-85	solute carrier family 3 member 2	Homo sapiens	165-180
25860033-3	2015	The TSHR HR contains a C-peptide segment that is removed during spontaneous TSHR intramolecular cleavage into disulfide linked A- and B-subunits.	Disulfides	110-119	thyroid stimulating hormone receptor	Homo sapiens	4-8
11707400-3	2001	Here we show that both human Ero1-Lalpha and Ero1-Lbeta (hEROs) facilitate disulfide bond formation in immunoglobulin subunits by selectively oxidizing PDI.	Disulfides	75-84	peptidyl arginine deiminase 1	Homo sapiens	152-155
25860033-3	2015	The TSHR HR contains a C-peptide segment that is removed during spontaneous TSHR intramolecular cleavage into disulfide linked A- and B-subunits.	Disulfides	110-119	thyroid stimulating hormone receptor	Homo sapiens	76-80
11707400-4	2001	Disulfide bond formation is controlled by hEROs, which stand at a crucial point of an electron-flow starting from nascent secretory proteins and passing through PDI.	Disulfides	0-9	peptidyl arginine deiminase 1	Homo sapiens	161-164
25708449-3	2015	NPGL is amidated at its C-terminus, contains an intramolecular disulfide bond, and is hydrophobic in nature.	Disulfides	63-72	family with sequence similarity 237 member A	Rattus norvegicus	0-4
25708449-6	2015	Furthermore, the disulfide bond of NPGL was formed with 20% yield with the use of glutathione-containing redox buffer and 50% acetonitrile.	Disulfides	17-26	family with sequence similarity 237 member A	Rattus norvegicus	35-39
11673531-6	2001	Likewise, we found that two of the intrachain disulfide bridges (Cys(13):Cys(101) and Cys(109):Cys(134)) were also required for the binding of pIgA to SC but, interestingly, not for IgA polymerization.	Disulfides	46-55	phosphatidylinositol glycan anchor biosynthesis class A	Homo sapiens	143-147
25798457-1	2015	We developed a real-time drug-reporting conjugate (CPT-SS-CyN) composed of a near-infrared (NIR) fluorescent cyanine-amine dye (CyN), a disulfide linker, and a model therapeutic drug (camptothecin, CPT).	Disulfides	136-145	choline phosphotransferase 1	Homo sapiens	51-54
11764282-1	2001	An important constituent of the cellular antioxidant buffering system that controls the redox state of proteins is thioredoxin (TRX), a 13 kDa protein that catalyzes thiol-disulfide exchange reactions, regulates activation of transcription factors, and possesses several other biologic functions similar to cytokines.	Disulfides	172-181	thioredoxin	Homo sapiens	115-126
25758790-1	2015	The insulin receptor (IR) and insulin-like growth factor-1 receptor (IGF1R) are highly related receptor tyrosine kinases with a disulfide-linked homodimeric architecture.	Disulfides	128-137	insulin like growth factor 1 receptor	Homo sapiens	69-74
11764282-1	2001	An important constituent of the cellular antioxidant buffering system that controls the redox state of proteins is thioredoxin (TRX), a 13 kDa protein that catalyzes thiol-disulfide exchange reactions, regulates activation of transcription factors, and possesses several other biologic functions similar to cytokines.	Disulfides	172-181	thioredoxin	Homo sapiens	128-131
11557028-11	2001	In Western blot analysis, hLAT1 and h4F2hc have been confirmed to be linked to each other via a disulfide bond in T24 human bladder carcinoma cells.	Disulfides	96-105	solute carrier family 7 member 5	Homo sapiens	26-31
25886739-3	2015	Human tPA is composed of 527 amino acids residues and contains 17 disulfide bonds.	Disulfides	66-75	chromosome 20 open reading frame 181	Homo sapiens	6-9
25886739-5	2015	However, the functional expression of full-length tPA that contains multiple disulfide bonds on an industrial scale remains challenging.	Disulfides	77-86	chromosome 20 open reading frame 181	Homo sapiens	50-53
25886739-9	2015	In addition, similar yields of recombinant protein were produced at temperatures of 33, 35, and 37 C. The E. coli strain origami 2 could increase disulfide bond formation in cytoplasmic tPA and produce purified soluble recombinant protein (~0.9 mg/l medium).	Disulfides	146-155	chromosome 20 open reading frame 181	Homo sapiens	186-189
11557028-11	2001	In Western blot analysis, hLAT1 and h4F2hc have been confirmed to be linked to each other via a disulfide bond in T24 human bladder carcinoma cells.	Disulfides	96-105	solute carrier family 3 member 2	Homo sapiens	37-42
11533296-5	2001	Na(+)-independent glutamine transporter genes encoding for System L (LAT1, LAT2) and System b(0,+) (b(0,+)AT) have also been recently isolated, and similar to y(+)L, have been shown to function as disulfide-linked heterodimers with the 4F2 heavy chain (CD98) or rBAT (related to b(0,+) amino acid transporter).	Disulfides	197-206	solute carrier family 7 member 5	Homo sapiens	69-73
25533459-4	2015	Proteolytic inhibition requires covalent binding of STC2 to PAPP-A and is mediated by a disulfide bond, which involves Cys-120 of STC2.	Disulfides	88-97	stanniocalcin 2	Homo sapiens	130-134
25699251-4	2015	Using a peptide-protein binding assay, we found that Nox2 peptides containing a (369)CysGlyCys(371) triad (CGC) bound p67 (phox) with high affinity, dependent upon the establishment of a disulfide bond between the two cysteines.	Disulfides	187-196	cytochrome b-245 beta chain	Homo sapiens	53-57
25699251-7	2015	This led to the hypothesis that Nox2 establishes disulfide bonds with p67 (phox) via a thiol-dilsulfide exchange reaction and, thus, functions as a PDI.	Disulfides	49-58	cytochrome b-245 beta chain	Homo sapiens	32-36
11511095-0	2001	Disulfide bridge conformers of mature BMP are inhibitors for heterotopic ossification.	Disulfides	0-9	bone morphogenetic protein 1	Homo sapiens	38-41
25699251-9	2015	We propose a model of oxidase assembly in which binding of p67 (phox) to Nox2 via disulfide bonds, by virtue of the intrinsic PDI activity of Nox2, stabilizes the primary interaction between the two components.	Disulfides	82-91	cytochrome b-245 beta chain	Homo sapiens	73-77
25205735-5	2015	The autoantibody only recognizes the nonreduced form of PLA2R, suggesting that disulfide bonds determine the antigenic epitope conformation.	Disulfides	79-88	phospholipase A2 receptor 1	Homo sapiens	56-61
11511095-4	2001	Stable BMP variants derived from the identical amino acid sequence but with different disulfide bridge configurations have been investigated and found to be capable of inhibiting ossification in vitro and in vivo in rodents.	Disulfides	86-95	bone morphogenetic protein 1	Homo sapiens	7-10
11481439-7	2001	A model of the complex of TrxR with Trx suggests that electron transfer from NADPH to the disulfide of the substrate is possible without large conformational changes.	Disulfides	90-99	thioredoxin	Homo sapiens	26-29
11481439-8	2001	The C-terminal extension typical of mammalian TrxRs has two functions: (i) it extends the electron transport chain from the catalytic disulfide to the enzyme surface, where it can react with Trx, and (ii) it prevents the enzyme from acting as a GR by blocking the redox-active disulfide.	Disulfides	134-143	thioredoxin	Homo sapiens	46-49
11481439-8	2001	The C-terminal extension typical of mammalian TrxRs has two functions: (i) it extends the electron transport chain from the catalytic disulfide to the enzyme surface, where it can react with Trx, and (ii) it prevents the enzyme from acting as a GR by blocking the redox-active disulfide.	Disulfides	277-286	thioredoxin	Homo sapiens	46-49
25392302-2	2015	The main component of this pathway is the oxidoreductase Mia40, which introduces disulfides into its substrates.	Disulfides	81-91	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	57-62
11488928-8	2001	The two protein fragments of nicked or gapped alpha-LA are covalently linked by the four disulfide bridges of the native protein.	Disulfides	89-98	lactalbumin alpha	Bos taurus	46-54
11491658-0	2001	Osmotic stress-mediated activation of RET kinases involves intracellular disulfide-bonded dimer formation.	Disulfides	73-82	ret proto-oncogene	Homo sapiens	38-41
25149918-7	2015	In a recent promising step in therapeutic drug development, allosteric, disulfide-tethered fragments successfully modulated the activity of a protein kinase and K-Ras.	Disulfides	72-81	KRAS proto-oncogene, GTPase	Homo sapiens	161-166
24988310-5	2015	AIMS: We prove the hypothesis that this cysteine motif forms a redox-sensitive intramolecular disulfide bridge and, hence, the claudin-1-ECL1 constitutes a functional structure which is associated to ECLs of this and other TJ proteins.	Disulfides	94-103	claudin 1	Homo sapiens	127-136
24988310-11	2015	INNOVATION: The structural and functional model based on our in vitro and in vivo investigations suggested that claudin-1-ECL1 constitutes a functional and ECL-binding beta-sheet, stabilized by a shielded and redox-sensitive disulfide bond.	Disulfides	225-234	claudin 1	Homo sapiens	112-121
11491658-2	2001	A few percentage of RET proteins normally formed disulfide-bonded dimers in the cell, and osmotic stress promoted formation of these dimers.	Disulfides	49-58	ret proto-oncogene	Homo sapiens	20-23
11491658-4	2001	Osmotic stress also promoted activation and disulfide-bonded dimerization of the extracellular domain-depleted mutant RET (RET-PTC-1), suggesting that the target amino acid(s) for dimerization is located intracellularly rather than in the cysteine-rich region of the extracellular domain.	Disulfides	44-53	ret proto-oncogene	Homo sapiens	118-121
11491658-4	2001	Osmotic stress also promoted activation and disulfide-bonded dimerization of the extracellular domain-depleted mutant RET (RET-PTC-1), suggesting that the target amino acid(s) for dimerization is located intracellularly rather than in the cysteine-rich region of the extracellular domain.	Disulfides	44-53	ret proto-oncogene	Homo sapiens	123-126
26549544-12	2015	Immunologically, Vnn1 expression may influence cell signaling indirectly through maintenance of disulfide bonds or directly by interaction of pantetheinase on the cell surface.	Disulfides	96-105	vanin 1	Mus musculus	17-21
11294649-9	2001	These results demonstrate that hGST P1-1 is inactivated by 4-OHEN through two possible mechanisms: (1) covalent modification of cysteine residues and (2) oxidative damage leading to proteins inactivated by disulfide bond formation.	Disulfides	206-215	glutathione S-transferase pi 1	Homo sapiens	31-40
25481286-2	2015	In cell culture studies, this mutation leads to inefficient F3 secretion and higher intracellular steady state levels, likely due to F3 disulfide bonding and/or protein folding problems.	Disulfides	136-145	EGF containing fibulin extracellular matrix protein 1	Homo sapiens	60-62
25481286-2	2015	In cell culture studies, this mutation leads to inefficient F3 secretion and higher intracellular steady state levels, likely due to F3 disulfide bonding and/or protein folding problems.	Disulfides	136-145	EGF containing fibulin extracellular matrix protein 1	Homo sapiens	133-135
11361145-5	2001	Lungfish Lb-FABP is one of the two FABPs reported to have a disulfide bridge.	Disulfides	60-69	liver basic fatty acid binding protein	Gallus gallus	9-16
25286400-1	2015	Stem cell factor (SCF) known as the c-kit ligand is a two disulfide bridge-containing cytokine in the regulation of the development and function of hematopoietic cell lineages and other cells such as mast cells, germ cells, and melanocytes.	Disulfides	58-67	KIT ligand	Homo sapiens	0-16
25286400-1	2015	Stem cell factor (SCF) known as the c-kit ligand is a two disulfide bridge-containing cytokine in the regulation of the development and function of hematopoietic cell lineages and other cells such as mast cells, germ cells, and melanocytes.	Disulfides	58-67	KIT ligand	Homo sapiens	18-21
25286400-1	2015	Stem cell factor (SCF) known as the c-kit ligand is a two disulfide bridge-containing cytokine in the regulation of the development and function of hematopoietic cell lineages and other cells such as mast cells, germ cells, and melanocytes.	Disulfides	58-67	KIT ligand	Homo sapiens	36-48
25551757-6	2014	The cysteine residues involved in the formation of the disulfide bridges in CD9 EC2 were all essential for inhibitory activity but a conserved glycine residue in the tetraspanin-defining "CCG" motif was not.	Disulfides	55-64	CD9 molecule	Homo sapiens	76-79
19075641-1	2008	The regulation of cellular reduction/oxidation (redox) balance is critically determined by several antioxidant systems such as the thioredoxin-1 (Trx-1) which reduces disulfides on targeted proteins.	Disulfides	167-177	thioredoxin 1	Mus musculus	131-144
19075641-1	2008	The regulation of cellular reduction/oxidation (redox) balance is critically determined by several antioxidant systems such as the thioredoxin-1 (Trx-1) which reduces disulfides on targeted proteins.	Disulfides	167-177	thioredoxin 1	Mus musculus	146-151
11275557-7	2001	The synthetic and intramolecularly disulfide-linked peptides of C27 and G25 (sC27 and sG25) also inhibited the chemotaxis induced by MCP-1, while their derivatives with serine in place of cysteine did not, suggesting the importance of the loop structure for the inhibition.	Disulfides	35-44	C-C motif chemokine ligand 2	Homo sapiens	133-138
18817872-5	2008	The levels of disulfide-reduced SOD1 peaked at the end stage of the disease, whereas protein disulfide isomerase (PDI), a chaperone capable of rearranging disulfide bonds between cysteine residues of SOD1, was increased prior to the end stage.	Disulfides	93-102	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	114-117
25545749-0	2014	Evidence for thiol/disulfide exchange reactions between tubulin and glyceraldehyde-3-phosphate dehydrogenase.	Disulfides	19-28	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	68-108
25545749-2	2014	Both tubulin and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) contain multiple cysteines that have been identified as targets for oxidation to disulfides, S-nitrosation and S-glutathionylation.	Disulfides	147-157	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	17-57
25545749-2	2014	Both tubulin and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) contain multiple cysteines that have been identified as targets for oxidation to disulfides, S-nitrosation and S-glutathionylation.	Disulfides	147-157	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	59-64
25545749-4	2014	We detected a threefold to fourfold increase in tubulin cysteine oxidation by hydrogen peroxide in the presence of rabbit muscle GAPDH by 5-iodoacetamidofluorescein labeling and by Western blot detection of higher molecular weight inter-chain tubulin disulfides.	Disulfides	251-261	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	129-134
25545749-5	2014	In thiol/disulfide exchange experiments, tubulin restored ~50% of oxidized GAPDH cysteines and the equilibrium favored reduced GAPDH.	Disulfides	9-18	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	75-80
25545749-5	2014	In thiol/disulfide exchange experiments, tubulin restored ~50% of oxidized GAPDH cysteines and the equilibrium favored reduced GAPDH.	Disulfides	9-18	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	127-132
11264342-5	2001	The release of E1 from the interaction with calnexin coincides with the beginning of E1 and E2 association into disulfide-linked heterodimers.	Disulfides	112-121	small nucleolar RNA, H/ACA box 73A	Homo sapiens	85-93
25545749-9	2014	Because the extent of tubulin repair of oxidized GAPDH was dependent on buffer strength, we conclude that electrostatics influence thiol/disulfide exchange between the two proteins.	Disulfides	137-146	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	49-54
25258311-2	2014	Ero1alpha oxidizes PDI to introduce disulfides into substrates, and PDI can feedback-regulate Ero1alpha activity.	Disulfides	36-46	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	0-9
18976165-15	2008	CONCLUSIONS: From these data, we proposed Cys 398 as a stable disulfide bond partner of Cys 283, corroborating with a model based on evolutionary history of TSHR across species.	Disulfides	62-71	thyroid stimulating hormone receptor	Homo sapiens	157-161
11152479-5	2001	Using recombinant proteins expressed in Escherichia coli, we demonstrated the activity of the Trx domain of TMX to cleave the interchain disulfide bridges in insulin in vitro.	Disulfides	137-146	thioredoxin	Homo sapiens	94-97
19007302-5	2008	There are two cysteine residues within the hydrophobic N terminus of SP-D that are critical for multimer assembly and have been proposed to be involved in stabilizing disulfide bonds.	Disulfides	167-176	surfactant protein D	Homo sapiens	69-73
25258311-3	2014	Here, we show the regulatory disulfide of Ero1alpha responds to the redox fluctuation in ER very sensitively, relying on the availability of redox active PDI.	Disulfides	29-38	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	42-51
25349987-3	2014	We detected two disulfide bonds, Cys250-Cys32 and Cys368-Cys369, in hAS3MT.	Disulfides	16-25	arsenite methyltransferase	Homo sapiens	68-74
18662787-2	2008	Native BLG contains two disulfide bonds and one free cysteine at position 121.	Disulfides	24-33	beta-lactoglobulin	Bos taurus	7-10
11259642-5	2001	TGR can reduce Trx, GSSG, and a GSH-linked disulfide in in vitro assays.	Disulfides	43-52	thioredoxin reductase 3	Homo sapiens	0-3
11259642-7	2001	These observations, together with the biochemical probing and molecular modeling of the TGR structure, suggest a mechanism whereby the C-terminal selenotetrapeptide serves a role of a protein-linked GSSG and shuttles electrons from the disulfide center within the TR domain to either the glutaredoxin domain or Trx.	Disulfides	236-245	thioredoxin reductase 3	Homo sapiens	88-91
11297410-0	2001	Effect of the disulfide bridge and the C-terminal extension on the oligomerization of the amyloid peptide ABri implicated in familial British dementia.	Disulfides	14-23	integral membrane protein 2B	Homo sapiens	106-110
18667425-4	2008	Chemical reduction of up to half of these disulfides was compatible with anti-E2 monoclonal antibody reaction, CD81 receptor binding, and viral entry, whereas complete reduction abrogated these properties.	Disulfides	42-52	CD81 molecule	Homo sapiens	111-115
25242142-4	2014	Activation of Get3"s chaperone function, which is a fully reversible process, involves disulfide bond formation, metal release, and its conversion into distinct, higher oligomeric structures.	Disulfides	87-96	guanine nucleotide exchange factor GET3	Saccharomyces cerevisiae S288C	14-18
25265386-2	2014	Thioredoxin-1 (Trx1) is a thiol antioxidant protecting against non-radical oxidants by controlling protein thiol/disulfide status; Trx1 translocates from cytoplasm to cell nuclei due to stress signaling, facilitates DNA binding of transcription factors, e.g., NF-kappaB, and potentiates inflammatory signaling.	Disulfides	113-122	thioredoxin 1	Mus musculus	0-13
18509164-9	2008	These results strongly suggest that cleavage of disulfide bonds in HK1S dimers contributes to the increases in HK activity and motility that occur when mouse sperm become activated.	Disulfides	48-57	hexokinase 1	Mus musculus	67-71
25265386-2	2014	Thioredoxin-1 (Trx1) is a thiol antioxidant protecting against non-radical oxidants by controlling protein thiol/disulfide status; Trx1 translocates from cytoplasm to cell nuclei due to stress signaling, facilitates DNA binding of transcription factors, e.g., NF-kappaB, and potentiates inflammatory signaling.	Disulfides	113-122	thioredoxin 1	Mus musculus	15-19
11297410-6	2001	Here we demonstrate that the intramolecular disulfide bond in ABri and the C-terminal extension are required to elongate initially formed dimers to oligomers and fibrils.	Disulfides	44-53	integral membrane protein 2B	Homo sapiens	62-66
11297410-10	2001	A molecular model of ABri containing three beta-strands, and two beta-hairpins annealed by a disulfide bond, has been constructed, and predicts a hydrophobic surface which is instrumental in promoting oligomerization.	Disulfides	93-102	integral membrane protein 2B	Homo sapiens	21-25
11370843-4	2001	Matrilin-3 and matrilin-1 were both present in disulfide-bonded tetrameric components.	Disulfides	47-56	matrilin 3	Homo sapiens	0-10
24983157-5	2014	The stability of the mixed disulfide intermediate is coupled energetically with hydrophobic interactions between Mia40 and the substrate.	Disulfides	27-36	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	113-118
24983157-6	2014	Based on these properties, we suggest a mechanism for Mia40, where the hydrophobic binding site is employed to select a substrate thiol for forming the initial mixed disulfide.	Disulfides	166-175	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	54-59
25135935-3	2014	The lumenally oriented active site CVVC motif in MagT1 is required for glycosylation of STT3B-dependent acceptor sites including those that are closely bracketed by disulfides or contain cysteine as the internal residue (NCT/S).	Disulfides	165-175	magnesium transporter 1	Homo sapiens	49-54
11231292-8	2001	By analogy with the structure of the LTP1, we discussed what structural changes are required to accommodate the LTP2 disulfide pattern.	Disulfides	117-126	non-specific lipid-transfer protein 4.1	Triticum aestivum	37-41
25135935-5	2014	The predominant form of MagT1 in vivo is oxidized, which is consistent with transient formation of mixed disulfides between MagT1 and a glycoprotein substrate to facilitate access of STT3B to unmodified acceptor sites.	Disulfides	105-115	magnesium transporter 1	Homo sapiens	24-29
25135935-5	2014	The predominant form of MagT1 in vivo is oxidized, which is consistent with transient formation of mixed disulfides between MagT1 and a glycoprotein substrate to facilitate access of STT3B to unmodified acceptor sites.	Disulfides	105-115	magnesium transporter 1	Homo sapiens	124-129
18699778-4	2008	Iba2 crystallized as a homodimer stabilized by a disulfide bridge and zinc ions.	Disulfides	49-58	allograft inflammatory factor 1 like	Homo sapiens	0-4
11080501-4	2001	Numbering GA733-2 cysteines sequentially from the N terminus, the first three disulfide linkages are Cys1-Cys4, Cys2-Cys6, and Cys3-Cys5, which is a novel pattern for a cysteine-rich domain instead of the expected epidermal growth factor-like disulfide structure.	Disulfides	78-87	cystin 1	Homo sapiens	101-105
18602640-3	2008	Upon reduction, circular dichroism confirms it spontaneously anneals with its internally complementary sequence to form the hairpin structure: 5"-HS-GCAGATTGCGCAATCTGC 3"-HS-CGTCTAACGCGTTAGACG The specific GFP-C/EBP protein-DNA complex, formed in solution at nM concentrations, could then be recovered (trapped) via thiol-disulfide exchange with a disulfide thiopropyl-Sepharose and eluted with dithiothreitol.	Disulfides	322-331	EBP cholestenol delta-isomerase	Homo sapiens	212-215
18602640-3	2008	Upon reduction, circular dichroism confirms it spontaneously anneals with its internally complementary sequence to form the hairpin structure: 5"-HS-GCAGATTGCGCAATCTGC 3"-HS-CGTCTAACGCGTTAGACG The specific GFP-C/EBP protein-DNA complex, formed in solution at nM concentrations, could then be recovered (trapped) via thiol-disulfide exchange with a disulfide thiopropyl-Sepharose and eluted with dithiothreitol.	Disulfides	348-357	EBP cholestenol delta-isomerase	Homo sapiens	212-215
11080501-4	2001	Numbering GA733-2 cysteines sequentially from the N terminus, the first three disulfide linkages are Cys1-Cys4, Cys2-Cys6, and Cys3-Cys5, which is a novel pattern for a cysteine-rich domain instead of the expected epidermal growth factor-like disulfide structure.	Disulfides	243-252	cystin 1	Homo sapiens	101-105
18573918-6	2008	We show that the substrate protein forms a disulfide-linked complex to Sec61p, suggesting that at least part of the retrotranslocation process involves Sec61p.	Disulfides	43-52	SEC61 translocon subunit alpha 1	Homo sapiens	71-77
18573918-6	2008	We show that the substrate protein forms a disulfide-linked complex to Sec61p, suggesting that at least part of the retrotranslocation process involves Sec61p.	Disulfides	43-52	SEC61 translocon subunit alpha 1	Homo sapiens	152-158
24867629-4	2014	By replacing Val248 and Thr251 with cysteines to create a disulfide bridge, the recombinant lipases reE-PcLipV248C-T251C (expressed in E. coli) and reP-PcLipV248C-T251C (expressed in P. pastoris) were obtained.	Disulfides	58-67	replication protein	Escherichia coli	148-151
25109988-7	2014	The consequences of the regulation of the FOXO4 (forkhead box O4) transcription factor by formation of intermolecular disulfides with both TNPO1 (transportin 1) and p300/CBP [CREB (cAMP-response-element-binding protein)-binding protein] are discussed in more detail.	Disulfides	118-128	cAMP responsive element binding protein 1	Homo sapiens	175-179
11080501-5	2001	The next three disulfide linkages are Cys7-Cys8, Cys9-Cys10, and Cys11-Cys12, consistent with the recently determined disulfide pattern of the thyroglobulin type 1A domain of insulin-like growth factor-binding proteins 1 and 6.	Disulfides	15-24	insulin like growth factor binding protein 1	Homo sapiens	175-226
24888638-3	2014	The flavoenzyme quiescin sulfhydryl oxidase (QSOX), a catalyst of disulfide bond formation with an interdomain electron transfer step in its catalytic cycle, provides a unique opportunity for exploring the structural environment of enzymatic dithiol/disulfide exchange.	Disulfides	66-75	quiescin sulfhydryl oxidase 1	Homo sapiens	45-49
11080501-5	2001	The next three disulfide linkages are Cys7-Cys8, Cys9-Cys10, and Cys11-Cys12, consistent with the recently determined disulfide pattern of the thyroglobulin type 1A domain of insulin-like growth factor-binding proteins 1 and 6.	Disulfides	118-127	insulin like growth factor binding protein 1	Homo sapiens	175-226
11288979-1	2001	Cleavage of thyrotropin receptors (TSHR) on the cell surface into disulfide-linked A and B subunits involves deletion of an intervening region that corresponds approximately to a 50 amino acid "insertion" in the TSHR relative to the noncleaving luteinizing hormone/choriogonadotropin receptor (LH/CGR).	Disulfides	66-75	luteinizing hormone/choriogonadotropin receptor	Homo sapiens	245-292
24636884-2	2014	Peroxiredoxin 2 (Prx2) is a major antioxidant enzyme that requires NADPH to recycle its oxidized (disulfide-bonded) form.	Disulfides	98-107	2,4-dienoyl-CoA reductase 1	Homo sapiens	67-72
24515105-0	2014	Ectodomain movements of an ATP-gated ion channel (P2X2 receptor) probed by disulfide locking.	Disulfides	75-84	purinergic receptor P2X 2	Rattus norvegicus	50-54
18358819-3	2008	We have successfully determined the disulfide linkages for Fn14 and independently confirmed those of the IgV domain of TIM-1, whose crystal structure was published recently.	Disulfides	36-45	hepatitis A virus cellular receptor 1	Homo sapiens	119-124
18593333-5	2008	Functional IL-12 is a heterodimer consisting of two disulfide-linked subunits, p35 and p40.	Disulfides	52-61	interleukin 12b	Mus musculus	87-90
11288979-1	2001	Cleavage of thyrotropin receptors (TSHR) on the cell surface into disulfide-linked A and B subunits involves deletion of an intervening region that corresponds approximately to a 50 amino acid "insertion" in the TSHR relative to the noncleaving luteinizing hormone/choriogonadotropin receptor (LH/CGR).	Disulfides	66-75	luteinizing hormone/choriogonadotropin receptor	Homo sapiens	294-300
11231127-8	2001	Interestingly, inhibiting TM self assembly in the constitutively active mutant EpoR R129C abrogates formation of disulfide-linked receptor homodimers and consequently results in the loss of ligand-independent signal transduction.	Disulfides	113-122	erythropoietin receptor	Mus musculus	79-83
11169440-2	2001	The tertiary structure of the C-terminal region of MSP-1 is maintained by five disulfide bonds.	Disulfides	79-88	salivary protein electrophoretic 1, regulator	Mus musculus	51-56
18096690-15	2008	Notably, G120R-G120R, despite its lack of an intact site 2 in either dimer partner, also promoted GHR disulfide linkage and JAK2 and STAT5 activation, albeit less potently than either GH or GH-GH.	Disulfides	102-111	growth hormone receptor	Homo sapiens	98-101
18164270-4	2008	Increased H2O2 triggers peroxiredoxin overoxidation to a sulphinic acid; however during apoptosis peroxiredoxin 3 was captured as a disulfide, suggesting impairment of the thioredoxin system responsible for maintaining peroxiredoxin 3 in its reduced form.	Disulfides	132-141	peroxiredoxin 3	Homo sapiens	98-113
18032414-2	2008	Using an Escherichia coli expression system, we have successfully expressed and purified the C-terminal biotinylated extracellular domain of human RAGE (hsRAGE), which consists of three immunoglobulin-like domains carrying three putative disulfide bonds.	Disulfides	238-247	advanced glycosylation end-product specific receptor	Homo sapiens	147-151
18039656-2	2008	The formation of a mixed disulfide between the heavy chain of Class I and components of the loading complex (ERp57, protein disulfide isomerase, and tapasin) suggests that these molecules are involved in the redox regulation of components during assembly and peptide loading.	Disulfides	25-34	thioredoxin domain containing 15	Homo sapiens	124-143
24515105-4	2014	In the present work, we examined this opening model by introducing pairs of cysteines into the rat P2X2 receptor that might form disulfide bonds within or between subunits.	Disulfides	129-138	purinergic receptor P2X 2	Rattus norvegicus	99-103
24569988-1	2014	Mia40-catalyzed disulfide formation drives the import of many proteins into the mitochondria.	Disulfides	16-25	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
24569988-4	2014	Mia40 accelerates Cox19 folding through the specific recognition of the third Cys in the second helical CX9C motif and the subsequent oxidation of the inner disulfide bond.	Disulfides	157-166	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
24569988-4	2014	Mia40 accelerates Cox19 folding through the specific recognition of the third Cys in the second helical CX9C motif and the subsequent oxidation of the inner disulfide bond.	Disulfides	157-166	cytochrome c oxidase assembly factor COX19	Homo sapiens	18-23
11169440-4	2001	CD4(+) T cell hybridomas took longer to recognize an epitope derived from the disulfide-bonded region whether native parasite or recombinant MSP-1 antigen was used.	Disulfides	78-87	salivary protein electrophoretic 1, regulator	Mus musculus	141-146
24403586-14	2014	The Env folding process involves extensive cross-linking of 10 Cys residues by disulfide bond formation and heavy N-glycosylation on ~30 Asn residues.	Disulfides	79-88	endogenous retrovirus group K member 20	Homo sapiens	4-7
11108290-4	2000	To address this issue, we deleted two disulfide bonds in the FSHbeta domain: cys 20-104 and cys 28-82, which correspond to the disulfide bonds 26-110 and 34-88, respectively, in the CGbeta-subunit.	Disulfides	38-47	follicle stimulating hormone subunit beta	Homo sapiens	61-68
24415753-2	2014	The aim of this study was to explain whether protein disulfide isomerase (PDI) is responsible for the thiol-disulfide rearrangement in the beta-actin molecule of adhering cells.	Disulfides	53-62	POTE ankyrin domain family member F	Homo sapiens	139-149
24415753-3	2014	First, we showed that PDI forms a disulfide-bonded complex with beta-actin with a molecular mass of 110 kDa.	Disulfides	34-43	POTE ankyrin domain family member F	Homo sapiens	64-74
24415753-10	2014	Our data suggest that PDI is released from subcellular compartments to the cytosol and translocated toward the periphery of the cell, where it forms a disulfide bond with beta-actin when MEG-01 cells adhere via the alphaIIbbeta3 integrin to fibronectin.	Disulfides	151-160	POTE ankyrin domain family member F	Homo sapiens	171-181
24415753-11	2014	Thus, PDI appears to regulate cytoskeletal reorganization by the thiol-disulfide exchange in beta-actin via a redox-dependent mechanism.	Disulfides	71-80	POTE ankyrin domain family member F	Homo sapiens	93-103
18166059-1	2008	The oxidative folding of bovine pancreatic trypsin inhibitor (BPTI) has served as a paradigm for the folding of disulfide-containing proteins from their reduced form, as well as for protein folding in general.	Disulfides	112-121	spleen trypsin inhibitor I	Bos taurus	62-66
18166059-3	2008	Under traditional conditions, 0.125 mM glutathione disulfide (GSSG) and no glutathione (GSH), the folding pathway of BPTI proceeds through a nonproductive route via N* (a two disulfide intermediate), or a productive route via N" (and other two disulfide intermediates which are in rapid equilibrium with N").	Disulfides	51-60	spleen trypsin inhibitor I	Bos taurus	117-121
18166059-3	2008	Under traditional conditions, 0.125 mM glutathione disulfide (GSSG) and no glutathione (GSH), the folding pathway of BPTI proceeds through a nonproductive route via N* (a two disulfide intermediate), or a productive route via N" (and other two disulfide intermediates which are in rapid equilibrium with N").	Disulfides	175-184	spleen trypsin inhibitor I	Bos taurus	117-121
11108290-4	2000	To address this issue, we deleted two disulfide bonds in the FSHbeta domain: cys 20-104 and cys 28-82, which correspond to the disulfide bonds 26-110 and 34-88, respectively, in the CGbeta-subunit.	Disulfides	127-136	follicle stimulating hormone subunit beta	Homo sapiens	61-68
17637825-5	2008	We show that the target antigen p200 is synthesized by both keratinocytes and fibroblasts, is disulfide-bonded, and participates in calcium-dependent molecular interactions.	Disulfides	94-103	AT-rich interaction domain 2	Homo sapiens	32-36
11087419-2	2000	Both mixed disulfides react with the skeletal myosin motor domain (S-1) as actin site-directed agents and label exclusively and stoichiometrically Cys 540 in the hydrophobic strong actin binding helix-loop-helix motif, causing only a 1.9-2.4-fold decrease in the V(max) for acto-S-1 ATPase.	Disulfides	11-21	myosin heavy chain 14	Homo sapiens	46-52
24573035-2	2014	Past efforts to investigate their functions have been limited by the difficulty of purifying correctly folded CRISPs from bacterial expression systems, which yield low quantities of correctly folded protein containing the eight disulfide bonds that define the CRISP family.	Disulfides	228-237	cysteine rich secretory protein 3	Homo sapiens	110-116
24573035-2	2014	Past efforts to investigate their functions have been limited by the difficulty of purifying correctly folded CRISPs from bacterial expression systems, which yield low quantities of correctly folded protein containing the eight disulfide bonds that define the CRISP family.	Disulfides	228-237	cysteine rich secretory protein 3	Homo sapiens	110-115
17669495-4	2008	Most of the putative N-glycosylation sites, as well as all 10 cysteine residues which are involved in disulfide bond formation in the mature trout clusterin-1 protein, are fully conserved when aligned with its orthologs from various species.	Disulfides	102-111	clusterin	Gallus gallus	147-156
11053035-7	2000	The lack of intersubunit disulfide bonds may contribute to the decreased heparin affinity and lower EC-SOD content in rabbit lung.	Disulfides	25-34	extracellular superoxide dismutase [Cu-Zn]	Oryctolagus cuniculus	100-106
24586769-0	2014	Disulfide linkages in Plasmodium falciparum plasmepsin-i are essential elements for its processing activity and multi-milligram recombinant production yield.	Disulfides	0-9	transmembrane protein 11	Homo sapiens	44-56
24586769-6	2014	We also show that the low preparation yield of purified semi-pro-PM-I with autoprocessing ability is mainly a result of structural instability of the refolded enzyme in acidic conditions due to incomplete formation of disulfide linkages.	Disulfides	218-227	transmembrane protein 11	Homo sapiens	65-69
24586769-7	2014	Upon formation of at least one of the two natural disulfide bonds, nearly all of the refolded semi-pro-PM-I could be activated to its mature form.	Disulfides	50-59	transmembrane protein 11	Homo sapiens	103-107
11035794-0	2000	A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.	Disulfides	87-96	growth factor, augmenter of liver regeneration	Homo sapiens	22-26
24328091-6	2014	The number of disulfide bridges in the extracellular region of a receptor anticorrelates with the range of molecular weights of its antagonists, highlighting the role of the entrance pathway in determining the size selectivity for GPCR antagonists.	Disulfides	14-23	vomeronasal 1 receptor 17 pseudogene	Homo sapiens	231-235
24254994-7	2014	No differences in the abundance of any protein were observed; however, FABP9 in Adcy10-null cauda epididymal spermatozoa contained fewer disulfide bonds than wild-type sperm cells.	Disulfides	137-146	fatty acid binding protein 9, testis	Mus musculus	71-76
18052073-1	2007	Masking amines with Dde and BOC groups provides an alternative to carrying protected alcohols and disulfides through an iterative synthesis.	Disulfides	98-108	BOC cell adhesion associated, oncogene regulated	Homo sapiens	28-31
11035794-0	2000	A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation.	Disulfides	87-96	growth factor, augmenter of liver regeneration	Homo sapiens	27-30
18042705-4	2007	Here, ultrafast 2D-IR vibrational echo spectroscopy is used to examine the constraints an intramolecular disulfide bond places on the structural fluctuations of the protein neuroglobin (Ngb).	Disulfides	105-114	neuroglobin	Homo sapiens	173-184
18042705-4	2007	Here, ultrafast 2D-IR vibrational echo spectroscopy is used to examine the constraints an intramolecular disulfide bond places on the structural fluctuations of the protein neuroglobin (Ngb).	Disulfides	105-114	neuroglobin	Homo sapiens	186-189
11035794-5	2000	When cells were infected with a mutant vaccinia virus in which the E10R gene encoding an ERV1/ALR family protein was repressed, the disulfide bonds of three other viral proteins-namely, the L1R and F9L proteins and the G4L glutaredoxin-were completely reduced.	Disulfides	132-141	growth factor, augmenter of liver regeneration	Homo sapiens	89-93
18042705-8	2007	However, in contrast to Mb, human Ngb has an intramolecular disulfide bond that affects its oxygen affinity and protein stability.	Disulfides	60-69	neuroglobin	Homo sapiens	34-37
18042705-9	2007	By using 2D-IR vibrational echo spectroscopy, we investigated the equilibrium protein dynamics of Ngb-CO by observing the CO spectral diffusion (time dependence of the 2D-IR line shapes) with and without the disulfide bond.	Disulfides	208-217	neuroglobin	Homo sapiens	98-101
24164050-8	2014	Some azoics and disulfides were selected depending on their affinity towards E6 zinc finger and thereby preventing E6-E6AP complex formation.	Disulfides	16-26	ubiquitin protein ligase E3A	Homo sapiens	118-122
18042705-10	2007	Despite the similarity of the linear FTIR spectra of Ngb-CO with and without the disulfide bond, 2D-IR measurements reveal that the equilibrium sampling of different protein configurations is accelerated by disruption of the disulfide bond.	Disulfides	225-234	neuroglobin	Homo sapiens	53-59
24164050-9	2014	Combinatorial nontoxic derivatives of these azoics and disulfides were docked and validated against the oncoprotein to inhibit E6-E6AP interaction.	Disulfides	55-65	ubiquitin protein ligase E3A	Homo sapiens	130-134
11035794-5	2000	When cells were infected with a mutant vaccinia virus in which the E10R gene encoding an ERV1/ALR family protein was repressed, the disulfide bonds of three other viral proteins-namely, the L1R and F9L proteins and the G4L glutaredoxin-were completely reduced.	Disulfides	132-141	growth factor, augmenter of liver regeneration	Homo sapiens	94-97
18042705-11	2007	The observations indicate that the intramolecular disulfide bond in Ngb acts as an inhibitor of fast protein dynamics even though eliminating it does not produce significant conformational change in the protein"s structure.	Disulfides	50-59	neuroglobin	Homo sapiens	68-71
10915799-2	2000	We show that TRP-1 folding process occurs much more rapidly than for tyrosinase, a highly homologous protein, being completed post-translationally by the formation of critical disulfide bonds.	Disulfides	176-185	tyrosinase	Mus musculus	69-79
17945253-4	2007	Site-directed mutagenesis studies show that removal of the intramolecular disulfide or introduction of cysteine residues in CLIC2, equivalent to those that form the intramolecular disulfide in CLIC1, does not cause dimer formation under oxidizing conditions.	Disulfides	180-189	chloride intracellular channel 1	Homo sapiens	193-198
17927979-1	2007	The QSOX1 protein, belonging to a new class of FAD-linked Quiescin/Sulfhydryl oxidase, catalyzes disulfide bond formation.	Disulfides	97-106	quiescin sulfhydryl oxidase 1	Homo sapiens	4-9
24176819-6	2014	The results indicated that the loss of this 3aa patch during evolution was compensated by the duplication of exon 4 in mammalian p35 to gain another cysteine residue to form a disulfide bond, evidenced by chicken p35 which does not contain NCF corresponding 3-aa patch nor exon 4 duplication.	Disulfides	176-185	interleukin 12A	Homo sapiens	129-132
10842180-4	2000	Using recombinant Dpl expressed in Escherichia coli and mouse neuroblastoma cells we demonstrate that wild type (wt) Dpl, like PrP(C), adopts a predominantly alpha-helical conformation, forms intramolecular disulfide bonds, has two N-linked oligosaccharides, and is presented on the cell surface via a glycosylphosphatidylinositol anchor.	Disulfides	207-216	prion like protein doppel	Mus musculus	117-120
17711389-5	2007	Here the authors demonstrate that PDI-1, PDI-2, and PDI-3 show comparable kinetic properties in catalyzing thiol:disulfide exchange reactions in two simple peptide-based assays.	Disulfides	113-122	Protein disulfide-isomerase 2	Caenorhabditis elegans	41-46
10964700-5	2000	Mouse EC-SOD exists primarily as a homotetramer composed of a pair of dimers linked through disulfide bonds present in the heparin-binding domains of each subunit.	Disulfides	92-101	superoxide dismutase 3, extracellular	Mus musculus	6-12
17644369-11	2007	These results suggest that the correct processing of haptoglobin (glycosylation, disulfide linkage, folding, and assembly) might be sensitive to ER stress and that, in the absence of GRP78-mediated assistance, Hp is degraded.	Disulfides	81-90	haptoglobin	Mus musculus	53-64
17890311-6	2007	Our studies show that CIII exists as a dimer under native conditions, aided by an intersubunit disulfide bond, which is dispensable for dimerization.	Disulfides	95-104	cIII	Escherichia virus Lambda	22-26
10783391-6	2000	Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.	Disulfides	94-103	glutathione S-transferase kappa 1	Homo sapiens	23-27
10897033-5	2000	Immunoprecipitation with B3 revealed that exogenous rat CD98HC proteins were associated with endogenous mouse CD98LC by a disulfide bond in BrH/Wild and C325S, but not in C103S and 103/325 transfectants.	Disulfides	122-131	solute carrier family 3 member 2	Homo sapiens	56-62
10897033-5	2000	Immunoprecipitation with B3 revealed that exogenous rat CD98HC proteins were associated with endogenous mouse CD98LC by a disulfide bond in BrH/Wild and C325S, but not in C103S and 103/325 transfectants.	Disulfides	122-131	solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2	Mus musculus	56-60
10897033-9	2000	These findings indicate that over-expression of CD98HC and its disulfide-linkage with CD98LC at the cell surface result in malignant transformation of murine fibroblasts.	Disulfides	63-72	solute carrier family 3 member 2	Homo sapiens	48-54
17869268-6	2007	The model also suggested the formation of an additional disulfide bridge in the alpha3 domain of UL18 between residues C240 and C255, not present in MHC-I.	Disulfides	56-65	membrane glycoprotein UL18	Human betaherpesvirus 5	97-101
10963989-7	2000	The gC1q domain of EMILIN-1 can form relatively stable and compact homotrimers and this association is then followed by a multimeric assembly of disulfide-bonded protomers.	Disulfides	145-154	elastin microfibril interfacer 1	Homo sapiens	19-27
17766010-4	2007	From all shorter peptides tested, only CART(74-86) and CART(62-86) containing disulfide bridges kept partial binding potency of the original molecule with K(i) in 10(-5) and 10(-4)M range.	Disulfides	78-87	CART prepropeptide	Rattus norvegicus	55-59
17766010-6	2007	The results showed that a compact structure containing three disulfide bridges is necessary for preservation of full biological activity of CART peptides.	Disulfides	61-70	CART prepropeptide	Rattus norvegicus	140-144
10751410-4	2000	Analysis of mutant human PrxV proteins in which each of these three Cys residues was individually replaced with serine suggested that the sulfhydryl group of Cys(48) is the site of oxidation by peroxides and that oxidized Cys(48) reacts with the sulfhydryl group of Cys(152) to form an intramolecular disulfide linkage.	Disulfides	301-310	peroxiredoxin 5	Homo sapiens	25-29
17673175-7	2007	All these tested Trx-independent MsrB enzymes lack an additional cysteine (resolving cysteine) that is capable of forming a disulfide bond on the enzyme during the catalytic reaction.	Disulfides	124-133	methionine sulfoxide reductase B2	Homo sapiens	33-37
17644519-8	2007	It was found that the ability to activate CCR5 was recovered upon reduction of the intermolecular disulfide cross-link by incubation with 1 mm dithiothreitol.	Disulfides	98-107	C-C motif chemokine receptor 5	Homo sapiens	42-46
10751410-5	2000	The oxidized intermediate of PrxV is thus distinct from those of other Prx enzymes, which form either an intermolecular disulfide or a sulfenic acid intermediate.	Disulfides	120-129	peroxiredoxin 5	Homo sapiens	29-33
17548047-2	2007	C93S-Trx2 was detected as a disulfide with mitochondrial peroxiredoxin-3 (Prx3) but not peroxiredoxin-5 (Prx5).	Disulfides	28-37	peroxiredoxin 3	Homo sapiens	57-72
10751410-6	2000	The disulfide formed by PrxV is reduced by thioredoxin but not by glutaredoxin or glutathione.	Disulfides	4-13	peroxiredoxin 5	Homo sapiens	24-28
17548047-2	2007	C93S-Trx2 was detected as a disulfide with mitochondrial peroxiredoxin-3 (Prx3) but not peroxiredoxin-5 (Prx5).	Disulfides	28-37	peroxiredoxin 3	Homo sapiens	74-78
10751410-6	2000	The disulfide formed by PrxV is reduced by thioredoxin but not by glutaredoxin or glutathione.	Disulfides	4-13	thioredoxin	Homo sapiens	43-54
10891063-0	2000	Structural constraints imposed by a non-native disulfide cause reversible changes in rhodopsin photointermediate kinetics.	Disulfides	47-56	rhodopsin	Bos taurus	85-94
17371294-9	2007	tPA possesses serine-protease activity, with 35 cysteine residues that participate in the formation of 17 disulfide bonds.	Disulfides	106-115	chromosome 20 open reading frame 181	Homo sapiens	0-3
10891063-1	2000	Suspensions of bovine rhodopsin in 2% lauryl maltoside detergent were treated with Cu(phen)(3)(2+) to form a disulfide bridge between cysteines 140 and 222 which occur naturally in the bovine rhodopsin sequence.	Disulfides	109-118	rhodopsin	Bos taurus	22-31
10891063-1	2000	Suspensions of bovine rhodopsin in 2% lauryl maltoside detergent were treated with Cu(phen)(3)(2+) to form a disulfide bridge between cysteines 140 and 222 which occur naturally in the bovine rhodopsin sequence.	Disulfides	109-118	rhodopsin	Bos taurus	192-201
10891063-5	2000	Since the 140-222 disulfide has previously been shown to block transducin activation, its effects on rhodopsin activation are of considerable interest.	Disulfides	18-27	rhodopsin	Bos taurus	101-110
10891063-8	2000	These results show that formation of disulfides in rhodopsin has potential as a tool for discriminating between the three isochromic, 380 nm absorbing intermediates involved in rhodopsin activation and for gaining insight into how their structures differ.	Disulfides	37-47	rhodopsin	Bos taurus	51-60
17622185-6	2007	This is highly relevant in the context of the Chemical Weapons Convention, since the disulfide bond connecting the two chains of ricin indicates the presence of an intact toxin and provides additional forensic evidence for the analytical results.	Disulfides	85-94	ricin	Ricinus communis	129-134
10891063-8	2000	These results show that formation of disulfides in rhodopsin has potential as a tool for discriminating between the three isochromic, 380 nm absorbing intermediates involved in rhodopsin activation and for gaining insight into how their structures differ.	Disulfides	37-47	rhodopsin	Bos taurus	177-186
10880522-1	2000	The B cell antigen receptor (BCR) is a large complex that consists of a disulfide-linked tetramer of two transmembrane heavy (mu) chains and two light (lambda or kappa) chains in association with a heterodimer of Igalpha and Igbeta.	Disulfides	72-81	CD79b molecule	Homo sapiens	225-231
17579916-6	2007	Importantly, disulfiram (tetraethylthiuram disulfide), a compound used to treat alcoholism, and other disulfide-containing compounds were shown to inhibit MAGL with good potency, likely through an interaction with cysteine residues.	Disulfides	43-52	monoglyceride lipase	Homo sapiens	155-159
10880960-5	2000	If the disulfide bond of the more N-terminally located Ig-like domain was destroyed by mutations, Bsg could not form oligomers.	Disulfides	7-16	basigin (Ok blood group)	Homo sapiens	98-101
10747912-0	2000	Disulfide bonds are required for folding and secretion of apolipoprotein B regardless of its lipidation state.	Disulfides	0-9	apolipoprotein B	Mus musculus	58-74
17215074-1	2007	Whey acidic protein (WAP) is a major component of whey, which has two or three WAP motif domains characterized by a four-disulfide core (4-DSC) structure similar to the serine protease inhibitor.	Disulfides	121-130	whey acidic protein	Mus musculus	0-19
10747912-3	2000	The role of these disulfides in the secretion of lipidated or unlipidated truncated forms of apoB was studied in C127 cells expressing apoB-17, apoB-29, or apoB-41.	Disulfides	18-28	apolipoprotein B	Mus musculus	93-97
17587197-5	2007	HLA-G exists in various forms, including beta2m-associated or -free disulfide-linked dimers that can be expressed either at the cell surface or in soluble form.	Disulfides	68-77	major histocompatibility complex, class I, G	Homo sapiens	0-5
17587197-7	2007	In this issue of the European Journal of Immunology, one article demonstrates that the disulfide-linked homodimer of beta2m-associated HLA-G is the major fraction expressed by trophoblast cells.	Disulfides	87-96	major histocompatibility complex, class I, G	Homo sapiens	135-140
17587197-9	2007	On the other hand, another recent report showed that beta2m-free disulfide-linked HLA-G dimers are produced by villous cytotrophoblast cells.	Disulfides	65-74	major histocompatibility complex, class I, G	Homo sapiens	82-87
17468103-10	2007	Glutaredoxin (GRx), which specifically catalyzes reduction of protein-SSG mixed disulfides, reversed inhibition of p65-NFkappaB DNA binding in extracts from cells treated with hypoxia plus NAC and restored NFkappaB activity.	Disulfides	80-90	X-linked Kx blood group	Homo sapiens	189-192
10747912-7	2000	Reduced apoB polypeptides were rescued following removal of dithiothreitol, as they underwent post-translational disulfide bonding, attained their mature form, and were subsequently secreted.	Disulfides	113-122	apolipoprotein B	Mus musculus	8-12
10747912-8	2000	Together the data suggest that in C127 cells the formation of native disulfides is critical for the folding and secretion of apoB independent of its length, its requirement for lipidation or microsomal triglyceride transfer protein expression.	Disulfides	69-79	apolipoprotein B	Mus musculus	125-129
10788477-3	2000	MTX possesses 53-68% sequence identity with HsTx1 and Pi1, two other K(+) channel short chain scorpion toxins cross-linked by four disulfide bridges.	Disulfides	131-140	serine (or cysteine) peptidase inhibitor, clade A, member 1A	Mus musculus	54-57
17379184-3	2007	Using co-immunoprecipitation and Bioluminescence Resonance Energy Transfer (BRET) techniques, we show here that 5-HT(4)R homodimerization but not 5-HT(4)R-beta(2) adrenergic receptor (beta(2)AR) heterodimerization is largely decreased under reducing conditions suggesting the participation of disulfide bonds in 5-HT(4)R dimerization.	Disulfides	293-302	5-hydroxytryptamine receptor 4	Homo sapiens	112-120
17208454-6	2007	By using mass spectrometry we demonstrated that application of 2-mercaptoethanol (2-ME) during purification leads to formation of its mixed disulfide adducts with Cox17.	Disulfides	140-149	cytochrome c oxidase copper chaperone COX17	Homo sapiens	163-168
17208454-7	2007	Moreover, partially reduced Cox17 can form mixed disulfide adducts also with the cellular reducing agent glutathione, which abolishes copper-binding ability of partially reduced Cox17.	Disulfides	49-58	cytochrome c oxidase copper chaperone COX17	Homo sapiens	28-33
17208454-7	2007	Moreover, partially reduced Cox17 can form mixed disulfide adducts also with the cellular reducing agent glutathione, which abolishes copper-binding ability of partially reduced Cox17.	Disulfides	49-58	cytochrome c oxidase copper chaperone COX17	Homo sapiens	178-183
10671557-3	2000	Here, we used these mutants to examine whether disulfide-linked receptor dimerization affects the biological and biochemical activities of the IL-3 receptor.	Disulfides	47-56	interleukin 3	Homo sapiens	143-147
17126869-6	2007	One form of trimeric Env was made by disrupting the gp120-gp41 cleavage site by mutagenesis (gp140(UNC)), the other contains an intramolecular disulfide bond to stabilize the cleaved gp120 and gp41 moieties (SOSIP.R6 gp140).	Disulfides	143-152	endogenous retrovirus group K member 20	Homo sapiens	21-24
17400055-6	2007	In addition, a disulfide-bonded dimer adopts an oblique conformation, providing the possibility of a 1:2 (HLA-G dimer:receptor) complex stoichiometry.	Disulfides	15-24	major histocompatibility complex, class I, G	Homo sapiens	106-111
10651631-0	2000	Disulfide bridge engineering in the tachykinin NK1 receptor.	Disulfides	0-9	tachykinin receptor 1	Homo sapiens	47-59
17245526-4	2007	The solution structure of the twelfth cysteine-rich ligand-binding repeat with class A motif found in megalin features two short beta-strands and two helical turns, yielding the typical fold with a I-III, II-V and IV-VI disulfide bridge connectivity pattern and a calcium coordination site at the C-terminal end.	Disulfides	220-229	LDL receptor related protein 2	Rattus norvegicus	102-109
10651631-1	2000	As in most other seven-transmembrane receptors, the central disulfide bridge from the extracellular end of TM-III to the middle of the second extracellular loop was essential for ligand binding in the NK1 receptor.	Disulfides	60-69	tachykinin receptor 1	Homo sapiens	201-213
17287397-5	2007	The oye2Delta phenotype can be completely suppressed by removing the potential for formation of the actin C285-C374 disulfide bond, the likely substrate of the Oye2p enzyme or by treating the cells with the clinically important reductant N-acetylcysteine.	Disulfides	116-125	NADPH dehydrogenase	Saccharomyces cerevisiae S288C	160-165
17336303-1	2007	The thiol oxidase Erv1 and the redox-regulated receptor Mia40/Tim40 are components of a disulfide relay system which mediates import of proteins into the intermembrane space (IMS) of mitochondria.	Disulfides	88-97	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	56-61
17336303-3	2007	After passage across the translocase of the mitochondrial outer membrane Erv1 interacts via disulfide bonds with Mia40.	Disulfides	92-101	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	113-118
10679983-0	2000	Determination of the carbohydrate composition and the disulfide bond linkages of bovine lactoperoxidase by mass spectrometry.	Disulfides	54-63	lactoperoxidase	Bos taurus	88-103
17110014-7	2007	In this study we show that authentic bovine fetuin-A disulfide-bridged two-chain forms, which include the original C-terminus, were liberated from the single-chain precursor by metalloproteinases MMP-3 (stromelysin-1) and MMP-7 (matrilysin), but not by elastase, cathepsin E and cathepsin G.	Disulfides	53-62	stromelysin-1	Bos taurus	196-201
17110014-7	2007	In this study we show that authentic bovine fetuin-A disulfide-bridged two-chain forms, which include the original C-terminus, were liberated from the single-chain precursor by metalloproteinases MMP-3 (stromelysin-1) and MMP-7 (matrilysin), but not by elastase, cathepsin E and cathepsin G.	Disulfides	53-62	stromelysin-1	Bos taurus	203-216
17110014-7	2007	In this study we show that authentic bovine fetuin-A disulfide-bridged two-chain forms, which include the original C-terminus, were liberated from the single-chain precursor by metalloproteinases MMP-3 (stromelysin-1) and MMP-7 (matrilysin), but not by elastase, cathepsin E and cathepsin G.	Disulfides	53-62	matrix metallopeptidase 7	Bos taurus	222-227
17110014-7	2007	In this study we show that authentic bovine fetuin-A disulfide-bridged two-chain forms, which include the original C-terminus, were liberated from the single-chain precursor by metalloproteinases MMP-3 (stromelysin-1) and MMP-7 (matrilysin), but not by elastase, cathepsin E and cathepsin G.	Disulfides	53-62	matrix metallopeptidase 7	Bos taurus	229-239
10679983-1	2000	The extent and distribution of N-glycosylation and the nature of most of the disulfide bond linkages were determined for bovine lactoperoxidase through proteolytic and glycolytic digestions combined with matrix-assisted laser desorption/ionization mass spectrometric analysis.	Disulfides	77-86	lactoperoxidase	Bos taurus	128-143
10800594-4	2000	Thioredoxin of mediated thiol-disulfide exchange interconverts eukaryotic PRKs between reduced (active) and oxidized (inactive) forms.	Disulfides	30-39	thioredoxin	Homo sapiens	0-11
17363302-3	2007	The 2 A crystal structure of the Tim-3 IgV domain demonstrated that four cysteines, which are invariant within the Tim family, form two noncanonical disulfide bonds, resulting in a surface not present in other immunoglobulin superfamily members.	Disulfides	149-158	hepatitis A virus cellular receptor 1	Homo sapiens	33-36
17363302-3	2007	The 2 A crystal structure of the Tim-3 IgV domain demonstrated that four cysteines, which are invariant within the Tim family, form two noncanonical disulfide bonds, resulting in a surface not present in other immunoglobulin superfamily members.	Disulfides	149-158	hepatitis A virus cellular receptor 1	Homo sapiens	115-118
17049605-4	2007	Important structural residues are maintained in the sbIL-10 protein, including the four cysteines responsible for the two intra-chain disulfide bridges reported for human IL-10.	Disulfides	134-143	interleukin 10	Homo sapiens	54-59
10674716-4	2000	The disulfide bond pairing of the synthetic peptide was determined by 1H-NMR spectroscopy and confirmed to be a Cys1-Cys6, Cys2-Cys4, Cys3-Cys5 arrangement similar to other mammalian alpha-defensin peptides.	Disulfides	4-13	cystin 1	Homo sapiens	112-116
10637293-6	2000	We found that UV irradiation promotes the disulfide bond-mediated dimerization of the Ret proteins, in close association with activation and superactivation of Ret kinases.	Disulfides	42-51	ret proto-oncogene	Homo sapiens	86-89
17189256-0	2007	Defining the native disulfide topology in the somatomedin B domain of human vitronectin.	Disulfides	20-29	vitronectin	Homo sapiens	46-59
17189256-0	2007	Defining the native disulfide topology in the somatomedin B domain of human vitronectin.	Disulfides	20-29	vitronectin	Homo sapiens	76-87
17189256-2	2007	Despite the functional importance of the Cys-rich SMB domain, how its four disulfide bridges are arranged in the molecule remains highly controversial, as evidenced by three different disulfide connectivities reported by several laboratories.	Disulfides	75-84	vitronectin	Homo sapiens	50-53
17189256-2	2007	Despite the functional importance of the Cys-rich SMB domain, how its four disulfide bridges are arranged in the molecule remains highly controversial, as evidenced by three different disulfide connectivities reported by several laboratories.	Disulfides	184-193	vitronectin	Homo sapiens	50-53
10637293-6	2000	We found that UV irradiation promotes the disulfide bond-mediated dimerization of the Ret proteins, in close association with activation and superactivation of Ret kinases.	Disulfides	42-51	ret proto-oncogene	Homo sapiens	160-163
17189256-3	2007	Using native chemical ligation and orthogonal protection of selected Cys residues, we chemically synthesized all three topological analogs of SMB with predefined disulfide connectivities corresponding to those previously published.	Disulfides	162-171	vitronectin	Homo sapiens	142-145
17189256-6	2007	Our results unequivocally define the native disulfide topology in the SMB domain of human vitronectin, providing biochemical as well as functional support to the structural findings on a recombinant SMB domain by Read and colleagues (Zhou, A., Huntington, J.	Disulfides	44-53	vitronectin	Homo sapiens	70-73
10574970-6	1999	When mouse LAT2 and human 4F2hc cRNAs were co-injected into Xenopus oocytes, disulfide-linked heterodimers were formed, and an L-type amino acid uptake was induced, which differed slightly from that produced by LAT1-4F2hc: the apparent affinity for L-phenylalanine was higher, and L-alanine was transported at physiological concentrations.	Disulfides	77-86	linker for activation of T cells family, member 2	Mus musculus	11-15
17189256-6	2007	Our results unequivocally define the native disulfide topology in the SMB domain of human vitronectin, providing biochemical as well as functional support to the structural findings on a recombinant SMB domain by Read and colleagues (Zhou, A., Huntington, J.	Disulfides	44-53	vitronectin	Homo sapiens	90-101
17283341-0	2007	Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones.	Disulfides	0-9	heat shock protein family D (Hsp60) member 1	Homo sapiens	45-50
17283341-3	2007	Here, we have monitored topology employing disulfide bond formation of a secretory protein, trypsinogen (TG), that behaves in vitro as a stringent, GroEL-GroES-requiring substrate.	Disulfides	43-52	heat shock protein family D (Hsp60) member 1	Homo sapiens	148-153
17283341-4	2007	Inside the long-lived cis chamber formed by SR1, a single-ring version of GroEL, complexed with GroES, we observed an ordered formation of disulfide bonds.	Disulfides	139-148	heat shock protein family D (Hsp60) member 1	Homo sapiens	74-79
24741575-4	2014	However, in recent years, new data has revealed the ability of HLA-G to form disulfide-linked dimeric complexes with high preferential binding and functional activities.	Disulfides	77-86	major histocompatibility complex, class I, G	Homo sapiens	63-68
24157611-5	2014	Recently, several studies proposed TPI as a potential target of different redox modifications including dithiol/disulfide interchanges, glutathionylation, and nitrosylation.	Disulfides	112-121	uncharacterized protein	Chlamydomonas reinhardtii	35-38
10574970-6	1999	When mouse LAT2 and human 4F2hc cRNAs were co-injected into Xenopus oocytes, disulfide-linked heterodimers were formed, and an L-type amino acid uptake was induced, which differed slightly from that produced by LAT1-4F2hc: the apparent affinity for L-phenylalanine was higher, and L-alanine was transported at physiological concentrations.	Disulfides	77-86	solute carrier family 3 member 2	Homo sapiens	26-31
17140600-11	2007	Thus, in addition to the protease disulfide bridge, reversible oxidation of cysteine and/or methionine residues in other domains of the Gag polyprotein or in related cellular proteins must be involved in the regulation of maturation.	Disulfides	34-43	endogenous retrovirus group K member 9	Homo sapiens	136-151
10610776-5	1999	Moreover, a novel intramolecular disulfide bond replaces the canonical one found in the thioredoxin family.	Disulfides	33-42	thioredoxin	Homo sapiens	88-99
17130129-6	2007	Escherichia coli reduced thioredoxin (Trx) cleaved the intersubunit disulfide bond to activate MST to 2.3- and 4.9-fold the levels of activation of dithiothreitol (DTT)-treated and DTT-untreated MST, respectively.	Disulfides	68-77	mercaptopyruvate sulfurtransferase	Rattus norvegicus	95-98
17130129-6	2007	Escherichia coli reduced thioredoxin (Trx) cleaved the intersubunit disulfide bond to activate MST to 2.3- and 4.9-fold the levels of activation of dithiothreitol (DTT)-treated and DTT-untreated MST, respectively.	Disulfides	68-77	mercaptopyruvate sulfurtransferase	Rattus norvegicus	195-198
24097801-4	2014	The structure of uromodulin is complex, with multiple disulfide bonds and typical domains of extracellular proteins.	Disulfides	54-63	uromodulin	Homo sapiens	17-27
10753067-6	1999	RESULTS: After transient transfection of COS-7 cells, IFNgammaR/IgG1 and IL-4/IgG1 fusion proteins are secreted in vitro as disulfide-linked homodimers, with the expected biological activity.	Disulfides	124-133	interleukin 4	Mus musculus	73-77
24075898-5	2013	Consistent with these results we find a dimeric form of LMP-1 that can be stabilized by disulfide crosslinking.	Disulfides	88-97	PDZ and LIM domain 7	Homo sapiens	56-61
17130129-11	2007	A consecutively formed disulfide bond between Trx and MST must be cleaved for the activation.	Disulfides	23-32	mercaptopyruvate sulfurtransferase	Rattus norvegicus	54-57
10549572-6	1999	However, S-LC-SMPT -mediated Fab-RTA, sterically hindered, showed an enhanced disulfide bond stability in vitro over S-LC-SPDP mediated one.	Disulfides	78-87	FA complementation group B	Homo sapiens	29-32
16595153-5	2007	It was revealed that Ficolin-2 has a high molecular weight due to extensive disulfide bridge formation.	Disulfides	76-85	ficolin 2	Homo sapiens	21-30
16595153-10	2007	Based on our findings we propose a model in which disulfide bridges located in the N-terminal region of the polypeptides explain the oligomerization pattern of human Ficolin-2.	Disulfides	50-59	ficolin 2	Homo sapiens	166-175
18045229-5	2007	Western blotting based on non-reducing Tricine-SDS-PAGE indicated that IGF-II expression coupled with IGFBP-6 might significantly avoid the mispairing of disulfide bonds compared with the IGF-II expressed alone.	Disulfides	154-163	insulin like growth factor binding protein 6	Homo sapiens	102-109
17659658-5	2007	Our results demonstrated that, upon H(2)O(2) treatment, four cysteines, which reside at the zinc-finger motif of the p70 subunit, could result in the formation of two pairs of intramolecular disulfides, Cys481-Cys486 and Cys500-Cys503; no cysteine sulfinic acid or cysteine sulfonic acid could be found.	Disulfides	191-201	annexin A6	Homo sapiens	117-120
24386359-4	2013	Furthermore, the study revealed the residues important for expression of the GLA activity, i.e., residues involved in construction of the active site, a disulfide bond or a dimer.	Disulfides	153-162	galactosidase alpha	Homo sapiens	77-80
24900791-1	2014	Peptide "B-2", which is one of the most potent kallikrein-related peptidase 3 (KLK3)-stimulating compounds, consists of 12 amino acids and is cyclized by a disulfide bridge between the N- and C-terminal cysteines.	Disulfides	156-165	immunoglobulin kappa variable 5-2	Homo sapiens	9-12
10549572-6	1999	However, S-LC-SMPT -mediated Fab-RTA, sterically hindered, showed an enhanced disulfide bond stability in vitro over S-LC-SPDP mediated one.	Disulfides	78-87	MAS related GPR family member F	Homo sapiens	33-36
24055038-6	2013	Further, we show that ERdj5 indeed interacted with two of the identified proteins via formation of intermolecular disulfide bond.	Disulfides	114-123	DnaJ heat shock protein family (Hsp40) member C10	Mus musculus	22-27
10504411-2	1999	The heterodimeric disulfide-linked cytotoxic protein is classified as type II ribosome inactivating protein (RIP).	Disulfides	18-27	receptor interacting serine/threonine kinase 1	Homo sapiens	109-112
23748428-2	2013	To get insights into possible causes of this heterogeneity of UAKD, we describe the new mutant mouse line Umod(C93F), leading to disruption of a putative disulfide bond which is also absent in a known human UMOD mutation, and compare the phenotype of this new mouse line with the recently published mouse line Umod(A227T).	Disulfides	154-163	uromodulin	Homo sapiens	207-211
10473564-2	1999	Pulse radiolytic reduction of disulfide bridges in ceruloplasmin yielding RSSR(-) radicals induces a cascade of intramolecular electron transfer (ET) processes.	Disulfides	30-39	ceruloplasmin	Homo sapiens	51-64
24081982-0	2013	Orai3 TM3 point mutation G158C alters kinetics of 2-APB-induced gating by disulfide bridge formation with TM2 C101.	Disulfides	74-83	tropomyosin 3	Homo sapiens	6-9
24081982-8	2013	We suggest that a disulfide bridge, formed between the introduced cysteine at TM3 position 158 and the endogenous cysteine at TM2 position 101, hinders transitions between Orai3 open and closed states.	Disulfides	18-27	tropomyosin 3	Homo sapiens	78-81
17128976-1	2006	Four covalent complexes between recombinant yeast cytochrome c and cytochrome c peroxidase (rCcP) were synthesized via disulfide bond formation using specifically designed protein mutants (Papa, H. S., and Poulos, T. L. (1995) Biochemistry 34, 6573-6580).	Disulfides	119-128	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	67-90
17002656-8	2006	Plasmin(ogen), vitronectin, glycoprotein 1balpha, integrin beta(3) and thrombomodulin also contain -RHStaple disulfides, and there is circumstantial evidence that the function of these proteins may involve cleavage/formation of these disulfide bonds.	Disulfides	109-119	vitronectin	Homo sapiens	15-26
10473564-3	1999	Based on the three-dimensional structure of ceruloplasmin identification of individual kinetically active disulfide groups and type 1 (T1) copper centers, the following is proposed.	Disulfides	106-115	ceruloplasmin	Homo sapiens	44-57
17056715-3	2006	HLA-G inherently exhibits various forms, including beta(2)-microglobulin (beta(2)m)-free and disulfide-linked dimer forms.	Disulfides	93-102	major histocompatibility complex, class I, G	Homo sapiens	0-5
23843626-4	2013	In the case of Fz4-FEVR, CRYAB prevents the formation of inter-chain disulfide bridges between the lumenal ectodomains of the aggregated mutant chains, which enables correct folding and promotes appropriate compartmentalization on the plasma membrane.	Disulfides	69-78	crystallin alpha B	Homo sapiens	25-30
10493586-4	1999	This guanylin molecule contains two disulfide bonds that are absolutely necessary for receptor activation.	Disulfides	36-45	guanylate cyclase activator 2A	Homo sapiens	5-13
23713614-1	2013	QSOX1 (quiescin sulfhydryl oxidase 1) efficiently catalyses the insertion of disulfide bonds into a wide range of proteins.	Disulfides	77-86	quiescin sulfhydryl oxidase 1	Homo sapiens	0-5
23713614-1	2013	QSOX1 (quiescin sulfhydryl oxidase 1) efficiently catalyses the insertion of disulfide bonds into a wide range of proteins.	Disulfides	77-86	quiescin sulfhydryl oxidase 1	Homo sapiens	7-36
23713614-3	2013	The function of QSOX1 is likely to involve disulfide formation in proteins entering the secretory pathway or outside the cell.	Disulfides	43-52	quiescin sulfhydryl oxidase 1	Homo sapiens	16-21
16891553-10	2006	Possible roles of subfamily I receptors and disulfide linkages in ETR1 receptor signal output mediated through the N terminus are discussed.	Disulfides	44-53	Signal transduction histidine kinase, hybrid-type, ethylene sensor	Arabidopsis thaliana	66-70
16864583-2	2006	A predominant one-disulfide intermediate in each case contains the canonical A20-B19 disulfide bridge (cystines 18-61 in IGF-I and 19-85 in human proinsulin).	Disulfides	18-27	immunoglobulin kappa variable 1-27	Homo sapiens	77-80
23713614-8	2013	The processing of QSOX1 suggests a novel level of regulation of secretion of this potent disulfide catalyst and producer of hydrogen peroxide.	Disulfides	89-98	quiescin sulfhydryl oxidase 1	Homo sapiens	18-23
10493586-5	1999	We demonstrate that the folding of the reduced 15-residue guanylin results almost completely in the formation of the two inactive disulfide isomers.	Disulfides	130-139	guanylate cyclase activator 2A	Homo sapiens	58-66
16864583-2	2006	A predominant one-disulfide intermediate in each case contains the canonical A20-B19 disulfide bridge (cystines 18-61 in IGF-I and 19-85 in human proinsulin).	Disulfides	85-94	immunoglobulin kappa variable 1-27	Homo sapiens	77-80
16864583-8	2006	We propose that nascent interactions within this subdomain orient the A20 and B19 thiolates for disulfide bond formation and stabilize the one-disulfide intermediate once formed.	Disulfides	96-105	immunoglobulin kappa variable 1-27	Homo sapiens	70-73
10493586-7	1999	Because proguanylin lacking the 31 NH2-terminal residues of the prosequence folds only to a minor extent to guanylin with the native disulfide bonds, it is evident that this NH2-terminal region contributes significantly to the correct disulfide-coupled folding.	Disulfides	235-244	guanylate cyclase activator 2A	Homo sapiens	11-19
16864583-8	2006	We propose that nascent interactions within this subdomain orient the A20 and B19 thiolates for disulfide bond formation and stabilize the one-disulfide intermediate once formed.	Disulfides	143-152	immunoglobulin kappa variable 1-27	Homo sapiens	70-73
10455116-4	1999	Cells lacking BdbC also showed decreased stability of cell-associated forms of E. coli TEM-beta-lactamase, containing one disulfide bond.	Disulfides	122-131	blaTEM	Escherichia coli	87-105
16876116-0	2006	Disulfide bond formation in NGR fiber-modified adenovirus is essential for retargeting to aminopeptidase N.	Disulfides	0-9	reticulon 4 receptor	Homo sapiens	28-31
16876116-5	2006	Finally, we show evidence that disulfide bond formation within an Ad bearing the CDCNGRCFC sequence is essential for retargeting to APN, suggesting that this sequence does indeed assume a cyclic structure which facilitates NGR binding to APN.	Disulfides	31-40	reticulon 4 receptor	Homo sapiens	84-87
23639297-1	2013	Human blood coagulation factor XII (FXII) is the one chain 80 kDa zymogen form of the active serine protease alpha-FXIIa, which consists of a heavy and light chain linked by a disulfide bond, the light chain being responsible for the proteolytical activity.	Disulfides	176-185	coagulation factor XII	Homo sapiens	12-34
23199280-4	2013	Using tandem mass spectrometry (MS), we identified a new disulfide complex located between Cys1045 and Cys1024 within VEGFR2 that was labile to H2S-mediated modification.	Disulfides	57-66	kinase insert domain receptor	Homo sapiens	118-124
23199280-5	2013	Kinase activity of the mutant VEGFR2 (C1045A) devoid of the Cys1045-Cys1024 disulfide bond was significantly higher than wild-type VEGFR2.	Disulfides	76-85	kinase insert domain receptor	Homo sapiens	30-36
23199280-8	2013	The formation of the Cys1045-Cys1024 disulfide bond disrupted the integrity of the active conformation of VEGFR2.	Disulfides	37-46	kinase insert domain receptor	Homo sapiens	106-112
10463612-1	1999	Thioredoxin (Trx) is a small redox-active protein that provides reducing equivalents for key cysteine residues of proteins through thiol-disulfide exchange, such as the transcription factor nuclear factor-kappaB (NF-kappaB).	Disulfides	137-146	thioredoxin	Homo sapiens	0-11
23199280-9	2013	Breaking the Cys1045-Cys1024 disulfide bond recovered the active conformation of VEGFR2.	Disulfides	29-38	kinase insert domain receptor	Homo sapiens	81-87
10463612-1	1999	Thioredoxin (Trx) is a small redox-active protein that provides reducing equivalents for key cysteine residues of proteins through thiol-disulfide exchange, such as the transcription factor nuclear factor-kappaB (NF-kappaB).	Disulfides	137-146	thioredoxin	Homo sapiens	13-16
16684962-0	2006	Abnormal disulfide-linked oligomerization results in ER retention and altered signaling by TNFR1 mutants in TNFR1-associated periodic fever syndrome (TRAPS).	Disulfides	9-18	tumor necrosis factor receptor superfamily, member 1a	Mus musculus	91-96
22901034-2	2013	This oxidative folding process depends on the disulfide donor/import receptor Mia40 and the flavin adenine dinucleotide oxidase Erv1 and concerns proteins involved in mitochondrial biogenesis, respiratory complex assembly, and metal transfer.	Disulfides	46-55	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	78-83
10428967-5	1999	Thioredoxin was able to reduce oxidized RsrA, suggesting that sigma(R), RsrA and the thioredoxin system comprise a novel feedback homeostasis loop that senses and responds to changes in the intracellular thiol-disulfide redox balance.	Disulfides	210-219	thioredoxin	Homo sapiens	0-11
16684962-0	2006	Abnormal disulfide-linked oligomerization results in ER retention and altered signaling by TNFR1 mutants in TNFR1-associated periodic fever syndrome (TRAPS).	Disulfides	9-18	tumor necrosis factor receptor superfamily, member 1a	Mus musculus	108-113
16684962-5	2006	Instead, TRAPS mutant TNFR1 formed abnormal disulfide-linked oligomers that failed to interact with wild-type TNFR1 molecules through the preligand assembly domain (PLAD) that normally governs receptor self-association.	Disulfides	44-53	tumor necrosis factor receptor superfamily, member 1a	Mus musculus	22-27
10428967-5	1999	Thioredoxin was able to reduce oxidized RsrA, suggesting that sigma(R), RsrA and the thioredoxin system comprise a novel feedback homeostasis loop that senses and responds to changes in the intracellular thiol-disulfide redox balance.	Disulfides	210-219	thioredoxin	Homo sapiens	85-96
16554059-3	2006	This thiol group was specifically reacted with DTNB (5,5"-dithiobis(2-nitrobenzoic acid)) at pH 7.5 and 2, producing a modified beta-lactoglobulin containing a mix disulfide bond with 5-thio-2-nitrobenzoic acid (TNB).	Disulfides	164-173	beta-lactoglobulin	Bos taurus	128-146
23868209-7	2013	Based on the MS and (13)C-NMR data of the products from degradation of [[(13)C3,(15)N]Cys(1)]OT, we postulate that the ultimate degradation products of OT are dimers composed of two pyruvoylated octapeptides held together by one disulfide bridge between the two Cys(6) residues and by one more, non-reducible, linkage resulting from an aldol-type condensation between the two N-terminal pyruvoyl groups.	Disulfides	229-238	oxytocin/neurophysin I prepropeptide	Homo sapiens	93-95
23868209-7	2013	Based on the MS and (13)C-NMR data of the products from degradation of [[(13)C3,(15)N]Cys(1)]OT, we postulate that the ultimate degradation products of OT are dimers composed of two pyruvoylated octapeptides held together by one disulfide bridge between the two Cys(6) residues and by one more, non-reducible, linkage resulting from an aldol-type condensation between the two N-terminal pyruvoyl groups.	Disulfides	229-238	oxytocin/neurophysin I prepropeptide	Homo sapiens	152-154
10406670-7	1999	All three cases were found to have the same FGFR2 Ser351Cys (1231C to G) mutation predicted to form an aberrant disulfide bond(s) and affect ligand binding.	Disulfides	112-121	fibroblast growth factor receptor 2	Homo sapiens	44-49
23790485-2	2013	Several proteins of the intermembrane space (IMS) are imported and localized through an oxidative process, being folded through the formation of structural disulfide bonds catalyzed by Mia40, and trapped in the IMS.	Disulfides	156-165	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	185-190
23486473-1	2013	The chloroplast CF0-CF1-ATP synthase (ATP synthase) is activated in the light and inactivated in the dark by thioredoxin-mediated redox modulation of a disulfide bridge on its gamma subunit.	Disulfides	152-161	ATP synthase	Arabidopsis thaliana	24-36
23486473-1	2013	The chloroplast CF0-CF1-ATP synthase (ATP synthase) is activated in the light and inactivated in the dark by thioredoxin-mediated redox modulation of a disulfide bridge on its gamma subunit.	Disulfides	152-161	ATP synthase	Arabidopsis thaliana	38-50
23486473-6	2013	In situ equilibrium redox titrations and thiol redox-sensitive labeling studies showed that the gamma subunit disulfide/sulfhydryl couple in the modified ATP synthase has a more reducing redox potential and thus remains predominantly oxidized under physiological conditions, implying that the highly conserved acidic residues in the gamma subunit influence thiol redox potential.	Disulfides	110-119	ATP synthase	Arabidopsis thaliana	154-166
23828656-1	2006	The cyclocystine ring structure (CRS, 3), which results from a disulfide-bond between adjacent cysteine residues, is a rare motif in protein structures and is functionally important to those few proteins that posses it.	Disulfides	63-72	CRSA	Homo sapiens	33-39
16455647-0	2006	Efficient leukocyte Ig-like receptor signaling and crystal structure of disulfide-linked HLA-G dimer.	Disulfides	72-81	major histocompatibility complex, class I, G	Homo sapiens	89-94
16455647-2	2006	HLA-G is expressed in disulfide-linked dimer form both in solution and at the cell surface.	Disulfides	22-31	major histocompatibility complex, class I, G	Homo sapiens	0-5
16455647-7	2006	We further determined the crystal structure of the wild-type dimer of HLA-G with the intermolecular Cys(42)-Cys(42) disulfide bond.	Disulfides	116-125	major histocompatibility complex, class I, G	Homo sapiens	70-75
10387094-4	1999	During biosynthetic processing, C8 alpha and C8 gamma associate to form a disulfide-linked dimer (C8 alpha-gamma) that binds to C8 beta through a site located on C8 alpha.	Disulfides	74-83	complement C8 alpha chain	Homo sapiens	32-40
10387094-4	1999	During biosynthetic processing, C8 alpha and C8 gamma associate to form a disulfide-linked dimer (C8 alpha-gamma) that binds to C8 beta through a site located on C8 alpha.	Disulfides	74-83	complement C8 alpha chain	Homo sapiens	98-106
10387094-4	1999	During biosynthetic processing, C8 alpha and C8 gamma associate to form a disulfide-linked dimer (C8 alpha-gamma) that binds to C8 beta through a site located on C8 alpha.	Disulfides	74-83	complement C8 alpha chain	Homo sapiens	98-106
16407285-4	2006	WARP is present in the guanidine-soluble fraction of cartilage matrix extracts as a disulfide-bonded multimer, indicating that WARP is a strongly interacting component of the cartilage matrix.	Disulfides	84-93	von Willebrand factor A domain containing 1	Mus musculus	0-4
16407285-4	2006	WARP is present in the guanidine-soluble fraction of cartilage matrix extracts as a disulfide-bonded multimer, indicating that WARP is a strongly interacting component of the cartilage matrix.	Disulfides	84-93	von Willebrand factor A domain containing 1	Mus musculus	127-131
16677073-1	2006	Disulfide bonds are formed in the endoplasmic reticulum (ER) by sequential interchange reactions: Ero1alpha and Ero1beta transfer oxidative equivalents to protein disulfide isomerase (PDI), which in turn oxidizes cargo proteins.	Disulfides	0-9	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	98-107
23634958-12	2013	Altered mobility under reducing and non-reducing conditions suggests the presence of an intramolecular disulfide-bond in AtMHX.	Disulfides	103-112	magnesium/proton exchanger	Arabidopsis thaliana	121-126
23444386-0	2013	Modification of the catalytic function of human hydroxysteroid sulfotransferase hSULT2A1 by formation of disulfide bonds.	Disulfides	105-114	sulfotransferase family 2A member 1	Homo sapiens	80-88
10369668-1	1999	The thiol/disulfide oxidoreductase DsbA is the strongest oxidant of the thioredoxin superfamily and is required for efficient disulfide bond formation in the periplasm of Escherichia coli.	Disulfides	10-19	thioredoxin	Homo sapiens	72-83
23444386-4	2013	We have examined the hypothesis that the formation of disulfide bonds in hSULT2A1 can reversibly regulate the catalytic function of the enzyme.	Disulfides	54-63	sulfotransferase family 2A member 1	Homo sapiens	73-81
23444386-7	2013	Studies on the kinetics of the hSULT2A1-catalyzed sulfation of dehydroepiandrosterone (DHEA) showed the effects of disulfide bond formation on the substrate inhibition characteristics of the enzyme.	Disulfides	115-124	sulfotransferase family 2A member 1	Homo sapiens	31-39
23444386-10	2013	Thus, the formation of disulfide bonds in hSULT2A1 is a potentially important reversible mechanism for alterations in the rates of sulfation of both endogenous and xenobiotic substrates.	Disulfides	23-32	sulfotransferase family 2A member 1	Homo sapiens	42-50
16677076-7	2006	Generally, there is a marked association of QSOX1 expression with cell types that have a high secretory load of disulfide-containing peptides and proteins.	Disulfides	112-121	quiescin sulfhydryl oxidase 1	Homo sapiens	44-49
16677077-4	2006	The formation and rearrangement of disulfide bonds is modulated by a family of enzymes known as the thiol isomerases, which include protein disulfide isomerase (PDI), ERp5, ERp57, and ERp72.	Disulfides	35-44	protein disulfide isomerase family A member 6	Homo sapiens	167-171
16375859-3	2006	Herein we show that ascorbic acid reduces protein disulfides in tubulin, tau, and microtubule-associated protein-2 that are formed by peroxynitrite anion.	Disulfides	50-60	microtubule associated protein 2	Homo sapiens	82-114
10329657-6	1999	Surface enzyme-linked immunosorbent assay detection of both mutant receptors showed &lt;10% expression, suggesting that a critical disulfide bridge between EL2 and the upper part of transmembrane 3, as found in many other G protein-coupled receptors, is required for proper trafficking of the P2Y1 receptor to the cell surface.	Disulfides	131-140	purinergic receptor P2Y1	Homo sapiens	293-306
23636475-2	2013	Each ABP is a heterodimer assembled as an ABPA subunit encoded by an Abpa gene and linked by disulfide bridges to an ABPBG subunit encoded by an Abpbg gene.	Disulfides	93-102	secretoglobin, family 1B, member 27	Mus musculus	5-8
10213608-0	1999	Engineering out motion: introduction of a de novo disulfide bond and a salt bridge designed to close a dynamic cleft on the surface of cytochrome b5.	Disulfides	50-59	cytochrome b5 type A	Homo sapiens	135-148
23556985-0	2013	The insoluble TGFBIp fraction of the cornea is covalently linked via a disulfide bond to type XII collagen.	Disulfides	71-80	transforming growth factor beta induced	Homo sapiens	14-20
23597483-1	2013	The mitochondrial disulfide relay system of Mia40 and Erv1/ALR facilitates import of the small translocase of the inner membrane (Tim) proteins and cysteine-rich proteins.	Disulfides	18-27	Mia40p	Saccharomyces cerevisiae S288C	44-49
23416299-3	2013	Additional disulfide cross-linking was observed between the N-terminus of subunit b and the periplasmic loop connecting TM4 and TM5 of subunit a.	Disulfides	11-20	tropomyosin 3	Homo sapiens	128-131
16325765-2	2006	Here we describe four sequences, TEH1-4, homologous to TipE in the Drosophila melanogaster genome, harboring all typical structures of both TipE and the beta-Subunit family of big-conductance Ca(2+)-activated potassium channels: short cytosolic N- and C-terminal stretches, two transmembrane domains, and a large extracellular loop with two disulfide bonds.	Disulfides	341-350	tipE homolog 1	Drosophila melanogaster	33-39
16325765-2	2006	Here we describe four sequences, TEH1-4, homologous to TipE in the Drosophila melanogaster genome, harboring all typical structures of both TipE and the beta-Subunit family of big-conductance Ca(2+)-activated potassium channels: short cytosolic N- and C-terminal stretches, two transmembrane domains, and a large extracellular loop with two disulfide bonds.	Disulfides	341-350	temperature-induced paralytic E	Drosophila melanogaster	55-59
16342937-13	2005	Partial disulfide bond assignment indicates that the intramolecular disulfide patterns in rat ZP1, ZP2, and ZP3 are identical to those of their corresponding mouse counterparts.	Disulfides	68-77	zona pellucida glycoprotein 2	Rattus norvegicus	99-102
16342937-13	2005	Partial disulfide bond assignment indicates that the intramolecular disulfide patterns in rat ZP1, ZP2, and ZP3 are identical to those of their corresponding mouse counterparts.	Disulfides	68-77	zona pellucida glycoprotein 3	Rattus norvegicus	108-111
16234242-3	2005	Activation of CuZn-SODs in eukaryotic cells occurs post-translationally and is generally dependent on the copper chaperone for SOD1 (CCS), which inserts the catalytic copper cofactor and catalyzes the oxidation of a conserved disulfide bond that is essential for activity.	Disulfides	226-235	Superoxide dismutase [Cu-Zn]	Caenorhabditis elegans	127-131
10213608-10	1999	The results suggest that a constraining disulfide bond can be designed to inhibit dynamic cleft formation on the surface of cyt b5.	Disulfides	40-49	cytochrome b5 type A	Homo sapiens	124-130
10213609-0	1999	Engineering out motion: a surface disulfide bond alters the mobility of tryptophan 22 in cytochrome b5 as probed by time-resolved fluorescence and 1H NMR experiments.	Disulfides	34-43	cytochrome b5 type A	Homo sapiens	89-102
16387713-3	2005	Thioredoxin (TRX) is a small thiol-mediated protein with a redox-active disulfide/dithiol within the conserved active site.	Disulfides	72-81	thioredoxin 1	Mus musculus	0-11
23536962-1	2013	INTRODUCTION: Quiescin sulfhydryl oxidase 1 (QSOX1) oxidizes sulfhydryl groups to form disulfide bonds in proteins.	Disulfides	87-96	quiescin sulfhydryl oxidase 1	Homo sapiens	23-43
10213609-17	1999	Taken together, the NMR and fluorescence studies support the proposal that an engineered disulfide bond inhibits the formation of a dynamic cleft on the surface of cyt b5.	Disulfides	89-98	cytochrome b5 type A	Homo sapiens	164-170
23536962-1	2013	INTRODUCTION: Quiescin sulfhydryl oxidase 1 (QSOX1) oxidizes sulfhydryl groups to form disulfide bonds in proteins.	Disulfides	87-96	quiescin sulfhydryl oxidase 1	Homo sapiens	45-50
16387713-3	2005	Thioredoxin (TRX) is a small thiol-mediated protein with a redox-active disulfide/dithiol within the conserved active site.	Disulfides	72-81	thioredoxin 1	Mus musculus	13-16
10196134-3	1999	NST1 is approximately spherical with an open cleft, and consists of a single alpha/beta fold with a central five-stranded parallel beta-sheet and a three-stranded anti-parallel beta-sheet bearing an interstrand disulfide bond.	Disulfides	211-220	N-deacetylase and N-sulfotransferase 1	Homo sapiens	0-4
23510202-2	2013	QSOX enzymes, which generate disulfide bonds and transfer them to substrate proteins, are present in a wide variety of eukaryotic species including metazoans and plants, but are absent from fungi.	Disulfides	29-38	quiescin sulfhydryl oxidase 1	Homo sapiens	0-4
23186364-4	2013	The yeast model for MIA consists of two critical components, the disulfide bond carrier Mia40 and sulfhydryl oxidase Erv1/ALR.	Disulfides	65-74	Mia40p	Saccharomyces cerevisiae S288C	88-93
10196131-6	1999	Two surface-exposed and thioredoxin-accessible disulfide bonds are present, one in the N-terminal extension and the other in the C-terminal extension.	Disulfides	47-56	thioredoxin	Homo sapiens	24-35
16186172-3	2005	We previously demonstrated that GAPDH readily undergoes disulfide bonding following oxidant exposure, although the consequence of disulfide bonding on GAPDH activity or function is unknown.	Disulfides	56-65	glyceraldehyde-3-phosphate dehydrogenase	Mus musculus	32-37
16186172-3	2005	We previously demonstrated that GAPDH readily undergoes disulfide bonding following oxidant exposure, although the consequence of disulfide bonding on GAPDH activity or function is unknown.	Disulfides	130-139	glyceraldehyde-3-phosphate dehydrogenase	Mus musculus	151-156
23275378-5	2013	Biochemical evidence showed that oxidized KCNB1 channels, which form oligomers held together by disulfide bridges involving Cys-73, accumulated in the plasma membrane as a result of defective endocytosis.	Disulfides	96-105	potassium voltage-gated channel subfamily B member 1	Homo sapiens	42-47
16186172-5	2005	Exposure of primary rat cortical neurons to the pro-oxidant amyloid beta peptide promotes nuclear accumulation of a disulfide-linked form of GAPDH, which becomes detergent-insoluble.	Disulfides	116-125	glyceraldehyde-3-phosphate dehydrogenase	Rattus norvegicus	141-146
10199409-2	1999	In seven affected families, we found six different missense mutations of the 55 kDa tumor necrosis factor receptor (TNFR1), five of which disrupt conserved extracellular disulfide bonds.	Disulfides	170-179	TNF receptor superfamily member 1A	Homo sapiens	116-121
16186172-6	2005	Disulfide bonding leads to a reduction in GAPDH enzymatic activity and correlates with the appearance of punctate aggregate-like GAPDH staining within the cytoplasm of both oxidant-treated HT22 cells and amyloid beta-treated primary cortical neurons.	Disulfides	0-9	glyceraldehyde-3-phosphate dehydrogenase	Mus musculus	42-47
16186172-6	2005	Disulfide bonding leads to a reduction in GAPDH enzymatic activity and correlates with the appearance of punctate aggregate-like GAPDH staining within the cytoplasm of both oxidant-treated HT22 cells and amyloid beta-treated primary cortical neurons.	Disulfides	0-9	glyceraldehyde-3-phosphate dehydrogenase	Mus musculus	129-134
16186172-7	2005	Our findings suggest that disulfide bonding of GAPDH and subsequent protein aggregate formation may have relevance to the pathophysiology of AD.	Disulfides	26-35	glyceraldehyde-3-phosphate dehydrogenase	Mus musculus	47-52
16617682-10	2005	Furthermore, non-halogenated phenolic compounds had inhibitory effects on the isomerase activities of PDI in addition to T3-binding activity, indicating that these compounds might also have adverse effects on protein folding, which PDI participates in by catalyzing rearrangements of disulfide bonds as an isomerase.	Disulfides	284-293	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	102-105
16617682-10	2005	Furthermore, non-halogenated phenolic compounds had inhibitory effects on the isomerase activities of PDI in addition to T3-binding activity, indicating that these compounds might also have adverse effects on protein folding, which PDI participates in by catalyzing rearrangements of disulfide bonds as an isomerase.	Disulfides	284-293	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	232-235
23385457-6	2013	TBN1 is mainly alpha-helical and is stabilized by four disulfide bridges.	Disulfides	55-64	endonuclease precursor-like	Solanum lycopersicum	0-4
10090736-2	1999	Site-directed mutagenesis of the three extracellular loops (ELs) of the human P2Y1 receptor indicates the existence of two essential disulfide bridges (Cys124 in EL1 and Cys202 in EL2; Cys42 in the N-terminal segment and Cys296 in EL3) and several specific ionic and H-bonding interactions (involving Glu209 and Arg287).	Disulfides	133-142	purinergic receptor P2Y1	Homo sapiens	78-91
10090736-2	1999	Site-directed mutagenesis of the three extracellular loops (ELs) of the human P2Y1 receptor indicates the existence of two essential disulfide bridges (Cys124 in EL1 and Cys202 in EL2; Cys42 in the N-terminal segment and Cys296 in EL3) and several specific ionic and H-bonding interactions (involving Glu209 and Arg287).	Disulfides	133-142	spectrin beta, erythrocytic	Homo sapiens	231-234
23273742-3	2012	determine the Hsp70(*)ATP structure utilizing engineered disulfide bonds, providing insights into the workings of this essential molecular machine.	Disulfides	57-66	heat shock protein family A (Hsp70) member 4	Homo sapiens	14-19
10066758-4	1999	Several proteins involved in disulfide exchange reactions contain the sequence Cys-X-X-Cys in their active sites, including thioredoxin and protein-disulfide isomerase.	Disulfides	29-38	thioredoxin	Homo sapiens	124-135
16300401-6	2005	We demonstrate that tethering the A and B subunits of TTR with a disulfide bond (as well as the symmetrically disposed C and D subunits) allows urea-mediated dissociation of the resulting (TTR-S-S-TTR)(2) construct, affording (TTR-S-S-TTR)(1) retaining a stable 16-stranded beta-sheet structure that is equivalent to the dimer not possessing a thyroid binding site.	Disulfides	65-74	transthyretin	Homo sapiens	54-57
23068612-1	2012	Quiescin Sulfhydryl Oxidase (QSOX), a catalyst of disulfide bond formation, is found in both plants and animals.	Disulfides	50-59	quiescin sulfhydryl oxidase 1	Homo sapiens	29-33
16300401-6	2005	We demonstrate that tethering the A and B subunits of TTR with a disulfide bond (as well as the symmetrically disposed C and D subunits) allows urea-mediated dissociation of the resulting (TTR-S-S-TTR)(2) construct, affording (TTR-S-S-TTR)(1) retaining a stable 16-stranded beta-sheet structure that is equivalent to the dimer not possessing a thyroid binding site.	Disulfides	65-74	transthyretin	Homo sapiens	189-192
9988687-5	1999	Similar to yeast Tsa1p, Ahp1p forms a disulfide-linked homodimer upon oxidation and in vivo requires the presence of the thioredoxin system but not of glutathione to perform its antioxidant protective function.	Disulfides	38-47	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	17-22
16300401-6	2005	We demonstrate that tethering the A and B subunits of TTR with a disulfide bond (as well as the symmetrically disposed C and D subunits) allows urea-mediated dissociation of the resulting (TTR-S-S-TTR)(2) construct, affording (TTR-S-S-TTR)(1) retaining a stable 16-stranded beta-sheet structure that is equivalent to the dimer not possessing a thyroid binding site.	Disulfides	65-74	transthyretin	Homo sapiens	189-192
16300401-6	2005	We demonstrate that tethering the A and B subunits of TTR with a disulfide bond (as well as the symmetrically disposed C and D subunits) allows urea-mediated dissociation of the resulting (TTR-S-S-TTR)(2) construct, affording (TTR-S-S-TTR)(1) retaining a stable 16-stranded beta-sheet structure that is equivalent to the dimer not possessing a thyroid binding site.	Disulfides	65-74	transthyretin	Homo sapiens	189-192
22992729-0	2012	Identification of the cysteine residue responsible for disulfide linkage of Na+ channel alpha and beta2 subunits.	Disulfides	55-64	hemoglobin, beta adult minor chain	Mus musculus	98-103
22992729-7	2012	WT beta2 subunits are resistant to live cell Triton X-100 detergent extraction from the hippocampal axon initial segment, whereas mutant beta2 subunits, which cannot form disulfide bonds with alpha, are removed by detergent.	Disulfides	171-180	hemoglobin, beta adult minor chain	Mus musculus	137-142
22992729-8	2012	Taken together, our results demonstrate that alpha-beta2 covalent association via a single, extracellular disulfide bond is required for beta2 targeting to specialized neuronal subcellular domains and for beta2 association with the neuronal cytoskeleton within those domains.	Disulfides	106-115	hemoglobin, beta adult minor chain	Mus musculus	51-56
22992729-8	2012	Taken together, our results demonstrate that alpha-beta2 covalent association via a single, extracellular disulfide bond is required for beta2 targeting to specialized neuronal subcellular domains and for beta2 association with the neuronal cytoskeleton within those domains.	Disulfides	106-115	hemoglobin, beta adult minor chain	Mus musculus	137-142
16300401-6	2005	We demonstrate that tethering the A and B subunits of TTR with a disulfide bond (as well as the symmetrically disposed C and D subunits) allows urea-mediated dissociation of the resulting (TTR-S-S-TTR)(2) construct, affording (TTR-S-S-TTR)(1) retaining a stable 16-stranded beta-sheet structure that is equivalent to the dimer not possessing a thyroid binding site.	Disulfides	65-74	transthyretin	Homo sapiens	189-192
10029517-6	1999	Native and mutant forms of CD39 lacking TMR were observed to undergo multimerization, associated with the formation of intermolecular disulfide bonds.	Disulfides	134-143	ectonucleoside triphosphate diphosphohydrolase 1	Homo sapiens	27-31
23044006-14	2012	It formed when the disulfide bonds between A-chain and B-chain of human insulin were cut by beta-mercaptoethanol, followed by cleavage of the B-chain by trypsin and carboxypeptidase B.	Disulfides	19-28	carboxypeptidase B1	Homo sapiens	165-183
10076060-4	1999	Fragmentation of alpha-lactalbumin by chymotrypsin yielded CKDDQNPH ISCDKF (residues (61-68)S-S(75-80)), also a polypeptide composed of two polypeptide chains held together by a disulfide bridge.	Disulfides	178-187	lactalbumin alpha	Bos taurus	17-34
22902630-7	2012	Interestingly, in response to peroxide, Prdx1 and Prdx3 transiently formed reducible higher molecular weight complexes, suggesting that multiple proteins are targets for Prdx-mediated oxidation via a disulfide-exchange mechanism.	Disulfides	200-209	peroxiredoxin 3	Homo sapiens	50-55
22918950-2	2012	The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins.	Disulfides	4-13	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	135-140
16081639-5	2005	Although the absence of JAK2 precluded GH-stimulated signaling, GH-induced GHR disulfide linkage (a proxy for the GH-induced conformational changes in the GHR dimer) proceeded independent of JAK2 expression, indicating that the earliest steps in GH-induced GHR triggering are not prevented by the absence of JAK2.	Disulfides	79-88	growth hormone receptor	Homo sapiens	75-78
10024465-11	1999	The absorption of 250-nm light by disulfide bonds also provided information regarding the proper folding of rat prolactin and bovine alpha-lactalbumin.	Disulfides	34-43	lactalbumin alpha	Bos taurus	133-150
22807577-6	2012	The two most effective consisted of our anti-FcRL5 antibody conjugated through cysteines to monomethylauristatin E (MMAE) by a maleimidocaproyl-valine-citrulline-p-aminobenzyloxycarbonyl (MC-vcPAB) linker (anti-FcRL5-MC-vcPAB-MMAE) or conjugated via lysines to the maytansinoid DM4 through a disulfide linker (anti-FcRL5-SPDB-DM4).	Disulfides	292-301	Fc receptor like 5	Homo sapiens	45-50
16210588-3	2005	Recently, we demonstrated that HLA-G forms disulfide-linked high molecular complexes on the surface of transfected cells.	Disulfides	43-52	major histocompatibility complex, class I, G	Homo sapiens	31-36
9915839-1	1999	4F2, also termed CD98, is an integral membrane protein consisting of a heavy chain linked to a light chain by disulfide bond.	Disulfides	110-119	solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2	Mus musculus	0-3
16185074-2	2005	In a previous study we demonstrated that ATTR Tyr114Cys forms intermolecular disulfide bonds, which partly impair fibril formation and result in a more amorphous morphology.	Disulfides	77-86	transthyretin	Homo sapiens	41-45
16185074-4	2005	To deduce the role of intermolecular disulfide bridging in fibril formation we generated and characterized the TTR Cys10Ala/Tyr114Cys double mutant.	Disulfides	37-46	transthyretin	Homo sapiens	111-114
16185074-6	2005	We also purified a disulfide-linked dimeric form of TTR Cys10Ala/Tyr114Cys, which was recognized by the anti-TTR amyloid-specific monoclonal antibody MAb (39-44).	Disulfides	19-28	transthyretin	Homo sapiens	52-55
16185074-6	2005	We also purified a disulfide-linked dimeric form of TTR Cys10Ala/Tyr114Cys, which was recognized by the anti-TTR amyloid-specific monoclonal antibody MAb (39-44).	Disulfides	19-28	transthyretin	Homo sapiens	109-112
22512645-2	2012	To explore the effects of disulfide bonds on antimicrobial activity of AvBD-6, two peptides with or without Cys residues were designed and expressed in Pichia Pastoris.	Disulfides	26-35	avian beta-defensin 6	Gallus gallus	71-77
9915839-1	1999	4F2, also termed CD98, is an integral membrane protein consisting of a heavy chain linked to a light chain by disulfide bond.	Disulfides	110-119	solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2	Mus musculus	17-21
22634549-3	2012	Here, we show that restriction of the flexibility of the loop by a disulfide cross-linking between cysteines within the loop results in the inefficient formation of a stable GroEL-polypeptide-GroES ternary complex and inefficient folding.	Disulfides	67-76	heat shock protein family D (Hsp60) member 1	Homo sapiens	174-179
9915857-4	1999	N-terminal disulfide-dependent dimerization was preserved at near wild type levels in the TM1-2 (at Cys-1) and TM2 proteins (at Cys-1 and Cys6), and to a lesser extent in TM1 (at Cys-1), but not in TM1-2-3.	Disulfides	11-20	cystin 1	Homo sapiens	100-105
22897429-5	2012	In this study, we synthetically linked two DV1 peptides with the formation of a disulfide bond between the two cysteine residues present in the peptide sequence to generate a dimeric molecule potentially capable of interacting with two CXCR4 receptors.	Disulfides	80-89	C-X-C motif chemokine receptor 4	Homo sapiens	236-241
16190664-1	2005	Bovine beta-lactoglobulin B (beta-LG) is susceptible to pressure treatment, which unfolds it, allowing thiol-catalyzed disulfide bond interchange to occur, facilitating intermolecular bonding (both noncovalent and disulfide).	Disulfides	119-128	beta-lactoglobulin	Bos taurus	7-27
16190664-1	2005	Bovine beta-lactoglobulin B (beta-LG) is susceptible to pressure treatment, which unfolds it, allowing thiol-catalyzed disulfide bond interchange to occur, facilitating intermolecular bonding (both noncovalent and disulfide).	Disulfides	119-128	beta-lactoglobulin	Bos taurus	29-36
9915857-4	1999	N-terminal disulfide-dependent dimerization was preserved at near wild type levels in the TM1-2 (at Cys-1) and TM2 proteins (at Cys-1 and Cys6), and to a lesser extent in TM1 (at Cys-1), but not in TM1-2-3.	Disulfides	11-20	cystin 1	Homo sapiens	128-133
16190664-1	2005	Bovine beta-lactoglobulin B (beta-LG) is susceptible to pressure treatment, which unfolds it, allowing thiol-catalyzed disulfide bond interchange to occur, facilitating intermolecular bonding (both noncovalent and disulfide).	Disulfides	214-223	beta-lactoglobulin	Bos taurus	7-27
9915857-4	1999	N-terminal disulfide-dependent dimerization was preserved at near wild type levels in the TM1-2 (at Cys-1) and TM2 proteins (at Cys-1 and Cys6), and to a lesser extent in TM1 (at Cys-1), but not in TM1-2-3.	Disulfides	11-20	cystin 1	Homo sapiens	128-133
16190664-1	2005	Bovine beta-lactoglobulin B (beta-LG) is susceptible to pressure treatment, which unfolds it, allowing thiol-catalyzed disulfide bond interchange to occur, facilitating intermolecular bonding (both noncovalent and disulfide).	Disulfides	214-223	beta-lactoglobulin	Bos taurus	29-36
22733835-5	2012	Quiescin Q6 (QSOX1), a protein involved in the formation of disulfide bridges, emerged as the best performing marker for ADHF (with an area under the receiver operator characteristic curve of 0.86, 95% confidence interval: 0.79-0.92), and novel isoforms of NPs were also identified.	Disulfides	60-69	quiescin sulfhydryl oxidase 1	Rattus norvegicus	13-18
10025946-3	1999	In this paper, we show (i) that both IGF-I and IGF-II are unable to form and maintain their native disulfide bonds at redox conditions that are similar to the situation in the secretory vesicles in vivo and (ii) that the presence of protein disulfide isomerase does not overcome this problem.	Disulfides	99-108	insulin like growth factor 2	Homo sapiens	47-53
9882436-0	1999	Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III.	Disulfides	8-17	serpin family C member 1	Homo sapiens	116-132
9878111-3	1998	These results suggest that the interchain disulfide bond between the TCR clonotypic chains is not required for TCR assembly and cell surface expression, but it plays an important role in maintaining the functional integrity of the TCR complex.	Disulfides	42-51	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	69-72
22716933-5	2012	Subcellular fractionation of isolated cerebral microvessels revealed that the bulk of P-glycoprotein constitutively traffics to membrane domains containing high molecular weight, disulfide-bonded P-glycoprotein-containing structures that cofractionate with membrane domains enriched with monomeric and high molecular weight, disulfide-bonded, caveolin-1-containing structures.	Disulfides	179-188	ATP-binding cassette, subfamily B (MDR/TAP), member 1B	Rattus norvegicus	86-100
22716933-5	2012	Subcellular fractionation of isolated cerebral microvessels revealed that the bulk of P-glycoprotein constitutively traffics to membrane domains containing high molecular weight, disulfide-bonded P-glycoprotein-containing structures that cofractionate with membrane domains enriched with monomeric and high molecular weight, disulfide-bonded, caveolin-1-containing structures.	Disulfides	179-188	ATP-binding cassette, subfamily B (MDR/TAP), member 1B	Rattus norvegicus	196-210
22716933-5	2012	Subcellular fractionation of isolated cerebral microvessels revealed that the bulk of P-glycoprotein constitutively traffics to membrane domains containing high molecular weight, disulfide-bonded P-glycoprotein-containing structures that cofractionate with membrane domains enriched with monomeric and high molecular weight, disulfide-bonded, caveolin-1-containing structures.	Disulfides	325-334	ATP-binding cassette, subfamily B (MDR/TAP), member 1B	Rattus norvegicus	86-100
16143573-7	2005	Step-by-step disulfide bond formation was considered to be critical for the complete refolding of denatured beta-LG.	Disulfides	13-22	beta-lactoglobulin	Bos taurus	108-115
9743336-4	1998	Reduction and carboxyamidomethylation of immunoprecipitated BY55 gave a band of 27 kDa, whereas reduction alone led to an 80-kDa species, suggesting that BY55 is a tightly disulfide-linked multimer.	Disulfides	172-181	CD160 molecule	Homo sapiens	60-64
16114871-10	2005	The third and fourth cysteines of PANDER, C91 and C229, were shown to form one disulfide bond and be functionally important.	Disulfides	79-88	CD244 molecule A	Mus musculus	42-45
16097802-11	2005	It is proposed that the reaction products of the reduction of selenite inhibited the activity of hGSTO1-1 by reacting with disulfides of glutathionylated cysteines to form bis (S-cysteinyl)selenide and S-selanylcysteine and had little or no interaction with the sulfhydryl of Cys-32 in the active site of the enzyme.	Disulfides	123-133	glutathione S-transferase omega 1	Homo sapiens	97-105
22771213-5	2012	The model-structure agrees with previous disulfide mapping studies and enables us to derive molecular interpretations of electrophysiological recordings that we obtained for two KCNE1 mutations.	Disulfides	41-50	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	178-183
9743336-4	1998	Reduction and carboxyamidomethylation of immunoprecipitated BY55 gave a band of 27 kDa, whereas reduction alone led to an 80-kDa species, suggesting that BY55 is a tightly disulfide-linked multimer.	Disulfides	172-181	CD160 molecule	Homo sapiens	154-158
9712313-6	1998	Glycosylation sites and disulfide bonds present in other species are generally conserved in the mink LIF sequence.	Disulfides	24-33	leukemia inhibitory factor	Mus musculus	101-104
22802670-5	2012	Furthermore, we found that an engineered, disulfide cross-linked ClpB hexamer is fully functional biochemically, suggesting that ClpB deoligomerization is not required for protein disaggregation.	Disulfides	42-51	caseinolytic mitochondrial matrix peptidase chaperone subunit B	Homo sapiens	65-69
22802670-5	2012	Furthermore, we found that an engineered, disulfide cross-linked ClpB hexamer is fully functional biochemically, suggesting that ClpB deoligomerization is not required for protein disaggregation.	Disulfides	42-51	caseinolytic mitochondrial matrix peptidase chaperone subunit B	Homo sapiens	129-133
15958486-9	2005	This timing coincided with the formation of disulfide bonds within tyrosinase and the cleavage of its signal sequence.	Disulfides	44-53	tyrosinase	Homo sapiens	67-77
15998238-0	2005	Zofenoprilat-glutathione mixed disulfide as a specific S-thiolating agent of bovine lens aldose reductase.	Disulfides	31-40	aldose reductase	Bos taurus	89-105
9680483-6	1998	In order to determine the critical interhelical interactions responsible for the molecular recognition between the c-Myc and Max LZs, the solution structure of the disulfide-linked c-Myc-Max heterodimeric LZ was solved by two-dimensional 1H-NMR techniques at 25 degreesC and pH 4.7.	Disulfides	164-173	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	115-120
22493502-4	2012	Here we show that, in the presence of b(0,+)AT, three disulfides were formed in the rBAT ectodomain.	Disulfides	54-64	solute carrier family 7 member 9	Homo sapiens	38-46
22493502-4	2012	Here we show that, in the presence of b(0,+)AT, three disulfides were formed in the rBAT ectodomain.	Disulfides	54-64	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	84-88
9680483-6	1998	In order to determine the critical interhelical interactions responsible for the molecular recognition between the c-Myc and Max LZs, the solution structure of the disulfide-linked c-Myc-Max heterodimeric LZ was solved by two-dimensional 1H-NMR techniques at 25 degreesC and pH 4.7.	Disulfides	164-173	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	181-186
15879598-6	2005	In this study we report that rat TrxR1 activity in Trx-dependent disulfide reduction was inhibited by curcumin.	Disulfides	65-74	thioredoxin reductase 1	Homo sapiens	33-38
22220984-7	2012	CRITICAL ISSUES: Besides disulfide-bond generation, Ero1alpha also regulates calcium release from the ER and the secretion of disulfide-linked oligomers through its reversible association with the chaperone ERp44.	Disulfides	126-135	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	52-61
9668102-4	1998	The thioredoxin domain of TRP32 has thioredoxin-like reducing activity, which can reduce the interchain disulfide bridges of insulin in vitro.	Disulfides	104-113	thioredoxin	Homo sapiens	4-15
22324914-8	2012	On the other hand, replacement of Cys6 or Cys69 with serine led to a complete loss of catalytic activity, indicating the necessity of these residues for maintaining an active conformation of human RNase kappa by forming a disulfide bond.	Disulfides	222-231	ribonuclease K	Homo sapiens	197-208
22324914-9	2012	Due to the absolute conservation of these cysteine residues, the Cys6-Cys69 disulfide bond is likely to exist in all RNase kappa family members.	Disulfides	76-85	ribonuclease K	Homo sapiens	117-128
22105604-7	2012	In a proof of concept murine model of hepatic necrosis induced by acetaminophen, during inflammation, the predominant form of serum HMGB1 is the active one, containing a C106 thiol group and a disulfide bond between C23 and C45, whereas the inactive form of HMGB1, containing terminally oxidized cysteines, accumulates during inflammation resolution and hepatic regeneration.	Disulfides	193-202	nucleolin	Mus musculus	216-219
15985154-9	2005	The homodimeric interface of CD9 was mapped, by disulfide cross-linking of single-cysteine mutants, to the vicinity of residues Leu14 and Phe17 in TM1 (positions g and c) and Gly77, Gly80 and Ala81 in TM2 (positions d, g and a, respectively).	Disulfides	48-57	CD9 molecule	Homo sapiens	29-32
9668102-4	1998	The thioredoxin domain of TRP32 has thioredoxin-like reducing activity, which can reduce the interchain disulfide bridges of insulin in vitro.	Disulfides	104-113	thioredoxin	Homo sapiens	36-47
9660813-6	1998	We have found that pro-IGF-2 can initially form two disulfide isomers that undergo rearrangement to a single conformation in vivo.	Disulfides	52-61	insulin like growth factor 2	Homo sapiens	23-28
15924415-11	2005	In conclusion, the heterodimer comprises one molecule each of TFF1 and TFIZ1, and the disulfide bond between TFF1 and TFIZ1 is the most important factor stabilizing the heterodimer.	Disulfides	86-95	gastrokine 2	Homo sapiens	71-76
15924415-11	2005	In conclusion, the heterodimer comprises one molecule each of TFF1 and TFIZ1, and the disulfide bond between TFF1 and TFIZ1 is the most important factor stabilizing the heterodimer.	Disulfides	86-95	gastrokine 2	Homo sapiens	118-123
22291015-9	2012	Our results argue that the main effect of intramolecular disulfide bond formation is to preferentially stabilize conformers within the unfolded ensemble that place the aggregation-prone tau subsequences, PHF6* and PHF6, in conformations that are inconsistent with the formation of cross-beta-structure.	Disulfides	57-66	PHD finger protein 6	Homo sapiens	204-208
22291015-9	2012	Our results argue that the main effect of intramolecular disulfide bond formation is to preferentially stabilize conformers within the unfolded ensemble that place the aggregation-prone tau subsequences, PHF6* and PHF6, in conformations that are inconsistent with the formation of cross-beta-structure.	Disulfides	57-66	PHD finger protein 6	Homo sapiens	214-218
22442221-4	2012	PPD6 is unique among the PsbP family of proteins in that it contains a conserved disulfide bond which can be reduced in vitro by thioredoxin.	Disulfides	81-90	thylakoid lumenal protein (Mog1/PsbP/DUF1795-like photosystem II reaction center PsbP family protein)	Arabidopsis thaliana	0-4
9665729-4	1998	Disulfide-linked dimers of tau constructs representing the repeat domain assemble into PHFs most efficiently, but other tau isoforms or constructs form bona fide PHFs as well.	Disulfides	0-9	microtubule associated protein tau	Homo sapiens	27-30
22002549-2	2012	Wild-type HspB1 and Cys mutants of HspB5, HspB6 and HspB8 containing a single Cys residue in position homologous to that of Cys137 of human HspB1 were able to generate heterodimers cross-linked by disulfide bond.	Disulfides	197-206	crystallin alpha B	Homo sapiens	35-40
15908390-3	2005	Previous studies have shown that both human and mouse airways express a variety of these molecules, including defensins, cathelicidins, and the four-disulfide core protein secretory leukocyte protease inhibitor.	Disulfides	149-158	secretory leukocyte peptidase inhibitor	Mus musculus	172-210
15820220-6	2005	One of the two predominant BPTI intermediates (Cys5-Cys14, Cys30-Cys51, Cys38-Cys55) contains a native disulfide Cys30-Cys51 and constitutes about 34% of the total BPTI folding intermediates.	Disulfides	103-112	spleen trypsin inhibitor I	Bos taurus	27-31
15820220-6	2005	One of the two predominant BPTI intermediates (Cys5-Cys14, Cys30-Cys51, Cys38-Cys55) contains a native disulfide Cys30-Cys51 and constitutes about 34% of the total BPTI folding intermediates.	Disulfides	103-112	spleen trypsin inhibitor I	Bos taurus	164-168
22278742-2	2012	We find that Cys-192 and Cys-331 of GARP disulfide link to the TGFbeta1 prodomain and that GARP with C192A and C331A mutations can also noncovalently associate with proTGFbeta1.	Disulfides	41-50	leucine rich repeat containing 32	Homo sapiens	36-40
9667953-6	1998	After binding of this hormone derivative to rat liver microsomes, followed by photolysis and subsequent reduction of disulfide bridges, the specific transfer of the radiolabeled moiety to prolactin receptor (PRL-R) was achieved.	Disulfides	117-126	prolactin receptor	Rattus norvegicus	188-206
22278742-6	2012	Activation requires the RGD motif of latent TGFbeta, disulfide linkage between GARP and latent TGFbeta, and membrane association of GARP.	Disulfides	53-62	leucine rich repeat containing 32	Homo sapiens	79-83
15761666-1	2005	The thioredoxins (Trxs) constitute a family of enzymes which catalyze the reduction of protein disulfide bonds.	Disulfides	95-104	thioredoxin 1	Mus musculus	4-16
15695509-3	2005	The meprin B isoform exists primarily as a cell-surface homooligomer composed of disulfide-linked, multidomain beta-subunits.	Disulfides	81-90	meprin A subunit beta	Homo sapiens	4-12
9667953-6	1998	After binding of this hormone derivative to rat liver microsomes, followed by photolysis and subsequent reduction of disulfide bridges, the specific transfer of the radiolabeled moiety to prolactin receptor (PRL-R) was achieved.	Disulfides	117-126	prolactin receptor	Rattus norvegicus	208-213
15705595-1	2005	Upon nonreducing Tris-Tricine-urea-SDS-PAGE, newly synthesized proinsulin from pancreatic islets of normal rodents forms a band fast mobility representing the native disulfide isomer, which is efficiently secreted.	Disulfides	166-175	insulin II	Mus musculus	63-73
15705595-4	2005	The "Akita-type" proinsulin mutation, which causes dominant-negative diabetes mellitus due to point mutation C(A7)Y that leaves B7-cysteine without its disulfide pairing partner, is recovered as a form that near quantitatively co-migrates with the aberrant isomer 1 band of proinsulin.	Disulfides	152-161	insulin II	Mus musculus	17-27
22214851-6	2012	CHCHD4.1 is identical to MIA40, the homolog of yeast Mia40, a key component of the mitochondrial disulfide relay system that regulates electron transfer to cytochrome c. Further analysis revealed that CHCHD4 proteins contain an evolutionarily conserved coiled-coil-helix-coiled-coil-helix (CHCH) domain important for mitochondrial localization.	Disulfides	97-106	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-6
22214851-6	2012	CHCHD4.1 is identical to MIA40, the homolog of yeast Mia40, a key component of the mitochondrial disulfide relay system that regulates electron transfer to cytochrome c. Further analysis revealed that CHCHD4 proteins contain an evolutionarily conserved coiled-coil-helix-coiled-coil-helix (CHCH) domain important for mitochondrial localization.	Disulfides	97-106	Mia40p	Saccharomyces cerevisiae S288C	25-30
22214851-6	2012	CHCHD4.1 is identical to MIA40, the homolog of yeast Mia40, a key component of the mitochondrial disulfide relay system that regulates electron transfer to cytochrome c. Further analysis revealed that CHCHD4 proteins contain an evolutionarily conserved coiled-coil-helix-coiled-coil-helix (CHCH) domain important for mitochondrial localization.	Disulfides	97-106	Mia40p	Saccharomyces cerevisiae S288C	53-58
9647238-2	1998	In C8 isolated from serum, these are arranged as a disulfide-linked C8 alpha-gamma dimer that is noncovalently associated with C8 beta.	Disulfides	51-60	complement C8 alpha chain	Homo sapiens	68-76
22214851-6	2012	CHCHD4.1 is identical to MIA40, the homolog of yeast Mia40, a key component of the mitochondrial disulfide relay system that regulates electron transfer to cytochrome c. Further analysis revealed that CHCHD4 proteins contain an evolutionarily conserved coiled-coil-helix-coiled-coil-helix (CHCH) domain important for mitochondrial localization.	Disulfides	97-106	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	201-207
22224850-1	2012	The oxidative folding mechanism in the intermembrane space of human mitochondria underpins a disulfide relay system consisting of the import receptor Mia40 and the homodimeric FAD-dependent thiol oxidase ALR.	Disulfides	93-102	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	150-155
22224850-4	2012	The intermediate critical for the electron-transfer process implies the formation of a specific inter-subunit disulfide which exclusively allows electron flow from Mia40 to FAD.	Disulfides	110-119	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	164-169
15708374-2	2005	This work reveals that mastin is composed of catalytic domain singlets and disulfide-linked dimers.	Disulfides	75-84	tryptase pseudogene 2	Homo sapiens	23-29
15736952-6	2005	In the models of the ASIP fragment complexed with both receptors, the core ligand tripeptide, Arg-Phe-Phe, positioned between TMHs 3 and 6, is shifted toward TMHs 2 and 7 relative to its position in the AGRP-hMC4R model, while the N-terminal loop and two central disulfides of the antagonists interact with EL2 of the receptors.	Disulfides	263-273	agouti signaling protein	Homo sapiens	21-25
22079049-5	2012	The JTB structure has a distant relationship to the midkine/pleiotrophin fold, particularly in the conservation of distinctive disulfide bridge patterns.	Disulfides	127-136	jumping translocation breakpoint	Homo sapiens	4-7
9603903-4	1998	The experiments reported here show that both MAO A and MAO B contain a redox-active disulfide at the catalytic center.	Disulfides	84-93	monoamine oxidase A	Homo sapiens	45-50
22194330-0	2012	The structure of the Bach2 POZ-domain dimer reveals an intersubunit disulfide bond.	Disulfides	68-77	BTB domain and CNC homolog 2	Homo sapiens	21-26
22194330-7	2012	The Bach2 POZ domain crystallized in two forms which differed by the presence of an intersubunit disulfide bond.	Disulfides	97-106	BTB domain and CNC homolog 2	Homo sapiens	4-9
22194330-8	2012	The intersubunit disulfide bond is present both in bacterially expressed Bach2 POZ domain in solution and in protein expressed in transfected eukaryotic cells.	Disulfides	17-26	BTB domain and CNC homolog 2	Homo sapiens	73-78
15766403-8	2005	CONCLUSION: Phage antibodies against NH-LBP were obtained successfully, which lays the foundation for preparing disulfide stabilized Fv fragments antibody (dsFv) against NH-LBP, understanding the function of LBP in vivo, and prevention and therapy of excessive inflammatory reaction.	Disulfides	112-121	lipopolysaccharide binding protein	Homo sapiens	40-43
15766403-8	2005	CONCLUSION: Phage antibodies against NH-LBP were obtained successfully, which lays the foundation for preparing disulfide stabilized Fv fragments antibody (dsFv) against NH-LBP, understanding the function of LBP in vivo, and prevention and therapy of excessive inflammatory reaction.	Disulfides	112-121	lipopolysaccharide binding protein	Homo sapiens	173-176
15766403-8	2005	CONCLUSION: Phage antibodies against NH-LBP were obtained successfully, which lays the foundation for preparing disulfide stabilized Fv fragments antibody (dsFv) against NH-LBP, understanding the function of LBP in vivo, and prevention and therapy of excessive inflammatory reaction.	Disulfides	112-121	lipopolysaccharide binding protein	Homo sapiens	173-176
9585516-2	1998	One of the sites predicted by the Dezymer computer program to introduce a tetrahedral tetrathiolate iron center included the intrinsic Cys32-Cys35 disulfide of wild-type thioredoxin and two additional mutants, Trp28Cys and Ile75Cys, thereby converting a disulfide into a metal-based redox center.	Disulfides	147-156	thioredoxin	Homo sapiens	170-181
15466936-1	2005	Formation and rearrangement of disulfide bonds during the correct folding of nascent proteins is modulated by a family of enzymes known as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERP5), and ERP57.	Disulfides	31-40	protein disulfide isomerase family A member 6	Homo sapiens	206-237
15466936-1	2005	Formation and rearrangement of disulfide bonds during the correct folding of nascent proteins is modulated by a family of enzymes known as thiol isomerases, which include protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERP5), and ERP57.	Disulfides	31-40	protein disulfide isomerase family A member 6	Homo sapiens	239-243
15683245-6	2005	For CRF2(a)-rNT, which bears five cysteine residues (C2-C6), the disulfide arrangement C2-C5 and C4-C6 was found, leaving C3 free.	Disulfides	65-74	corticotropin releasing hormone receptor 2	Rattus norvegicus	4-8
15683245-7	2005	This is consistent with the disulfide pattern of CRF1-rNT, which has six cysteines and in which C1 is paired with C3.	Disulfides	28-37	corticotropin releasing hormone receptor 1	Rattus norvegicus	49-53
21813750-3	2011	Several studies have suggested that prestin forms homo-oligomers that may be stabilized by disulfide bonds.	Disulfides	91-100	solute carrier family 26 member 5	Homo sapiens	36-43
21813750-13	2011	We suggest that no disulfide bond is essential for prestin function.	Disulfides	19-28	solute carrier family 26 member 5	Homo sapiens	51-58
9585516-2	1998	One of the sites predicted by the Dezymer computer program to introduce a tetrahedral tetrathiolate iron center included the intrinsic Cys32-Cys35 disulfide of wild-type thioredoxin and two additional mutants, Trp28Cys and Ile75Cys, thereby converting a disulfide into a metal-based redox center.	Disulfides	254-263	thioredoxin	Homo sapiens	170-181
9608841-2	1998	A genetically altered E. coli dihydrofolate reductase (DHFR-ASC) was attached to a carboxymethyldextran matrix layer covering the sensor surface of an SPR biosensor through a disulfide linkage at the engineered protein"s C-terminus.	Disulfides	175-184	Dihydrofolate reductase	Escherichia coli	30-53
21846901-7	2011	Decreased NOX2 activity additionally increased the phagosome"s ability to reduce disulfides, further enhancing the efficiency of the macrophage to degrade proteins containing disulfide bonds.	Disulfides	81-91	cytochrome b-245 beta chain	Homo sapiens	10-14
21846901-7	2011	Decreased NOX2 activity additionally increased the phagosome"s ability to reduce disulfides, further enhancing the efficiency of the macrophage to degrade proteins containing disulfide bonds.	Disulfides	81-90	cytochrome b-245 beta chain	Homo sapiens	10-14
15650193-0	2005	The fusion-controlling disulfide bond isomerase in retrovirus Env is triggered by protein destabilization.	Disulfides	23-32	endogenous retrovirus group K member 20	Homo sapiens	62-65
9605329-1	1998	Thiol/disulfide oxidoreductases like thioredoxin, glutaredoxin, DsbA, or protein disulfide isomerase (PDI) share the thioredoxin fold and a catalytic disulfide bond with the sequence Cys-Xaa-Xaa-Cys (Xaa corresponds to any amino acid).	Disulfides	6-15	protein-disulfide isomerase	Escherichia coli	73-100
15723641-0	2005	Prosequence-mediated disulfide coupled folding of the peptide hormones guanylin and uroguanylin.	Disulfides	21-30	guanylate cyclase activator 2B	Homo sapiens	84-95
15675818-4	2004	In model beta-LG systems, there is evidence that the aggregates of heated beta-LG are held together by a mixture of intermolecular non-covalent association and heat-induced non-native disulfide bonds.	Disulfides	184-193	beta-lactoglobulin	Bos taurus	74-81
15675818-6	2004	These interchange reactions were explored by examining the products of heat treatment to determine the novel disulfide bonds that form in the heated beta-LG aggregates.	Disulfides	109-118	beta-lactoglobulin	Bos taurus	149-156
15675818-8	2004	Comparisons of these peptide patterns showed that some of the Cys160 was in the reduced form in heated beta-LG aggregates, indicating that the Cys160-Cys66 disulfide bond had been broken during heating.	Disulfides	156-165	beta-lactoglobulin	Bos taurus	103-110
15675818-9	2004	This finding suggests that disulfide bond interchange reactions between beta-LG non-native monomers, or polymers, and other proteins could occur largely via Cys160.	Disulfides	27-36	beta-lactoglobulin	Bos taurus	72-79
15675819-2	2004	Disulfide bonding patterns between bovine beta-lactoglobulin and kappa-casein.	Disulfides	0-9	beta-lactoglobulin	Bos taurus	42-60
21978460-1	2011	BACKGROUND: Alpha 2 macroglobulin (A2M; also known as ovostatin), a homotetrameric protein with four disulfide-linked subunits, has the unique feature of inactivating/inhibiting most known proteases including serine-, threonine-, cysteine-, aspartic- and metalloproteases.	Disulfides	101-110	alpha-2-macroglobulin	Gallus gallus	12-33
21978460-1	2011	BACKGROUND: Alpha 2 macroglobulin (A2M; also known as ovostatin), a homotetrameric protein with four disulfide-linked subunits, has the unique feature of inactivating/inhibiting most known proteases including serine-, threonine-, cysteine-, aspartic- and metalloproteases.	Disulfides	101-110	alpha-2-macroglobulin	Gallus gallus	35-38
21936822-1	2011	We have previously demonstrated that the genes of SCPs (semen coagulum proteins) and the WFDC (whey acidic protein four-disulfide core)-type protease inhibitor elafin are homologous in spite of lacking similarity between their protein products.	Disulfides	120-129	protease inhibitor 3, skin-derived (SKALP)	Bos taurus	160-166
21177054-8	2011	A defective disulfide bond in PLP protein could be important in the pathogenesis of PMD.	Disulfides	12-21	proteolipid protein 1	Homo sapiens	30-33
9605329-1	1998	Thiol/disulfide oxidoreductases like thioredoxin, glutaredoxin, DsbA, or protein disulfide isomerase (PDI) share the thioredoxin fold and a catalytic disulfide bond with the sequence Cys-Xaa-Xaa-Cys (Xaa corresponds to any amino acid).	Disulfides	6-15	protein-disulfide isomerase	Escherichia coli	102-105
9598993-5	1998	The PSPI-21 molecule consists of two disulfide-linked polypeptide chains with molecular masses of 16.5 kDa and 4.5 kDa.	Disulfides	37-46	Kunitz-type protease inhibitor precursor	Solanum tuberosum	4-11
21866314-2	2011	We compared the activity of synthetic rat N-terminal POMC fragment 1-28 with disulfide bridges (N-POMC(w)) and without disulfide bridges (N-POMC(w/o)), with the activity of fibroblast growth factor (FGF2), a widely studied adrenal growth factor, and ACTH, in well-characterized pure cultures of both isolated adrenal Glomerulosa (G) and Fasciculata/Reticularis (F/R) cells.	Disulfides	77-86	proopiomelanocortin	Rattus norvegicus	53-57
15606776-9	2004	These experiments indicated that the C-terminal region of cN-II contains a cysteine prone to form a disulfide bond, thereby inactivating the enzyme.	Disulfides	100-109	5'-nucleotidase, cytosolic II	Homo sapiens	58-63
9605422-9	1998	The disulfides inhibited the hTrx-dependent proliferation of MCF-7 breast cancer cells with IC50 values for III-2 and IV-2 of 0.2 and 1.2 microM, respectively.	Disulfides	4-14	thioredoxin	Homo sapiens	29-33
9605422-10	1998	The results show that although the catalytic sites of TR and hTrx are reversibly inhibited by the 2-imidazolyl disulfides, it is the irreversible thioalkylation of Cys73 of hTrx by the disulfides that most probably accounts for the inhibition of thioredoxin-dependent cell growth by the disulfides.	Disulfides	111-121	thioredoxin	Homo sapiens	61-65
21704585-0	2011	EPR investigation of the role of B10 phenylalanine in neuroglobin - evidence that B10Phe mediates structural changes in the heme region upon disulfide-bridge formation.	Disulfides	141-150	ectonucleotide pyrophosphatase/phosphodiesterase 3	Homo sapiens	33-36
15531707-8	2004	Both Trx y were poor activators of fructose-1,6-bisphosphatase and NADP-MDH; however, a detailed study of the activation of NADP-MDH using site-directed mutants of its regulatory cysteines suggested that Trx y was able to reduce the less negative regulatory disulfide but not the more negative regulatory disulfide.	Disulfides	258-267	lactate/malate dehydrogenase family protein	Arabidopsis thaliana	124-132
21704585-0	2011	EPR investigation of the role of B10 phenylalanine in neuroglobin - evidence that B10Phe mediates structural changes in the heme region upon disulfide-bridge formation.	Disulfides	141-150	neuroglobin	Homo sapiens	54-65
15531707-8	2004	Both Trx y were poor activators of fructose-1,6-bisphosphatase and NADP-MDH; however, a detailed study of the activation of NADP-MDH using site-directed mutants of its regulatory cysteines suggested that Trx y was able to reduce the less negative regulatory disulfide but not the more negative regulatory disulfide.	Disulfides	305-314	lactate/malate dehydrogenase family protein	Arabidopsis thaliana	124-132
9605422-10	1998	The results show that although the catalytic sites of TR and hTrx are reversibly inhibited by the 2-imidazolyl disulfides, it is the irreversible thioalkylation of Cys73 of hTrx by the disulfides that most probably accounts for the inhibition of thioredoxin-dependent cell growth by the disulfides.	Disulfides	185-195	thioredoxin	Homo sapiens	61-65
21704585-2	2011	In human neuroglobin (NGB), the formation of a disulfide bridge between the CysCD7 and CysD5 is known to affect the heme environment and its ligand-binding kinetics.	Disulfides	47-56	neuroglobin	Homo sapiens	9-20
21704585-2	2011	In human neuroglobin (NGB), the formation of a disulfide bridge between the CysCD7 and CysD5 is known to affect the heme environment and its ligand-binding kinetics.	Disulfides	47-56	neuroglobin	Homo sapiens	22-25
9605422-10	1998	The results show that although the catalytic sites of TR and hTrx are reversibly inhibited by the 2-imidazolyl disulfides, it is the irreversible thioalkylation of Cys73 of hTrx by the disulfides that most probably accounts for the inhibition of thioredoxin-dependent cell growth by the disulfides.	Disulfides	185-195	thioredoxin	Homo sapiens	173-177
21704585-4	2011	While formation of a disulfide bridge in ferric wild-type NGB leads to a considerable change of its EPR parameters, only minor changes are observed in the case of ferric PheB10Leu NGB.	Disulfides	21-30	neuroglobin	Homo sapiens	58-61
15173163-0	2004	Assignment of the four disulfides in the N-terminal somatomedin B domain of native vitronectin isolated from human plasma.	Disulfides	23-33	vitronectin	Homo sapiens	52-65
9559273-4	1998	These studies indicate that receptor-associated protein interacts with LDL receptor-related protein at multiple sites and assists the proper folding and disulfide bond formation of LDL receptor-related protein within the endoplasmic reticulum.	Disulfides	153-162	low density lipoprotein receptor	Homo sapiens	71-83
15173163-0	2004	Assignment of the four disulfides in the N-terminal somatomedin B domain of native vitronectin isolated from human plasma.	Disulfides	23-33	vitronectin	Homo sapiens	83-94
15173163-1	2004	The primary sequence of the N-terminal somatomedin B (SMB) domain of native vitronectin contains 44 amino acids, including a framework of four disulfide bonds formed by 8 closely spaced cysteines in sequence patterns similar to those found in the cystine knot family of proteins.	Disulfides	143-152	vitronectin	Homo sapiens	39-52
15070828-6	2004	Three (ovine TKDP-3, bovine TKDP-3, and bovine TKDP-4) lacked the conserved cysteines at residues 14 and 38 that form one of the highly conserved disulfide bonds that are structurally important in all known mammalian Kunitz proteins.	Disulfides	146-155	trophoblast Kunitz domain protein 4	Bos taurus	47-53
21875933-3	2011	MSP binding to RON requires proteolytic conversion of the inactive single-chain form (pro-MSP) into the disulfide-linked alpha/beta heterodimer.	Disulfides	104-113	macrophage stimulating 1 receptor	Homo sapiens	15-18
21507943-6	2011	Thus, for the first time, we demonstrated that GP Ibbeta/GP IX mediates the disulfide-linked GP Ibalpha localization to the GEMs, which is critical for vWf interaction at high shear.	Disulfides	76-85	glycoprotein Ib platelet subunit beta	Homo sapiens	47-56
21507943-6	2011	Thus, for the first time, we demonstrated that GP Ibbeta/GP IX mediates the disulfide-linked GP Ibalpha localization to the GEMs, which is critical for vWf interaction at high shear.	Disulfides	76-85	glycoprotein Ib platelet subunit alpha	Homo sapiens	93-103
21401803-0	2011	A new disulfide-linked dimer of a single-chain antibody fragment against human CD47 induces apoptosis in lymphoid malignant cells via the hypoxia inducible factor-1alpha pathway.	Disulfides	6-15	CD47 molecule	Homo sapiens	79-83
15499198-1	2004	The binding properties of the disulfide covalent bond between N-acetyl-L-cysteine (NAC) and human serum albumin (HSA) were investigated.	Disulfides	30-39	X-linked Kx blood group	Homo sapiens	83-86
9559273-4	1998	These studies indicate that receptor-associated protein interacts with LDL receptor-related protein at multiple sites and assists the proper folding and disulfide bond formation of LDL receptor-related protein within the endoplasmic reticulum.	Disulfides	153-162	low density lipoprotein receptor	Homo sapiens	181-193
9521781-0	1998	Role of the [Fe4S4] cluster in mediating disulfide reduction in spinach ferredoxin:thioredoxin reductase.	Disulfides	41-50	thioredoxin	Homo sapiens	83-94
21686078-4	2011	TA-G1-COOH has a thioctic acid moiety, which is a 5-member ring containing a disulfide group that cleaves to produce two anchoring thiols to bond with the gold surface.	Disulfides	77-86	contactin 2	Homo sapiens	0-5
9530514-2	1998	TP1 dimer with intermolecular disulfide bond had similar DNA-melting activity to TP1, but was not detected in extracts from boar late spermatid nuclei.	Disulfides	30-39	transition protein 1	Homo sapiens	0-3
21575181-2	2011	The Ig-fold of the DraD possesses two major characteristics distinguishing it from the family of fimbrial subunits: 1) a distortion of the beta-barrel structure in the region of the acceptor cleft, demonstrated by a disturbance of the main-chain hydrogen bonds network, and 2) an unusually located disulfide bond connecting B and F strands - the localization exclusively observed in the subfamily of DraD/AfaD-type subunits.	Disulfides	298-307	EGF containing fibulin extracellular matrix protein 1	Homo sapiens	19-23
21575181-6	2011	3) The DraD specific disulfide bond is crucial at the folding stage and has little stability effect in the mature protein.	Disulfides	21-30	EGF containing fibulin extracellular matrix protein 1	Homo sapiens	7-11
15212484-2	2004	HRGS treatment of myofibrils caused cross-linking of myosin heavy chains (MHC) via disulfide bonding, an increase in Ca-ATPase activity, and a decrease in K-ATPase activity, suggesting that thiol groups of myosin including those at the active site were modified.	Disulfides	83-92	myosin, heavy chain 11, smooth muscle	Gallus gallus	53-72
15212484-2	2004	HRGS treatment of myofibrils caused cross-linking of myosin heavy chains (MHC) via disulfide bonding, an increase in Ca-ATPase activity, and a decrease in K-ATPase activity, suggesting that thiol groups of myosin including those at the active site were modified.	Disulfides	83-92	myosin, heavy chain 11, smooth muscle	Gallus gallus	74-77
9551909-7	1998	Whereas wild-type DM forms noncovalent alphabeta dimers, such dimers form inefficiently in 7.12.6; many mutant DM beta-chains instead form a disulfide-bonded dimer with DM alpha.	Disulfides	141-150	major histocompatibility complex, class II, DM alpha	Homo sapiens	169-177
15276181-6	2004	These might reduce disulfide bonds of VKORC1-like enzymes as a prerequisite for their catalytic activities.	Disulfides	19-28	Vitamin-K epoxide reductase	Drosophila melanogaster	38-44
15116395-5	2004	Finally, selected double immunohistochemistry showed that in the hypothalamus the highest levels of QSOX labeling were colocalized in neuron populations that express disulfide-bounded neuropeptides.	Disulfides	166-175	quiescin sulfhydryl oxidase 1	Rattus norvegicus	100-104
21440316-1	2011	Hepcidin is a highly conserved disulfide-bonded peptide that plays a central role in iron homeostasis.	Disulfides	31-40	hepcidin	Ovis aries	0-8
21377473-4	2011	We identified two previously undocumented disulfide bridges in the crystal structure of properly folded S100A3: one disulfide bridge is between Cys30 in the N-terminal pseudo-EF-hand and Cys68 in the C-terminal EF-hand (SS1), and another disulfide bridge attaches Cys99 in the C-terminal coil structure to Cys81 in helix IV (SS2).	Disulfides	116-125	butyrophilin like 2	Homo sapiens	325-328
21377473-4	2011	We identified two previously undocumented disulfide bridges in the crystal structure of properly folded S100A3: one disulfide bridge is between Cys30 in the N-terminal pseudo-EF-hand and Cys68 in the C-terminal EF-hand (SS1), and another disulfide bridge attaches Cys99 in the C-terminal coil structure to Cys81 in helix IV (SS2).	Disulfides	116-125	butyrophilin like 2	Homo sapiens	325-328
9538514-2	1998	These missense mutations consist of C127W and C139G transitions and result in a loss of one of three disulfide bonds in the fourth cysteine-rich repeat of the ligand-binding domain of the low-density lipoprotein receptor.	Disulfides	101-110	low density lipoprotein receptor	Homo sapiens	188-220
21410235-5	2011	(1) Elaboration of the scope of diversity of disulfide folding pathways, including the two opposite extreme models, represented by bovine pancreatic trypsin inhibitor (BPTI) and hirudin.	Disulfides	45-54	spleen trypsin inhibitor I	Bos taurus	131-166
21410235-5	2011	(1) Elaboration of the scope of diversity of disulfide folding pathways, including the two opposite extreme models, represented by bovine pancreatic trypsin inhibitor (BPTI) and hirudin.	Disulfides	45-54	spleen trypsin inhibitor I	Bos taurus	168-172
15157736-3	2004	Sequence analysis suggested that processing of the rat and mouse KiSS-1 proteins produces 52-amino-acid peptides, each with an amidated carboxyl terminal and with a single possible disulfide bond, corresponding to rat and mouse metastins.	Disulfides	181-190	KiSS-1 metastasis-suppressor	Mus musculus	65-71
15109270-0	2004	Disulfide bond rearrangement during formation of the chorionic gonadotropin beta-subunit cystine knot in vivo.	Disulfides	0-9	chorionic gonadotropin subunit beta 3	Homo sapiens	53-88
15109270-1	2004	The intracellular kinetic folding pathway of the human chorionic gonadotropin beta-subunit (hCG-beta) reveals the presence of a disulfide between Cys residues 38-57 that is not detected by X-ray analysis of secreted hCG-beta.	Disulfides	128-137	chorionic gonadotropin subunit beta 3	Homo sapiens	55-90
15109270-1	2004	The intracellular kinetic folding pathway of the human chorionic gonadotropin beta-subunit (hCG-beta) reveals the presence of a disulfide between Cys residues 38-57 that is not detected by X-ray analysis of secreted hCG-beta.	Disulfides	128-137	chorionic gonadotropin subunit beta 3	Homo sapiens	92-100
15109270-1	2004	The intracellular kinetic folding pathway of the human chorionic gonadotropin beta-subunit (hCG-beta) reveals the presence of a disulfide between Cys residues 38-57 that is not detected by X-ray analysis of secreted hCG-beta.	Disulfides	128-137	chorionic gonadotropin subunit beta 3	Homo sapiens	216-224
15109270-2	2004	This led us to propose that disulfide rearrangement is an essential feature of cystine knot formation during CG-beta folding.	Disulfides	28-37	chorionic gonadotropin subunit beta 3	Homo sapiens	109-116
21617224-3	2011	Protein disulfide isomerase (PDI) has been studied extensively as a key enzyme involving in the formation of the correct pattern of disulfide bonds in newly synthesized proteins.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	29-32
21556330-1	2011	BACKGROUND: Canonical serine protease inhibitors commonly bind to their targets through a rigid loop stabilised by an internal hydrogen bond network and disulfide bond(s).	Disulfides	153-162	complement component 1, s subcomponent 1	Mus musculus	22-37
15109270-8	2004	Thus, while defining the intracellular kinetic protein folding pathway of a monkey homologue of CG-beta, we detected the previously predicted disulfide exchange event crucial for CG-beta cystine knot formation and attainment of CG-beta assembly competence.	Disulfides	142-151	chorionic gonadotropin subunit beta 3	Homo sapiens	96-103
15109270-8	2004	Thus, while defining the intracellular kinetic protein folding pathway of a monkey homologue of CG-beta, we detected the previously predicted disulfide exchange event crucial for CG-beta cystine knot formation and attainment of CG-beta assembly competence.	Disulfides	142-151	chorionic gonadotropin subunit beta 3	Homo sapiens	179-186
21430264-2	2011	Here, we apply a site-directed technology, disulfide trapping, to interrogate structurally and functionally how an allosteric site on the Ser/Thr kinase, 3-phosphoinositide-dependent kinase 1 (PDK1)--the PDK1-interacting-fragment (PIF) pocket--is engaged by an activating peptide motif on downstream substrate kinases (PIFtides) and by small molecule fragments.	Disulfides	43-52	pyruvate dehydrogenase kinase 1	Homo sapiens	193-197
10027003-4	1998	MEN2A mutations involve cysteine residues present in the Ret extracellular domain and induce disulfide-linked Ret dimerization on the cell surface.	Disulfides	93-102	ret proto-oncogene	Homo sapiens	0-5
21167253-7	2011	The results showed that similarly to modified N-POMC without disulfide bridges, administration of synthetic N-POMC with disulfide bridges and the combination of ACTH and N-POMC promoted an increase of BrdU-positive nuclei in adrenal cortex.	Disulfides	61-70	proopiomelanocortin	Rattus norvegicus	110-114
21167253-7	2011	The results showed that similarly to modified N-POMC without disulfide bridges, administration of synthetic N-POMC with disulfide bridges and the combination of ACTH and N-POMC promoted an increase of BrdU-positive nuclei in adrenal cortex.	Disulfides	61-70	proopiomelanocortin	Rattus norvegicus	110-114
21167253-7	2011	The results showed that similarly to modified N-POMC without disulfide bridges, administration of synthetic N-POMC with disulfide bridges and the combination of ACTH and N-POMC promoted an increase of BrdU-positive nuclei in adrenal cortex.	Disulfides	120-129	proopiomelanocortin	Rattus norvegicus	110-114
15033933-1	2004	A missense mutation of the insulin 2 gene (Cys96Tyr) in Akita mice disrupting one of the two interchain disulfide bonds results in intracellular accumulation of misfolded proinsulin.	Disulfides	104-113	insulin II	Mus musculus	27-36
21167253-7	2011	The results showed that similarly to modified N-POMC without disulfide bridges, administration of synthetic N-POMC with disulfide bridges and the combination of ACTH and N-POMC promoted an increase of BrdU-positive nuclei in adrenal cortex.	Disulfides	120-129	proopiomelanocortin	Rattus norvegicus	110-114
15033933-1	2004	A missense mutation of the insulin 2 gene (Cys96Tyr) in Akita mice disrupting one of the two interchain disulfide bonds results in intracellular accumulation of misfolded proinsulin.	Disulfides	104-113	insulin II	Mus musculus	171-181
10027003-4	1998	MEN2A mutations involve cysteine residues present in the Ret extracellular domain and induce disulfide-linked Ret dimerization on the cell surface.	Disulfides	93-102	ret proto-oncogene	Homo sapiens	57-60
21167253-10	2011	In summary, the effect of synthetic N-POMC with disulfide bridges was similar to modified synthetic N-POMC, increasing proliferation in the adrenal cortex, confirming previous evidence that disulfide bridges are not essential to the N-POMC mitogenic effect.	Disulfides	48-57	proopiomelanocortin	Rattus norvegicus	38-42
10027003-4	1998	MEN2A mutations involve cysteine residues present in the Ret extracellular domain and induce disulfide-linked Ret dimerization on the cell surface.	Disulfides	93-102	ret proto-oncogene	Homo sapiens	110-113
9407079-1	1997	A catalyst of disulfide formation and isomerization during protein folding, protein-disulfide isomerase (PDI) has two catalytic sites housed in two domains homologous to thioredoxin, one near the N terminus and the other near the C terminus.	Disulfides	14-23	thioredoxin	Homo sapiens	170-181
15067095-10	2004	These data indicate that disulfide-linked intracellular H chain complexes are more prone to form and bind BiP in disease-prone wild-type B27 and B27-C67S rats than in disease-resistant HLA-B7 rats.	Disulfides	25-34	heat shock protein family A (Hsp70) member 5	Rattus norvegicus	106-109
9407079-2	1997	The thioredoxin domains, by themselves, can catalyze disulfide formation, but they are unable to catalyze disulfide isomerizations (Darby, N. J. and Creighton, T. E. (1995) Biochemistry 34, 11725-11735).	Disulfides	53-62	thioredoxin	Homo sapiens	4-15
21262965-6	2011	Moreover, mutations of a single Cys residue within the TMD of Cosmc prevent formation of disulfide-bonded dimers of Cosmc and eliminate ER retention.	Disulfides	89-98	C1GALT1 specific chaperone 1	Homo sapiens	62-67
14592831-0	2004	Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entry.	Disulfides	6-15	C-X-C motif chemokine receptor 4	Homo sapiens	47-52
9388210-5	1997	The affinity of other IGFBPs for insulin can be enhanced by modifications that disrupt disulfide bonds or remove the conserved COOH terminus.	Disulfides	87-96	insulin like growth factor binding protein 3	Homo sapiens	22-28
14592831-0	2004	Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entry.	Disulfides	6-15	endogenous retrovirus group K member 20	Homo sapiens	66-74
21262965-6	2011	Moreover, mutations of a single Cys residue within the TMD of Cosmc prevent formation of disulfide-bonded dimers of Cosmc and eliminate ER retention.	Disulfides	89-98	C1GALT1 specific chaperone 1	Homo sapiens	116-121
21383138-1	2011	Oxidative protein folding in the mitochondrial intermembrane space requires the transfer of a disulfide bond from MIA40 to the substrate.	Disulfides	94-103	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	114-119
14668347-1	2004	Mammalian heteromeric amino acid transporters (HATs) are composed of a multi-transmembrane spanning catalytic protein covalently associated with a type II glycoprotein (e.g. 4F2hc, rBAT) through a disulfide bond.	Disulfides	197-206	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	181-185
21383138-3	2011	Here we present the mechanistic basis of ALR-MIA40 interaction at atomic resolution by biochemical and structural analyses of the mitochondrial ALR isoform and its covalent mixed disulfide intermediate with MIA40.	Disulfides	179-188	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	45-50
9398631-5	1997	Under these conditions IGFBP-3 and IGFBP-5, but not the other IGFBPs, formed high molecular weight disulfide-linked multimers.	Disulfides	99-108	insulin like growth factor binding protein 3	Homo sapiens	23-30
21383138-3	2011	Here we present the mechanistic basis of ALR-MIA40 interaction at atomic resolution by biochemical and structural analyses of the mitochondrial ALR isoform and its covalent mixed disulfide intermediate with MIA40.	Disulfides	179-188	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	207-212
15017976-4	2004	Among these redox-regulated PTPs, PTEN, Cdc25 and low molecular weight PTP are known to form a disulfide bond between two cysteines, one in the active site and the other nearby, during oxidation by H(2)O(2).	Disulfides	95-104	protein tyrosine phosphatase non-receptor type 22	Homo sapiens	28-31
14764894-6	2004	Reaction of Keap1 with inducers results in formation of intermolecular disulfide bridges, probably between C273 of one Keap1 molecule and C288 of a second.	Disulfides	71-80	kelch-like ECH-associated protein 1	Mus musculus	12-17
20923387-5	2011	In addition, 279 +- 28 and 139 +- 22 mumol disulfide bonds per gram polymer, respectively, were identified on PAA-ATP1 and PAA-ATP2.	Disulfides	43-52	ATP synthase F1 subunit alpha	Homo sapiens	114-118
9369469-4	1997	A recent crystal structure determination of human thioredoxin revealed an inactive dimeric form of the protein covalently linked through a disulfide bond involving Cys 73 from each monomer [Weichsel et al.	Disulfides	139-148	thioredoxin	Homo sapiens	50-61
21105877-0	2011	Tryptophan hydroxylase 2 aggregates through disulfide cross-linking upon oxidation: possible link to serotonin deficits and non-motor symptoms in Parkinson"s disease.	Disulfides	44-53	tryptophan hydroxylase 2	Homo sapiens	0-24
21105877-9	2011	Sequential non-reducing/reducing 2-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting confirmed that TPH2 was one of a small number of cytosolic proteins that form disulfide-bonded aggregates.	Disulfides	202-211	tryptophan hydroxylase 2	Homo sapiens	139-143
14764894-6	2004	Reaction of Keap1 with inducers results in formation of intermolecular disulfide bridges, probably between C273 of one Keap1 molecule and C288 of a second.	Disulfides	71-80	kelch-like ECH-associated protein 1	Mus musculus	119-124
14713336-1	2004	Most cells contain high levels of glutathione and multiple glutaredoxins, which utilize the reducing power of glutathione to catalyze disulfide reductions in the presence of NADPH and glutathione reductase (the glutaredoxin system).	Disulfides	134-143	2,4-dienoyl-CoA reductase 1	Homo sapiens	174-179
9354654-2	1997	We have isolated a soluble, disulfide-linked dimer of murine KL (KL-CD) by expressing KL in Escherichia coli and refolding the denatured protein under conditions that promote the formation of both noncovalent dimers (KL-NC) and KL-CD.	Disulfides	28-37	kit ligand	Mus musculus	61-63
15040427-3	2004	The formation of a disulfide bridge between Cys 284 and Cys 373 in ISC beta-actin leads to actin filaments which depolymerize poorly at 37 degrees C. Glutathiolation of cysteines within spectrin results in this key membrane skeletal protein losing it"s E2/E3 ubiquitin-ligating/conjugating activity and therefore ability to self ubiquitinate.	Disulfides	19-28	POTE ankyrin domain family member F	Homo sapiens	71-81
21106880-2	2011	The TSHR is also unique among the glycoprotein hormone receptor in undergoing in vivo intramolecular cleavage into disulfide-linked A- and B-subunits with removal of an intervening "C-peptide" region.	Disulfides	115-124	thyroid stimulating hormone receptor	Homo sapiens	4-8
21278127-2	2011	Protein disulfide isomerase (PDI) family oxidoreductase PDIL2;3, an ortholog of human P5, contains a conserved structural disulfide in the redox-inactive thioredoxin-like (TRX) domain and was efficiently targeted to the surface of PB-I in a redox active site-dependent manner, whereas PDIL1;1, an ortholog of human PDI, was localized in the ER lumen.	Disulfides	8-17	submaxillary gland androgen regulated protein 3A	Homo sapiens	231-235
21278127-8	2011	We discuss PDIL2;3-dependent and PDIL2;3-independent oxidation pathways that sustain disulfide bonds of crP10 in PB-I.	Disulfides	85-94	submaxillary gland androgen regulated protein 3A	Homo sapiens	113-117
9354654-2	1997	We have isolated a soluble, disulfide-linked dimer of murine KL (KL-CD) by expressing KL in Escherichia coli and refolding the denatured protein under conditions that promote the formation of both noncovalent dimers (KL-NC) and KL-CD.	Disulfides	28-37	kit ligand	Mus musculus	65-70
21145477-1	2010	In this issue of Molecular Cell, Ron and colleagues (Zito et al., 2010b) show that an enzyme responsible for cleaning up hydrogen peroxide in the endoplasmic reticulum can contribute productively to disulfide bond formation.	Disulfides	199-208	macrophage stimulating 1 receptor	Homo sapiens	33-36
15036292-0	2004	Coupling of the heme and an internal disulfide bond in human neuroglobin.	Disulfides	37-46	neuroglobin	Homo sapiens	61-72
9354654-2	1997	We have isolated a soluble, disulfide-linked dimer of murine KL (KL-CD) by expressing KL in Escherichia coli and refolding the denatured protein under conditions that promote the formation of both noncovalent dimers (KL-NC) and KL-CD.	Disulfides	28-37	kit ligand	Mus musculus	65-67
15036292-4	2004	In the case of human neuroglobin, cysteines at positions CD7 and D5 are sufficiently close to form an internal disulfide bond.	Disulfides	111-120	neuroglobin	Homo sapiens	21-32
21145486-4	2010	Peroxiredoxin IV (PRDX4) stood out in this list, as the related cytosolic peroxiredoxins are known to form disulfides in the presence of hydroperoxides.	Disulfides	107-117	peroxiredoxin 4	Homo sapiens	0-16
9354654-2	1997	We have isolated a soluble, disulfide-linked dimer of murine KL (KL-CD) by expressing KL in Escherichia coli and refolding the denatured protein under conditions that promote the formation of both noncovalent dimers (KL-NC) and KL-CD.	Disulfides	28-37	kit ligand	Mus musculus	228-233
21145486-4	2010	Peroxiredoxin IV (PRDX4) stood out in this list, as the related cytosolic peroxiredoxins are known to form disulfides in the presence of hydroperoxides.	Disulfides	107-117	peroxiredoxin 4	Homo sapiens	18-23
21145486-4	2010	Peroxiredoxin IV (PRDX4) stood out in this list, as the related cytosolic peroxiredoxins are known to form disulfides in the presence of hydroperoxides.	Disulfides	107-117	peroxiredoxin 4	Homo sapiens	74-88
9353278-7	1997	Furthermore, the disulfide loop in the Gla domain of prothrombin is not required for complete carboxylation.	Disulfides	17-26	alpha-galactosidase A	Cricetulus griseus	39-42
21151939-1	2010	The CD94 transmembrane-anchored glycoprotein forms disulfide-bonded heterodimers with the NKG2A subunit to form an inhibitory receptor or with the NKG2C or NKG2E subunits to assemble a receptor complex with activating DAP12 signaling proteins.	Disulfides	51-60	killer cell lectin like receptor D1	Homo sapiens	4-8
9341233-1	1997	The 98 residue C-terminal domain of the cell-surface receptor protein CD2 (CD2.D1) has a beta-sandwich fold belonging to the immunoglobulin superfamily but lacking the usual disulfide bridges.	Disulfides	174-183	CD2 molecule	Homo sapiens	70-73
14504270-0	2003	Mutationally induced disulfide bond formation within the third extracellular loop causes melanocortin 4 receptor inactivation in patients with obesity.	Disulfides	21-30	melanocortin 4 receptor	Homo sapiens	89-112
14645556-10	2003	The results of these experiments support a model in which the cysteine residue at position 102 of GP(2b) forms an intermolecular cystine bridge with one of the cysteines of the GP(4) protein, while the cysteine residues at positions 48 and 137 of GP(2b) are linked by an intrachain disulfide bond.	Disulfides	282-291	integrin subunit alpha 2b	Homo sapiens	98-103
14645556-11	2003	In this model, another cysteine residue in the GP(4) protein is responsible for the covalent association of GP(3) with the disulfide-linked GP(2b)/GP(4) heterodimer.	Disulfides	123-132	integrin subunit alpha 2b	Homo sapiens	140-145
9341233-1	1997	The 98 residue C-terminal domain of the cell-surface receptor protein CD2 (CD2.D1) has a beta-sandwich fold belonging to the immunoglobulin superfamily but lacking the usual disulfide bridges.	Disulfides	174-183	CD2 molecule	Homo sapiens	75-81
20615094-2	2010	The spp24 BMP-2-binding/transforming growth factor receptor II homology-1 (TRH1) domain is a highly conserved N-to-C terminally disulfide-bonded 19-amino acid residue loop similar to those in fetuin and the BMP receptor II.	Disulfides	128-137	bone morphogenetic protein 2	Bos taurus	10-15
14529283-0	2003	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.	Disulfides	44-53	ectonucleoside triphosphate diphosphohydrolase 6	Homo sapiens	90-98
14529283-0	2003	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.	Disulfides	44-53	ectonucleoside triphosphate diphosphohydrolase 6	Homo sapiens	100-106
9372187-0	1997	SNAP-25 can self-associate to form a disulfide-linked complex.	Disulfides	37-46	synaptosome associated protein 25	Homo sapiens	0-7
21059944-4	2010	The disulfide bond (C125-C127) at the tip of Loop3 is important for determining the unique topology of Loop3, and docking E126 close to RANKL, which was supported by the inability of C127A or E126A mutants of RANK to bind to RANKL.	Disulfides	4-13	TNF superfamily member 11	Homo sapiens	136-141
21059944-4	2010	The disulfide bond (C125-C127) at the tip of Loop3 is important for determining the unique topology of Loop3, and docking E126 close to RANKL, which was supported by the inability of C127A or E126A mutants of RANK to bind to RANKL.	Disulfides	4-13	TNF superfamily member 11	Homo sapiens	225-230
21059946-2	2010	A class of such proteins with alpha-helical hairpin structure bridged by two intramolecular disulfides is trapped by a Mia40-dependent oxidative process.	Disulfides	92-102	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	119-124
20833783-1	2010	Recombinant human tissue plasminogen activator (rPA) is a truncated version of tissue plasminogen activator (tPA), which contains nine disulfide bonds and is prone to forming inactive inclusion bodies when expressed in bacteria.	Disulfides	135-144	chromosome 20 open reading frame 181	Homo sapiens	18-46
9372187-3	1997	Here we show that SNAP-25 can self-associate to form a disulfide-linked complex.	Disulfides	55-64	synaptosome associated protein 25	Homo sapiens	18-25
20833783-1	2010	Recombinant human tissue plasminogen activator (rPA) is a truncated version of tissue plasminogen activator (tPA), which contains nine disulfide bonds and is prone to forming inactive inclusion bodies when expressed in bacteria.	Disulfides	135-144	chromosome 20 open reading frame 181	Homo sapiens	79-107
12882976-0	2003	Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10.	Disulfides	59-68	translocase of inner mitochondrial membrane 10	Homo sapiens	109-114
9372187-6	1997	We also show that monomeric SNAP-25 and disulfide-linked SNAP-25 complexes are palmitoylated and that both can be cleaved by botulinum neurotoxin E.	Disulfides	40-49	synaptosome associated protein 25	Homo sapiens	57-64
12882976-8	2003	Taken together these data reveal this specific intramolecular disulfide bonding as the crucial mechanism for Tim10 folding and show that the inner cysteine pair has a more prominent role in this process.	Disulfides	62-71	translocase of inner mitochondrial membrane 10	Homo sapiens	109-114
9363441-9	1997	In summary, these results demonstrate that GalNAcT forms homodimers as a result of intermolecular disulfide bond formation in the ER.	Disulfides	98-107	beta-1,4-N-acetyl-galactosaminyl transferase 1	Mus musculus	43-50
14517240-3	2003	Here we show that ERp44 mediates Ero1alpha ER localization through the formation of reversible mixed disulfides.	Disulfides	101-111	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	33-42
20935509-7	2010	Moreover, the intramolecular disulfide bridge (C23/45) of HMGB1 is required for binding to Beclin 1 and sustaining autophagy.	Disulfides	29-38	beclin 1	Homo sapiens	91-99
20802033-0	2010	A periplasmic LolA derivative with a lethal disulfide bond activates the Cpx stress response system.	Disulfides	44-53	EBP cholestenol delta-isomerase	Homo sapiens	73-76
9287323-5	1997	Mutation of highly conserved cysteines in the amino-terminal domain and third extracellular loop of CCR2, but not in the fusion protein, resulted in a dramatic loss of MCP-1 binding, suggesting the existence of a critical intramolecular disulfide bond that positions the amino-terminal protein for ligand interaction.	Disulfides	237-246	C-C motif chemokine ligand 2	Homo sapiens	168-173
20214493-5	2010	Proteins destined to the intermembrane space are trapped by a disulfide relay mechanism that involves an electron cascade from the incoming substrate to Mia40, then on to Erv1, and finally to molecular oxygen via cytochrome c.	Disulfides	62-71	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	153-158
20657012-0	2010	The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1alpha.	Disulfides	43-53	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	125-134
20657012-1	2010	Disulfide formation in newly synthesized proteins entering the mammalian endoplasmic reticulum is catalyzed by protein disulfide isomerase (PDI), which is itself thought to be directly oxidized by Ero1alpha.	Disulfides	0-9	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	197-206
12974644-4	2003	Studies with Zn(2+), as a redox inactive surrogate for copper, show that one Zn(2+) binds to four-electron-reduced QSOX by diverting electrons away from the flavin and into two of the three redox active disulfide bridges in the enzyme.	Disulfides	203-212	quiescin sulfhydryl oxidase 1	Homo sapiens	115-119
12919313-1	2003	The thyrotropin receptor (TSHR) undergoes a cleavage at the cell membrane, leading to a heterodimer, comprising an alpha extracellular and a beta-transmembrane and intracellular subunits, held together by disulfide bonds.	Disulfides	205-214	thyroid stimulating hormone receptor	Homo sapiens	4-24
12919313-1	2003	The thyrotropin receptor (TSHR) undergoes a cleavage at the cell membrane, leading to a heterodimer, comprising an alpha extracellular and a beta-transmembrane and intracellular subunits, held together by disulfide bonds.	Disulfides	205-214	thyroid stimulating hormone receptor	Homo sapiens	26-30
20657012-2	2010	The activity of Ero1alpha is tightly regulated by the formation of noncatalytic disulfides, which need to be broken to activate the enzyme.	Disulfides	80-90	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	16-25
20657012-7	2010	These results demonstrate that the specificity of Ero1alpha toward the active sites of PDI requires the presence of the regulatory disulfides.	Disulfides	131-141	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	50-59
9288795-21	1997	The results indicate that the secretion of PSA in LNCaP cells is constitutive instead of regulated and that the disruption of intramolecular disulfide bonds affects the transport of PSA from the endoplasmic reticulum to the Golgi apparatus.	Disulfides	141-150	kallikrein related peptidase 3	Homo sapiens	182-185
12773530-11	2003	This phenotype, as well as the location of the disulfide bridges between the serpin and the non-serpin domain of C1-Inh, suggests that the function of the N-terminal region may be similar to one of the effects of heparin in antithrombin III, maintenance of the metastable serpin conformation.	Disulfides	47-56	serpin family G member 1	Homo sapiens	113-119
9309586-9	1997	The results obtained show that both disulfide bonds are necessary for GC-C activation.	Disulfides	36-45	natriuretic peptide receptor 3	Homo sapiens	70-74
20862248-8	2010	The molecular effect of the founder mutation on ADAMTSL2 is formation of disulfide-bonded dimers.	Disulfides	73-82	ADAMTS like 2	Canis lupus familiaris	48-56
20819940-7	2010	Moreover, the intramolecular disulfide bridge (C23/45) of HMGB1 is required for binding to Beclin1 and sustaining autophagy.	Disulfides	29-38	beclin 1	Homo sapiens	91-98
9310380-6	1997	These and a few other differences are apparently due to two extra disulfide bonds and two deletions/insertions in C. elegans BM-40 and can be partly interpreted from the X-ray structure of a large part of human BM-40.	Disulfides	66-75	secreted protein acidic and cysteine rich	Homo sapiens	211-216
12873136-0	2003	Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions.	Disulfides	12-22	transthyretin	Homo sapiens	28-41
21073418-9	2010	The human fibrillarin form without disulfide bridges is included into the mobile protein fraction and is consistent with its functionally active state.	Disulfides	35-44	fibrillarin	Homo sapiens	10-21
9236191-3	1997	CD3-epsilon, one of the subunits that initiates the assembly of the TCR in living cells, forms misfolded, disulfide-linked homooligomers when translated alone.	Disulfides	106-115	CD3 epsilon subunit of T-cell receptor complex	Homo sapiens	0-11
20486671-6	2010	When used in conjunction with intact protein MALDI mass measurement, a positive identification of ricin (or any of the other RIPs) was achieved including confirmation of the integrity of the disulfide bond between the A and B chains.	Disulfides	191-200	ricin	Ricinus communis	98-103
19967419-0	2010	Mimetics of the disulfide bridge between the N- and C-terminal cysteines of the KLK3-stimulating peptide B-2.	Disulfides	16-25	immunoglobulin kappa variable 5-2	Homo sapiens	105-108
20361855-7	2010	Reversible oxidation of thiols in serine threonine protein phosphatase PP2A and in protein tyrosin phosphatases SHP1, SHP2 and CD45 leads to their inactivation generally by formation of intramolecular disulfides.	Disulfides	201-211	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	118-122
9288573-2	1997	The mature protein consists of 7 exons and 6 introns, with 5 tandem disulfide bridges which are essential for the binding of corticotropin-releasing hormone (CRH).	Disulfides	68-77	corticotropin releasing hormone	Homo sapiens	125-156
20361855-7	2010	Reversible oxidation of thiols in serine threonine protein phosphatase PP2A and in protein tyrosin phosphatases SHP1, SHP2 and CD45 leads to their inactivation generally by formation of intramolecular disulfides.	Disulfides	201-211	protein tyrosine phosphatase receptor type C	Homo sapiens	127-131
20479109-4	2010	Using cysteine cross-linking, we biochemically screened over 300 cysteine pairs in the KCNQ1-KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain.	Disulfides	184-193	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	93-98
20479109-4	2010	Using cysteine cross-linking, we biochemically screened over 300 cysteine pairs in the KCNQ1-KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain.	Disulfides	184-193	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	230-235
12522011-2	2003	Recent results with an adhesion blocking antibody (RAM.1) against GPIb beta, which is disulfide linked to GPIb alpha, have suggested a novel function of this subunit in regulating VWF-mediated platelet adhesion, possibly involving its intracellular face.	Disulfides	86-95	glycoprotein Ib platelet subunit alpha	Homo sapiens	106-116
12582175-0	2003	Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge.	Disulfides	120-129	phosphatidylinositol glycan anchor biosynthesis class K	Homo sapiens	59-63
12582175-4	2003	Here we report that two subunits of mammalian GPI transamidase, GPI8 and PIG-T, form a functionally important disulfide bond between conserved cysteine residues.	Disulfides	110-119	phosphatidylinositol glycan anchor biosynthesis class K	Homo sapiens	64-68
12582175-8	2003	Antibodies against GPI8 and PIG-T revealed that endogenous as well as exogenous proteins formed a disulfide bond.	Disulfides	98-107	phosphatidylinositol glycan anchor biosynthesis class K	Homo sapiens	19-23
9288573-2	1997	The mature protein consists of 7 exons and 6 introns, with 5 tandem disulfide bridges which are essential for the binding of corticotropin-releasing hormone (CRH).	Disulfides	68-77	corticotropin releasing hormone	Homo sapiens	158-161
9242375-3	1997	The majority of MEN2A and FMTC mutations are clustered in the extra-cellular cysteine-rich domain and result in constitutive activation of the tyrosine kinase through the formation of disulfide-bonded RET homodimers.	Disulfides	184-193	ret proto-oncogene	Homo sapiens	16-21
12582175-9	2003	Furthermore trypanosome GPI8 forms a similar intermolecular disulfide bond via its conserved cysteine residue, suggesting that the trypanosome GPI transamidase is also a multimeric complex likely containing the orthologue of PIG-T.	Disulfides	60-69	phosphatidylinositol glycan anchor biosynthesis class K	Homo sapiens	24-28
20471945-5	2010	Guided by crystal structures of related homohexameric prokaryotic ATPases, we use disulfide engineering to show that the eukaryotic ATPases form a ring with the arrangement Rpt1-Rpt2-Rpt6-Rpt3-Rpt4-Rpt5 in fully assembled proteasomes.	Disulfides	82-91	proteasome 26S subunit, ATPase 4	Homo sapiens	188-192
9242375-3	1997	The majority of MEN2A and FMTC mutations are clustered in the extra-cellular cysteine-rich domain and result in constitutive activation of the tyrosine kinase through the formation of disulfide-bonded RET homodimers.	Disulfides	184-193	ret proto-oncogene	Homo sapiens	201-204
20194792-4	2010	Disulfide cross-linking shows that ORAI1 assembles as a tetramer or a higher oligomer with TM1 centrally located.	Disulfides	0-9	ORAI calcium release-activated calcium modulator 1	Homo sapiens	35-40
12784609-6	2003	The roles of the carbohydrate moieties and cysteine residues involved in the disulfide bridges of OVM were also examined, and we found that they were not important in recognition by the T cell/antigen presenting cell.	Disulfides	77-86	serine peptidase inhibitor, Kazal type 7 (putative)	Gallus gallus	98-101
9375378-1	1997	Inactivation of cytosolic enzymes by disulfides and its redox regulation by thioltransferase.	Disulfides	37-47	glutaredoxin-1	Bos taurus	76-92
12642668-0	2003	The role of disulfide bonds in the assembly and function of MD-2.	Disulfides	12-21	lymphocyte antigen 96	Homo sapiens	60-64
12642668-10	2003	Our data are consistent with a model in which most, possibly all sulfhydryls lie on the surface of a stable MD-2 core structure where they form both intra- and interchain disulfide bridges.	Disulfides	171-180	lymphocyte antigen 96	Homo sapiens	108-112
20159461-5	2010	The structures also underscore the importance of a redox-sensitive disulfide in affecting AKAP binding.	Disulfides	67-76	A-kinase anchoring protein 1	Homo sapiens	90-94
19896952-2	2010	IDE can also rapidly degrade hormones that are held together by intramolecular disulfide bond(s) without their reduction.	Disulfides	79-88	insulin degrading enzyme	Homo sapiens	0-3
19896952-7	2010	Furthermore, the presence of a disulfide bond in amylin allows IDE to cut at an additional site in the middle of the peptide (amino acids 18-19).	Disulfides	31-40	insulin degrading enzyme	Homo sapiens	63-66
19896952-8	2010	Our amylin-bound IDE structure offers insight into how the structural constraint from a disulfide bond in amylin can alter IDE cleavage sites.	Disulfides	88-97	insulin degrading enzyme	Homo sapiens	17-20
19896952-8	2010	Our amylin-bound IDE structure offers insight into how the structural constraint from a disulfide bond in amylin can alter IDE cleavage sites.	Disulfides	88-97	insulin degrading enzyme	Homo sapiens	123-126
9225993-7	1997	Previous observations with other RNA and DNA viruses consistently showed that GSH antiviral effect occurred at late stages of virus replication and was related to the selective decrease of specific glycoproteins, such as gp120, which are particularly rich in disulfide bonds.	Disulfides	259-268	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	221-226
19995902-7	2010	Crystallographic studies and dynamic light scattering revealed that Bet v 1d demonstrated a high tendency to form disulfide-linked aggregates due to a serine to cysteine exchange at residue 113.	Disulfides	114-123	delta/notch-like EGF repeat containing	Mus musculus	68-71
12538647-4	2003	Disulfide bonds are frequently considered essential for the stability of protein aggregates and since in the TTR monomers there is one cysteine residue, it is important to determine unambiguously the redox state of sulfur present in the fibrils.	Disulfides	0-9	transthyretin	Homo sapiens	109-112
12584183-5	2003	We report that PKC delta is stimulated 2.0-2.5 fold by GSSG, (Cys-Gly)(2) and cystine, under conditions where PKC gamma and PKC epsilon are fully inactivated by cystine, and PKC alpha activity is affected marginally or not at all by the disulfides.	Disulfides	237-247	protein kinase C, delta	Mus musculus	15-24
9430198-0	1997	Human IgG is substrate for the thioredoxin system: differential cleavage pattern of interchain disulfide bridges in IgG subclasses.	Disulfides	95-104	thioredoxin	Homo sapiens	31-42
20062808-5	2010	A role for disulfide bonds in stabilizing the ETR1 protein complex was demonstrated by use of reducing agents and mutation of Cys4 and Cys6 of ETR1.	Disulfides	11-20	Signal transduction histidine kinase, hybrid-type, ethylene sensor	Arabidopsis thaliana	46-50
20062808-5	2010	A role for disulfide bonds in stabilizing the ETR1 protein complex was demonstrated by use of reducing agents and mutation of Cys4 and Cys6 of ETR1.	Disulfides	11-20	Signal transduction histidine kinase, hybrid-type, ethylene sensor	Arabidopsis thaliana	143-147
20419425-2	2010	The newly synthesised precursors are trapped in the IMS by a disulfide relay mechanism that involves introduction of disulfides from the sulfhydryl oxidase Erv1 to the redox-regulated import receptor Mia40 and then on to the substrate.	Disulfides	61-70	Mia40p	Saccharomyces cerevisiae S288C	200-205
9430198-2	1997	wt protein with two redox-active cysteine residues, together with thioredoxin reductase and NADPH, may reduce protein disulfides and thereby act as a molecular probe of their structure and reactivity.	Disulfides	118-128	thioredoxin	Homo sapiens	66-77
9430198-3	1997	Interchain and intrachain disulfides are structural elements in all immunoglobulins and therefore potential substrates for the reduced thioredoxin, Trx(SH)2.	Disulfides	26-36	thioredoxin	Homo sapiens	135-146
19847013-6	2009	The results clearly show that purified C. reinhardtii ICL can be inactivated by glutathionylation and reactivated by glutaredoxin, whereas thioredoxin does not appear to regulate ICL activity, and no inter- or intramolecular disulfide bond could be formed under any of the conditions tested.	Disulfides	225-234	uncharacterized protein	Chlamydomonas reinhardtii	54-57
9430198-3	1997	Interchain and intrachain disulfides are structural elements in all immunoglobulins and therefore potential substrates for the reduced thioredoxin, Trx(SH)2.	Disulfides	26-36	thioredoxin	Homo sapiens	148-156
9430198-4	1997	It was investigated whether such disulfides are cleaved in human polyclonal IgG and IgG subclass myeloma proteins by both the human and the Escherichia coli thioredoxin systems.	Disulfides	33-43	thioredoxin	Homo sapiens	157-168
9430198-6	1997	Human IgG was a substrate for both prokaryotic and eukaryotic Trx(SH)2, which directly reduced IgG disulfides in a time and dose-dependent manner.	Disulfides	99-109	thioredoxin	Homo sapiens	62-70
12533475-7	2003	The major structural subunit of the plasmid-encoded fimbriae, PefA, contains a disulfide bond that must be oxidized in order for PefA stability to be maintained and for plasmid-encoded fimbriae to be assembled.	Disulfides	79-88	plasmid-encoded major fimbrial subunit	Salmonella enterica subsp. enterica serovar Typhimurium	62-66
9430198-12	1997	The structural and functional importance of interchain disulfides in immunoglobulins suggests physiological implications of the thioredoxin system.	Disulfides	55-65	thioredoxin	Homo sapiens	128-139
12533475-7	2003	The major structural subunit of the plasmid-encoded fimbriae, PefA, contains a disulfide bond that must be oxidized in order for PefA stability to be maintained and for plasmid-encoded fimbriae to be assembled.	Disulfides	79-88	plasmid-encoded major fimbrial subunit	Salmonella enterica subsp. enterica serovar Typhimurium	129-133
19837666-2	2009	Meanwhile, we previously presented that oxidative stress induced disulfide-bonded GAPDH aggregation in vitro.	Disulfides	65-74	glyceraldehyde-3-phosphate dehydrogenase	Mus musculus	82-87
9314099-0	1997	Fluoresceinthiocarbamyl-insulin: a potential analytical tool for the assay of disulfide bond reduction.	Disulfides	78-87	insulin	Bos taurus	24-31
19782948-6	2009	Further structure-function analysis identified that C452-C499 disulfide bond within the fifth extracellular Ig domain was indispensible for CD146-mediated signaling and tube formation.	Disulfides	62-71	melanoma cell adhesion molecule	Homo sapiens	140-145
12533475-8	2003	SrgA efficiently oxidizes the disulfide bond of PefA, while the S. enterica serovar Typhimurium chromosomally encoded disulfide oxidoreductase DsbA does not.	Disulfides	30-39	putative thiol-disulfide isomerase or thioredoxin	Salmonella enterica subsp. enterica serovar Typhimurium	0-4
9314099-6	1997	On this basis, di-fluoresceinthiocarbamyl-insulin constitutes an analytical tool to test the capacity of biochemical preparations in the reduction of disulfide bonds.	Disulfides	150-159	insulin	Bos taurus	42-49
9183003-3	1997	Two disulfide bridges/dimer, probably between Cys47 and Cys101, have been formed during the reaction of GST P1-1 with calvatic acid and its diazocyanide analogue.	Disulfides	4-13	glutathione S-transferase pi 1	Homo sapiens	104-110
12690627-3	2003	Thioredoxin, a 12 kD small protein with a redox-active dithiol/disulfide in the conserved active site: -Cys-Gly-Pro-Cys-, is a key molecule for redox regulation as well as glutathione(GSH).	Disulfides	63-72	thioredoxin 1	Mus musculus	0-11
19573605-8	2009	Production of C1C5 RANTES was highly impaired in CHO cells, with a dramatic yield reduction compared to that of wild type RANTES and secretion of the molecule as disulfide-linked dimer.	Disulfides	162-171	C-C motif chemokine ligand 5	Homo sapiens	19-25
19712047-8	2009	HRG fragments, generated by plasmin cleavage, are held together by disulfide linkages and are not released from the molecule under non-reducing conditions.	Disulfides	67-76	histidine rich glycoprotein	Homo sapiens	0-3
9127002-1	1997	The bioactivity of IL-12 is mediated by heterodimers of disulfide-linked p35 and p40 protein subunits.	Disulfides	56-65	interleukin 12a	Mus musculus	73-76
19788412-7	2009	Furthermore, in ERdj5-knockout cells, the expression of exogenous ERdj5 mitigated the ER stress caused by overproduction of alpha-amylase, which is one of the most abundant proteins in saliva and has five intramolecular disulfide bonds.	Disulfides	220-229	DnaJ heat shock protein family (Hsp40) member C10	Mus musculus	66-71
12218052-0	2003	Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion.	Disulfides	8-17	C-X-C motif chemokine receptor 4	Homo sapiens	115-120
12218052-1	2003	The human immunodeficiency virus (HIV) envelope (Env) glycoprotein (gp) 120 is a highly disulfide-bonded molecule that attaches HIV to the lymphocyte surface receptors CD4 and CXCR4.	Disulfides	88-97	C-X-C motif chemokine receptor 4	Homo sapiens	176-181
12218052-6	2003	We conclude that on average two of the nine disulfides of gp120 are reduced during interaction with the lymphocyte surface after CXCR4 binding prior to fusion and that cell surface PDI catalyzes this process.	Disulfides	44-54	C-X-C motif chemokine receptor 4	Homo sapiens	129-134
9111051-9	1997	After prebinding of Shiga(C242S) toxin to wells coated with the Shiga toxin receptor, Gb3, trypsin treatment induced dissociation of A1 from the toxin-receptor complex demonstrating that in addition to stabilizing the A-chain, the disulfide bond prevents dissociation of the A1 fragment from the toxin-receptor complex.	Disulfides	231-240	alpha 1,4-galactosyltransferase (P blood group)	Homo sapiens	86-89
12674505-6	2003	Although both complexes are partially resistant to SDS denaturation, disulfide bonding is absolutely required for the stability of beta2AR oligomers but not dimers in SDS-PAGE.	Disulfides	69-78	adrenoceptor beta 2	Homo sapiens	131-138
19573017-3	2009	We have examined a neuronal type III RPTP, PTPRO; we find that PTPRO can form dimers in living cells, and that disulfide linkages in PTPROs intracellular domain likely regulate dimerization.	Disulfides	111-120	protein tyrosine phosphatase receptor type O	Homo sapiens	43-48
9293773-0	1997	Beta 2-microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins.	Disulfides	72-81	beta-2-microglobulin	Homo sapiens	0-20
19577304-3	2009	Human SP-D includes trimeric subunits and multimeric assemblies of trimeric subunits, which are stabilized by N-terminal interchain disulfide crosslinks.	Disulfides	132-141	surfactant protein D	Homo sapiens	6-10
9293773-2	1997	Here, we show that class I proteins rapidly form disulfide bonds, and that the process is highly reversible in Daudi cells lacking beta 2m.	Disulfides	49-58	beta-2-microglobulin	Homo sapiens	131-138
9307065-4	1997	The extracellular domains of the murine D10 TCR (Valpha2, Vbeta8.2) were expressed in insect cells and secreted as a disulfide-linked heterodimer.	Disulfides	117-126	T cell receptor alpha variable 6-3	Mus musculus	44-47
19667201-1	2009	The mitochondrial intermembrane space (IMS) contains many small cysteine-bearing proteins, and their passage across the outer membrane and subsequent folding require recognition and disulfide bond transfer by an oxidative translocator Tim40/Mia40 in the inner membrane facing the IMS.	Disulfides	182-191	Mia40p	Saccharomyces cerevisiae S288C	235-240
19667201-1	2009	The mitochondrial intermembrane space (IMS) contains many small cysteine-bearing proteins, and their passage across the outer membrane and subsequent folding require recognition and disulfide bond transfer by an oxidative translocator Tim40/Mia40 in the inner membrane facing the IMS.	Disulfides	182-191	Mia40p	Saccharomyces cerevisiae S288C	241-246
12507971-2	2003	Furthermore, some partially degraded forms of hCG and its subunits have become of potential clinical importance, e.g., "nicked" forms of hCG (hCGn) and hCGbeta (hCGbetan), which contain cuts in the peptide backbone between amino acids 44-45 or 47-48 in hCGbeta, and a fragment of hCGbeta (hCGbetacf) consisting of amino acids 6-40 and 55-92 bound together by disulfide bridges.	Disulfides	359-368	chorionic gonadotropin subunit beta 3	Homo sapiens	152-159
12507971-2	2003	Furthermore, some partially degraded forms of hCG and its subunits have become of potential clinical importance, e.g., "nicked" forms of hCG (hCGn) and hCGbeta (hCGbetan), which contain cuts in the peptide backbone between amino acids 44-45 or 47-48 in hCGbeta, and a fragment of hCGbeta (hCGbetacf) consisting of amino acids 6-40 and 55-92 bound together by disulfide bridges.	Disulfides	359-368	chorionic gonadotropin subunit beta 3	Homo sapiens	161-168
12507971-2	2003	Furthermore, some partially degraded forms of hCG and its subunits have become of potential clinical importance, e.g., "nicked" forms of hCG (hCGn) and hCGbeta (hCGbetan), which contain cuts in the peptide backbone between amino acids 44-45 or 47-48 in hCGbeta, and a fragment of hCGbeta (hCGbetacf) consisting of amino acids 6-40 and 55-92 bound together by disulfide bridges.	Disulfides	359-368	chorionic gonadotropin subunit beta 3	Homo sapiens	161-168
19500143-2	2009	Of them, only the dsbA mutant lacking the disulfide bond isomerase exhibited significantly increased attachment to the polystyrene surface.	Disulfides	42-51	thiol:disulfide interchange protein DsbA/DsbL	Pseudomonas putida KT2440	18-22
9054580-3	1997	After disulfide bridge formation and purification, monomeric GCP-2 was recovered as a 6-kDa protein; the pure synthetic protein showed a molecular mass of 8076 Da as determined by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS).	Disulfides	6-15	C-X-C motif chemokine ligand 6	Homo sapiens	61-66
19457862-6	2009	Activity assays carried out using a series of cysteine mutants and various reductants combined with measurements of free thiols under distinct oxidation conditions and mass spectrometry experiments show that the 2-Cys MSRB2 is reduced by Trx through a dithiol-disulfide exchange involving both redox-active Cys of the two partners.	Disulfides	260-269	methionine sulfoxide reductase B 2	Arabidopsis thaliana	218-223
14608614-8	2003	This disulfide-bonded residue, [41-70]S-S[149-162], might thus be involved in the specific complexation of parinaric acid to beta-lactoglobulin.	Disulfides	5-14	beta-lactoglobulin	Bos taurus	125-143
9165076-5	1997	The linear peptide uPA(19-31) and its more stable disulfide-bridged cyclic form (cyclo(19,31)uPA(19-31)) displayed uPAR-binding activity whereas other peptides such as uPA(18-30), uPA(20-32) or uPA(20-30) did not react with uPAR.	Disulfides	50-59	plasminogen activator, urokinase receptor	Homo sapiens	115-119
9020092-7	1997	The engineered disulfide bond should also prove useful in the creation of more stable serpin variants; for example, such a bond in plasminogen activator inhibitor-1 would prevent it from becoming latent by locking strand 1C onto the C beta-sheet.	Disulfides	15-24	serpin family E member 1	Homo sapiens	131-164
12466503-0	2002	Stabilizing the integrin alpha M inserted domain in alternative conformations with a range of engineered disulfide bonds.	Disulfides	105-114	integrin subunit alpha M	Homo sapiens	16-32
19463727-6	2009	Furthermore, the inactivated JUNV particles retained the immunoreactivity of the surface glycoprotein GP1 suggesting that this disulfide may be useful in the pursuit of an inactivating agent to obtain a vaccine antigen or diagnostic tool.	Disulfides	127-136	GTP binding protein 1	Homo sapiens	102-105
19194580-1	2009	Thiorhodamine-based chemodosimeter A, a disulfide linked dimer, was designed for Hg2+ recognition by virtue of the strong affinity of mercury for sulfur.	Disulfides	40-49	polycystin 1, transient receptor potential channel interacting pseudogene 2	Homo sapiens	81-84
9006939-8	1997	Trx2 possessed a dithiol-reducing enzymatic activity and, with mammalian thioredoxin reductase and NADPH, was able to reduce the interchain disulfide bridges of insulin.	Disulfides	140-149	thioredoxin 2	Homo sapiens	0-4
19017646-1	2009	The redox reactivity of the three disulfide bridges and the flavin present in each protomer of the wild-type Arabidopsis thaliana mitochondrial sulfhydryl oxidase (AtErv1) homodimer has been investigated.	Disulfides	34-43	Erv1/Alr family protein	Arabidopsis thaliana	164-170
12441378-3	2002	The reduction by dithiothreitol of the three intramolecular disulfide bonds of the fifth domain was accelerated in the presence of stoichiometric amounts of GroEL, indicating that the fifth domain was destabilized upon interaction with GroEL.	Disulfides	60-69	heat shock protein family D (Hsp60) member 1	Homo sapiens	236-241
9003184-0	1997	Effects of the intramolecular disulfide bond on ligand binding dynamics in myoglobin.	Disulfides	30-39	myoglobin	Homo sapiens	75-84
12403615-0	2002	Disulfide-bond formation in the transthyretin mutant Y114C prevents amyloid fibril formation in vivo and in vitro.	Disulfides	0-9	transthyretin	Homo sapiens	32-45
12403615-3	2002	Furthermore, we demonstrate in vitro that the ATTR Y114C mutant exists in three forms: one unstable but nativelike tetrameric form, one highly aggregated form in which a network of disulfide bonds is formed, and one fibrillar form.	Disulfides	181-190	transthyretin	Homo sapiens	46-50
12403615-6	2002	In a previous study, we have linked exposure of this epitope in TTR to a three-residue shift in beta-strand D. The X-ray crystallographic structure of reduced tetrameric ATTR Y114C shows a structure similar to that of the wild type but with a more buried position of Cys10 and with beta-mercaptoethanol associated with Cys114, verifying the strong tendency for this residue to form disulfide bonds.	Disulfides	382-391	transthyretin	Homo sapiens	64-67
12403615-6	2002	In a previous study, we have linked exposure of this epitope in TTR to a three-residue shift in beta-strand D. The X-ray crystallographic structure of reduced tetrameric ATTR Y114C shows a structure similar to that of the wild type but with a more buried position of Cys10 and with beta-mercaptoethanol associated with Cys114, verifying the strong tendency for this residue to form disulfide bonds.	Disulfides	382-391	transthyretin	Homo sapiens	170-174
12403615-7	2002	Combined with the ex vivo data, our in vitro findings suggest that ATTR Y114C can lead to disease either by forming regular unbranched amyloid fibrils or by forming disulfide-linked aggregates that maintain amyloid-like properties but are unable to form regular amyloid fibrils.	Disulfides	165-174	transthyretin	Homo sapiens	67-71
19131515-0	2009	Location of KCNE1 relative to KCNQ1 in the I(KS) potassium channel by disulfide cross-linking of substituted cysteines.	Disulfides	70-79	potassium voltage-gated channel subfamily KQT member 1	Cricetulus griseus	30-35
19121228-10	2009	A disulfide mediated binary complex formation between GlgB and WhiB1C40S was shown by both in-solution protein-protein interaction and thioredoxin affinity chromatography.	Disulfides	2-11	1,4-alpha-glucan branching protein	Mycobacterium tuberculosis H37Rv	54-58
19121228-13	2009	CONCLUSION: We conclude that M. tuberculosis GlgB has one intra-molecular disulfide bond which is formed between C193 and C617.	Disulfides	74-83	1,4-alpha-glucan branching protein	Mycobacterium tuberculosis H37Rv	45-49
19121228-14	2009	WhiB1, a thioredoxin like protein interacts with GlgB and transfers its electrons to the disulfide thus reduces the intra-molecular disulfide bond of GlgB.	Disulfides	89-98	1,4-alpha-glucan branching protein	Mycobacterium tuberculosis H37Rv	49-53
19121228-14	2009	WhiB1, a thioredoxin like protein interacts with GlgB and transfers its electrons to the disulfide thus reduces the intra-molecular disulfide bond of GlgB.	Disulfides	89-98	1,4-alpha-glucan branching protein	Mycobacterium tuberculosis H37Rv	150-154
19121228-14	2009	WhiB1, a thioredoxin like protein interacts with GlgB and transfers its electrons to the disulfide thus reduces the intra-molecular disulfide bond of GlgB.	Disulfides	132-141	1,4-alpha-glucan branching protein	Mycobacterium tuberculosis H37Rv	49-53
19121228-14	2009	WhiB1, a thioredoxin like protein interacts with GlgB and transfers its electrons to the disulfide thus reduces the intra-molecular disulfide bond of GlgB.	Disulfides	132-141	1,4-alpha-glucan branching protein	Mycobacterium tuberculosis H37Rv	150-154
9003184-1	1997	In order to investigate the effects of an intramolecular disulfide bond on protein structure and ligand binding dynamics in myoglobin, we prepared a mutant myoglobin having a disulfide bond at the EF corner by introducing two cysteine at the position of Ile 75 and Glu 85.	Disulfides	57-66	myoglobin	Homo sapiens	124-133
9003184-1	1997	In order to investigate the effects of an intramolecular disulfide bond on protein structure and ligand binding dynamics in myoglobin, we prepared a mutant myoglobin having a disulfide bond at the EF corner by introducing two cysteine at the position of Ile 75 and Glu 85.	Disulfides	57-66	myoglobin	Homo sapiens	156-165
9003184-1	1997	In order to investigate the effects of an intramolecular disulfide bond on protein structure and ligand binding dynamics in myoglobin, we prepared a mutant myoglobin having a disulfide bond at the EF corner by introducing two cysteine at the position of Ile 75 and Glu 85.	Disulfides	175-184	myoglobin	Homo sapiens	156-165
9035103-1	1997	Interleukin-12 (IL-12) is unique amongst cytokines in being a disulfide-linked heterodimer of two separately encoded subunits (p35 and p40).	Disulfides	62-71	interleukin 12a	Mus musculus	127-130
18978082-6	2008	Additionally, it was suggested that T9A nukacin(4-27), a mutant with a 3-methyllanthionine substitution, binds to NukH via an intermolecular disulfide bond after it is weakly recognized by NukH.	Disulfides	141-150	NukH	Staphylococcus warneri	114-118
12391223-2	2002	In IgA1, Cys(133) in C(H)1 forms the disulfide bond to the L chain.	Disulfides	37-46	immunoglobulin heavy constant alpha 1	Homo sapiens	3-7
18845190-5	2008	Furthermore, the Sun1 tertiary structure involves interchain disulfide bonds that might contribute to higher homo-oligomer formation, although the overall dynamics of the Sun1 C-terminus remains unaffected when the cysteins involved are mutated.	Disulfides	61-70	Sad1 and UNC84 domain containing 1	Homo sapiens	17-21
8985176-4	1996	The RNA-induced assembly of PHFs is dependent on the formation of intermolecular disulfide bridges involving Cys322 in the third repeat of tau, and it includes the dimerization of tau as an early intermediate.	Disulfides	81-90	microtubule associated protein tau	Homo sapiens	139-142
18835810-2	2008	Here we demonstrate that thioredoxin reductase-1 (TR1), a selenium-containing pyridine nucleotide-disulfide oxidoreductase that reduces protein disulfides to free thiols, negatively regulates the activity of the HIV-1 encoded transcriptional activator, Tat, in human macrophages.	Disulfides	144-154	thioredoxin reductase 1	Homo sapiens	50-53
18835810-2	2008	Here we demonstrate that thioredoxin reductase-1 (TR1), a selenium-containing pyridine nucleotide-disulfide oxidoreductase that reduces protein disulfides to free thiols, negatively regulates the activity of the HIV-1 encoded transcriptional activator, Tat, in human macrophages.	Disulfides	144-154	Tat	Human immunodeficiency virus 1	253-256
18835810-6	2008	Furthermore, in vitro biochemical assays with recombinant Tat protein confirmed that TR1 targets two disulfide bonds within the Cys-rich motif required for efficient HIV-1 transactivation.	Disulfides	101-110	Tat	Human immunodeficiency virus 1	58-61
12350100-2	2002	Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) analysis under non-reducing and reducing conditions showed that in the early stages of the aggregation of beta-lactoglobulin disulfide linked aggregates were formed on heating at pH 6.7, but not at pH 4.9.	Disulfides	195-204	beta-lactoglobulin	Bos taurus	176-194
8954088-9	1996	C28, but not C53, also existed as an oligomer in the absence of 2-mercaptoethanol, suggesting that the 438-661 region present in C53 prevents intermolecular disulfide bond formation at the carboxyl-terminal cysteine residue.	Disulfides	157-166	CDK5 regulatory subunit associated protein 3	Homo sapiens	129-132
12196024-0	2002	Heterologous expression and characterization of human glutaminyl cyclase: evidence for a disulfide bond with importance for catalytic activity.	Disulfides	89-98	glutaminyl-peptide cyclotransferase	Homo sapiens	54-72
12163607-5	2002	A soluble form of Env, SOS gp140, can be made that has gp120 stably linked to the gp41 ectodomain by an intermolecular disulfide bond.	Disulfides	119-128	endogenous retrovirus group K member 20	Homo sapiens	18-21
18835810-6	2008	Furthermore, in vitro biochemical assays with recombinant Tat protein confirmed that TR1 targets two disulfide bonds within the Cys-rich motif required for efficient HIV-1 transactivation.	Disulfides	101-110	thioredoxin reductase 1	Homo sapiens	85-88
18937500-1	2008	The flavin-dependent quiescin-sulfhydryl oxidase (QSOX) inserts disulfide bridges into unfolded reduced proteins with the reduction of molecular oxygen to form hydrogen peroxide.	Disulfides	64-73	quiescin sulfhydryl oxidase 1	Homo sapiens	50-54
18937500-2	2008	This work investigates how QSOX and protein disulfide isomerase (PDI) cooperate in vitro to generate native pairings in two unfolded reduced proteins: ribonuclease A (RNase, four disulfide bonds and 105 disulfide isomers of the fully oxidized protein) and avian riboflavin binding protein (RfBP, nine disulfide bonds and more than 34 million corresponding disulfide pairings).	Disulfides	179-188	quiescin sulfhydryl oxidase 1	Homo sapiens	27-31
18937500-2	2008	This work investigates how QSOX and protein disulfide isomerase (PDI) cooperate in vitro to generate native pairings in two unfolded reduced proteins: ribonuclease A (RNase, four disulfide bonds and 105 disulfide isomers of the fully oxidized protein) and avian riboflavin binding protein (RfBP, nine disulfide bonds and more than 34 million corresponding disulfide pairings).	Disulfides	179-188	quiescin sulfhydryl oxidase 1	Homo sapiens	27-31
18937500-2	2008	This work investigates how QSOX and protein disulfide isomerase (PDI) cooperate in vitro to generate native pairings in two unfolded reduced proteins: ribonuclease A (RNase, four disulfide bonds and 105 disulfide isomers of the fully oxidized protein) and avian riboflavin binding protein (RfBP, nine disulfide bonds and more than 34 million corresponding disulfide pairings).	Disulfides	179-188	quiescin sulfhydryl oxidase 1	Homo sapiens	27-31
18852299-6	2008	The ternary complex represents a transient and intermediate step in the oxidation of intermembrane space precursors, where the oxidase Erv1 promotes disulfide transfer to the precursor while both oxidase and precursor are associated with the disulfide carrier Mia40.	Disulfides	242-251	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	260-265
12163165-4	2002	Moreover, cyclic CDR-H1 peptides bridged by disulfide inhibited NS3 protease more potently.	Disulfides	44-53	KRAS proto-oncogene, GTPase	Homo sapiens	64-67
8968078-1	1996	Thioredoxin (TRX), a disulfide-reducing intracellular protein, functions as a cellular defense mechanism against oxidative stress.	Disulfides	21-30	thioredoxin	Homo sapiens	0-11
18619974-10	2008	Our results demonstrate the ability of combinatorial chemistry to optimize a disulfide-containing miniprotein, and of structural biology to decipher the resultant interplay between binding affinity, neutralization breadth, molecular mimicry, and induced affinity for CCR5.	Disulfides	77-86	C-C motif chemokine receptor 5	Homo sapiens	267-271
8968078-1	1996	Thioredoxin (TRX), a disulfide-reducing intracellular protein, functions as a cellular defense mechanism against oxidative stress.	Disulfides	21-30	thioredoxin	Homo sapiens	13-16
12135781-7	2002	Here, we report that a full-length Reelin forms a disulfide-linked homodimer.	Disulfides	50-59	reelin	Homo sapiens	35-41
8943374-0	1996	Human natural killer cell receptors involved in MHC class I recognition are disulfide-linked heterodimers of CD94 and NKG2 subunits.	Disulfides	76-85	killer cell lectin like receptor C1	Homo sapiens	118-122
12081481-4	2002	Like all G protein-coupled receptors, mutating disulfide bond-forming cysteines in the first (Cys118) and second (Cys197) extracellular loops in CCR6 led to complete elimination of receptor activity, which for CCR6 was also associated with the accumulation of the receptor intracellularly.	Disulfides	47-56	C-C motif chemokine receptor 6	Homo sapiens	145-149
12081481-4	2002	Like all G protein-coupled receptors, mutating disulfide bond-forming cysteines in the first (Cys118) and second (Cys197) extracellular loops in CCR6 led to complete elimination of receptor activity, which for CCR6 was also associated with the accumulation of the receptor intracellularly.	Disulfides	47-56	C-C motif chemokine receptor 6	Homo sapiens	210-214
12081481-9	2002	We propose that CCR6 forms only a disulfide bond between the first (Cys118) and second (Cys197) extracellular loops, which confines a helical bundle together with the N-terminus adjacent to the third extracellular loop, creating the structural organization critical for ligand binding and therefore for receptor signaling.	Disulfides	34-43	C-C motif chemokine receptor 6	Homo sapiens	16-20
18585389-9	2008	The critical residues for dimerization are Cys261, forming a disulfide bridge between subunits in phot1-LOV1 domain, and Thr217 and Met232 in phot2-LOV1.	Disulfides	61-70	NAC domain containing protein 35	Arabidopsis thaliana	104-108
8943374-2	1996	We now demonstrate that CD94 glycoproteins form disulfide-bonded heterodimers with the NKG2A/B, NKG2C, and NKG2E glycoproteins.	Disulfides	48-57	killer cell lectin like receptor C1	Homo sapiens	87-94
18585389-9	2008	The critical residues for dimerization are Cys261, forming a disulfide bridge between subunits in phot1-LOV1 domain, and Thr217 and Met232 in phot2-LOV1.	Disulfides	61-70	NAC domain containing protein 35	Arabidopsis thaliana	148-152
12060617-1	2002	Ki-4.dgA is an anti-CD30 immunotoxin (IT) constructed by coupling the monoclonal antibody Ki-4 via a sterically hindered disulfide linker to deglycosylated ricin A-chain.	Disulfides	121-130	TNF receptor superfamily member 8	Homo sapiens	20-24
8973812-7	1996	This immunotoxin, which consists of a monoclonal antibody to DBH coupled by a disulfide bond to saporin (a ribosome inactivating protein), has been shown to be selectively toxic to peripheral noradrenergic sympathetic neurons in rats after systemic injection.	Disulfides	78-87	dopamine beta-hydroxylase	Rattus norvegicus	61-64
12009900-8	2002	Examination of various compounds with Ava in positions 9,10 and/or 14,15 revealed that the Leu(9)-Gly(10) and Arg(14)-Pro(15) segments of the disulfide ring are the principal structural elements determining hMCH-1R selectivity and ability to act as a hMCH-1R antagonist.	Disulfides	142-151	CD7 molecule	Homo sapiens	91-96
11859118-4	2002	In this study, we demonstrate that swapping the disulfide-linked CPNKEKEC sequence (residues 169-176) in the beta(2) I domain with a corresponding beta(3) sequence, or mutating Lys(174) to Thr, constitutively activates alpha(L)beta(2) binding to ICAM-1.	Disulfides	48-57	intercellular adhesion molecule 1	Homo sapiens	246-252
18544535-5	2008	Similar findings were obtained when the TNFR1- and TNFR2-transfected cells were pretreated with a cell-impermeable oxidase, DsbA, that catalyzes disulfide bond formation between thiol groups on cysteine residues.	Disulfides	145-154	TNF receptor superfamily member 1B	Homo sapiens	51-56
18452709-4	2008	We further identified MsrB2- or MsrB3-Trx complexes formed through intermolecular disulfide bonds involving catalytic residue of Trx.	Disulfides	82-91	methionine sulfoxide reductase B2	Homo sapiens	22-27
18452709-4	2008	We further identified MsrB2- or MsrB3-Trx complexes formed through intermolecular disulfide bonds involving catalytic residue of Trx.	Disulfides	82-91	methionine sulfoxide reductase B3	Homo sapiens	32-37
18480461-0	2008	Intersubunit disulfide isomerization controls membrane fusion of human T-cell leukemia virus Env.	Disulfides	13-22	endogenous retrovirus group K member 20	Homo sapiens	93-96
8910521-4	1996	Approximately 30% of the Escherichia coli-derived NF-YB subunit existed as intermolecular disulfide-linked dimers.	Disulfides	90-99	nuclear transcription factor Y subunit beta	Homo sapiens	50-55
18480461-2	2008	Here we have tested whether this motif is used for isomerization of the intersubunit disulfide of Env and whether this rearrangement is required for membrane fusion.	Disulfides	85-94	endogenous retrovirus group K member 20	Homo sapiens	98-101
18587263-1	2008	CD98, a disulfide-linked 125-kDa heterodimeric type II transmembrane glycoprotein, regulates beta1 integrin- mediated cell adhesion.	Disulfides	8-17	integrin subunit beta 1	Homo sapiens	93-107
11866530-3	2002	Three classes of disulfide-constrained peptides that antagonize binding of the VEGF dimer to its receptors, KDR and Flt-1, were identified previously using phage display methods.	Disulfides	17-26	kinase insert domain receptor	Homo sapiens	108-111
11679582-3	2002	Here, we show that the disulfide bond between Cys-119 and Cys-201 in CD38 may be involved in CD38 dimerization and internalization.	Disulfides	23-32	CD38 antigen	Mus musculus	69-73
8914835-0	1996	S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione.	Disulfides	49-59	thioredoxin	Homo sapiens	105-116
11679582-3	2002	Here, we show that the disulfide bond between Cys-119 and Cys-201 in CD38 may be involved in CD38 dimerization and internalization.	Disulfides	23-32	CD38 antigen	Mus musculus	93-97
11719509-5	2002	Recombinantly expressed R122C mutant human trypsinogen was found to undergo greatly reduced autoactivation and cathepsin B-induced activation, which is most likely caused by misfolding or disulfide mismatches of the mutant zymogen.	Disulfides	188-197	cathepsin B	Homo sapiens	111-122
11838022-0	2002	Characterization of the elusive disulfide bridge forming human Hb variant: Hb Ta-Li beta83 (EF7)Gly --&gt; Cys by electrospray mass spectrometry.	Disulfides	32-41	FAM3 metabolism regulating signaling molecule D	Homo sapiens	92-95
11682471-3	2002	We demonstrate that CDT6 is a secreted protein that folds into disulfide-linked homotetramers by coiled-coil interactions.	Disulfides	63-72	angiopoietin like 7	Homo sapiens	20-24
11750654-5	2002	CD16A-Ig is secreted as a disulfide-linked homodimer of 70kDa.	Disulfides	26-35	Fc gamma receptor IIIa	Homo sapiens	0-8
11489908-1	2001	We report the use of thiol chemistry to define specific and reversible disulfide interactions of Cys-substituted NK2 receptor mutants with analogues of neurokinin A (NKA) containing single cysteine substitutions.	Disulfides	71-80	tachykinin receptor 2	Homo sapiens	113-125
11489908-3	2001	N-biotinyl-[Tyr1,Cys9]NKA, N-biotinyl-[Tyr1,Cys10]NKA were both found to reversibly disulfide bond to the NK2 receptor mutant Met297 --&gt; Cys.	Disulfides	84-93	tachykinin receptor 2	Homo sapiens	106-118
11580274-0	2001	Thiol/disulfide interconversion in bovine lens aldose reductase induced by intermediates of glutathione turnover.	Disulfides	6-15	aldose reductase	Bos taurus	47-63
11574464-3	2001	Unexpectedly, the crystal structure of IL-17F reveals that IL-17 family members adopt a monomer fold typical of cystine knot growth factors, despite lacking the disulfide responsible for defining the canonical "knot" structure.	Disulfides	161-170	interleukin 17A	Homo sapiens	39-44
11454874-0	2001	Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane-spanning domains.	Disulfides	96-105	CD47 molecule	Homo sapiens	39-43
11454874-0	2001	Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane-spanning domains.	Disulfides	96-105	CD47 molecule	Homo sapiens	45-72
11454874-3	2001	Conservation of Cys residues among CD47 homologues suggested the existence of a disulfide bond between the Ig and MMS domains that was confirmed by chemical digestion and mapped to Cys(33) and Cys(263).	Disulfides	80-89	CD47 molecule	Homo sapiens	35-39
11454874-5	2001	Mutagenesis to prevent formation of this disulfide completely disrupted CD47 signaling independent of effects on ligand binding, as assessed by T cell interleukin-2 secretion and Ca(2+) responses.	Disulfides	41-50	CD47 molecule	Homo sapiens	72-76
11454874-7	2001	Thus, a disulfide bond between the Ig and MMS domains of CD47 is required for normal ligand binding and signal transduction.	Disulfides	8-17	CD47 molecule	Homo sapiens	57-61
11435433-3	2001	BPTI is a 58-residue protein and contains three disulfide groups between residues 5 and 55, 14 and 38, as well as 30 and 51.	Disulfides	48-57	spleen trypsin inhibitor I	Bos taurus	0-4
11435433-4	2001	Mutants of BPTI that contained only a single disulfide were reduced, and the free cysteines were labeled with either thiol-specific spin labels or pyrene maleimide.	Disulfides	45-54	spleen trypsin inhibitor I	Bos taurus	11-15
11514736-1	2001	The 12 cysteine residues in the flavivirus NS1 protein are strictly conserved, suggesting that they form disulfide bonds that are critical for folding the protein into a functional structure.	Disulfides	105-114	influenza virus NS1A binding protein	Homo sapiens	43-46
11514736-2	2001	In this study, we examined the intramolecular disulfide bond arrangement of NS1 of Murray Valley encephalitis virus and elucidated three of the six cysteine-pairing arrangements.	Disulfides	46-55	influenza virus NS1A binding protein	Homo sapiens	76-79
11467967-3	2001	In vitro biochemical studies revealed that the enzyme product derived from one of them (APR1) is activated by oxidation, probably through the formation of a disulfide bond.	Disulfides	157-166	APS reductase 1	Arabidopsis thaliana	88-92
11454166-3	2001	The purpose of this study was to delineate the role of the disulfide bonds of hCGbeta in receptor binding of the hormone.	Disulfides	59-68	chorionic gonadotropin subunit beta 3	Homo sapiens	78-85
11454166-4	2001	Six disulfide peptides incorporating each of the six disulfide bonds of hCGbeta were synthesized and screened, along with their linear counterparts, for their ability to competitively inhibit the binding of [125I] hCG to sheep ovarian corpora luteal LH/CG receptor.	Disulfides	4-13	chorionic gonadotropin subunit beta 3	Homo sapiens	72-79
11454166-4	2001	Six disulfide peptides incorporating each of the six disulfide bonds of hCGbeta were synthesized and screened, along with their linear counterparts, for their ability to competitively inhibit the binding of [125I] hCG to sheep ovarian corpora luteal LH/CG receptor.	Disulfides	53-62	chorionic gonadotropin subunit beta 3	Homo sapiens	72-79
11397160-8	2001	The reactivities of aromatic and aliphatic thiols with 2-pyridyldithioethanol (2-PDE), a small molecule disulfide, were determined.	Disulfides	104-113	aldehyde dehydrogenase 7 family member A1	Homo sapiens	81-84
11359822-8	2001	Hence, human IgM carries functionally inactive IL-18 forming a disulfide-bridged complex, and this IL-18 moiety is from 10- to 100-fold higher than the conventional type 1 IL-18 in blood circulation in approximately 30% normal subjects.	Disulfides	63-72	interleukin 18	Homo sapiens	99-104
11098061-11	2001	Furthermore, we postulate that domain 5 may play a role in the disulfide-linked homodimerization and activation process of gp130.	Disulfides	63-72	Neutrophil migration (granulocyte glycoprotein)	Homo sapiens	123-128
11157944-2	2001	Besides these pul genes, efficient pullulanase secretion also requires the host dsbA gene, encoding a periplasmic disulfide oxidoreductase, independently of disulfide bond formation in pullulanase itself.	Disulfides	114-123	oxidoreductase	Escherichia coli	124-138
11266609-2	2001	Twenty hCG beta-subunit residues, termed the seatbelt, are wrapped around alpha-subunit loop 2 (alpha 2) and their positions "latched" by a disulfide formed by cysteines at the end of the seatbelt (Cys 110) and in the beta-subunit core (Cys 26).	Disulfides	140-149	chorionic gonadotropin subunit beta 3	Homo sapiens	7-15
12549186-2	2001	It is a disulfide-linked heterodimer composed of a 35 kD light chain (P35) and a 40 kD heavy chain (P40).	Disulfides	8-17	interleukin 12A	Homo sapiens	70-73
11141057-9	2001	Finally, the use of another mutant in which Cys 77 was replaced by serine enabled confirmation of the location of the MIC-1 interchain disulfide bond.	Disulfides	135-144	growth differentiation factor 15	Homo sapiens	118-123
11693578-3	2001	To that end, the influence of cadmium on the rat liver GR potential to form intramolecular and intermolecular disulfide bonds under nonreducing conditions and under oxidizing conditions produced by the addition of hydrogen peroxide (H2O2) to the cytosol was examined by nonreducing SDS-PAGE and immunoblotting.	Disulfides	110-119	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	55-57
11693578-4	2001	The results show that cadmium inhibits formation of disulfide bonds within the GR both in the absence and in the presence of H2O2.	Disulfides	52-61	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	79-81
11693578-5	2001	The creation of intermolecular disulfide linkages between the apo-GR and associated heat shock proteins Hsp90 and Hsp70, which was evident in the presence of H2O2, was also significantly impaired after cadmium administration.	Disulfides	31-40	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	66-68
21340764-5	2001	Urinary beta-CF consists of residues 6-40 disulfide bridged to residues 55-92 of the beta-subunit of hCG (3,4), suggesting that it may be a degradative product of hCGbeta.	Disulfides	42-51	chorionic gonadotropin subunit beta 3	Homo sapiens	163-170
11101293-7	2000	The protein, which exists as a disulfide-linked homodimer on the cell surface, crystallizes as a symmetrical dimer, similar to those formed by the related NK cell receptors Ly49A and CD94.	Disulfides	31-40	killer cell lectin like receptor D1	Homo sapiens	183-187
10827170-8	2000	These data indicate that the propeptide has two roles in proper folding: the disulfide-coupled folding of the mature region and the dimerization of pro-GCAP-II.	Disulfides	77-86	guanylate cyclase activator 2B	Homo sapiens	152-159
10801834-0	2000	The gene for a novel member of the whey acidic protein family encodes three four-disulfide core domains and is asynchronously expressed during lactation.	Disulfides	81-90	whey acidic protein	Mus musculus	35-54
10880975-0	2000	Crystal structure of the disulfide bond-deficient azurin mutant C3A/C26A: how important is the S-S bond for folding and stability?	Disulfides	25-34	complement C3	Homo sapiens	64-67
10819974-0	2000	Partial IGF affinity of circulating N- and C-terminal fragments of human insulin-like growth factor binding protein-4 (IGFBP-4) and the disulfide bonding pattern of the C-terminal IGFBP-4 domain.	Disulfides	136-145	insulin like growth factor binding protein 4	Homo sapiens	180-187
10819974-8	2000	Proteolytic digestion and subsequent biochemical analysis showed that the six cysteines of the C-terminal IGFBP-4 fragment are linked between residues 153-183, 194-205, and 207-228 (disulfide bonding pattern, 1-2, 3-4, and 5-6).	Disulfides	182-191	insulin like growth factor binding protein 4	Homo sapiens	106-113
10759156-1	2000	Serum transthyretin has several isoforms, most of which are caused by disulfide linkage with cysteine residue at position 10.	Disulfides	70-79	transthyretin	Homo sapiens	6-19
10686155-1	2000	Human CD94 is a subunit of the disulfide-linked, heterodimeric natural killer (NK) cell surface receptor CD94/NKG2.	Disulfides	31-40	killer cell lectin like receptor D1	Homo sapiens	6-10
10686155-1	2000	Human CD94 is a subunit of the disulfide-linked, heterodimeric natural killer (NK) cell surface receptor CD94/NKG2.	Disulfides	31-40	killer cell lectin like receptor D1	Homo sapiens	105-109
10715549-0	2000	Additional N-glycosylation at Asn(13) rescues the human LHbeta-subunit from disulfide-linked aggregation.	Disulfides	76-85	luteinizing hormone subunit beta	Homo sapiens	56-62
10715549-2	2000	Despite the considerable homology between LHbeta and CGbeta, we previously demonstrated that, when expressed in GH(3) cells, the secreted form of LHbeta showed mispaired disulfide-linked aggregation in addition to monomer, whereas no aggregation was observed in CGbeta.	Disulfides	170-179	luteinizing hormone subunit beta	Homo sapiens	146-152
10716178-6	2000	Comparing the structure of TAP in TAP-BPTI with TAP bound to factor Xa(Xa) suggests a massive reorganization in the N-terminal tetrapeptide and the first disulfide loop of TAP (Cys5T-Cys15T) upon binding to Xa.	Disulfides	154-163	spleen trypsin inhibitor I	Bos taurus	38-42
18393449-1	2008	The flavoprotein quiescin-sulfhydryl oxidase (QSOX) rapidly inserts disulfide bonds into unfolded, reduced proteins with the concomitant reduction of oxygen to hydrogen peroxide.	Disulfides	68-77	quiescin sulfhydryl oxidase 1	Homo sapiens	17-44
18393449-1	2008	The flavoprotein quiescin-sulfhydryl oxidase (QSOX) rapidly inserts disulfide bonds into unfolded, reduced proteins with the concomitant reduction of oxygen to hydrogen peroxide.	Disulfides	68-77	quiescin sulfhydryl oxidase 1	Homo sapiens	46-50
18393449-4	2008	Previous studies on avian QSOX led to a model in which reducing equivalents were proposed to relay through the enzyme from the first thioredoxin domain (C70-C73) to a distal disulfide (C509-C512), then across the dimer interface to the FAD-proximal disulfide (C449-C452), and finally to the FAD.	Disulfides	174-183	quiescin sulfhydryl oxidase 1	Homo sapiens	26-30
18393449-4	2008	Previous studies on avian QSOX led to a model in which reducing equivalents were proposed to relay through the enzyme from the first thioredoxin domain (C70-C73) to a distal disulfide (C509-C512), then across the dimer interface to the FAD-proximal disulfide (C449-C452), and finally to the FAD.	Disulfides	249-258	quiescin sulfhydryl oxidase 1	Homo sapiens	26-30
18393449-9	2008	C452, of the proximal disulfide, is shown to be the charge-transfer donor to the flavin ring of QSOX, and its partner, C449, is expected to be the interchange thiol, forming a mixed disulfide with C70 in the thioredoxin domain.	Disulfides	22-31	quiescin sulfhydryl oxidase 1	Homo sapiens	96-100
18393449-9	2008	C452, of the proximal disulfide, is shown to be the charge-transfer donor to the flavin ring of QSOX, and its partner, C449, is expected to be the interchange thiol, forming a mixed disulfide with C70 in the thioredoxin domain.	Disulfides	182-191	quiescin sulfhydryl oxidase 1	Homo sapiens	96-100
18393449-10	2008	These data demonstrate that all the internal redox steps occur within the same polypeptide chain of mammalian QSOX and commence with a direct interaction between the reduced thioredoxin domain and the proximal disulfide of the Erv/ALR domain.	Disulfides	210-219	quiescin sulfhydryl oxidase 1	Homo sapiens	110-114
18052930-9	2008	Furthermore, Prx IV oligomeric interactions are stabilized by additional non-catalytic disulfide bonds, indicative of a primary role other than peroxide elimination.	Disulfides	87-96	peroxiredoxin 4	Homo sapiens	13-19
18093982-3	2008	The NMR solution structure of the partially oxidized Cox17 (Cox17(2S-S)) consists of a coiled coil-helix-coiled coil-helix domain stabilized by two disulfide bonds involving Cys(25)-Cys(54) and Cys(35)-Cys(44), preceded by a flexible and completely unstructured N-terminal tail.	Disulfides	148-157	cytochrome c oxidase copper chaperone COX17	Homo sapiens	53-58
18093982-3	2008	The NMR solution structure of the partially oxidized Cox17 (Cox17(2S-S)) consists of a coiled coil-helix-coiled coil-helix domain stabilized by two disulfide bonds involving Cys(25)-Cys(54) and Cys(35)-Cys(44), preceded by a flexible and completely unstructured N-terminal tail.	Disulfides	148-157	cytochrome c oxidase copper chaperone COX17	Homo sapiens	60-65
18258262-8	2008	The cross-linking of the N-terminal region of recombinant yeast cofilin to actin residues 346 and 374 with dithio-bis-maleimidoethane (12.4 A) and via disulfide bond formation was also documented.	Disulfides	151-160	cofilin	Saccharomyces cerevisiae S288C	64-71
18178549-3	2008	Here we show that ERp44 interacts with FGE forming heterodimeric and, to a lesser extent, also heterotetrameric and octameric complexes, which are stabilized through disulfide bonding between cysteine 29 of ERp44 and cysteines 50 and 52 in the N-terminal region of FGE.	Disulfides	166-175	sulfatase modifying factor 1	Homo sapiens	39-42
18178549-3	2008	Here we show that ERp44 interacts with FGE forming heterodimeric and, to a lesser extent, also heterotetrameric and octameric complexes, which are stabilized through disulfide bonding between cysteine 29 of ERp44 and cysteines 50 and 52 in the N-terminal region of FGE.	Disulfides	166-175	sulfatase modifying factor 1	Homo sapiens	265-268
17933489-2	2008	The disulfide oxidoreductase, DsbA, introduces disulfide bonds into exported proteins from the cytoplasm.	Disulfides	4-13	oxidoreductase	Escherichia coli	14-28
17945326-4	2008	Furthermore, our results suggest that residues located in the C2 disulfide-bonded loop in FeLV-C Cdom are critical for SU binding to FLVCR1 and for virus infection.	Disulfides	65-74	FLVCR heme transporter 1	Homo sapiens	133-139
17956189-5	2008	A specific protein disulfide oxidoreductase (PDO) has a key role in intracellular disulfide shuffling in thermophiles.	Disulfides	19-28	thioredoxin reductase 1	Homo sapiens	29-43
18537614-2	2008	Diverse classes of chemical compounds including nucleotide analogues, adenosine analogues, aminobenzoic derivatives, polyphenols, hydrazines, phthalides, disulfides and antisenses are being discovered and evaluated as DNMT inhibitors targeting DNA hypermethylation.	Disulfides	154-164	DNA methyltransferase 1	Homo sapiens	218-222
17978092-4	2008	Import of the precursors requires the essential intermembrane space proteins Mia40 and Erv1 that were proposed to form a relay for disulfide formation in the precursor proteins.	Disulfides	131-140	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	77-82
18855755-3	2008	Formation of aggregated beta-LG is completed at 95 degrees C. Circular dichroism results indicate that formation of aggregated beta-LG is accompanied by the scrambling of disulfide bonds (creation of new intramolecular and intermolecular disulfide bridges and rearrangement of old intramolecular disulfide bridges).	Disulfides	171-180	beta-lactoglobulin	Bos taurus	24-31
18855755-3	2008	Formation of aggregated beta-LG is completed at 95 degrees C. Circular dichroism results indicate that formation of aggregated beta-LG is accompanied by the scrambling of disulfide bonds (creation of new intramolecular and intermolecular disulfide bridges and rearrangement of old intramolecular disulfide bridges).	Disulfides	171-180	beta-lactoglobulin	Bos taurus	127-134
18855755-3	2008	Formation of aggregated beta-LG is completed at 95 degrees C. Circular dichroism results indicate that formation of aggregated beta-LG is accompanied by the scrambling of disulfide bonds (creation of new intramolecular and intermolecular disulfide bridges and rearrangement of old intramolecular disulfide bridges).	Disulfides	238-247	beta-lactoglobulin	Bos taurus	24-31
18855755-3	2008	Formation of aggregated beta-LG is completed at 95 degrees C. Circular dichroism results indicate that formation of aggregated beta-LG is accompanied by the scrambling of disulfide bonds (creation of new intramolecular and intermolecular disulfide bridges and rearrangement of old intramolecular disulfide bridges).	Disulfides	238-247	beta-lactoglobulin	Bos taurus	127-134
18855755-3	2008	Formation of aggregated beta-LG is completed at 95 degrees C. Circular dichroism results indicate that formation of aggregated beta-LG is accompanied by the scrambling of disulfide bonds (creation of new intramolecular and intermolecular disulfide bridges and rearrangement of old intramolecular disulfide bridges).	Disulfides	238-247	beta-lactoglobulin	Bos taurus	24-31
18855755-3	2008	Formation of aggregated beta-LG is completed at 95 degrees C. Circular dichroism results indicate that formation of aggregated beta-LG is accompanied by the scrambling of disulfide bonds (creation of new intramolecular and intermolecular disulfide bridges and rearrangement of old intramolecular disulfide bridges).	Disulfides	238-247	beta-lactoglobulin	Bos taurus	127-134
17959606-0	2007	A point mutation in atpC1 raises the redox potential of the Arabidopsis chloroplast ATP synthase gamma-subunit regulatory disulfide above the range of thioredoxin modulation.	Disulfides	122-131	ATPase, F1 complex, gamma subunit protein	Arabidopsis thaliana	20-25
17959606-0	2007	A point mutation in atpC1 raises the redox potential of the Arabidopsis chloroplast ATP synthase gamma-subunit regulatory disulfide above the range of thioredoxin modulation.	Disulfides	122-131	ATP synthase	Arabidopsis thaliana	84-96
17959606-6	2007	This work provides in situ validation of the concept that thioredoxin-dependent reduction of the gamma-subunit regulatory disulfide modulates the proton electrochemical potential energy requirement for activation of the chloroplast ATP synthase and that the activation state of the ATP synthase can limit leaf level photosynthesis.	Disulfides	122-131	ATP synthase	Arabidopsis thaliana	232-244
17959606-6	2007	This work provides in situ validation of the concept that thioredoxin-dependent reduction of the gamma-subunit regulatory disulfide modulates the proton electrochemical potential energy requirement for activation of the chloroplast ATP synthase and that the activation state of the ATP synthase can limit leaf level photosynthesis.	Disulfides	122-131	ATP synthase	Arabidopsis thaliana	282-294
18070357-10	2007	CONCLUSION: We conclude that glutathionylation of beta-actin may occur via spontaneous oxidation of a cysteinyl residue to a sulfenic acid that readily reacts with GSH to form a mixed disulfide.	Disulfides	184-193	POTE ankyrin domain family member F	Homo sapiens	50-60
17965184-3	2007	SGK1 exists as a dimer formed by two intermolecular disulfide bonds between Cys258 in the activation loop and Cys193.	Disulfides	52-61	serum/glucocorticoid regulated kinase 1	Homo sapiens	0-4
17672825-3	2007	Mammalian Cox17 exists in three oxidative states, each characterized by distinct metal-binding properties: fully reduced mammalian Cox17(0S-S) binds co-operatively to four Cu+; Cox17(2S-S), with two disulfide bridges, binds to one of either Cu+ or Zn2+; and Cox17(3S-S), with three disulfide bridges, does not bind to any metal ions.	Disulfides	199-208	cytochrome c oxidase copper chaperone COX17	Homo sapiens	10-15
17672825-3	2007	Mammalian Cox17 exists in three oxidative states, each characterized by distinct metal-binding properties: fully reduced mammalian Cox17(0S-S) binds co-operatively to four Cu+; Cox17(2S-S), with two disulfide bridges, binds to one of either Cu+ or Zn2+; and Cox17(3S-S), with three disulfide bridges, does not bind to any metal ions.	Disulfides	199-208	cytochrome c oxidase copper chaperone COX17	Homo sapiens	131-136
17672825-3	2007	Mammalian Cox17 exists in three oxidative states, each characterized by distinct metal-binding properties: fully reduced mammalian Cox17(0S-S) binds co-operatively to four Cu+; Cox17(2S-S), with two disulfide bridges, binds to one of either Cu+ or Zn2+; and Cox17(3S-S), with three disulfide bridges, does not bind to any metal ions.	Disulfides	199-208	cytochrome c oxidase copper chaperone COX17	Homo sapiens	131-136
17672825-3	2007	Mammalian Cox17 exists in three oxidative states, each characterized by distinct metal-binding properties: fully reduced mammalian Cox17(0S-S) binds co-operatively to four Cu+; Cox17(2S-S), with two disulfide bridges, binds to one of either Cu+ or Zn2+; and Cox17(3S-S), with three disulfide bridges, does not bind to any metal ions.	Disulfides	199-208	cytochrome c oxidase copper chaperone COX17	Homo sapiens	131-136
17672825-3	2007	Mammalian Cox17 exists in three oxidative states, each characterized by distinct metal-binding properties: fully reduced mammalian Cox17(0S-S) binds co-operatively to four Cu+; Cox17(2S-S), with two disulfide bridges, binds to one of either Cu+ or Zn2+; and Cox17(3S-S), with three disulfide bridges, does not bind to any metal ions.	Disulfides	282-291	cytochrome c oxidase copper chaperone COX17	Homo sapiens	10-15
17672825-3	2007	Mammalian Cox17 exists in three oxidative states, each characterized by distinct metal-binding properties: fully reduced mammalian Cox17(0S-S) binds co-operatively to four Cu+; Cox17(2S-S), with two disulfide bridges, binds to one of either Cu+ or Zn2+; and Cox17(3S-S), with three disulfide bridges, does not bind to any metal ions.	Disulfides	282-291	cytochrome c oxidase copper chaperone COX17	Homo sapiens	131-136
17672825-3	2007	Mammalian Cox17 exists in three oxidative states, each characterized by distinct metal-binding properties: fully reduced mammalian Cox17(0S-S) binds co-operatively to four Cu+; Cox17(2S-S), with two disulfide bridges, binds to one of either Cu+ or Zn2+; and Cox17(3S-S), with three disulfide bridges, does not bind to any metal ions.	Disulfides	282-291	cytochrome c oxidase copper chaperone COX17	Homo sapiens	131-136
17672825-3	2007	Mammalian Cox17 exists in three oxidative states, each characterized by distinct metal-binding properties: fully reduced mammalian Cox17(0S-S) binds co-operatively to four Cu+; Cox17(2S-S), with two disulfide bridges, binds to one of either Cu+ or Zn2+; and Cox17(3S-S), with three disulfide bridges, does not bind to any metal ions.	Disulfides	282-291	cytochrome c oxidase copper chaperone COX17	Homo sapiens	131-136
17664073-3	2007	The domain composition is similar to the mammalian WFDC5 (WAP four disulfide core) and secretory leukocyte proteinase inhibitor (SLPI).	Disulfides	67-76	WAP four-disulfide core domain 5	Homo sapiens	51-56
17555889-3	2007	However, the internal disulfide bond (CD7-D5) of human neuroglobin can be reduced by thioredoxin reductase.	Disulfides	22-31	neuroglobin	Homo sapiens	55-66
17540772-7	2007	Oxidized HO-2, which contains an intramolecular disulfide bond linking Cys(265) of HRM1 and Cys(282) of HRM2, binds heme tightly.	Disulfides	48-57	ectodysplasin A receptor	Homo sapiens	83-87
17540772-7	2007	Oxidized HO-2, which contains an intramolecular disulfide bond linking Cys(265) of HRM1 and Cys(282) of HRM2, binds heme tightly.	Disulfides	48-57	hair curvature, variation in	Homo sapiens	104-108
17493883-5	2007	In the present study, PSP94 was purified from human seminal plasma and characterized further and it showed the presence of five disulfide bonds.	Disulfides	128-137	microseminoprotein beta	Homo sapiens	22-27
17379184-5	2007	We show that disulfide bridges between Cys112 and Cys145 located within TM3 and TM4, respectively, are of critical importance for 5-HT(4)R dimer formation.	Disulfides	13-22	tropomyosin 3	Homo sapiens	72-75
17379184-5	2007	We show that disulfide bridges between Cys112 and Cys145 located within TM3 and TM4, respectively, are of critical importance for 5-HT(4)R dimer formation.	Disulfides	13-22	5-hydroxytryptamine receptor 4	Homo sapiens	130-138
17499047-4	2007	Consistent with visualization of bound polypeptide distributed over many parts of the central cavity, disulfide crosslinking could be carried out between a cysteine in a bound substrate protein and cysteines substituted anywhere inside GroEL.	Disulfides	102-111	heat shock protein family D (Hsp60) member 1	Homo sapiens	236-241
17385893-1	2007	Thioredoxin reductase (TR) from Drosophila melanogaster (DmTR) is a member of the glutathione reductase (GR) family of pyridine nucleotide disulfide oxidoreductases and catalyzes the reduction of the redox-active disulfide bond of thioredoxin.	Disulfides	139-148	uncharacterized protein	Drosophila melanogaster	0-11
17385893-1	2007	Thioredoxin reductase (TR) from Drosophila melanogaster (DmTR) is a member of the glutathione reductase (GR) family of pyridine nucleotide disulfide oxidoreductases and catalyzes the reduction of the redox-active disulfide bond of thioredoxin.	Disulfides	139-148	uncharacterized protein	Drosophila melanogaster	231-242
17305365-4	2007	Another distinctive feature of IGFBP-6 is its unique N-terminal disulfide linkages; the N-domains of IGFBPs 1-5 contain six disulfides and share a conserved GCGCC motif, but IGFBP-6 lacks the two adjacent cysteines in this motif, so its first three N-terminal disulfide linkages differ from those of the other IGFBPs.	Disulfides	64-73	insulin like growth factor binding protein 6	Homo sapiens	31-38
17305365-4	2007	Another distinctive feature of IGFBP-6 is its unique N-terminal disulfide linkages; the N-domains of IGFBPs 1-5 contain six disulfides and share a conserved GCGCC motif, but IGFBP-6 lacks the two adjacent cysteines in this motif, so its first three N-terminal disulfide linkages differ from those of the other IGFBPs.	Disulfides	124-134	insulin like growth factor binding protein 6	Homo sapiens	31-38
17305365-4	2007	Another distinctive feature of IGFBP-6 is its unique N-terminal disulfide linkages; the N-domains of IGFBPs 1-5 contain six disulfides and share a conserved GCGCC motif, but IGFBP-6 lacks the two adjacent cysteines in this motif, so its first three N-terminal disulfide linkages differ from those of the other IGFBPs.	Disulfides	124-134	insulin like growth factor binding protein 4	Homo sapiens	101-107
17305365-4	2007	Another distinctive feature of IGFBP-6 is its unique N-terminal disulfide linkages; the N-domains of IGFBPs 1-5 contain six disulfides and share a conserved GCGCC motif, but IGFBP-6 lacks the two adjacent cysteines in this motif, so its first three N-terminal disulfide linkages differ from those of the other IGFBPs.	Disulfides	124-133	insulin like growth factor binding protein 6	Homo sapiens	31-38
17305365-4	2007	Another distinctive feature of IGFBP-6 is its unique N-terminal disulfide linkages; the N-domains of IGFBPs 1-5 contain six disulfides and share a conserved GCGCC motif, but IGFBP-6 lacks the two adjacent cysteines in this motif, so its first three N-terminal disulfide linkages differ from those of the other IGFBPs.	Disulfides	124-133	insulin like growth factor binding protein 4	Homo sapiens	101-107
17315952-1	2007	Alpha-conotoxins isolated from Conus venoms contain 11-19 residues and preferentially fold into the globular conformation that possesses a specific disulfide pairing pattern (C1-3, C2-4).	Disulfides	148-157	homeobox C13	Homo sapiens	175-179
17302442-0	2007	An engineered second disulfide bond restricts lymphotactin/XCL1 to a chemokine-like conformation with XCR1 agonist activity.	Disulfides	21-30	X-C motif chemokine ligand 1	Homo sapiens	46-58
17302442-0	2007	An engineered second disulfide bond restricts lymphotactin/XCL1 to a chemokine-like conformation with XCR1 agonist activity.	Disulfides	21-30	X-C motif chemokine ligand 1	Homo sapiens	59-63
17302442-2	2007	Lymphotactin (Ltn) is a unique chemokine in that it contains only one disulfide and exhibits large-scale structural heterogeneity.	Disulfides	70-79	X-C motif chemokine ligand 1	Homo sapiens	0-12
17302442-2	2007	Lymphotactin (Ltn) is a unique chemokine in that it contains only one disulfide and exhibits large-scale structural heterogeneity.	Disulfides	70-79	X-C motif chemokine ligand 1	Homo sapiens	14-17
17106881-7	2007	Disulfide bond disruption significantly attenuated recombinant lubricin and LUB-C binding to cartilage surfaces, demonstrating a requirement for protein secondary structure in facilitating the appropriate localization of lubricin at relevant tissue interfaces.	Disulfides	0-9	ubiquitin conjugating enzyme E2 L1 (pseudogene)	Homo sapiens	76-81
17196658-4	2007	Sea bass IL-12 p40 and p35 conserve most cysteines involved in the intra-chain disulfide bonds of human IL-12 subunits as well as the important structural residues for human IL-12 heterodimerization.	Disulfides	79-88	interleukin 12A	Homo sapiens	23-26
17322536-4	2007	CAR-D2 is shown to be a beta-sandwich motif comprised of two beta-sheets, which are stabilized by two disulfide bonds.	Disulfides	102-111	CXADR Ig-like cell adhesion molecule	Homo sapiens	0-3
17083647-0	2007	Trp207Gly in platelet glycoprotein Ibalpha is a novel mutation that disrupts the connection between the leucine-rich repeat domain and the disulfide loop structure and causes Bernard-Soulier syndrome.	Disulfides	139-148	glycoprotein Ib platelet subunit alpha	Homo sapiens	22-42
17083647-6	2007	The crystal structure of the N-terminus of GPIbalpha (PDB: 1SQ0) indicates that Trp207 is completely buried and located in a disulfide loop structure that interacts with the leucine-rich repeat (LRR) domain.	Disulfides	125-134	glycoprotein Ib platelet subunit alpha	Homo sapiens	43-52
17083647-7	2007	CONCLUSION: A novel mutation, Trp207Gly, causes BSS and predicts disruption of the interaction between a disulfide loop and the LRR domain that is essential for the integrity of GPIbalpha structure.	Disulfides	105-114	glycoprotein Ib platelet subunit alpha	Homo sapiens	178-187
17158912-4	2006	Modifications of the large extracellular loop of UPIb, such as mutation of the N-glycosylation site or the cysteines involved in the formation of three disulfide bridges, or exchanging the large luminal loop of UPIb with that of UPIa did not affect the ability of UPIb to reach the cell surface.	Disulfides	152-161	uroplakin 1B	Homo sapiens	49-53
16978236-9	2006	These results suggest that despite disruption of the disulfide linkage between GPIbalpha and GPIbbeta, GPIb/IX is formed, but its stability may be impaired, resulting in low levels of the complex on the platelet membranes.	Disulfides	53-62	glycoprotein Ib platelet subunit alpha	Homo sapiens	79-88
16978236-9	2006	These results suggest that despite disruption of the disulfide linkage between GPIbalpha and GPIbbeta, GPIb/IX is formed, but its stability may be impaired, resulting in low levels of the complex on the platelet membranes.	Disulfides	53-62	glycoprotein Ib platelet subunit beta	Homo sapiens	93-101
16930137-1	2006	Interleukin (IL)-12 is a 70-kDa cytokine comprised of two disulfide-linked proteins (p35 and p40) and is essential for the initiation of effective immune response.	Disulfides	58-67	interleukin 12A	Homo sapiens	85-88
16780799-1	2006	Thioredoxin reductase catalyzes the NADPH-dependent reduction of the catalytic disulfide bond of thioredoxin.	Disulfides	79-88	Thioredoxin	Caenorhabditis elegans	97-108
16895479-3	2006	We generated four double-mutants of AtPreP1 by introducing cysteines at positions where disulfide bonds can be formed in order to lock and unlock the protease and tested the activity under oxidizing and reducing conditions.	Disulfides	88-97	presequence protease 1	Arabidopsis thaliana	36-43
16916653-1	2006	The human T-cell receptor-CD3 complex consists of at least eight polypeptide chains; CD3gamma- and delta-dimers associate with the disulfide linked alphabeta- and zetazeta-dimers to form a functional receptor complex.	Disulfides	131-140	CD3 gamma subunit of T-cell receptor complex	Homo sapiens	85-104
16555311-1	2006	Plant LTP1 are small helical proteins stabilized by four disulfide bridges and are characterized by the presence of an internal cavity, in which various hydrophobic ligands can be inserted.	Disulfides	57-66	non-specific lipid-transfer protein 1	Nicotiana tabacum	6-10
16480776-7	2006	Human, monkey and mouse CD4 have the cystein and the disulfide bond, but pig, cat, whale and dog CD4, like that of the bat, lacked the cystein.	Disulfides	53-62	CD4 antigen	Mus musculus	24-27
16626737-8	2006	When isolated from Escherichia coli, a major proportion of recombinant AtSFGH was recovered with the Cys59 forming a mixed disulfide with glutathione.	Disulfides	123-132	S-formylglutathione hydrolase	Arabidopsis thaliana	71-77
16290109-0	2006	Preparation and crystallization of the disulfide-linked HLA-G dimer.	Disulfides	39-48	major histocompatibility complex, class I, G	Homo sapiens	56-61
16290109-2	2006	HLA-G can be expressed as a disulfide-liked dimer both in solution and at the cell surface.	Disulfides	28-37	major histocompatibility complex, class I, G	Homo sapiens	0-5
16290109-4	2006	Here, we report the crystallization of the disulfide-linked dimer form of HLA-G by adding dithiothreitol (DTT), enabling a 3.2-A data set to be collected.	Disulfides	43-52	major histocompatibility complex, class I, G	Homo sapiens	74-79
16290109-5	2006	We also show that DTT promotes disulfide bond exchange of refolded HLA-G, whose free cysteine was protected, thus facilitating its dimerization.	Disulfides	31-40	major histocompatibility complex, class I, G	Homo sapiens	67-72
16475797-1	2006	Goat alpha-lactalbumin (GLA) contains four tryptophan (Trp) residues and four disulfide bonds.	Disulfides	78-87	alpha-galactosidase A	Capra hircus	24-27
16475797-7	2006	While photolysis of Cys6-Cys120 and Cys73-Cys91 disulfide bonds in GLA has been reported, cleavage of the Cys61-Cys77 disulfide bonds has not been previously detected.	Disulfides	48-57	alpha-galactosidase A	Capra hircus	67-70
16475797-9	2006	The substitution of each Trp residue led to less thiol production compared to that for wild-type GLA, showing that each Trp residue in GLA contributed to the photolytic cleavage of disulfide bridges.	Disulfides	181-190	alpha-galactosidase A	Capra hircus	97-100
16475797-9	2006	The substitution of each Trp residue led to less thiol production compared to that for wild-type GLA, showing that each Trp residue in GLA contributed to the photolytic cleavage of disulfide bridges.	Disulfides	181-190	alpha-galactosidase A	Capra hircus	135-138
16357268-11	2006	Incubation of the casein micelles with the reducing agent beta-mercaptoethanol revealed that disulfide bonds formed between PG and casein or between PG and casein-bound beta-LG are the mechanisms for heat-induced PG binding to casein micelles.	Disulfides	93-102	beta-lactoglobulin	Bos taurus	169-176
16365463-1	2006	The thyrotropin receptor (TSHR), the major autoantigen in Graves" disease, is posttranslationally modified by intramolecular cleavage to form disulfide-linked A- and B-subunits.	Disulfides	142-151	thyroid stimulating hormone receptor	Homo sapiens	4-24
16365463-1	2006	The thyrotropin receptor (TSHR), the major autoantigen in Graves" disease, is posttranslationally modified by intramolecular cleavage to form disulfide-linked A- and B-subunits.	Disulfides	142-151	thyroid stimulating hormone receptor	Homo sapiens	26-30
16342940-0	2005	Disulfide structure of the leucine-rich repeat C-terminal cap and C-terminal stalk region of Nogo-66 receptor.	Disulfides	0-9	reticulon 4 receptor	Homo sapiens	93-109
15979762-9	2005	Therefore, while the MIT-like ACTX family appears to adopt the ancestral disulfide-directed beta-hairpin protein fold of MIT1, a motif believed to be shared by other AVIT family peptides, variations in the amino acid sequence and surface charge result in a loss of activity on prokineticin receptors.	Disulfides	73-82	prokineticin 2	Homo sapiens	121-125
16307473-0	2005	Proinsulin lacking the A7-B7 disulfide bond, Ins2Akita, tends to aggregate due to the exposed hydrophobic surface.	Disulfides	29-38	insulin II	Mus musculus	0-10
16307473-1	2005	A single mutation (C96Y) in the Ins2 gene, which disrupts the A7-B7 disulfide bond, causes the diabetic phenotype in Akita mice.	Disulfides	68-77	insulin II	Mus musculus	32-36
16307473-3	2005	Gel filtration chromatography and dynamic light scattering revealed that the apparent size of the mutant proinsulin molecules was significantly larger than that of wild-type proinsulin, even in the absence of intermolecular disulfide bonds.	Disulfides	224-233	insulin II	Mus musculus	105-115
16081415-0	2005	SIRPbeta1 is expressed as a disulfide-linked homodimer in leukocytes and positively regulates neutrophil transepithelial migration.	Disulfides	28-37	signal regulatory protein beta 1	Homo sapiens	0-9
16081415-5	2005	Furthermore, although SIRPalpha (Bit/PTPNS-1) is expressed as a monomer, we showed that SIRPbeta1 is expressed on the cell surface as a disulfide-linked homodimer with bond formation mediated by Cys-320 in the membrane-proximal Ig loop.	Disulfides	136-145	signal regulatory protein beta 1	Homo sapiens	88-97
16107341-3	2005	To enable disulfide-dependent and spontaneous formation of active Stat1 homodimer (as was done previously for Stat3), we engineered Stat1-CC with double-cysteine substitutions in the Src homology 2 (SH2)-homodimerization domain (at Ala-656 and Asn-658).	Disulfides	10-19	signal transducer and activator of transcription 1	Homo sapiens	66-71
16143573-0	2005	Complete refolding of bovine beta-lactoglobulin requires disulfide bond formation under strict conditions.	Disulfides	57-66	beta-lactoglobulin	Bos taurus	29-47
16044415-2	2005	The 87-132 amino acid C-terminal domain of hAGRP possesses five disulfide bridges and a well-defined three-dimensional structure that displays full biological activity as compared to the full-length protein.	Disulfides	64-73	agouti related neuropeptide	Homo sapiens	43-48
16054449-8	2005	Serum NAMLAA had a C398-C404 disulfide, partial phosphorylation of S218, and deamidation of N253 and N301.	Disulfides	29-38	peptidoglycan recognition protein 2	Homo sapiens	6-12
16081815-3	2005	disulfide-linked H chain complexes in the endoplasmic reticulum (ER), bind the ER chaperone BiP/Grp78, and undergo ER-associated degradation.	Disulfides	0-9	heat shock protein family A (Hsp70) member 5	Rattus norvegicus	92-95
16081815-3	2005	disulfide-linked H chain complexes in the endoplasmic reticulum (ER), bind the ER chaperone BiP/Grp78, and undergo ER-associated degradation.	Disulfides	0-9	heat shock protein family A (Hsp70) member 5	Rattus norvegicus	96-101
15955808-2	2005	In this study, we report the x-ray crystal structure of the Bre5 NTF2-like domain and show that it forms a homodimeric structure that is similar to other NTF2-like domains, except for the presence of an intermolecular disulfide bond in the crystals.	Disulfides	218-227	nuclear transport factor 2	Homo sapiens	65-69
15955808-2	2005	In this study, we report the x-ray crystal structure of the Bre5 NTF2-like domain and show that it forms a homodimeric structure that is similar to other NTF2-like domains, except for the presence of an intermolecular disulfide bond in the crystals.	Disulfides	218-227	nuclear transport factor 2	Homo sapiens	154-158
15955808-3	2005	Sedimentation equilibrium studies reveal that under non-reducing conditions, the Bre5 NTF2-like domain is exclusively dimeric, whereas a disulfide bond-deficient mutant undergoes a monomer-dimer equilibrium with a dissociation constant in the midnanomolar range, suggesting that dimer formation and possibly also disulfide bond formation may modulate Bre5 function in vivo.	Disulfides	313-322	nuclear transport factor 2	Homo sapiens	86-90
16097806-2	2005	Using this approach, the endoplasmic reticulum chaperone, protein disulfide isomerase (PDI), which participates in the maturation of newly synthesized proteins through promoting correct disulfide formation, was consistently found to be modified by 4-HNE.	Disulfides	66-75	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	87-90
15989945-1	2005	In this issue of Cell, show that there is a disulfide relay system in the intermembrane space (IMS) of mitochondria that is comprised of the proteins Mia40 and Erv1.	Disulfides	44-53	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	150-155
15989945-3	2005	Oxidized Mia40 traps newly imported proteins through mixed disulfide bridges.	Disulfides	59-68	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	9-14
15989945-5	2005	The reduced Mia40 generated is then reoxidized by the sulfhydryl oxidase Erv1, promoting the next round of disulfide exchange.	Disulfides	107-116	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	12-17
10604595-6	1999	In addition, the mutant [Ala64,104]HCC-2-(48-113) lacking the third disulfide bond that discriminates HCC-2 from most other chemokines was synthesized.	Disulfides	68-77	C-C motif chemokine ligand 15	Homo sapiens	35-40
10604596-0	1999	Disulfide assignment of the C-terminal cysteine knot of agouti-related protein (AGRP) by direct sequencing analysis.	Disulfides	0-9	agouti related neuropeptide	Homo sapiens	56-78
10604596-0	1999	Disulfide assignment of the C-terminal cysteine knot of agouti-related protein (AGRP) by direct sequencing analysis.	Disulfides	0-9	agouti related neuropeptide	Homo sapiens	80-84
10585186-3	1999	Our results showed that yeast PDI expressed into the periplasm could catalyze the formation of disulfide bonds in alkaline phosphatase, restoring the phoA(+) phenotype in dsbA(-) mutants.	Disulfides	95-104	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	30-33
10441134-0	1999	Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin.	Disulfides	8-17	vitronectin	Homo sapiens	85-96
8914835-0	1996	S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione.	Disulfides	49-59	protein-disulfide isomerase	Escherichia coli	118-145
8914835-1	1996	The disulfide-reducing activities of glutaredoxin, thioredoxin, protein disulfide isomerase, glutathione, and cysteine were directly compared with a mixture of hepatocyte 35S-glutathiolated proteins as the substrate.	Disulfides	4-13	protein-disulfide isomerase	Escherichia coli	64-91
8914835-19	1996	Thus, protein disulfide isomerase and thioredoxin are more effective than glutaredoxin as reductants of insulin protein disulfides.	Disulfides	120-130	protein-disulfide isomerase	Escherichia coli	6-33
10441134-14	1999	In summary, these studies indicate that PDI functions to form disulfide-linked complexes of vitronectin with thrombin-AT.	Disulfides	62-71	vitronectin	Homo sapiens	92-103
8914835-19	1996	Thus, protein disulfide isomerase and thioredoxin are more effective than glutaredoxin as reductants of insulin protein disulfides.	Disulfides	120-130	thioredoxin	Homo sapiens	38-49
15992811-4	2005	XCL1 differs from other chemokines in that it contains only a single disulfide bond and a mucin-like domain at its carboxy terminus that is glycosylated.	Disulfides	69-78	X-C motif chemokine ligand 1	Homo sapiens	0-4
8914835-23	1996	A glutathione binding site at the dithiol region of glutaredoxin may be of primary importance for its function in protein dethiolation, while a different specific peptide binding site in thioredoxin may be more suited to certain protein disulfide structures.	Disulfides	237-246	thioredoxin	Homo sapiens	187-198
8900144-4	1996	SDS-polyacrylamide gel electrophoresis and electrospray mass spectrometry revealed the 32-kDa species was dimeric beta-globin formed by an intermolecular disulfide bond, while the 16-kDa species was authentic monomeric beta-globin.	Disulfides	154-163	hemoglobin subunit beta	Homo sapiens	114-125
15986330-5	2005	As expected, from barley to malt and to beer, most of the heat-stable proteins are disulfide-rich proteins, implicated in the defense of plants against their bio-aggressors, e.g., serpin-like chymotrypsin inhibitors (protein Z), amylase and amylase-protease inhibitors, and lipid transfer proteins (LTP1 and LTP2).	Disulfides	83-92	non-specific lipid transport protein 1	Hordeum vulgare	299-312
10400663-1	1999	Residues 1-127 of human TIMP-2 (N-TIMP-2), comprising three of the disulfide-bonded loops of the TIMP-2 molecule, is a discrete protein domain that folds independently of the C-terminal domain.	Disulfides	67-76	TIMP metallopeptidase inhibitor 2	Homo sapiens	24-30
8900144-8	1996	Disulfide-bonded beta-globin dimers showed a slight increase in thermal stability compared with beta-globin; however, dimers were still more unstable than tetrameric Hb A.	Disulfides	0-9	hemoglobin subunit beta	Homo sapiens	17-28
10400663-1	1999	Residues 1-127 of human TIMP-2 (N-TIMP-2), comprising three of the disulfide-bonded loops of the TIMP-2 molecule, is a discrete protein domain that folds independently of the C-terminal domain.	Disulfides	67-76	TIMP metallopeptidase inhibitor 2	Homo sapiens	32-40
15966731-3	2005	Each subunit of the transthyretin (TTR) tetramer has a single Cys residue that can exist in the SH form or as a mixed disulfide with the amino acid Cys or the peptide glutathione or fragments of the latter.	Disulfides	118-127	transthyretin	Mus musculus	35-38
15966731-8	2005	Our in vitro data reveal that the C10S/V30M and V30M TTR homotetramers have identical amyloidogenicity and stability, implying that Cys-10 mixed disulfide formation enhances amyloidogenesis in V30M transgenic mice.	Disulfides	145-154	transthyretin	Mus musculus	53-56
8900156-5	1996	Native disulfide-linked homodimers of CD28 and CTLA-4 bound with two kinetically distinct binding sites, one of high avidity and slow dissociation and one of low avidity and more rapid dissociation.	Disulfides	7-16	cytotoxic T-lymphocyte associated protein 4	Homo sapiens	47-53
15966731-9	2005	Given the high proportion of TTR subunits having mixed disulfide modifications in human plasma ( approximately 50%), and the data within demonstrating their increased amyloidogenicity, we submit that disulfide metabolite modifications have the potential to influence the course of amyloidoses, including TTR amyloidoses caused by mutations.	Disulfides	55-64	transthyretin	Homo sapiens	29-32
15966731-9	2005	Given the high proportion of TTR subunits having mixed disulfide modifications in human plasma ( approximately 50%), and the data within demonstrating their increased amyloidogenicity, we submit that disulfide metabolite modifications have the potential to influence the course of amyloidoses, including TTR amyloidoses caused by mutations.	Disulfides	200-209	transthyretin	Homo sapiens	29-32
15966731-9	2005	Given the high proportion of TTR subunits having mixed disulfide modifications in human plasma ( approximately 50%), and the data within demonstrating their increased amyloidogenicity, we submit that disulfide metabolite modifications have the potential to influence the course of amyloidoses, including TTR amyloidoses caused by mutations.	Disulfides	200-209	transthyretin	Homo sapiens	304-307
10400663-1	1999	Residues 1-127 of human TIMP-2 (N-TIMP-2), comprising three of the disulfide-bonded loops of the TIMP-2 molecule, is a discrete protein domain that folds independently of the C-terminal domain.	Disulfides	67-76	TIMP metallopeptidase inhibitor 2	Homo sapiens	34-40
8824296-0	1996	Beta1,4-N-acetylgalactosaminyltransferase (GM2 synthase) is released from Golgi membranes as a neuraminidase-sensitive, disulfide-bonded dimer by a cathepsin D-like protease.	Disulfides	120-129	cathepsin D	Cricetulus griseus	148-159
10350489-3	1999	We propose an additional modification that has implications for the in vivo regulation of protein tyrosine phosphatase 1B (PTP1B, EC 3.1.3.48): the glutathionylation of Cys215 to a mixed protein disulfide.	Disulfides	195-204	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	90-121
15814611-2	2005	Glutaredoxin (Grx) and protein-disulfide isomerase (PDI) are members of the thioredoxin superfamily of thiol/disulfide exchange catalysts.	Disulfides	31-40	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	52-55
15814611-5	2005	It catalyzes protein disulfide formation in a redox buffer with an initial velocity that is 30-fold faster than PDI.	Disulfides	21-30	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	112-115
15814611-8	2005	Grx1 is a good oxidase because of the high reactivity of a Grx1-glutathione mixed disulfide, and PDI is a good oxidase because of the high reactivity of the disulfide between the two active site cysteines.	Disulfides	157-166	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	97-100
15814611-10	2005	It catalyzes the reduction of nonnative disulfides in scrambled ribonuclease and protein-glutathione mixed disulfides 30-180 times faster than PDI.	Disulfides	40-50	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	143-146
15814611-12	2005	Grx1 and PDI have both found mechanisms to enhance active site reactivity toward proteins, particularly in the kinetically difficult direction: Grx1 by providing a reactive glutathione mixed disulfide to supplement its oxidase activity and PDI by utilizing its multidomain structure to supplement its reductase activity.	Disulfides	191-200	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	9-12
10350489-3	1999	We propose an additional modification that has implications for the in vivo regulation of protein tyrosine phosphatase 1B (PTP1B, EC 3.1.3.48): the glutathionylation of Cys215 to a mixed protein disulfide.	Disulfides	195-204	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	123-128
8964512-1	1996	Thioredoxin (TRX) is an ubiquitous and relatively conserved oxidoreductant enzyme which is involved in a multitude of redox reactions through the formation of reversible disulfide bonds.	Disulfides	170-179	thioredoxin	Homo sapiens	0-11
15820220-3	2005	Two extensively unfolded homologous isomers (beads-form) of BPTI (Cys5-Cys14, Cys30-Cys38, Cys51-Cys55) and TAP (Cys5-Cys15, Cys33-Cys39, Cys55-Cys59) were allowed to refold in parallel via disulfide shuffling of 13 potential isomers to form the native structure.	Disulfides	190-199	spleen trypsin inhibitor I	Bos taurus	60-64
15890001-7	2005	These mechanisms include the formation of disulfide bonds or the formation of a sulfenamide bond, a novel mechanism that was identified for PTP1B.	Disulfides	42-51	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	140-145
8964512-1	1996	Thioredoxin (TRX) is an ubiquitous and relatively conserved oxidoreductant enzyme which is involved in a multitude of redox reactions through the formation of reversible disulfide bonds.	Disulfides	170-179	thioredoxin	Homo sapiens	13-16
10346877-1	1999	The anti-Tac disulfide-bonded variable region fragment (dsFv) is a genetically engineered, 25 kDa, murine monoclonal antibody fragment that recognizes the alpha subunit of the interleukin-2 receptor (IL-2Ralpha).	Disulfides	13-22	interleukin 2 receptor, alpha chain	Mus musculus	200-210
8784198-1	1996	Thioredoxin reduction in chloroplasts is catalyzed by a unique class of disulfide reductases which use a [2Fe-2S]2+/+ ferredoxin as the electron donor and contain an Fe-S cluster as the sole prosthetic group in addition to the active-site disulfide.	Disulfides	72-81	thioredoxin	Homo sapiens	0-11
10090736-10	1999	The two disulfide bridges present in the human P2Y1 receptor play a major role in the structure and stability of the receptor, to constrain the loops within the receptor, specifically stretching the EL2 over the opening of the TM cleft and thus defining the path of access to the binding site.	Disulfides	8-17	spectrin alpha, erythrocytic 1	Homo sapiens	199-202
15893662-4	2005	An isomerization of one disulfide bond from Cys(26)/Cys(57) to Cys(24)/Cys(57) is required prior to Cu(I) binding to form the Cu(1)Cox17 complex.	Disulfides	24-33	cytochrome c oxidase copper chaperone COX17	Homo sapiens	131-136
8702885-2	1996	TNF-R p75 belongs to the TNF receptor superfamily characterized by cysteine-rich extracellular regions composed of three to six disulfide-linked domains.	Disulfides	128-137	TNF receptor superfamily member 1A	Homo sapiens	0-5
15752764-2	2005	The structure is very similar to the structure of bone morphogenetic factor 7 (BMP7) and consists of two banana-shaped monomers, linked via a disulfide bridge.	Disulfides	142-151	bone morphogenetic protein 7	Homo sapiens	79-83
9920835-0	1999	Molecular genetic analysis of a compound heterozygote for the glycoprotein (GP) IIb gene associated with Glanzmann"s thrombasthenia: disruption of the 674-687 disulfide bridge in GPIIb prevents surface exposure of GPIIb-IIIa complexes.	Disulfides	159-168	integrin subunit alpha 2b	Homo sapiens	62-83
8702617-2	1996	Natriuretic peptide receptor C (NPR-C) is a disulfide-linked homodimer with an approximately 440-amino acid extracellular domain and a 37-amino acid cytoplasmic domain; it functions in the internalization and degradation of bound ligand.	Disulfides	44-53	natriuretic peptide receptor 3	Rattus norvegicus	0-30
9920835-0	1999	Molecular genetic analysis of a compound heterozygote for the glycoprotein (GP) IIb gene associated with Glanzmann"s thrombasthenia: disruption of the 674-687 disulfide bridge in GPIIb prevents surface exposure of GPIIb-IIIa complexes.	Disulfides	159-168	integrin subunit alpha 2b	Homo sapiens	179-184
9920835-6	1999	Virtually all of the proband"s GPIIb-mRNA was accounted for by the allele inherited from the mother showing a T2113-->C transition that changes Cys674-->Arg674 disrupting the 674-687 intramolecular disulfide bridge.	Disulfides	198-207	integrin subunit alpha 2b	Homo sapiens	31-36
9920835-9	1999	Thus, the intramolecular 674-687 disulfide bridge in GPIIb is essential for the normal processing of GPIIb-IIIa complexes.	Disulfides	33-42	integrin subunit alpha 2b	Homo sapiens	53-58
9920835-9	1999	Thus, the intramolecular 674-687 disulfide bridge in GPIIb is essential for the normal processing of GPIIb-IIIa complexes.	Disulfides	33-42	integrin subunit alpha 2b	Homo sapiens	101-106
15819897-3	2005	Moreover, flash photolysis experiments at high temperatures reveal that Ngb remains functional at 90 degrees C. Human Ngb may have a disulfide bond in the CD loop region; reduction of the disulfide bond increases the affinity of the iron atom for the distal (E7) histidine, and leads to a 3 degrees C increase in the T(m) for ferrous Ngb.	Disulfides	133-142	neuroglobin	Homo sapiens	72-75
15819897-3	2005	Moreover, flash photolysis experiments at high temperatures reveal that Ngb remains functional at 90 degrees C. Human Ngb may have a disulfide bond in the CD loop region; reduction of the disulfide bond increases the affinity of the iron atom for the distal (E7) histidine, and leads to a 3 degrees C increase in the T(m) for ferrous Ngb.	Disulfides	133-142	neuroglobin	Homo sapiens	118-121
15819897-3	2005	Moreover, flash photolysis experiments at high temperatures reveal that Ngb remains functional at 90 degrees C. Human Ngb may have a disulfide bond in the CD loop region; reduction of the disulfide bond increases the affinity of the iron atom for the distal (E7) histidine, and leads to a 3 degrees C increase in the T(m) for ferrous Ngb.	Disulfides	133-142	neuroglobin	Homo sapiens	118-121
15819897-3	2005	Moreover, flash photolysis experiments at high temperatures reveal that Ngb remains functional at 90 degrees C. Human Ngb may have a disulfide bond in the CD loop region; reduction of the disulfide bond increases the affinity of the iron atom for the distal (E7) histidine, and leads to a 3 degrees C increase in the T(m) for ferrous Ngb.	Disulfides	188-197	neuroglobin	Homo sapiens	72-75
15819897-3	2005	Moreover, flash photolysis experiments at high temperatures reveal that Ngb remains functional at 90 degrees C. Human Ngb may have a disulfide bond in the CD loop region; reduction of the disulfide bond increases the affinity of the iron atom for the distal (E7) histidine, and leads to a 3 degrees C increase in the T(m) for ferrous Ngb.	Disulfides	188-197	neuroglobin	Homo sapiens	118-121
15819897-3	2005	Moreover, flash photolysis experiments at high temperatures reveal that Ngb remains functional at 90 degrees C. Human Ngb may have a disulfide bond in the CD loop region; reduction of the disulfide bond increases the affinity of the iron atom for the distal (E7) histidine, and leads to a 3 degrees C increase in the T(m) for ferrous Ngb.	Disulfides	188-197	neuroglobin	Homo sapiens	118-121
15685601-3	2005	BP7, an enzyme with potential applications in biotechnology, was used to test Pir4, a disulfide bound cell wall protein, as a fusion partner for the expression of recombinant proteins in standard or glycosylation-deficient mnn9 strains of Saccharomyces cerevisiae.	Disulfides	86-95	Cis3p	Saccharomyces cerevisiae S288C	78-82
8702617-2	1996	Natriuretic peptide receptor C (NPR-C) is a disulfide-linked homodimer with an approximately 440-amino acid extracellular domain and a 37-amino acid cytoplasmic domain; it functions in the internalization and degradation of bound ligand.	Disulfides	44-53	natriuretic peptide receptor 3	Rattus norvegicus	32-37
8702529-1	1996	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.	Disulfides	47-56	selectin P ligand	Homo sapiens	0-32
15900090-5	2005	It was concluded that disulfide bonds play an essential role in the association of p23 with the nuclear matrix and that p23 is mostly localized in the nuclear matrix interior.	Disulfides	22-31	RAS related	Rattus norvegicus	83-86
15537792-3	2005	The XEEL protein is a homohexamer of 43-kDa N-glycosylated peptide subunits linked by disulfide bonds.	Disulfides	86-95	intelectin 1 L homeolog	Xenopus laevis	4-8
9890969-1	1999	Among the glycoprotein hormone receptors, only the thyrotropin receptor (TSHR) cleaves (at two sites) into disulfide-linked A and B subunits.	Disulfides	107-116	thyroid stimulating hormone receptor	Homo sapiens	51-71
9890969-1	1999	Among the glycoprotein hormone receptors, only the thyrotropin receptor (TSHR) cleaves (at two sites) into disulfide-linked A and B subunits.	Disulfides	107-116	thyroid stimulating hormone receptor	Homo sapiens	73-77
15567420-3	2005	Complex formation between LAP and LTBP is mediated by an intramolecular disulfide exchange between the third 8-cysteine (8-Cys3) domain of LTBP with a pair of cysteine residues in LAP.	Disulfides	72-81	TNF receptor associated factor 3	Homo sapiens	26-29
8702529-1	1996	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.	Disulfides	47-56	selectin P ligand	Homo sapiens	34-40
15567420-3	2005	Complex formation between LAP and LTBP is mediated by an intramolecular disulfide exchange between the third 8-cysteine (8-Cys3) domain of LTBP with a pair of cysteine residues in LAP.	Disulfides	72-81	TNF receptor associated factor 3	Homo sapiens	180-183
8702529-1	1996	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.	Disulfides	47-56	selectin E	Homo sapiens	146-156
15625724-0	2005	Engineering disulfide bonds of the novel human beta-defensins hBD-27 and hBD-28: differences in disulfide formation and biological activity among human beta-defensins.	Disulfides	12-21	defensin beta 128	Homo sapiens	73-79
15625724-4	2005	Here we report for the first time the chemical synthesis of the new fully disulfide-bonded beta-defensins hBD-27 and hBD-28, and compare the results with synthetic procedures to obtain the known hBD-2 and hBD-3.	Disulfides	74-83	defensin beta 128	Homo sapiens	117-123
10493174-1	1999	The T cell coreceptor CD8 is a cell-surface glycoprotein expressed either as a disulfide-linked homodimer of two CD8alpha monomers, or a heterodimer of CD8alpha and CD8beta.	Disulfides	79-88	CD8a molecule	Homo sapiens	22-25
8764057-9	1996	To determine the disulfide bond arrangement of the eight cysteines of gC1(457t),the protein was cleaved with cyanogen bromide.	Disulfides	17-26	solute carrier family 25 member 22	Homo sapiens	70-73
10493174-1	1999	The T cell coreceptor CD8 is a cell-surface glycoprotein expressed either as a disulfide-linked homodimer of two CD8alpha monomers, or a heterodimer of CD8alpha and CD8beta.	Disulfides	79-88	CD8a molecule	Homo sapiens	113-121
10614055-12	1999	Recently, peripherin/rds-containing tetramers have been shown to form disulfide-mediated higher-order oligomers.	Disulfides	70-79	peripherin 2	Homo sapiens	21-24
15625724-5	2005	While hBD-27 was readily converted into a product with the desired disulfide pattern by oxidative folding, hBD-28 required a selective protective group strategy to introduce the three disulfide bonds.	Disulfides	184-193	defensin beta 128	Homo sapiens	107-113
8812832-9	1996	From these studies with CHO-K1 transfectants, we conclude that (i) cysteines 135 and 175 are both necessary for efficient secretion of a biologically active N-terminal BPI fragment, presumably through the formation of a disulfide bond, (ii) cysteine 132 is responsible for dimer formation, and (iii) only the C132A modification yields a stable, biologically active, N-terminal BPI fragment (designated rBPI21) that is free of dimeric species.	Disulfides	220-229	bactericidal permeability increasing protein	Homo sapiens	168-171
15674109-2	2005	IL-12 is a heterodimeric protein comprising 2 disulfide-linked subunits designated p35 and p40.	Disulfides	46-55	interleukin 12A	Homo sapiens	83-86
9829970-4	1998	Using both co-immunoprecipitation and nonreducing SDS-polyacrylamide gel electrophoresis, we demonstrated that MLK-3 forms disulfide bridged homo-dimers and that the LZs motif is sufficient for MLK-3 homodimerization.	Disulfides	123-132	mitogen-activated protein kinase kinase kinase 11	Homo sapiens	111-116
8755573-5	1996	In vitro kinase assay results indicate that FGFR2 receptors containing Crouzon mutations have increased tyrosine kinase activity and, when analyzed under nonreducing conditions, exhibited disulfide-bonded dimers.	Disulfides	188-197	fibroblast growth factor receptor 2	Homo sapiens	44-49
9826543-4	1998	The candidates that might form disulfide bonds with actin were identified by monoclonal antibody to be GpIIb and/or GpIIIa.	Disulfides	31-40	integrin subunit alpha 2b	Homo sapiens	103-108
15615519-3	2004	The endogenous hAGRP protein is 132 amino acids in length, possesses five disulfide bridges at the C-terminus of the molecule, and is expressed in the hypothalamus of the brain.	Disulfides	74-83	agouti related neuropeptide	Homo sapiens	15-20
15596720-7	2004	This motif lies directly at the docking point of COX I helix 3 and cytochrome c, and modeling of bovine COX I suggests the possibility of an unprecedented helix-terminating disulfide bridge that could alter COX/cytochrome c dissociation kinetics.	Disulfides	173-182	cytochrome c oxidase subunit 7A1	Bos taurus	49-52
15596720-7	2004	This motif lies directly at the docking point of COX I helix 3 and cytochrome c, and modeling of bovine COX I suggests the possibility of an unprecedented helix-terminating disulfide bridge that could alter COX/cytochrome c dissociation kinetics.	Disulfides	173-182	cytochrome c oxidase subunit 7A1	Bos taurus	104-107
15596720-7	2004	This motif lies directly at the docking point of COX I helix 3 and cytochrome c, and modeling of bovine COX I suggests the possibility of an unprecedented helix-terminating disulfide bridge that could alter COX/cytochrome c dissociation kinetics.	Disulfides	173-182	cytochrome c oxidase subunit 7A1	Bos taurus	104-107
8755573-6	1996	Thus the human developmental abnormality Crouzon syndrome arises from constitutive activation of FGFR2 due to aberrant intermolecular disulfide-bonding.	Disulfides	134-143	fibroblast growth factor receptor 2	Homo sapiens	97-102
8776888-0	1996	Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels.	Disulfides	20-29	vimentin	Homo sapiens	59-67
15589826-4	2004	Mutation in the D8C at Cys217 in human UMOD is associated with familial juvenile hyperuricaemic nephropathy, which might be due to the disruption of the disulfide bridge.	Disulfides	153-162	uromodulin	Homo sapiens	39-43
15675819-5	2004	The reaction at 60 degrees C between beta-LG A and an activated kappa-CN formed small disulfide-bonded aggregates.	Disulfides	86-95	beta-lactoglobulin	Bos taurus	37-44
15675819-6	2004	The tryptic peptides from this model system included a peptide with a disulfide bond between a Cys residue in the triple-Cys peptide [beta-LG(102-124)] and kappa-CN Cys(88) and others between kappa-CN Cys(88) or kappa-CN Cys(11) and beta-LG Cys(160).	Disulfides	70-79	beta-lactoglobulin	Bos taurus	134-141
15561148-7	2004	We show also that the redox-active C79 can form a disulfide-link to the matrix protein vitronectin, suggesting that vitronectin can stabilize active PAI-2 in extracellular compartments.	Disulfides	50-59	vitronectin	Homo sapiens	87-98
9687533-0	1998	T cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-linked dimer associated with the TCR-CD3-zeta complex, recruits intracellular signaling proteins to the plasma membrane.	Disulfides	59-68	T cell receptor associated transmembrane adaptor 1	Homo sapiens	44-48
9687533-4	1998	TRIM is a disulfide-linked homodimer which is comprised of a short extracellular domain of 8 amino acids, a 19-amino acid transmembrane region, and a 159-amino acid cytoplasmic tail.	Disulfides	10-19	T cell receptor associated transmembrane adaptor 1	Homo sapiens	0-4
15561148-7	2004	We show also that the redox-active C79 can form a disulfide-link to the matrix protein vitronectin, suggesting that vitronectin can stabilize active PAI-2 in extracellular compartments.	Disulfides	50-59	vitronectin	Homo sapiens	116-127
9684891-7	1998	Both synthetic circulin B and CPT are identical to the natural products and, thus, the total synthesis confirms the disulfide connectivity of circulin B and CPT contain a cystine-knot motif of 1-4, 2-5, and 3-6.	Disulfides	116-125	choline phosphotransferase 1	Homo sapiens	142-160
8844830-4	1996	Biochemical data and the modeled theoretical structure of maspin reveal the absence of disulfide bonds in the molecule and the presence of an unstable RSL that adopts a distorted helical structure.	Disulfides	87-96	serpin family B member 5	Homo sapiens	58-64
9600961-7	1998	The two additional cysteines of HCC-2 form a third disulfide bond, which anchors the COOH-terminal domain to the core of the molecule.	Disulfides	51-60	C-C motif chemokine ligand 15	Homo sapiens	32-37
9572862-4	1998	In contrast to the disulfide linkage at the center of the dimer interface in Cro V55C, polypeptide linkers that join the two subunits allow single-chain Cro repressors to bind operator DNA with picomolar affinities.	Disulfides	19-28	cro	Escherichia virus Lambda	77-80
9650071-0	1998	The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25.	Disulfides	31-40	heat shock protein 1	Mus musculus	122-127
9650071-2	1998	Interestingly, Hsp25 can exist within the cell as covalently bound dimer which is linked by an intermolecular disulfide bond between two monomers.	Disulfides	110-119	heat shock protein 1	Mus musculus	15-20
9650071-10	1998	Hence, the overall secondary structure, the degree of oligomerization and the chaperone activity of Hsp25 seem independent of the formation of the intermolecular disulfide bond and only the stability of the hydrophobic N-terminal part of the molecule is influenced by formation of this bound.	Disulfides	162-171	heat shock protein 1	Mus musculus	100-105
9506953-4	1998	Here we have analyzed the receptor binding and activating properties of several cysteine mutants of VEGF-C including those (Cys156 and Cys165), which in other platelet-derived growth factor/VEGF family members mediate interchain disulfide bonding.	Disulfides	229-238	vascular endothelial growth factor A	Bos taurus	100-104
9461574-12	1998	Intrasubunit disulfide-bridged S100B monomer and disulfide-bonded S100B dimer are phosphorylated by the catalytic CKII-alpha subunit on Ser-62 with a Km of 0.5 microM and a Vmax of 10 pmol/min/100 pmol of S100B.	Disulfides	13-22	casein kinase 2 alpha 2	Homo sapiens	114-124
9466927-1	1998	Native bovine pancreatic trypsin inhibitor (BPTI) contains three disulfide bonds: Cys5-Cys55, Cys14-Cys38 and Cys30-Cys51.	Disulfides	65-74	spleen trypsin inhibitor I	Bos taurus	44-48
9466927-4	1998	All 15 single-disulfide variants of BPTI (three native and 12 non-native combinations) have been expressed in Escherichia coli.	Disulfides	14-23	spleen trypsin inhibitor I	Bos taurus	36-40
9466927-8	1998	Binding constants of these four single disulfide variants were at least two orders of magnitude lower than for native BPTI.	Disulfides	39-48	spleen trypsin inhibitor I	Bos taurus	118-122
9419340-3	1998	Herein we demonstrate that nitric oxide and other thiol oxidants can inhibit the autokinase activity of rat JAK2 in vitro, presumably through oxidation of crucial dithiols to disulfides within JAK2.	Disulfides	175-185	Janus kinase 2	Rattus norvegicus	108-112
9419340-3	1998	Herein we demonstrate that nitric oxide and other thiol oxidants can inhibit the autokinase activity of rat JAK2 in vitro, presumably through oxidation of crucial dithiols to disulfides within JAK2.	Disulfides	175-185	Janus kinase 2	Rattus norvegicus	193-197
21390786-1	1998	The CD44 molecule is a transmembrane glycoprotein, it is an acidic, sul fated protein that contains multiple phosphoserine residues and several intrachain disulfide bonds.	Disulfides	155-164	CD44 molecule (Indian blood group)	Homo sapiens	4-8
9388228-5	1997	Trx2 together with thioredoxin reductase and NADPH is an efficient electron donor for the essential enzyme ribonucleotide reductase and is also able to reduce the interchain disulfide bridges of insulin.	Disulfides	174-183	2,4-dienoyl-CoA reductase 1	Homo sapiens	45-50
9374479-6	1997	Treatment of hGHE2t protein by beta-mercaptoethanol, but not by heat and SDS, significantly reduced its reactivity to the antibodies of patient sera, suggesting that intermolecular and/or intramolecular disulfide bonds are important for its ability to recognize its specific antibody and that the E2 protein contains discontinuous antigenic epitope(s).	Disulfides	203-212	cystatin 12, pseudogene	Homo sapiens	16-18
9398598-3	1997	Here, we report that a transfected Chinese hamster ovary (CHO) cell line expressing a murine CD4 fragment containing the first two N-terminal domains secretes both monomeric molecules and disulfide-linked multimers.	Disulfides	188-197	CD4 antigen	Mus musculus	93-96
9514118-4	1997	SF9 insect cells infected with baculovirus carrying both I-E(d)alpha and HA110-120-I-E(d)beta-Fcgamma2a genes, secreted a disulfide-stabilized dimer of the HA110-120-I-E(d)alphabeta-Fcgamma2a molecule, designated as DEF.	Disulfides	122-131	G protein-coupled receptor 149	Mus musculus	57-68
9346940-2	1997	Surface biotinylation followed by wheat germ agglutinin column chromatography and anti-CD44-mediated immunoprecipitation indicate that both CD44s and p185(HER2) are expressed on the cell surface and most importantly, that these two molecules are physically linked to each other via interchain disulfide bonds.	Disulfides	293-302	eukaryotic translation initiation factor 3 subunit A	Homo sapiens	150-154
9317167-8	1997	It is concluded that disulfide bond formation plays a critical role in the maintenance of antigenic structure and that the autoantibodies to IA-2/IA-2 beta in IDDM sera recognize conformational epitopes.	Disulfides	21-30	protein tyrosine phosphatase receptor type N	Homo sapiens	141-145
9300690-9	1997	Activation-induced clustering followed by disulfide bond-mediated dimerization of CD44 represents an additional signal transduction mechanism for regulating receptor-ligand interactions.	Disulfides	42-51	CD44 molecule (Indian blood group)	Homo sapiens	82-86
9263012-0	1997	Interplay of J chain and disulfide bonding in assembly of polymeric IgM.	Disulfides	25-34	immunoglobulin heavy constant mu	Mus musculus	68-71
9263012-8	1997	These results imply that disulfide bonding can occur differently from the pattern depicted in conventional models of IgM structure.	Disulfides	25-34	immunoglobulin heavy constant mu	Mus musculus	117-120
9218587-10	1997	It has one characteristic that is unique to IL-15: four conserved cysteines allowing for two intrachain disulfide bonds.	Disulfides	104-113	interleukin 15	Homo sapiens	44-49
9223434-1	1997	We have generated a C-terminally-truncated form of recombinant tissue inhibitor of metalloproteinases-2 (designated rTIMP-2 delta) in which the region of the inhibitor extending from residue 128 to 194 and including 3 of the 6 disulfide bonds is deleted.	Disulfides	227-236	TIMP metallopeptidase inhibitor 2	Homo sapiens	63-103
9116284-0	1997	Missense mutations of the glycoprotein (GP) Ib beta gene impairing the GPIb alpha/beta disulfide linkage in a family with giant platelet disorder.	Disulfides	87-96	glycoprotein Ib platelet subunit alpha	Homo sapiens	26-51
9085173-2	1997	Complement C3 was detected as a molecule composed of a 115-kDa alpha-chain linked to a 70-kDa beta-chain by disulfide bonds, and C3 levels ranged from 45 to 650 micrograms/ml (n = 15).	Disulfides	108-117	complement C3	Homo sapiens	0-13
9079718-3	1997	An estimated 60% of ATAC (Val22-Gly114) is secreted as an unmodified protein with a molecular mass of 10,271.72 Da (apparent molecular mass of 12 kDa in SDS-polyacrylamide gel electrophoresis) and in which Cys32 and Cys69 are linked by a disulfide bridge.	Disulfides	238-247	X-C motif chemokine ligand 1	Homo sapiens	20-24
9132026-11	1997	Furthermore, the results provide a theoretical explanation for the observed 1000-fold diminution in the rate of 5-55 disulfide bond formation, relative to that of 14-38 bond formation, from the one-disulfide (30-51) intermediate in the wild-type BPTI refolding reaction.	Disulfides	117-126	spleen trypsin inhibitor I	Bos taurus	246-250
9132026-11	1997	Furthermore, the results provide a theoretical explanation for the observed 1000-fold diminution in the rate of 5-55 disulfide bond formation, relative to that of 14-38 bond formation, from the one-disulfide (30-51) intermediate in the wild-type BPTI refolding reaction.	Disulfides	198-207	spleen trypsin inhibitor I	Bos taurus	246-250
9033398-7	1997	When the subunits of MASH-GGC were linked through a disulfide bond, the folded conformation was stable over a wide concentration range (2.5 nM to 2 microM) even in the absence of DNA.	Disulfides	52-61	gamma-glutamylcyclotransferase	Homo sapiens	26-29
8994597-2	1997	Introduction of cysteines into the external mouth of the drk1 K channel pore resulted in the formation of disulfide bonds that were incompatible with channel function.	Disulfides	106-115	potassium voltage-gated channel subfamily B member 1	Homo sapiens	57-61
9524771-2	1997	The presence of conserved triple disulfide loops (kringles) places pro-MSP in a family of coagulation system serine protease zymogens that are activated by proteolytic cleavage.	Disulfides	33-42	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	71-74
15535978-3	2004	The amino acid sequence of CRP1 was deduced from its N-terminal amino acid sequence, amino acid composition and the sequence of a partial cDNA, indicating that CRP1 is a 57-amino-acid polypeptide containing 12 cysteine residues with a calculated molecular mass of 5841 Da (5829 Da when oxidized to form six disulfide bridges).	Disulfides	307-316	cysteine-rich protein 1 (intestinal)	Mus musculus	27-31
15535978-3	2004	The amino acid sequence of CRP1 was deduced from its N-terminal amino acid sequence, amino acid composition and the sequence of a partial cDNA, indicating that CRP1 is a 57-amino-acid polypeptide containing 12 cysteine residues with a calculated molecular mass of 5841 Da (5829 Da when oxidized to form six disulfide bridges).	Disulfides	307-316	cysteine-rich protein 1 (intestinal)	Mus musculus	160-164
15297466-6	2004	Although native Crp4 and the alpha-defensin moiety of proCrp4 resisted proteolysis completely, all disulfide variants were degraded extensively by MMP-7.	Disulfides	99-108	matrix metallopeptidase 7	Mus musculus	147-152
15173163-1	2004	The primary sequence of the N-terminal somatomedin B (SMB) domain of native vitronectin contains 44 amino acids, including a framework of four disulfide bonds formed by 8 closely spaced cysteines in sequence patterns similar to those found in the cystine knot family of proteins.	Disulfides	143-152	vitronectin	Homo sapiens	54-57
15173163-1	2004	The primary sequence of the N-terminal somatomedin B (SMB) domain of native vitronectin contains 44 amino acids, including a framework of four disulfide bonds formed by 8 closely spaced cysteines in sequence patterns similar to those found in the cystine knot family of proteins.	Disulfides	143-152	vitronectin	Homo sapiens	76-87
15173163-3	2004	Through a combination of techniques, including stepwise reduction and alkylation at acidic pH, peptide mapping with matrix-assisted laser desorption ionization mass spectrometry and NMR, the disulfide bonds contained in the SMB domain have been determined to be Cys(5):Cys(9), Cys(19):Cys(31), Cys(21):Cys(32), and Cys(25):Cys(39).	Disulfides	191-200	vitronectin	Homo sapiens	224-227
15173163-4	2004	This pattern of disulfides differs from two other connectivities that have been reported previously for recombinant forms of the SMB domain expressed in Escherichia coli.	Disulfides	16-26	vitronectin	Homo sapiens	129-132
15173163-5	2004	This arrangement of disulfide bonds in the SMB domain from native vitronectin forms a rigid core around the Cys(19): Cys(31) and Cys(21):Cys(32) disulfides.	Disulfides	20-29	vitronectin	Homo sapiens	43-46
15173163-5	2004	This arrangement of disulfide bonds in the SMB domain from native vitronectin forms a rigid core around the Cys(19): Cys(31) and Cys(21):Cys(32) disulfides.	Disulfides	20-29	vitronectin	Homo sapiens	66-77
15173163-5	2004	This arrangement of disulfide bonds in the SMB domain from native vitronectin forms a rigid core around the Cys(19): Cys(31) and Cys(21):Cys(32) disulfides.	Disulfides	145-155	vitronectin	Homo sapiens	43-46
15173163-5	2004	This arrangement of disulfide bonds in the SMB domain from native vitronectin forms a rigid core around the Cys(19): Cys(31) and Cys(21):Cys(32) disulfides.	Disulfides	145-155	vitronectin	Homo sapiens	66-77
15184375-2	2004	We report that peroxynitrite- and hydrogen peroxide-induced disulfides in the neuron-specific microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the ubiquitous thioredoxin reductase system composed of thioredoxin reductase, human or Escherichia coli thioredoxin, and NADPH.	Disulfides	60-70	microtubule associated protein 2	Homo sapiens	134-166
15184375-4	2004	Cysteine oxidation of tau and microtubule-associated protein-2 to disulfides altered the ability of the proteins to promote the assembly of microtubules from purified porcine tubulin.	Disulfides	66-76	microtubule associated protein 2	Homo sapiens	30-62
15284220-6	2004	Recombinant Ang3 and Ang4 formed disulfide-linked dimers.	Disulfides	33-42	angiogenin, ribonuclease A family, member 4	Mus musculus	21-25
15136577-0	2004	Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum.	Disulfides	73-82	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	39-48
15138265-7	2004	Taken together, our results lead us to conclude that FANCA and FANCG uniquely respond to oxidative damage by forming complex(es) via intermolecular disulfide linkage(s), which may be crucial in forming such complexes and in determining their function.	Disulfides	148-157	FA complementation group A	Homo sapiens	53-58
15197269-4	2004	We also show that constitutively active mutants of Toll form multimers that contain intermolecular disulfide linkages.	Disulfides	99-108	Toll	Drosophila melanogaster	51-55
15197269-6	2004	Furthermore, systematic mutational analysis revealed that a conserved cysteine-containing motif, different from the cysteines used for the intermolecular disulfide linkages, serves as a self-inhibitory module of Toll.	Disulfides	154-163	Toll	Drosophila melanogaster	212-216
15157085-0	2004	Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin.	Disulfides	0-9	vitronectin	Homo sapiens	54-67
15157085-0	2004	Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin.	Disulfides	0-9	vitronectin	Homo sapiens	84-95
15157085-2	2004	We previously showed that the eight cysteine residues of recombinant SMB (rSMB) are organized into four disulfide bonds in a linear uncrossed pattern (Cys(5)-Cys(9), Cys(19)-Cys(21), Cys(25)-Cys(31), and Cys(32)-Cys(39)).	Disulfides	104-113	vitronectin	Homo sapiens	69-72
15067095-0	2004	HLA-B27 in transgenic rats forms disulfide-linked heavy chain oligomers and multimers that bind to the chaperone BiP.	Disulfides	33-42	heat shock protein family A (Hsp70) member 5	Rattus norvegicus	113-116
15039220-1	2004	IL-12 consists of two disulfide-linked subunits, p40 and p35, that form functionally active heterodimers for the induction of Th1 cells.	Disulfides	22-31	interleukin 12b	Mus musculus	49-52
14871470-0	2004	TMX, a human transmembrane oxidoreductase of the thioredoxin family: the possible role in disulfide-linked protein folding in the endoplasmic reticulum.	Disulfides	90-99	thioredoxin related transmembrane protein 1	Homo sapiens	0-3
15134831-5	2004	This region comprises a unique disulfide loop in tropoelastin that is not essential for the interaction.	Disulfides	31-40	elastin	Homo sapiens	49-61
14963174-0	2004	Contribution of disulfide bridging to epitope expression of the dengue type 2 virus envelope glycoprotein.	Disulfides	16-25	endogenous retrovirus group K member 20	Homo sapiens	84-105
14978246-10	2004	Finally, we have exploited MRP4 (ABCC4) to demonstrate that disulfiram can inhibit ATP binding by forming disulfide bonds between cysteines located in the vicinity of, although not in, the active site.	Disulfides	106-115	ATP binding cassette subfamily C member 4	Homo sapiens	27-31
14978246-10	2004	Finally, we have exploited MRP4 (ABCC4) to demonstrate that disulfiram can inhibit ATP binding by forming disulfide bonds between cysteines located in the vicinity of, although not in, the active site.	Disulfides	106-115	ATP binding cassette subfamily C member 4	Homo sapiens	33-38
14729456-6	2004	We also investigated the oligomeric structures and protein levels of Mid1 and found that Mid1 forms a 200-kDa oligomer by disulfide bonding.	Disulfides	122-131	Mid1p	Saccharomyces cerevisiae S288C	89-93
14750857-3	2004	The fusion structure (GOx-linker-cysteine) enables the enzyme to immobilize on gold surfaces with a Cys-S-Au bond or to immobilize on a silanized glass surface via disulfide chemistry.	Disulfides	164-173	hydroxyacid oxidase 1	Homo sapiens	22-25
14687577-7	2004	Disulfide bonds can be formed in double-cysteine mutants with substitutions at positions P11 or P13 of the RCL and neighboring residues in beta-sheet A.	Disulfides	0-9	2'-deoxynucleoside 5'-phosphate N-hydrolase 1	Homo sapiens	107-110
14709140-1	2004	C-type natriuretic peptide (CNP) belongs to the natriuretic peptide family that consists of three structurally related peptides with a 17-amino acid ring linked by a disulfide bond.	Disulfides	166-175	natriuretic peptide C	Homo sapiens	0-26
14709140-1	2004	C-type natriuretic peptide (CNP) belongs to the natriuretic peptide family that consists of three structurally related peptides with a 17-amino acid ring linked by a disulfide bond.	Disulfides	166-175	natriuretic peptide C	Homo sapiens	28-31
14532268-7	2003	In addition, 15d-PGJ2 can promote the oligomerization of a fraction of c-Jun through the formation of intermolecular disulfide bonds or 15d-PGJ2-bonded dimers.	Disulfides	117-126	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	71-76
14522956-0	2003	Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity.	Disulfides	8-17	adiponectin, C1Q and collagen domain containing	Rattus norvegicus	27-33
14522956-0	2003	Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity.	Disulfides	8-17	adiponectin, C1Q and collagen domain containing	Rattus norvegicus	34-45
14522956-6	2003	Although not necessary for trimer formation or stability, two of the three monomers in an Acrp30 trimer are covalently linked by a disulfide bond between cysteine residues at position 22.	Disulfides	131-140	adiponectin, C1Q and collagen domain containing	Rattus norvegicus	90-96
14522956-7	2003	In contrast, assembly of hexameric and higher molecular weight (HMW) forms of Acrp30 depends upon formation of Cys22-mediated disulfide bonds because their reduction with dithiothreitol or substitution of Cys22 with alanine led exclusively to trimers.	Disulfides	126-135	adiponectin, C1Q and collagen domain containing	Rattus norvegicus	78-84
14674681-5	2003	NO-induced loss of the catalytic activity of PKC-zeta was restored by incubation with the disulfide reducing agent dithiothreitol (DTT) as well as by purified thioredoxin or thioredoxin reductase.	Disulfides	90-99	protein kinase C zeta	Homo sapiens	45-53
15206165-2	2003	Human AM consists of 52 amino acids with a 6-member ring structure linked by a disulfide bond and amidated COOH terminal, which belongs to calcitonin gene-related peptide (CGRP) and amylin.	Disulfides	79-88	adrenomedullin	Homo sapiens	6-8
14965763-2	2003	Several CART peptides that contain multiple disulfide bonds were produced by overexpression in Escherichia coli bacteria as fusion products with a C-terminal histidine tag.	Disulfides	44-53	CART prepropeptide	Rattus norvegicus	8-12
14607928-5	2003	MD-2 binding to TLR4 was dependent on Cys(95) and Cys(105), which might form an intramolecular disulfide bond.	Disulfides	95-104	lymphocyte antigen 96	Homo sapiens	0-4
14694904-1	2003	Mouse salivary androgen-binding protein (ABP) is a pair of dimers, composed of an alpha subunit disulfide bridged to either a beta or a gamma subunit.	Disulfides	96-105	secretoglobin, family 1B, member 27	Mus musculus	15-39
14694904-1	2003	Mouse salivary androgen-binding protein (ABP) is a pair of dimers, composed of an alpha subunit disulfide bridged to either a beta or a gamma subunit.	Disulfides	96-105	secretoglobin, family 1B, member 27	Mus musculus	41-44
12957712-1	2003	Several cyclic disulfide alpha-melanocyte stimulating hormone (alpha-MSH) analogues containing the aromatic fluorescent amino acid beta-(2-naphthyl)-D-alanine (D-Nal) have high affinity and selectivity for the melanocortin (MC)-4 receptor.	Disulfides	15-24	melanocortin 4 receptor	Homo sapiens	210-238
14614987-0	2003	Disulfide-linked heterodimeric clusterin is a component of the chicken eggshell matrix and egg white.	Disulfides	0-9	clusterin	Gallus gallus	31-40
14614987-1	2003	Clusterin is a widely expressed secretory glycoprotein which is found in mammals as a disulfide-bonded alpha/beta heterodimer generated by cleavage of the single-chain precursor.	Disulfides	86-95	clusterin	Gallus gallus	0-9
14614987-4	2003	This extracellular clusterin originates in the uterine fluid, where it is a disulfide-bonded heterodimer derived from the precursor polypeptide by proteolytic cleavage at the same site as in mammals.	Disulfides	76-85	clusterin	Gallus gallus	19-28
12873136-7	2003	Under mildly acidic conditions (pH 4.8), the amyloidogenesis rates of the mixed disulfide TTR variants are much faster than the WT rate.	Disulfides	80-89	transthyretin	Homo sapiens	90-93
12873136-9	2003	Conversion of the Cys10 SH group to a mixed disulfide with the amino acid Cys, the CysGly peptide, or glutathione increases amyloidogenicity and the amyloidogenesis rate above pH 4.6, conditions under which TTR probably forms fibrils in humans.	Disulfides	44-53	transthyretin	Homo sapiens	207-210
12860132-6	2003	RIalpha D/D is a compact docking module, with unusual interchain disulfide bonds that help maintain the AKAP interaction surface.	Disulfides	65-74	A-kinase anchoring protein 1	Homo sapiens	104-108
12719415-5	2003	The results indicated that betaig-h3 is associated with collagen VI in tissues by reducible covalent bonding, presumably disulfide bridges.	Disulfides	121-130	transforming growth factor beta induced	Homo sapiens	27-36
12813025-5	2003	Among the glycoprotein hormone receptors, only the TSHR undergoes intramolecular cleavage into disulfide-linked subunits with consequent shedding of some of the extracellular, autoantibody-binding A subunits.	Disulfides	95-104	thyroid stimulating hormone receptor	Homo sapiens	51-55
12624089-5	2003	While the oxidized refolding process of HPI was quenched, four obvious intermediates (namely P1, P2, P3, and P4, respectively) with three disulfide bridges were isolated and characterized.	Disulfides	138-147	crystallin gamma F, pseudogene	Homo sapiens	93-111
12547830-2	2003	Recently, we noticed the ends of loop E-2 are linked by an ion pair between residues Arg-177 and Asp-190, near the highly conserved disulfide bond.	Disulfides	132-141	cystatin 12, pseudogene	Homo sapiens	38-41
12752442-1	2003	The formation of disulfide bonds in the endoplasmic reticulum requires protein disulfide isomerase (PDI) and endoplasmic reticulum oxidoreductin 1 (ERO1) that reoxidizes PDI.	Disulfides	17-26	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	71-98
12752442-1	2003	The formation of disulfide bonds in the endoplasmic reticulum requires protein disulfide isomerase (PDI) and endoplasmic reticulum oxidoreductin 1 (ERO1) that reoxidizes PDI.	Disulfides	17-26	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	100-103
12752442-1	2003	The formation of disulfide bonds in the endoplasmic reticulum requires protein disulfide isomerase (PDI) and endoplasmic reticulum oxidoreductin 1 (ERO1) that reoxidizes PDI.	Disulfides	17-26	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	170-173
12584183-4	2003	In this report, we show that PKC-regulatory S-thiolation modifications produced by physiological disulfides elicit opposing effects on PKC delta and PKC epsilon activity.	Disulfides	97-107	protein kinase C, delta	Mus musculus	135-144
12535610-3	2003	This paper describes the results of our studies on the role of the disulfide bonds of hCG-beta in heterodimer formation with the alpha-subunit.	Disulfides	67-76	chorionic gonadotropin subunit beta 3	Homo sapiens	86-94
12535610-4	2003	Six disulfide peptides incorporating each of the six disulfide bonds of hCG-beta were screened, along with their linear counterparts, for their ability to competitively inhibit the recombination of alpha- and beta-subunits.	Disulfides	4-13	chorionic gonadotropin subunit beta 3	Homo sapiens	72-80
12535610-4	2003	Six disulfide peptides incorporating each of the six disulfide bonds of hCG-beta were screened, along with their linear counterparts, for their ability to competitively inhibit the recombination of alpha- and beta-subunits.	Disulfides	53-62	chorionic gonadotropin subunit beta 3	Homo sapiens	72-80
9524771-3	1997	Although pro-MSP has lost enzymic activity, it has retained the activation mechanism, in that proteolytic cleavage at a single site yields biologically active disulfide-linked alpha beta-chain heterodimeric MSP.	Disulfides	159-168	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	13-16
9524771-3	1997	Although pro-MSP has lost enzymic activity, it has retained the activation mechanism, in that proteolytic cleavage at a single site yields biologically active disulfide-linked alpha beta-chain heterodimeric MSP.	Disulfides	159-168	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	207-210
9281220-5	1997	The 230 kD protein turned out to be an only partly reduced beta 1 integrin disulfide bonded dimer.	Disulfides	75-84	integrin subunit beta 1	Homo sapiens	59-74
12446677-7	2003	We speculate that for the folding of some proteins in the ER, chaperoning by BiP and formation of proper disulfide bonds may synchronously occur in a JPDI-dependent manner.	Disulfides	105-114	DnaJ heat shock protein family (Hsp40) member C10	Mus musculus	150-154
8662901-8	1996	Swapping of the disulfide bridges in IGF-I and the C-region mutants decreased the affinity dramatically for IGFBP-3, primarily by decreasing the association rate.	Disulfides	16-25	insulin like growth factor binding protein 3	Homo sapiens	108-115
12368274-2	2002	The alpha(L) I domain can be mutationally locked with disulfide bonds into two distinct conformations, open and closed, which have high and low affinity for the ligand intercellular adhesion molecule 1 (ICAM-1), respectively.	Disulfides	54-63	intercellular adhesion molecule 1	Homo sapiens	203-209
8955416-1	1996	Disulfide-cross-linked UmuD2 derivatives were cleaved poorly upon incubation with activated RecA.	Disulfides	0-9	RAD51 recombinase	Homo sapiens	92-96
8639560-2	1996	Key to this process appears to be the interaction of the tyrosine kinase SH2 domains with the tyrosine-phosphorylated cytoplasmic domain of Ig-alpha, a disulfide-bonded heterodimeric (with Ig-beta or Ig-gamma) transmembrane protein that noncovalently associates with the antigen receptor immunoglobin chains.	Disulfides	152-161	CD79b molecule	Homo sapiens	189-196
8955416-2	1996	Reducing the disulfide bonds prior to incubating the derivatives with RecA dramatically increased their extent of cleavage.	Disulfides	13-22	RAD51 recombinase	Homo sapiens	70-74
12454284-0	2002	Disulfide bond-mediated dimerization of HLA-G on the cell surface.	Disulfides	0-9	major histocompatibility complex, class I, G	Homo sapiens	40-45
12454284-2	2002	Here, we demonstrate that HLA-G forms disulfide-linked dimers that are present on the cell surface.	Disulfides	38-47	major histocompatibility complex, class I, G	Homo sapiens	26-31
8668334-5	1996	The DeltaV-TCRbeta chain appears at the cell surface as a disulfide-linked DeltaV-TCRbeta/pTalpha dimer in association with CD3gamma and -episilon, but not with CD3delta.	Disulfides	58-67	T cell receptor beta chain	Mus musculus	11-18
12419261-6	2002	Cofilin inhibited strongly the rate of interprotomer disulfide cross-linking of Cys41 to Cys374 on yeast Q41C mutant F-actin.	Disulfides	53-62	cofilin	Saccharomyces cerevisiae S288C	0-7
8668334-5	1996	The DeltaV-TCRbeta chain appears at the cell surface as a disulfide-linked DeltaV-TCRbeta/pTalpha dimer in association with CD3gamma and -episilon, but not with CD3delta.	Disulfides	58-67	T cell receptor beta chain	Mus musculus	82-89
12383115-8	2002	The results indicated that among the four disulfide bonds for long-chain scorpion toxins, loss of either bridge C22-C46 or C26-C48 is fatal for the general folding of the molecule.	Disulfides	42-51	Sp7 transcription factor 7	Mus musculus	112-115
9055015-6	1996	In the light of recent evidence on the role of nef gene defects/attenuations in long-term survival of HIV-1 infected patients, it may be that the nef gene defect created by gene duplication, which eliminated the cysteine-206 crucial in disulfide bond formation, may play a role in chronic HIV-1 infection in this patient.	Disulfides	236-245	Nef	Human immunodeficiency virus 1	47-50
8732764-1	1996	alpha-Lactalbumin is a small, globular protein that is stabilized by four disulfide bonds and contains two structural domains.	Disulfides	74-83	lactalbumin alpha	Bos taurus	0-17
8896764-0	1996	Disulfide bond formation between the n-terminal region of p56LCK and the cytoplasmic domain of CD8 studied by electrospray ionization and matrix-assisted desorption/ionization time-of-flight mass spectrometry.	Disulfides	0-9	CD8a molecule	Homo sapiens	95-98
8896764-6	1996	The only disulfide-mediated complex formed was hetero-dimer (CD8 alpha C-p56lckN) and none of homo-dimers (CD8 alpha C-CD8 alpha C or p56lckN-p56lckN) were observed from ESI and MALDI-TOF mass spectrometry.	Disulfides	9-18	CD8a molecule	Homo sapiens	61-70
8896764-6	1996	The only disulfide-mediated complex formed was hetero-dimer (CD8 alpha C-p56lckN) and none of homo-dimers (CD8 alpha C-CD8 alpha C or p56lckN-p56lckN) were observed from ESI and MALDI-TOF mass spectrometry.	Disulfides	9-18	CD8a molecule	Homo sapiens	61-64
12379124-0	2002	Activation of glucuronidation through reduction of a disulfide bond in rat UDP-glucuronosyltransferase 1A6.	Disulfides	53-62	UDP glucuronosyltransferase family 1 member A6	Rattus norvegicus	75-106
12379124-6	2002	Immunoblot analysis of rat hepatic microsomes on nonreducing SDS-PAGE gels revealed that most of the UGT1A6 migrated as a monomer, suggesting that DTT could affect an intramolecular disulfide bond in the UGT1A6 that may be responsible for the activation.	Disulfides	182-191	UDP glucuronosyltransferase family 1 member A6	Rattus norvegicus	101-107
12379124-7	2002	To identify which of the ten cysteines in UGT1A6 are involved in the disulfide bond, rat UGT1A6 wild type and a set of mutants, each with a cysteine to serine substitution, were constructed and expressed in COS cells.	Disulfides	69-78	UDP glucuronosyltransferase family 1 member A6	Rattus norvegicus	42-48
12379124-10	2002	These results demonstrate that both Cys 121 and Cys 125 are responsible for the activation of the activity through the disulfide bond in rat UGT1A6.	Disulfides	119-128	UDP glucuronosyltransferase family 1 member A6	Rattus norvegicus	141-147
12379133-8	2002	The formation of a disulfide cross-link between TnI121 and TnC48 or TnC82 abolished the Ca2+-absent inhibitory activity of Tn, indicating that the movement of the Met121 region of TnI out of TnC"s N-domain cleft is essential for the occurrence of further events in the inhibitory process of skeletal muscle contraction.	Disulfides	19-28	tenascin C	Homo sapiens	59-62
8794751-0	1996	The disulfide folding pathway of tick anticoagulant peptide (TAP), a Kunitz-type inhibitor structurally homologous to BPTI.	Disulfides	4-13	spleen trypsin inhibitor I	Bos taurus	118-122
8732764-5	1996	The three-disulfide form, having a reduced Cys 6-Cys 120 disulfide bond with carboxymethylated cysteines, is similar to intact alpha-lactalbumin in secondary and tertiary structure as judged by its ellipticity in the near and far UV.	Disulfides	10-19	lactalbumin alpha	Bos taurus	127-144
8794751-3	1996	The picture of TAP folding differs significantly from the well-documented case of bovine pancreatic trypsin inhibitor (BPTI), despite the fact that both proteins share close structural homology in term of 3-D conformation and disulfide pattern.	Disulfides	226-235	spleen trypsin inhibitor I	Bos taurus	82-117
12206676-1	2002	Illumination of goat alpha-lactalbumin (GLA) with 280 or 295 nm light results in tryptophan-mediated photolysis of disulfide bonds within the protein.	Disulfides	115-124	alpha-galactosidase A	Capra hircus	40-43
8732764-6	1996	the two-disulfide form of alpha-lactalbumin, having reduced Cys 6-Cys 120 and Cys 28-Cys 111 disulfide bonds with carboxymethylated cysteines, retains about half the secondary and tertiary structure of the intact alpha-lactalbumin.	Disulfides	8-17	lactalbumin alpha	Bos taurus	26-43
12176051-1	2002	Members of the Quiescin-sulfhydryl oxidase (QSOX) family utilize a thioredoxin domain and a small FAD-binding domain homologous to the yeast ERV1p protein to oxidize sulfhydryl groups to disulfides with the reduction of oxygen to hydrogen peroxide.	Disulfides	187-197	quiescin sulfhydryl oxidase 1	Homo sapiens	44-48
8732764-6	1996	the two-disulfide form of alpha-lactalbumin, having reduced Cys 6-Cys 120 and Cys 28-Cys 111 disulfide bonds with carboxymethylated cysteines, retains about half the secondary and tertiary structure of the intact alpha-lactalbumin.	Disulfides	8-17	lactalbumin alpha	Bos taurus	213-230
12176051-4	2002	Mixtures of avian QSOX and protein disulfide isomerase catalyze the rapid insertion of the correct disulfide pairings in reduced RNase.	Disulfides	35-44	quiescin sulfhydryl oxidase 1	Homo sapiens	18-22
12176051-6	2002	Consistent with this role in the formation of disulfide bonds, QSOX is typically found in the cell in the endoplasmic reticulum and Golgi and outside the cell.	Disulfides	46-55	quiescin sulfhydryl oxidase 1	Homo sapiens	63-67
8732764-8	1996	We conclude that, in the two disulfide form, alpha-lactalbumin retains its calcium-binding beta-domain, whereas the alpha-domain is unfolded.	Disulfides	29-38	lactalbumin alpha	Bos taurus	45-62
8626570-0	1996	NK-lysin, a disulfide-containing effector peptide of T-lymphocytes, is reduced and inactivated by human thioredoxin reductase.	Disulfides	12-21	thioredoxin	Homo sapiens	104-115
8886269-0	1996	Beta 1 integrin subunit dimerization via disulfide bonds.	Disulfides	41-50	integrin subunit beta 1	Homo sapiens	0-15
8626570-7	1996	NK-lysin is the first identified macromolecular disulfide substrate for human thioredoxin reductase apart from human thioredoxin.	Disulfides	48-57	thioredoxin	Homo sapiens	78-89
8886269-4	1996	After reduction the major part of the beta 1 immunoreactive material migrated from the 205 kD to 130 kD region, indicating that beta 1 integrin subunit dimers were formed via disulfide bonds.	Disulfides	175-184	integrin subunit beta 1	Homo sapiens	128-143
12114439-0	2002	Novel anti-CD30 recombinant immunotoxins containing disulfide-stabilized Fv fragments.	Disulfides	52-61	TNF receptor superfamily member 8	Homo sapiens	11-15
8620037-3	1996	The fragment contains an intrachain disulfide bond between 1308Cys and 1423Cys corresponding to that between 1304Cys and 1419Cys in alpha 2-macroglobulin.	Disulfides	36-45	alpha-2-macroglobulin	Homo sapiens	132-153
12114439-14	2002	CONCLUSIONS: Four anti-CD30 disulfide stabilized Fv immunotoxins were successfully produced.	Disulfides	28-37	TNF receptor superfamily member 8	Homo sapiens	23-27
12036872-9	2002	Replacing the N-terminal disulfide loops of GPIb beta (amino acids 1-14) with the corresponding disulfide loops of GPIX (amino acids 1-22) resulted in surface expression of coexpressed wildtype GPIX.	Disulfides	25-34	glycoprotein Ib platelet subunit beta	Homo sapiens	44-53
12061140-2	2002	HGF is one of the largest disulfide-linked cytokines, consisting of a 60-kDa heavy chain and a 35-kDa light chain.	Disulfides	26-35	hepatocyte growth factor	Rattus norvegicus	0-3
8706025-2	1996	Anti-Tac disulfide-stabilized Fv fragment (dsFv) was derived from a murine monoclonal antibody that recognizes the alpha subunit of the interleukin-2 receptor (IL-2R alpha).	Disulfides	9-18	interleukin 2 receptor, alpha chain	Mus musculus	160-171
8664271-0	1996	A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterization.	Disulfides	15-24	peroxiredoxin 5	Homo sapiens	33-54
11966324-7	2002	Mostly mediated by mixed-NPSH disulfide formation, the activity of the redox-sensitive cysteine protease, cathepsin H, was inhibited by the S-nitrosothiols, with WR-1065 nitrosothiol &gt; cysteine nitrosothiol &gt; N-acetyl-L-cysteine nitrosothiol and GSH nitrosothiol.	Disulfides	30-39	cathepsin H	Homo sapiens	106-117
8664271-0	1996	A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterization.	Disulfides	15-24	thioredoxin	Homo sapiens	33-44
8664271-8	1996	In order to provide evidence for the proposed conformational change, a complex between TrR and its substrate Tr involving a mixed disulfide between TrR and Tr was prepared.	Disulfides	130-139	peroxiredoxin 5	Homo sapiens	87-90
8702502-11	1996	The data obtained indicate that the amount of detectable hCG-beta-chaperone complexes correlates with the rate or extent of folding, that the complexes of hCG-beta with ER chaperones lead to the formation of secretable beta, and that the complexes of hCG-beta with chaperones involve the formation of intermolecular disulfide bonds.	Disulfides	316-325	chorionic gonadotropin subunit beta 3	Homo sapiens	57-65
8664271-8	1996	In order to provide evidence for the proposed conformational change, a complex between TrR and its substrate Tr involving a mixed disulfide between TrR and Tr was prepared.	Disulfides	130-139	peroxiredoxin 5	Homo sapiens	148-151
8702502-11	1996	The data obtained indicate that the amount of detectable hCG-beta-chaperone complexes correlates with the rate or extent of folding, that the complexes of hCG-beta with ER chaperones lead to the formation of secretable beta, and that the complexes of hCG-beta with chaperones involve the formation of intermolecular disulfide bonds.	Disulfides	316-325	chorionic gonadotropin subunit beta 3	Homo sapiens	155-163
8664271-9	1996	The redox active disulfide of TrR is composed of Cys135 and Cys138, and the redox active disulfide of Tr is made up of Cys32 and Cys35.	Disulfides	17-26	peroxiredoxin 5	Homo sapiens	30-33
12061835-1	2002	IL-12 is a 75 kDa heterodimeric cytokine composed of two disulfide-linked subunits, p35 and p40, which plays an important role in the regulation of the immune response.	Disulfides	57-66	interleukin 12A	Homo sapiens	84-87
8702502-11	1996	The data obtained indicate that the amount of detectable hCG-beta-chaperone complexes correlates with the rate or extent of folding, that the complexes of hCG-beta with ER chaperones lead to the formation of secretable beta, and that the complexes of hCG-beta with chaperones involve the formation of intermolecular disulfide bonds.	Disulfides	316-325	chorionic gonadotropin subunit beta 3	Homo sapiens	155-163
8664271-17	1996	Reductive titrations show that approximately 1 equiv of sodium dithionite or NADPH is required to fully reduce C135S-C32S, and treatment with NH4Cl and DTT demonstrates that the mixed disulfide between Cys138 of TrR C135S and Cys35 of TrC32S that locks the structure in a conformation where FAD can be reduced by NADPH, but electrons cannot flow from FADH2 to the mixed disulfide bond.	Disulfides	184-193	peroxiredoxin 5	Homo sapiens	212-215
11795902-4	2002	Using these procedures, we identified ERP72 and ERP60, two members of the protein disulfide isomerase family, creatine kinase, glyceraldehyde-3-phosphate dehydrogenase, phospholipase C-gamma1, and thioredoxin reductase as the targets of DA-derived H2O2.	Disulfides	82-91	protein disulfide isomerase family A, member 4	Rattus norvegicus	38-43
8671648-1	1996	Thioredoxin (Trx), a ubiquitous protein intimately involved in redox and protein disulfide reductions, has been shown to be released from cells and to have cytokine-like activities.	Disulfides	81-90	thioredoxin	Homo sapiens	0-11
11747427-2	2001	The cysteine-rich C-terminal domain of this protein, corresponding to AGRP(87-132), contains five disulfide bonds and exhibits receptor binding affinity and antagonism equivalent to that of the full-length protein.	Disulfides	98-107	agouti related neuropeptide	Homo sapiens	70-74
11747427-5	2001	The relative spatial positioning of the disulfide cross-links demonstrates that the ordered region of AGRP(87-132) adopts the inhibitor cystine knot (ICK) fold previously identified for numerous invertebrate toxins.	Disulfides	40-49	agouti related neuropeptide	Homo sapiens	102-106
8872531-0	1996	Investigation of the 35-62 conserved helix and disulfide loop of bovine prothrombin using an anti-peptide antibody.	Disulfides	47-56	coagulation factor II, thrombin	Bos taurus	72-83
8671648-1	1996	Thioredoxin (Trx), a ubiquitous protein intimately involved in redox and protein disulfide reductions, has been shown to be released from cells and to have cytokine-like activities.	Disulfides	81-90	thioredoxin	Homo sapiens	13-16
8755737-7	1996	Although these disulfide loops constitute less than 5% of the total sequence of the protein, they contribute to the overall structural stabilization of tACE.	Disulfides	15-24	ADAM metallopeptidase domain 17	Homo sapiens	152-156
8601842-1	1996	Cartilage matrix protein (CMP) is a major component of different cartilages and consists of a disulfide-linked homotrimer.	Disulfides	94-103	matrilin 1	Homo sapiens	0-24
8637013-3	1996	The binding constant was estimated to be in the order of 10(5) M-1 by analyzing the kinetic data quantitatively and was found to be much weaker than the binding between GroEL and disulfide-bond reduced alpha-lactalbumin, whose binding constant is in the order of 10(7) M-1.	Disulfides	179-188	heat shock protein family D (Hsp60) member 1	Homo sapiens	169-174
11600494-6	2001	It was abolished by certain deletions and by mutations of cysteine residues preventing formation of a disulfide link between the first and second extracellular loops, suggesting that conformation of Delta32 is important for its interaction with CCR5.	Disulfides	102-111	C-C motif chemokine receptor 5	Homo sapiens	245-249
8601842-1	1996	Cartilage matrix protein (CMP) is a major component of different cartilages and consists of a disulfide-linked homotrimer.	Disulfides	94-103	matrilin 1	Homo sapiens	26-29
11535591-8	2001	This further suggested that cleavage of the holoreceptor into its two-subunit structure, comprising disulfide-linked TSHR-alpha and TSHR-beta subunits, was required for the formation of TSHR dimers and higher order complexes.	Disulfides	100-109	thyroid stimulating hormone receptor	Homo sapiens	117-121
11535591-8	2001	This further suggested that cleavage of the holoreceptor into its two-subunit structure, comprising disulfide-linked TSHR-alpha and TSHR-beta subunits, was required for the formation of TSHR dimers and higher order complexes.	Disulfides	100-109	thyroid stimulating hormone receptor	Homo sapiens	132-136
8634448-3	1996	CD27 is a transmembrane disulfide-linked 55-kD homodimer present on most peripheral blood T cells and on a subset of B cells.	Disulfides	24-33	CD27 molecule	Homo sapiens	0-4
11535591-8	2001	This further suggested that cleavage of the holoreceptor into its two-subunit structure, comprising disulfide-linked TSHR-alpha and TSHR-beta subunits, was required for the formation of TSHR dimers and higher order complexes.	Disulfides	100-109	thyroid stimulating hormone receptor	Homo sapiens	132-136
11746826-6	2001	This is a novel protein fold consisting of five alpha helices held together by two disulfide bonds for which the CD81 protein is the first solved representative.	Disulfides	83-92	CD81 molecule	Homo sapiens	113-117
8631865-1	1996	Eukaryotic protein disulfide isomerase (PDI) is a 55-kDa enzyme with cysteine oxidoreductase, chaperone, and antichaperone activities that catalyzes disulfide formation and rearrangement in the eukaryotic endoplasmic reticulum.	Disulfides	19-28	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	40-43
8631865-3	1996	We show that rat PDI (rPDI) secreted in the periplasmic space of Escherichia coli can catalyze the formation of disulfide bonds and complement several of the phenotypes of dsbA mutants.	Disulfides	112-121	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	17-20
8631865-3	1996	We show that rat PDI (rPDI) secreted in the periplasmic space of Escherichia coli can catalyze the formation of disulfide bonds and complement several of the phenotypes of dsbA mutants.	Disulfides	112-121	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	22-26
11816713-1	2001	GPIbbeta is disulfide-linked to GPIbalpha to form GPIb, a platelet receptor for von Willebrand factor (vWF).	Disulfides	12-21	glycoprotein Ib platelet subunit beta	Homo sapiens	0-8
8631927-9	1996	Thus, two independent approaches identify Cys-55 of PRK in the intermolecular disulfide pairing with Trx.	Disulfides	78-87	thioredoxin	Homo sapiens	101-104
11816713-1	2001	GPIbbeta is disulfide-linked to GPIbalpha to form GPIb, a platelet receptor for von Willebrand factor (vWF).	Disulfides	12-21	glycoprotein Ib platelet subunit alpha	Homo sapiens	32-41
9816187-1	1996	Thioredoxin (TRX) is a widely distributed Mr 13,000 protein with a redox-active dithiol/disulfide in the active site.	Disulfides	88-97	thioredoxin	Homo sapiens	0-11
11429404-3	2001	Our previous results demonstrated that in vitro LMW-PTP is oxidized by either H(2)O(2) or nitric oxide with the formation of a disulfide bond between Cys-12 and Cys-17.	Disulfides	127-136	acid phosphatase 1	Homo sapiens	48-55
9816187-1	1996	Thioredoxin (TRX) is a widely distributed Mr 13,000 protein with a redox-active dithiol/disulfide in the active site.	Disulfides	88-97	thioredoxin	Homo sapiens	13-16
9328633-4	1996	The redox reaction between Cd2+ and receptor thiols may result in binding of the metal into stable (di)thiol-cadmium complexes rather than in the formation of disulfide and liberation of the reduced metal.	Disulfides	159-168	CD2 molecule	Homo sapiens	27-30
11562191-1	2001	A 25-residue disulfide-cross-linked peptide, termed "oxidized core module" (OxCM), that includes essentially all of the secondary structural elements of bovine pancreatic trypsin inhibitor (BPTI) most refractory to hydrogen exchange, was shown previously to favor nativelike beta-sheet structure [Carulla, N., Woodward, C., and Barany, G. (2000) Synthesis and Characterization of a beta-Hairpin Peptide That Represents a "Core Module" of Bovine Pancreatic Trypsin Inhibitor (BPTI).	Disulfides	13-22	spleen trypsin inhibitor I	Bos taurus	153-188
11562191-1	2001	A 25-residue disulfide-cross-linked peptide, termed "oxidized core module" (OxCM), that includes essentially all of the secondary structural elements of bovine pancreatic trypsin inhibitor (BPTI) most refractory to hydrogen exchange, was shown previously to favor nativelike beta-sheet structure [Carulla, N., Woodward, C., and Barany, G. (2000) Synthesis and Characterization of a beta-Hairpin Peptide That Represents a "Core Module" of Bovine Pancreatic Trypsin Inhibitor (BPTI).	Disulfides	13-22	spleen trypsin inhibitor I	Bos taurus	190-194
8605189-0	1996	Identification of the disulfide-linked peptide in irreversibly sickled cell beta-actin.	Disulfides	22-31	POTE ankyrin domain family member F	Homo sapiens	76-86
8605189-9	1996	In this article, we directly demonstrate the existence of the disulfide bridge between cysteine284 and cysteine373 in ISC beta-actin.	Disulfides	62-71	POTE ankyrin domain family member F	Homo sapiens	122-132
8639895-1	1996	The platelet membrane glycoprotein (Gp) Ib complex consists of four polypeptides: the disulfide-linked GpIb alpha and GpIb beta subunits; GpIX, tightly, but noncovalently associated with GpIb alpha-beta; and the more weakly associated GpV.	Disulfides	86-95	glycoprotein Ib platelet subunit alpha	Homo sapiens	103-113
11514736-3	2001	Disulfide linkages were identified by separating tryptic-digested NS1 by reverse-phase high pressure liquid chromatography and analysing the resulting peptide peaks by protein sequencing, amino acid analysis and/or electrospray mass spectrometry.	Disulfides	0-9	influenza virus NS1A binding protein	Homo sapiens	66-69
9226457-11	1996	We have demonstrated that the carboxyl terminal cystine residue of apo-B100, cysteine-4326, is required for apo-B100"s disulfide linkage with apo(a) to form lipoprotein (a).	Disulfides	119-128	apolipoprotein B	Mus musculus	67-75
9226457-11	1996	We have demonstrated that the carboxyl terminal cystine residue of apo-B100, cysteine-4326, is required for apo-B100"s disulfide linkage with apo(a) to form lipoprotein (a).	Disulfides	119-128	apolipoprotein B	Mus musculus	108-116
11399755-6	2001	Sptrx appears to have a multimeric structure in native conditions and is able to reduce insulin disulfide bonds in the presence of NADPH and thioredoxin reductase.	Disulfides	96-105	thioredoxin domain containing 2	Homo sapiens	0-5
11399763-10	2001	Collectively, these experiments suggest that the anti-angiogenic activity of tumstatin is localized to a 25-amino acid region of tumstatin and it is independent of disulfide bond linkage.	Disulfides	164-173	collagen, type IV, alpha 3	Mus musculus	77-86
8786303-1	1996	The allelic human platelet alloantigens PIA1/PIA2 are determined by a 33 Leu-Pro substitution in the second disulfide loop of the integrin beta3 subunit of the fibrinogen receptor, alphaIIb beta3 (GPIIb-IIIa).	Disulfides	108-117	integrin beta 3	Mus musculus	130-144
8551235-2	1996	HCC-1 has a relative molecular mass of 8,673 and consists of 74 amino acids including four cysteines linked to disulfide bonds.	Disulfides	111-120	C-C motif chemokine ligand 14	Homo sapiens	0-5
8786303-3	1996	We studied the suppression of specific Ab production to a disulfide-looped peptide spanning the polymorphic region of integrin beta3, 24AWCSDEALPLGSPRCD39 (LPL).	Disulfides	58-67	integrin beta 3	Mus musculus	118-132
8786303-3	1996	We studied the suppression of specific Ab production to a disulfide-looped peptide spanning the polymorphic region of integrin beta3, 24AWCSDEALPLGSPRCD39 (LPL).	Disulfides	58-67	lipoprotein lipase	Mus musculus	143-146
11478847-6	2001	Following III(3), FN2 contains a unique 20-amino-acid C-terminal tail that is different from the C-terminus of FN1, lacking the two cysteines that are usually involved in the formation of interchain disulfide bonds.	Disulfides	199-208	fibronectin 1a	Danio rerio	18-21
8566791-6	1995	Cysteine aa involved in intra- and inter-chain disulfide-bonded secondary and tertiary structure are absolutely conserved in ferret gamma FBG.	Disulfides	47-56	fibrinogen gamma chain	Mustela putorius furo	132-141
11356854-2	2001	A significant proportion of the alpha2,6-sialyltransferase of protein Asn-linked glycosylation (ST6Gal I) forms disulfide-bonded dimers that exhibit decreased activity, but retain the ability to bind asialoglycoprotein substrates.	Disulfides	112-121	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	96-104
11356854-4	2001	Pulse-chase analysis demonstrated that the ST6Gal I disulfide-bonded dimer forms in the endoplasmic reticulum.	Disulfides	52-61	ST6 beta-galactoside alpha-2,6-sialyltransferase 1	Homo sapiens	43-51
8868284-4	1996	MESS-Bz-EDTA was coupled with a thiolated monoclonal antibody (OST7, IgG1) prepared by reducing its disulfide bonds to introduce the ester bond close and proximal to the antibody molecule.	Disulfides	100-109	LOC105243590	Mus musculus	69-73
7499372-0	1995	Thiol-disulfide exchange of ribonuclease inhibitor bound to ribonuclease A.	Disulfides	6-15	ribonuclease/angiogenin inhibitor 1	Sus scrofa	28-50
11390397-8	2001	Several of these mutations resulted in the formation of soluble disulfide-bonded ICAM-1 dimers (domain 1 dimers).	Disulfides	64-73	intercellular adhesion molecule 1	Homo sapiens	81-87
12750762-1	2001	Endothelins (ET-1, ET-2 and ET-3) are 21-amino-acid peptides with two disulfide bonds that belong to the sarafotoxin family.	Disulfides	70-79	endothelin 2	Homo sapiens	19-23
12750762-1	2001	Endothelins (ET-1, ET-2 and ET-3) are 21-amino-acid peptides with two disulfide bonds that belong to the sarafotoxin family.	Disulfides	70-79	endothelin 3	Homo sapiens	28-32
7490766-5	1995	We show that the stability and the helicity of the disulfide-linked c-Myc-Max heterostranded coiled-coil is modulated by pH, with a maximum around pH 4.5, supporting the existence of stabilizing and specific interhelical electrostatic interactions.	Disulfides	51-60	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	68-73
11278376-8	2001	These data suggest that an N-terminal disulfide-bonded loop between Cys(41) and Cys(29) or its close neighbor Cys(31) comprises, in part, the highly conformational epitope for TSAb at the critical N terminus of the TSHR.	Disulfides	38-47	thyroid stimulating hormone receptor	Homo sapiens	215-219
7592682-9	1995	Disulfide cross-linking of the Q42C subunit c and E31C subunit epsilon leads to inhibition of ATPase coupled H+ transport, as might be expected in a model where the catalytic sites of the F1 ATPase alternate during H+ transport-coupled ATP hydrolysis/synthesis.	Disulfides	0-9	ATPase	Escherichia coli	94-100
7592682-9	1995	Disulfide cross-linking of the Q42C subunit c and E31C subunit epsilon leads to inhibition of ATPase coupled H+ transport, as might be expected in a model where the catalytic sites of the F1 ATPase alternate during H+ transport-coupled ATP hydrolysis/synthesis.	Disulfides	0-9	ATPase	Escherichia coli	191-197
8524260-14	1995	Therefore, it can be inferred that some LTBP-2 is bound covalently to the microfibrils by reducible disulfide linkages.	Disulfides	100-109	latent transforming growth factor beta binding protein 2	Bos taurus	40-46
7540212-3	1995	A derivative of BPTI containing only the 5-55 disulfide bond, termed [5-55]Ala, has been shown previously to fold into a structure very similar to that of native BPTI and to be a functional trypsin inhibitor.	Disulfides	46-55	spleen trypsin inhibitor I	Bos taurus	16-20
11594463-8	2001	The bond SS2 is the most important disulfide bond for oxidative folding of lysozymes.	Disulfides	35-44	butyrophilin like 2	Homo sapiens	9-12
8521814-4	1995	This domain appears to be functionally conserved in the erythropoietin (EPO) receptor because substitution of cysteines for residues in the analogous region causes EPO-independent receptor activation via disulfide-linked homodimerization.	Disulfides	204-213	erythropoietin	Mus musculus	56-70
11309371-5	2001	Proper initial folding of AGA in the endoplasmic reticulum (ER) is dependent on intramolecular disulfide bridge formation and dimerization of two precursor polypeptides.	Disulfides	95-104	aspartylglucosaminidase	Homo sapiens	26-29
11098061-0	2001	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.	Disulfides	21-30	Neutrophil migration (granulocyte glycoprotein)	Homo sapiens	126-131
7768912-3	1995	In this report, characterization of the protein purified from mastocytomas reveals an N-glycosylated, high molecular weight, tryptic serine protease, which appears to be a tetramer of catalytic subunits, approximately half of which are linked by disulfide bonds.	Disulfides	246-255	chymase 1	Canis lupus familiaris	133-148
8521814-4	1995	This domain appears to be functionally conserved in the erythropoietin (EPO) receptor because substitution of cysteines for residues in the analogous region causes EPO-independent receptor activation via disulfide-linked homodimerization.	Disulfides	204-213	erythropoietin	Mus musculus	72-75
11118436-3	2001	The primary structure deduced from the corresponding cDNA was confirmed using amino acid sequence determination, which supported the finding that SVS VII consists of 76 amino acid residues with five disulfide bridges.	Disulfides	199-208	prostate and testis expressed 4	Mus musculus	146-153
8521814-4	1995	This domain appears to be functionally conserved in the erythropoietin (EPO) receptor because substitution of cysteines for residues in the analogous region causes EPO-independent receptor activation via disulfide-linked homodimerization.	Disulfides	204-213	erythropoietin	Mus musculus	164-167
11118436-5	2001	The CD spectrum of SVS VII in 50 mm phosphate buffer at pH 7.4 appeared as one negative band arising from the beta form at 217 nm and several fine structures due to nonpeptide chromophores including a prominent band for the disulfide bond at 250 nm.	Disulfides	224-233	prostate and testis expressed 4	Mus musculus	19-26
7588732-8	1995	Affinity labeling indicated that NPR-D exists as a disulfide-linked tetramer.	Disulfides	51-60	neuronal pentraxin receptor	Rattus norvegicus	33-36
11238442-5	2001	In this work, we asked whether the remaining cysteines in the hCaR VFT, namely Cys(236) and Cys(482), form disulfide bond(s) with cysteines in the Cys-rich domain.	Disulfides	107-116	CXADR Ig-like cell adhesion molecule	Homo sapiens	62-66
7852406-5	1995	The disulfide bond crucial for catalytic activity, subunit processing, and biological transport of glycosylasparaginase was located close to the carboxyl terminus of the heavy chain at positions 163 and 179.	Disulfides	4-13	aspartylglucosaminidase	Homo sapiens	99-119
7588735-1	1995	The two heads of porcine aorta smooth muscle myosin can be cross-linked by a disulfide bridge between the two 17-kDa essential light chains with 5,5"-dithiobis(2-nitrobenzoic acid) [Katoh, T., Tanahashi, K., Hasegawa, Y.	Disulfides	77-86	myosin heavy chain 14	Homo sapiens	45-51
7795886-5	1995	Like the latter two proteins, human TIMP-3 contains intrachain disulfide bonds and displays altered electrophoretic mobility in the presence of beta-mercaptoethanol.	Disulfides	63-72	TIMP metallopeptidase inhibitor 3	Homo sapiens	36-42
11297032-4	2001	Western blotting confirmed these results and showed moreover that there was a decreased disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	88-97	glycoprotein Ib platelet subunit alpha	Homo sapiens	123-133
11297032-4	2001	Western blotting confirmed these results and showed moreover that there was a decreased disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	88-97	glycoprotein Ib platelet subunit beta	Homo sapiens	138-147
8561847-9	1995	However, the other zinc-binding site(s) likely reflect the different ways that astacin and the MMP subfamilies are stabilized, i.e., disulfides in astacin and metal ions in the MMPs.	Disulfides	133-143	matrix metallopeptidase 7	Homo sapiens	95-98
11297032-9	2001	Our present observation of a decreased disulfide bridge formation between GPIb alpha and GPIb beta shows that GPIX is not only needed for the correct assembly of the complex but might also be needed for the disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	39-48	glycoprotein Ib platelet subunit alpha	Homo sapiens	74-84
11297032-9	2001	Our present observation of a decreased disulfide bridge formation between GPIb alpha and GPIb beta shows that GPIX is not only needed for the correct assembly of the complex but might also be needed for the disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	39-48	glycoprotein Ib platelet subunit beta	Homo sapiens	89-98
7843232-1	1995	Interleukin-12 (IL-12) is a cytokine that has regulatory effects on T and natural killer (NK) cells and is composed of two disulfide-bonded subunits, p40 and p35.	Disulfides	123-132	interleukin 12b	Mus musculus	150-153
7843232-7	1995	Purified mouse p40 produced in a baculovirus expression system was found to consist of two species: the p40 monomer and a disulfide-linked p40 dimer [(p40)2].	Disulfides	122-131	interleukin 12b	Mus musculus	15-18
11297032-9	2001	Our present observation of a decreased disulfide bridge formation between GPIb alpha and GPIb beta shows that GPIX is not only needed for the correct assembly of the complex but might also be needed for the disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	39-48	glycoprotein Ib platelet subunit alpha	Homo sapiens	242-252
11297032-9	2001	Our present observation of a decreased disulfide bridge formation between GPIb alpha and GPIb beta shows that GPIX is not only needed for the correct assembly of the complex but might also be needed for the disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	39-48	glycoprotein Ib platelet subunit beta	Homo sapiens	257-266
11297032-9	2001	Our present observation of a decreased disulfide bridge formation between GPIb alpha and GPIb beta shows that GPIX is not only needed for the correct assembly of the complex but might also be needed for the disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	207-216	glycoprotein Ib platelet subunit alpha	Homo sapiens	74-84
11297032-9	2001	Our present observation of a decreased disulfide bridge formation between GPIb alpha and GPIb beta shows that GPIX is not only needed for the correct assembly of the complex but might also be needed for the disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	207-216	glycoprotein Ib platelet subunit beta	Homo sapiens	89-98
11297032-9	2001	Our present observation of a decreased disulfide bridge formation between GPIb alpha and GPIb beta shows that GPIX is not only needed for the correct assembly of the complex but might also be needed for the disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	207-216	glycoprotein Ib platelet subunit alpha	Homo sapiens	242-252
8561847-9	1995	However, the other zinc-binding site(s) likely reflect the different ways that astacin and the MMP subfamilies are stabilized, i.e., disulfides in astacin and metal ions in the MMPs.	Disulfides	133-143	matrix metallopeptidase 7	Homo sapiens	177-181
11297032-9	2001	Our present observation of a decreased disulfide bridge formation between GPIb alpha and GPIb beta shows that GPIX is not only needed for the correct assembly of the complex but might also be needed for the disulfide bridge formation between GPIb alpha and GPIb beta.	Disulfides	207-216	glycoprotein Ib platelet subunit beta	Homo sapiens	257-266
8561853-2	1995	The results of proton NMR studies on the Cys-102 acetamide-derivatized monomer of iso-1 ferricytochrome c indicate that the conformational characteristics of the heme environment in this protein derivative are intermediate between those of the unmodified monomer and disulfide dimer forms of the protein.	Disulfides	267-276	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	82-87
8561853-3	1995	Measurements of the pKa of the alkaline transitions of the five forms of iso-1 ferricytochrome c provided values of 8.89, 8.82, 8.67, 8.47, and 8.50 for the unmodified monomer, S-methylated monomer, acetamide-derivatized monomer, thionitrobenzoate-derivatized monomer, and disulfide dimer, respectively.	Disulfides	273-282	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	73-78
8561853-4	1995	The results of proton NMR studies of the reduced form of these proteins suggest that the heme environments of the unmodified monomer and disulfide dimer derivatives of iso-1 ferrocytochrome c are similar and indicate that treatment of the thionitrobenzoate-derivatized and disulfide dimer forms of the protein with sodium dithionite results in cleavage of the disulfide bonds at position 102.	Disulfides	137-146	threonine ammonia-lyase ILV1	Saccharomyces cerevisiae S288C	168-173
7548166-1	1995	Asymmetric acetylcholinesterase (AChE) contains three tetrameric sets of catalytic subunits disulfide-linked to structural subunits of a collagenic tail.	Disulfides	92-101	acetylcholinesterase	Rattus norvegicus	33-37
11462985-5	2001	Our model peptide, the pseudosubstrate sequence of protein kinase C-zeta (PKC-zeta), was associated to the pentapeptide Gly-Arg-Gly-Arg-Lys(Pam)-NH2 through thiazolidine, thioether, disulfide, or hydrazone linkages.	Disulfides	182-191	protein kinase C zeta	Homo sapiens	51-72
11462985-5	2001	Our model peptide, the pseudosubstrate sequence of protein kinase C-zeta (PKC-zeta), was associated to the pentapeptide Gly-Arg-Gly-Arg-Lys(Pam)-NH2 through thiazolidine, thioether, disulfide, or hydrazone linkages.	Disulfides	182-191	protein kinase C zeta	Homo sapiens	74-82
11462985-5	2001	Our model peptide, the pseudosubstrate sequence of protein kinase C-zeta (PKC-zeta), was associated to the pentapeptide Gly-Arg-Gly-Arg-Lys(Pam)-NH2 through thiazolidine, thioether, disulfide, or hydrazone linkages.	Disulfides	182-191	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	140-143
7538845-0	1994	Hydrogen exchange in BPTI variants that do not share a common disulfide bond.	Disulfides	62-71	spleen trypsin inhibitor I	Bos taurus	21-25
7538845-1	1994	Bovine pancreatic trypsin inhibitor (BPTI) is stabilized by 3 disulfide bonds, between cysteines 30-51, 5-55, and 14-38.	Disulfides	62-71	spleen trypsin inhibitor I	Bos taurus	0-35
7538845-1	1994	Bovine pancreatic trypsin inhibitor (BPTI) is stabilized by 3 disulfide bonds, between cysteines 30-51, 5-55, and 14-38.	Disulfides	62-71	spleen trypsin inhibitor I	Bos taurus	37-41
7574684-3	1995	Six disulfide linkages were determined to be Cys1-Cys7, Cys5-Cys14, Cys121-Cys145, Cys123-Cys163, Cys187-Cys235, and Cys271-Cys314, respectively.	Disulfides	4-13	cystin 1	Homo sapiens	45-49
7538845-3	1994	These proteins resemble disulfide-bonded intermediates that accumulate in the BPTI folding pathway.	Disulfides	24-33	spleen trypsin inhibitor I	Bos taurus	78-82
11119600-4	2001	The immunoprecipitated complex contained disulfide-bonded dimers of A33R protein that were noncovalently linked to A36R protein.	Disulfides	41-50	EEV membrane phosphoglycoprotein	Vaccinia virus	68-72
7669916-3	1995	A wide range of local energy mining were identified even though two disulfide bridges (Cys1-Cys15 and Cys3-Cys11) constrain the structure of the peptide.	Disulfides	68-77	cystin 1	Homo sapiens	87-91
11161827-8	2001	This mutation helps to define two homologous regions of the AVP-NPII precursor bounded by disulfide bridges between C13 and C27 and between C61 and C73 that have structural homology and contain the majority of amino acid substitutions associated with ADNDI.	Disulfides	90-99	homeobox C13	Homo sapiens	116-119
11095748-1	2000	A family of octapeptide derivatives of somatostatin cyclized via a disulfide bridge (des-AA(1,2,4,5,12,13)[d-2Nal(8)]-somatostatin-14, ODN-8) was identified that has high affinity and selectivity for the human sst(3) somatostatin receptor subtype transfected in CCL39 cells.	Disulfides	67-76	somatostatin	Homo sapiens	118-133
7740449-4	1994	The most potent peptide synthesized was a disulfide-bridged, 19 amino acid peptide, ATS29-47, which inhibited Factor Xa with a Ki = 35 nM, and increased plasma clotting times by over 4-fold at a concentration of 33 uM.	Disulfides	42-51	coagulation factor X	Homo sapiens	110-119
7631157-4	1995	Spodoptera frugiperda insect cells infected with the recombinant virus produced MAdCAM-1-Fc as a disulfide-linked homodimer of 82 kDa polypeptides, which was secreted into the culture medium at &gt; 1 microgram/ml.	Disulfides	97-106	mucosal vascular addressin cell adhesion molecule 1	Homo sapiens	80-88
7961823-1	1994	Lipoprotein(a) (Lp(a)) consists of a low density lipoprotein particle in which apolipoprotein(a) (apo(a)), is disulfide linked to apoB.	Disulfides	110-119	apolipoprotein(a)	Papio anubis	0-14
7961823-1	1994	Lipoprotein(a) (Lp(a)) consists of a low density lipoprotein particle in which apolipoprotein(a) (apo(a)), is disulfide linked to apoB.	Disulfides	110-119	apolipoprotein(a)	Papio anubis	16-21
7961823-1	1994	Lipoprotein(a) (Lp(a)) consists of a low density lipoprotein particle in which apolipoprotein(a) (apo(a)), is disulfide linked to apoB.	Disulfides	110-119	apolipoprotein(a)	Papio anubis	79-96
7961823-1	1994	Lipoprotein(a) (Lp(a)) consists of a low density lipoprotein particle in which apolipoprotein(a) (apo(a)), is disulfide linked to apoB.	Disulfides	110-119	apolipoprotein(a)	Papio anubis	98-104
11068050-1	2000	Trypsin treatment of HeLa cells results in a limited proteolysis of the coxsackievirus and adenovirus receptor (CAR) after which the cleaved CAR remains cell-associated and tryptic peptides remain associated through disulfide bonds.	Disulfides	216-225	CXADR Ig-like cell adhesion molecule	Homo sapiens	112-115
11027142-5	2000	The cooperativity of the interaction is due to binding of the inhibitor molecule to a dimeric or oligomeric form of SR-BI held together by disulfide bridges.	Disulfides	139-148	scavenger receptor class B member 1	Oryctolagus cuniculus	116-121
7664482-8	1995	The complete amino acid sequence of human serum cholinesterase and the location of disulfide bonds within the sequence have been described.	Disulfides	83-92	butyrylcholinesterase	Homo sapiens	48-62
11052772-5	2000	Circular dichroism shows that glycated LTP1 having all their disulfide bridges reduced are totally unfolded.	Disulfides	61-70	non-specific lipid transport protein 1	Hordeum vulgare	39-43
11009104-0	2000	A disulfide-linked natural killer cell receptor dimer has higher affinity for HLA-C than wild-type monomer.	Disulfides	2-11	major histocompatibility complex, class I, C	Homo sapiens	78-83
7756638-4	1995	However, disruption of disulfide bonds located at or near the N-terminus of GPIIIa abolished the binding of all the anti-PlA1 alloantibodies tested.	Disulfides	23-32	POU class 2 homeobox 3	Homo sapiens	121-125
10995359-7	2000	For the development of biodegradable materials with good mechanical properties from these biopolymers, disulfide bonds between the keratin molecules are needed.	Disulfides	103-112	keratin	Gallus gallus	131-138
7929256-11	1994	This contrasts with observations of the hCG beta subunit where all the disulfide bonds are required for efficient combination and folding (Suganuma, N., Matzuk, M., and Boime, I.	Disulfides	71-80	chorionic gonadotropin subunit beta 3	Homo sapiens	40-48
7551559-1	1995	Patients with anti-epiligrin cicatricial pemphigoid have anti-basement membrane autoantibodies that immunoprecipitate a set of disulfide-linked human keratinocyte polypeptides that co-migrate in sodium dodecyl sulfate polyacrylamide gel electrophoresis with the same complex identified by monoclonal anti-epiligrin (P1E1) and monoclonal anti-nicein/kalinin (GB3) antibodies.	Disulfides	127-136	alpha 1,4-galactosyltransferase (P blood group)	Homo sapiens	358-361
7931296-5	1994	In tetrameric SS-AChE, two pairs of disulfide-linked dimers are associated by hydrophobic forces located in the C terminus.	Disulfides	36-45	acetylcholinesterase	Bos taurus	17-21
11045618-3	2000	This thiol group was specifically reacted with 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB) in the presence of 1.0 M Gdn-HCI at pH 7.5, producing a modified beta-lactoglobulin (TNB-bIg) containing a mixed disulfide bond with 5-thio-2-nitrobenzoic acid (TNB).	Disulfides	203-212	beta-lactoglobulin	Bos taurus	155-173
7577807-1	1995	Adult T cell leukemia-derived factor (ADF), which is identical to a disulfide reducing enzyme human thioredoxin (TRX), is produced and released by activated or virus-infected lymphocytes.	Disulfides	68-77	thioredoxin	Homo sapiens	38-41
11045618-12	2000	Upon reducing the mixed disulfide of TNB-bIg with dithiothreitol, the intact beta-lactoglobulin was regenerated.	Disulfides	24-33	beta-lactoglobulin	Bos taurus	77-95
10956021-2	2000	We previously reported that Cys-containing, Arg-rich peptide-substrate analogues spontaneously form disulfide-linked complexes with PKC isozymes, resulting in isozyme inactivation.	Disulfides	100-109	protein kinase C, gamma	Rattus norvegicus	132-135
7978820-0	1994	Human TIMP-1 binds to pro-M(r) 92K GL (gelatinase B, MMP-9) through the "second disulfide knot".	Disulfides	80-89	matrix metallopeptidase 9	Homo sapiens	53-58
7577807-1	1995	Adult T cell leukemia-derived factor (ADF), which is identical to a disulfide reducing enzyme human thioredoxin (TRX), is produced and released by activated or virus-infected lymphocytes.	Disulfides	68-77	thioredoxin	Homo sapiens	100-111
7913623-13	1994	This also indicates that gamma-GT-dependent uptake of cystine accounts for a portion of the induced uptake of this disulfide into these M199-medium-pretreated cells.	Disulfides	115-124	inactive glutathione hydrolase 2	Homo sapiens	25-33
10956021-3	2000	This suggested that PKC might be inactivated by oxidant-induced S-glutathiolation, i.e., disulfide linkage of the endogenous molecule glutathione (GSH) to PKC.	Disulfides	89-98	protein kinase C, gamma	Rattus norvegicus	20-23
10956021-3	2000	This suggested that PKC might be inactivated by oxidant-induced S-glutathiolation, i.e., disulfide linkage of the endogenous molecule glutathione (GSH) to PKC.	Disulfides	89-98	protein kinase C, gamma	Rattus norvegicus	155-158
7577807-1	1995	Adult T cell leukemia-derived factor (ADF), which is identical to a disulfide reducing enzyme human thioredoxin (TRX), is produced and released by activated or virus-infected lymphocytes.	Disulfides	68-77	thioredoxin	Homo sapiens	113-116
10827170-4	2000	Here, we report an essential region in pro-GCAP-II for the correct disulfide pairing of the mature peptide, GCAP-II.	Disulfides	67-76	guanylate cyclase activator 2B	Homo sapiens	43-50
7513556-3	1994	The present study investigates the effect of DsbA on the well-characterized disulfide-coupled refolding processes of BPTI and of alpha-lactalbumin.	Disulfides	76-85	spleen trypsin inhibitor I	Bos taurus	117-121
7648447-6	1995	The IL-2/IL-2R gamma c, but not the IL-2/IL-2R beta, complex exhibited enhanced mobility after SDS-polyacrylamide gel electrophoresis under nonreducing conditions, suggesting a more compact structure for gamma c as a result of intrachain disulfide bonds.	Disulfides	238-247	interleukin 2	Mus musculus	4-8
7513556-4	1994	Disulfide-bonded DsbA in stoichiometric amounts proved to be a very potent donor of disulfide bonds to reduced BPTI but showed little catalytic activity at neutral pH in the presence of a glutathione redox buffer.	Disulfides	0-9	spleen trypsin inhibitor I	Bos taurus	111-115
10827170-4	2000	Here, we report an essential region in pro-GCAP-II for the correct disulfide pairing of the mature peptide, GCAP-II.	Disulfides	67-76	guanylate cyclase activator 2B	Homo sapiens	108-115
7648447-6	1995	The IL-2/IL-2R gamma c, but not the IL-2/IL-2R beta, complex exhibited enhanced mobility after SDS-polyacrylamide gel electrophoresis under nonreducing conditions, suggesting a more compact structure for gamma c as a result of intrachain disulfide bonds.	Disulfides	238-247	interleukin 2	Mus musculus	9-13
7513556-4	1994	Disulfide-bonded DsbA in stoichiometric amounts proved to be a very potent donor of disulfide bonds to reduced BPTI but showed little catalytic activity at neutral pH in the presence of a glutathione redox buffer.	Disulfides	84-93	spleen trypsin inhibitor I	Bos taurus	111-115
7721838-0	1995	The disulfide folding pathway of human epidermal growth factor.	Disulfides	4-13	epidermal growth factor	Homo sapiens	39-62
7513556-7	1994	Thiol-disulfide exchange is normally very slow at acidic pH but occurs rapidly with DsbA; consequently, DsbA catalyzed the disulfide folding of BPTI under acidic conditions.	Disulfides	6-15	spleen trypsin inhibitor I	Bos taurus	144-148
7513556-7	1994	Thiol-disulfide exchange is normally very slow at acidic pH but occurs rapidly with DsbA; consequently, DsbA catalyzed the disulfide folding of BPTI under acidic conditions.	Disulfides	123-132	spleen trypsin inhibitor I	Bos taurus	144-148
7513654-7	1994	The assignment of the bridge in bovine alpha 2AP is at variance with the previous assignment of the two disulfide bridges in human alpha 2AP [Lijnen, H.R.	Disulfides	104-113	serpin family F member 2	Homo sapiens	131-140
10843779-1	2000	The observation that the level of S-thiolated proteins (protein-thiol mixed disulfides) was transiently increased in the lens epithelial cells correlation with the transient inactivation of glyceraldehyde-3-phosphate dehydrogenase (G-3PD), a key glycolytic enzyme, when the cells were treated with a bolus of hydrogen peroxide, prompted our speculation that G-3PD may have been transiently thiolated at the SH sensitive active center.	Disulfides	76-86	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	190-230
10843779-1	2000	The observation that the level of S-thiolated proteins (protein-thiol mixed disulfides) was transiently increased in the lens epithelial cells correlation with the transient inactivation of glyceraldehyde-3-phosphate dehydrogenase (G-3PD), a key glycolytic enzyme, when the cells were treated with a bolus of hydrogen peroxide, prompted our speculation that G-3PD may have been transiently thiolated at the SH sensitive active center.	Disulfides	76-86	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	232-237
10843779-1	2000	The observation that the level of S-thiolated proteins (protein-thiol mixed disulfides) was transiently increased in the lens epithelial cells correlation with the transient inactivation of glyceraldehyde-3-phosphate dehydrogenase (G-3PD), a key glycolytic enzyme, when the cells were treated with a bolus of hydrogen peroxide, prompted our speculation that G-3PD may have been transiently thiolated at the SH sensitive active center.	Disulfides	76-86	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	358-363
10843779-2	2000	In the meantime, thioltransferase (TTase), a thiol regulating enzyme, whose activity remained constant under the same condition, may be regulating G-3PD and other sulfhydryl-sensitive glycolytic enzymes through thiol-disulfide exchange reactions ( Lou et al., 1998 ).	Disulfides	217-226	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	147-152
7721838-1	1995	Human epidermal growth factor (EGF) contains three disulfides and 53 amino acids.	Disulfides	51-61	epidermal growth factor	Homo sapiens	6-29
7721838-1	1995	Human epidermal growth factor (EGF) contains three disulfides and 53 amino acids.	Disulfides	51-61	epidermal growth factor	Homo sapiens	31-34
7731044-2	1995	Here, we have established a kinetic model for the folding of the Fab fragment of the antibody MAK 33 with intact disulfide bonds.	Disulfides	113-122	FA complementation group B	Homo sapiens	65-68
10874667-2	2000	PDGF exists as disulfide-linked homo- or heterodimers composed of two polypeptide chains encoded by distinct genes, designated PDGF-A and PDGF-B.	Disulfides	15-24	platelet derived growth factor subunit B	Homo sapiens	138-144
7578928-5	1995	A mono-adduct homodimer resulting from alkylation at Cys-6 and disulfide bridge formation through Cys-1 was also identified.	Disulfides	63-72	cystin 1	Homo sapiens	98-103
10745207-1	2000	Glutathione is excreted in a dose-dependent, non-stoichiometric fashion from Saccharomyces cerevisiae cells expressing and secreting Bovine Pancreatic Trypsin Inhibitor (BPTI), a small, disulfide-bonded protein.	Disulfides	186-195	spleen trypsin inhibitor I	Bos taurus	133-168
10745207-1	2000	Glutathione is excreted in a dose-dependent, non-stoichiometric fashion from Saccharomyces cerevisiae cells expressing and secreting Bovine Pancreatic Trypsin Inhibitor (BPTI), a small, disulfide-bonded protein.	Disulfides	186-195	spleen trypsin inhibitor I	Bos taurus	170-174
10806385-7	2000	In this paper, we demonstrate that Tris(2-carboxyethyl)phosphine, a specific disulfide reducing agent, allows a continuous reduction of the lipoyl group associated with the H-protein during the course of the reaction catalysed by the L-protein.	Disulfides	77-86	myosin binding protein H	Homo sapiens	173-182
8135801-1	1994	The two cysteines C494 and C569, located in the first and second extracellular loop, respectively, of the thyrotropin (TSH) receptor, were mutated to serines to test the functional significance of the putative disulfide bond between these two cysteines.	Disulfides	210-219	thyroid stimulating hormone receptor	Homo sapiens	106-132
7719941-2	1995	We demonstrate that TCR assembly proceeds by initial association of TCR alpha with CD3 delta epsilon proteins and by association of TCR beta with CD3 gamma epsilon proteins to form alpha delta epsilon and beta gamma epsilon trimers; these trimers then associate to form alpha delta epsilon-beta gamma epsilon complexes, within which alpha-beta disulfide bond formation occurs.	Disulfides	344-353	T cell receptor beta chain	Mus musculus	132-140
8300559-4	1994	The deduced amino acid sequence encodes a protein that lacks one of the seven disulfide bridges found in similar PLA2s and, therefore, represents a class of enzymes distinct from the mammalian group I and group II enzymes.	Disulfides	78-87	phospholipase A2 group IIA	Homo sapiens	113-118
10826533-1	2000	Thioredoxin is a small, multifunctional protein with a redox-active disulfide/dithiol in the active site.	Disulfides	68-77	thioredoxin 1	Mus musculus	0-11
7547690-8	1995	Furthermore, MP6 medium showed Trx activity with NADPH and Trx reductase using an insulin disulfide reduction assay.	Disulfides	90-99	thioredoxin	Homo sapiens	59-62
10938586-6	2000	The results obtained show that the 41 degrees C stress leads to formation of intermolecular disulfide bonds between apo-GR and associated heat shock proteins (Hsp90, Hsp70).	Disulfides	92-101	heat shock protein family A (Hsp70) member 4	Homo sapiens	166-171
7787424-4	1995	In both peptides, disulfide bonds link Cys1 with Cys13 and Cys7 with Cys19, and the side chain of Asp9 forms an amide bond with the N-terminus.	Disulfides	18-27	cystin 1	Homo sapiens	39-43
10729132-8	2000	We present evidence for a disulfide bond requirement in TVB(S1) for ALV-E infection but not for ALV-B infection.	Disulfides	26-35	tumor necrosis factor receptor superfamily, member 10b	Gallus gallus	56-59
10734121-2	2000	The encoded protein, designated as Asc-1 (asc-type amino acid transporter 1), was found to be structurally related to recently identified mammalian amino acid transporters for the transport systems L, y(+)L, x(C)(-), and b(0,+), which are linked, via a disulfide bond, to the type II membrane glycoproteins, 4F2 heavy chain (4F2hc), or rBAT (related to b(0,+) amino acid transporter).	Disulfides	253-262	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	336-340
7903969-1	1994	The nonhydrolyzable ATP analogue ATP gamma S (adenosine 5"-3-O-(thio)triphosphate) is affinity cross-linked to GroEL by formation of a disulfide bridge in a peroxide-promoted reaction.	Disulfides	135-144	heat shock protein family D (Hsp60) member 1	Homo sapiens	111-116
7786412-1	1995	The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers.	Disulfides	139-148	peptidyl arginine deiminase 1	Homo sapiens	107-110
7786412-1	1995	The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers.	Disulfides	255-264	colony stimulating factor 2	Homo sapiens	90-96
8289254-12	1994	The four disulfide bonds and two calcium sites, which are lacking in CCP, are conserved in ARP and LiP.	Disulfides	9-18	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	69-72
10722657-1	2000	The disulfide folding pathway of bovine pancreatic trypsin inhibitor (BPTI) is characterized by the predominance of folding intermediates with native-like structures.	Disulfides	4-13	spleen trypsin inhibitor I	Bos taurus	33-68
10722657-1	2000	The disulfide folding pathway of bovine pancreatic trypsin inhibitor (BPTI) is characterized by the predominance of folding intermediates with native-like structures.	Disulfides	4-13	spleen trypsin inhibitor I	Bos taurus	70-74
7786412-1	1995	The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers.	Disulfides	255-264	peptidyl arginine deiminase 1	Homo sapiens	107-110
7786412-1	1995	The studies on PDI-, PPI- and chaperone-catalyzed refolding of recombinant human IL-2 and GM-CSF show that PDI can prevent the mismatch of disulfide bonds and formation of aggregates by interchains linkage; furthermore, PDI can correct the mismatching of disulfide bonds in IL-2 isomers.	Disulfides	255-264	peptidyl arginine deiminase 1	Homo sapiens	107-110
7698350-5	1995	Therefore, interactions between the two chains, stabilized by the interchain disulfide within the Fab fragment, are essential for formation of the alternatively folded state.	Disulfides	77-86	FA complementation group B	Homo sapiens	98-101
10700381-4	2000	Controlled proteolysis of wild-type glucokinase by proteinase K revealed that the SH group oxidizing agent alloxan can induce the formation of multiple intramolecular disulfide bridges corresponding to a double-band pattern of glucokinase protein in nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Disulfides	167-176	glucokinase	Homo sapiens	36-47
10700381-4	2000	Controlled proteolysis of wild-type glucokinase by proteinase K revealed that the SH group oxidizing agent alloxan can induce the formation of multiple intramolecular disulfide bridges corresponding to a double-band pattern of glucokinase protein in nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Disulfides	167-176	glucokinase	Homo sapiens	227-238
8253791-1	1993	Previous studies have shown that CD8 can be present at the cell surface either as a disulfide-linked homodimer of CD8 alpha or as a disulfide-linked heterodimer of CD8 alpha and CD8 beta.	Disulfides	84-93	CD8a molecule	Homo sapiens	33-36
7788289-0	1995	Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide.	Disulfides	109-118	thioredoxin	Homo sapiens	0-11
10720769-4	2000	The data indicate that activation of hsp70 is linked to changes in thiol-disulfide redox perturbations while grp78 activation may be caused by loss of calcium from the endoplasmic reticulum.	Disulfides	73-82	heat shock protein family A (Hsp70) member 4	Homo sapiens	37-42
8253791-1	1993	Previous studies have shown that CD8 can be present at the cell surface either as a disulfide-linked homodimer of CD8 alpha or as a disulfide-linked heterodimer of CD8 alpha and CD8 beta.	Disulfides	132-141	CD8a molecule	Homo sapiens	33-36
7788289-1	1995	The recent high-resolution solution structures of human and Escherichia coli thioredoxin in their oxidized and reduced states support a catalytic model of protein disulfide reduction involving binding of a target protein and nucleophilic attack by the active-site Cys32 thiolate to form a transition state mixed disulfide.	Disulfides	163-172	thioredoxin	Homo sapiens	77-88
7788289-1	1995	The recent high-resolution solution structures of human and Escherichia coli thioredoxin in their oxidized and reduced states support a catalytic model of protein disulfide reduction involving binding of a target protein and nucleophilic attack by the active-site Cys32 thiolate to form a transition state mixed disulfide.	Disulfides	312-321	thioredoxin	Homo sapiens	77-88
7788295-0	1995	Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B.	Disulfides	51-60	thioredoxin	Homo sapiens	28-39
10699328-0	2000	Reversible protection of disulfide bonds followed by oxidative folding render recombinant hCGbeta highly immunogenic.	Disulfides	25-34	chorionic gonadotropin subunit beta 3	Homo sapiens	90-97
7788295-3	1995	Using multidimensional heteronuclear-edited and hetero-nuclear-filtered NMR spectroscopy, we have solved the solution structure of a complex of human thioredoxin and a 13-residue peptide extending from residues 56-68 of p50, representing a kinetically stable mixed disulfide intermediate along the reaction pathway.	Disulfides	265-274	thioredoxin	Homo sapiens	150-161
7788295-6	1995	CONCLUSIONS: In addition to the intermolecular disulfide bridge between Cys32 of human thioredoxin and Cys62 of the peptide, the complex is stabilized by numerous hydrogen-bonding, electrostatic and hydrophobic interactions which involve residues 57-65 of the NF kappa B peptide and confer substrate specificity.	Disulfides	47-56	thioredoxin	Homo sapiens	87-98
7788295-7	1995	These structural features permit one to suggest the specificity requirements for human thioredoxin-catalyzed disulfide bond reduction of proteins.	Disulfides	109-118	thioredoxin	Homo sapiens	87-98
8408080-5	1993	In the presence of millimolar concentration of DTT, HepG2 cells synthesize fully reduced RBP within the endoplasmic reticulum (ER) which, upon removal of DTT, forms disulfide bonds post-translationally.	Disulfides	165-174	retinol binding protein 4	Homo sapiens	89-92
7876079-2	1995	Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism involving transfer of electrons from NADPH via FAD to a redox-active disulfide.	Disulfides	80-89	thioredoxin	Homo sapiens	6-17
8408080-7	1993	Using nonreducing gel electrophoresis, we resolved disulfide-bonded RBP folding intermediates.	Disulfides	51-60	retinol binding protein 4	Homo sapiens	68-71
10677561-5	2000	NPII is an intracellular carrier protein for AVP during the axonal transport from the hypothalamus to the posterior pituitary and contains 14 conserved cysteine residues forming 7 disulfide bonds.	Disulfides	180-189	neuronal pentraxin 2	Homo sapiens	0-4
7876079-2	1995	Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism involving transfer of electrons from NADPH via FAD to a redox-active disulfide.	Disulfides	80-89	thioredoxin	Homo sapiens	102-113
10688888-9	2000	We have expressed recombinant wild-type human gammaD crystallin (HGD) and its Arg-14 to Cys mutant (R14C) in Escherichia coli and show that R14C forms disulfide-linked oligomers, which markedly raise the phase separation temperature of the protein solution.	Disulfides	151-160	homogentisate 1,2-dioxygenase	Homo sapiens	65-68
8408081-3	1993	Upon removal of DTT, RBP forms disulfide bonds and a folding intermediate, compact II, accumulates within the ER.	Disulfides	31-40	retinol binding protein 4	Homo sapiens	21-24
7533087-3	1995	Here, we show that a disulfide-bonded dimer of CD44, formed by substituting the transmembrane region of CD3 zeta chain for that of CD44, binds Fl-HA, even when the cytoplasmic domain of the CD44 dimer is absent.	Disulfides	21-30	CD247 molecule	Homo sapiens	104-118
10688888-11	2000	In contrast, HGD slowly forms only disulfide-linked dimers and no oligomers.	Disulfides	35-44	homogentisate 1,2-dioxygenase	Homo sapiens	13-16
7867625-1	1995	Eel natriuretic peptide receptor C (NPR-C) was cloned, characterized and found to have a unique interchain disulfide linkage when compared to that of mammalian NPR-C.	Disulfides	107-116	natriuretic peptide receptor 3	Homo sapiens	36-41
10965118-5	2000	In addition, and similarly to BACE, BACE2 differs from the other members of the human aspartic protease family in the number and distribution of putative disulfide bonds and in the presence of an extended C-terminal region which contains a predicted transmembrane segment.	Disulfides	154-163	beta-secretase 2	Homo sapiens	36-41
11156708-7	2000	It seemed that the BAT1 gene is responsible for non-Type I cystinuria and that its protein was a subunit linked to the rBAT protein via a disulfide bond.	Disulfides	138-147	solute carrier family 7 member 9	Homo sapiens	19-23
11156708-7	2000	It seemed that the BAT1 gene is responsible for non-Type I cystinuria and that its protein was a subunit linked to the rBAT protein via a disulfide bond.	Disulfides	138-147	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	119-123
7690589-5	1993	A unique and reproducible unfolding pathway for an intermediate of BPTI lacking the [30,51] disulfide bond is obtained.	Disulfides	92-101	spleen trypsin inhibitor I	Bos taurus	67-71
8274523-9	1993	When GALA, a water soluble, membrane-destabilizing peptide, is covalently attached to the dendrimer via a disulfide linkage, transfection efficiency of the 1:1 complex is increased by 2-3 orders of magnitude.	Disulfides	106-115	galactosidase alpha	Homo sapiens	5-9
8344931-3	1993	Based on the gel migration of folding intermediates, the kinetic relationships between these intermediates, and on the order of formation of six disulfide bonds, we have found that the in vitro folding pathway of the human chorionic gonadotropin beta subunit (hCG-beta) is indistinguishable from the intracellular folding pathway.	Disulfides	145-154	chorionic gonadotropin subunit beta 3	Homo sapiens	223-258
7867625-2	1995	The NPR-C cDNA was obtained from an eel gill cDNA library; the open reading frame codes for a polypeptide of 502 amino acids exhibiting the known features of NPR-C, including a weak ligand specificity and a disulfide-linked homodimeric structure.	Disulfides	207-216	natriuretic peptide receptor 3	Homo sapiens	4-9
7867625-4	1995	Site-directed mutagenesis revealed that eel and mammalian NPR-C are quite different in their interchain disulfide-bonding pattern; eel uses the second Cys residue and mammals the fifth Cys residue for the covalent dimerization.	Disulfides	104-113	natriuretic peptide receptor 3	Homo sapiens	58-63
7775391-1	1995	Protein disulfide isomerase (PDI), which catalyses the folding of newly synthesized or denatured proteins through correct disulfide formation, was purified from soybean (Glycine max).	Disulfides	8-17	protein disulfide-isomerase	Glycine max	29-32
8344931-3	1993	Based on the gel migration of folding intermediates, the kinetic relationships between these intermediates, and on the order of formation of six disulfide bonds, we have found that the in vitro folding pathway of the human chorionic gonadotropin beta subunit (hCG-beta) is indistinguishable from the intracellular folding pathway.	Disulfides	145-154	chorionic gonadotropin subunit beta 3	Homo sapiens	260-268
8344931-8	1993	In vitro, assembly was increased after reduction of two of the carboxyl-terminal disulfide bonds of hCG-beta by PDI.	Disulfides	81-90	chorionic gonadotropin subunit beta 3	Homo sapiens	100-108
10588648-2	1999	Here we identify the permease-like protein b(0,+)AT as the catalytic subunit that associates by a disulfide bond with rBAT to form a hetero-oligomeric b(0,+) amino acid transporter complex.	Disulfides	98-107	solute carrier family 7 member 9	Homo sapiens	43-51
10588648-2	1999	Here we identify the permease-like protein b(0,+)AT as the catalytic subunit that associates by a disulfide bond with rBAT to form a hetero-oligomeric b(0,+) amino acid transporter complex.	Disulfides	98-107	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	118-122
7474539-6	1995	A disulfide-reducing reagent, 1,4-dithiothreitol (DTT), recovered the increased [Ca2+]i and decreased pHi to the control levels.	Disulfides	2-11	glucose-6-phosphate isomerase	Rattus norvegicus	102-105
10551877-0	1999	Disulfide linkage of growth hormone (GH) receptors (GHR) reflects GH-induced GHR dimerization.	Disulfides	0-9	growth hormone receptor	Homo sapiens	52-55
10551877-0	1999	Disulfide linkage of growth hormone (GH) receptors (GHR) reflects GH-induced GHR dimerization.	Disulfides	0-9	growth hormone receptor	Homo sapiens	77-80
10551877-6	1999	By using the GH antagonist, G120K, and an antibody recognizing a dimerization-sensitive GHR epitope, we demonstrated that GH-induced GHR disulfide linkage reflects GH-induced GHR dimerization.	Disulfides	137-146	growth hormone receptor	Homo sapiens	88-91
8344348-2	1993	Whereas the ectodomain of CD16 is the receptor for Fc gamma domains of immunoglobulins, disulfide-linked homo- and heterodimers composed of zeta and gamma are required for the cell surface expression, and signal transduction properties of the complex.	Disulfides	88-97	Fc gamma receptor IIIa	Homo sapiens	26-30
10551877-6	1999	By using the GH antagonist, G120K, and an antibody recognizing a dimerization-sensitive GHR epitope, we demonstrated that GH-induced GHR disulfide linkage reflects GH-induced GHR dimerization.	Disulfides	137-146	growth hormone receptor	Homo sapiens	133-136
7882029-3	1994	To circumvent these drawbacks, an immunotoxin was constructed using a monoclonal antibody against the noradrenergic specific enzyme dopamine beta-hydroxylase (D beta H) coupled via a disulfide bond to saporin, a ribosomal inactivating protein.	Disulfides	183-192	dopamine beta-hydroxylase	Rattus norvegicus	132-157
10551877-6	1999	By using the GH antagonist, G120K, and an antibody recognizing a dimerization-sensitive GHR epitope, we demonstrated that GH-induced GHR disulfide linkage reflects GH-induced GHR dimerization.	Disulfides	137-146	growth hormone receptor	Homo sapiens	133-136
10551877-7	1999	GH, not G120K, promoted both GHR disulfide linkage and enhanced association with JAK2.	Disulfides	33-42	growth hormone receptor	Homo sapiens	29-32
10551877-9	1999	By using both transient and stable expression systems, we determined that cysteine 241 (an unpaired extracellular cysteine) was critical for GH-induced GHR disulfide linkage; however, GH-induced GHR dimerization, GHR-JAK2 interaction, and GHR, JAK2, and STAT5 tyrosine phosphorylation still proceeded when this cysteine residue was mutated.	Disulfides	156-165	growth hormone receptor	Homo sapiens	152-155
10551877-10	1999	We conclude GH-induced GHR disulfide linkage is not required for GHR dimerization, and activation and GH-enhanced GHR-JAK2 association depends more on GHR dimerization than on GHR and/or JAK2 tyrosine phosphorylation.	Disulfides	27-36	growth hormone receptor	Homo sapiens	23-26
8484779-1	1993	CSF-1 is a dimeric peptide growth factor, stabilized by disulfide bonds.	Disulfides	56-65	colony stimulating factor 1 (macrophage)	Mus musculus	0-5
8489700-0	1993	Refolding of cytochrome b562 and its structural stabilization by introducing a disulfide bond.	Disulfides	79-88	mitochondrially encoded cytochrome b	Homo sapiens	13-25
7983029-2	1994	The wild-type protein contains two redox active thiol/disulfide sites near the N and C terminus that are homologous to the redox center of thioredoxin.	Disulfides	54-63	thioredoxin	Homo sapiens	139-150
8437238-0	1993	Disulfide bond formation in the human immunodeficiency virus type 1 Nef protein.	Disulfides	0-9	Nef	Human immunodeficiency virus 1	68-71
10571052-1	1999	The single disulfide loop (Cys178-Cys213) of the prion protein (PrP) may stabilize the conformation of this protein by bridging the C-terminal alpha-helices.	Disulfides	11-20	major prion protein	Cricetulus griseus	64-67
10506124-4	1999	The band was shifted to 41 kDa in the reducing condition, confirming that BAT1 and rBAT are linked via a disulfide bond.	Disulfides	105-114	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	83-87
7947768-1	1994	Guanylin is a 15 amino acid mammalian hormone containing two disulfide bonds.	Disulfides	61-70	guanylate cyclase activator 2A	Homo sapiens	0-8
10597631-1	1999	Protein disulfide isomerase (PDI) is a protein-thiol oxidoreductase that catalyzes the oxidation, reduction and isomerization of protein disulfides.	Disulfides	137-147	thioredoxin reductase 1	Homo sapiens	53-67
10493790-7	1999	The E-FABP crystal structure is unique in the FABP family because of the presence of a disulfide bridge between cysteines 120 and 127 that may be physiologically as well as pathophysiologically relevant.	Disulfides	87-96	fatty acid binding protein 5	Homo sapiens	4-10
8420937-8	1993	The results indicate that the disulfide formed by equimolar Nbs2 lies within a 15-residue region of the PEPCK sequence that includes Cys399, Cys407, and Cys413.	Disulfides	30-39	phosphoenolpyruvate carboxykinase 1	Rattus norvegicus	104-109
10508396-0	1999	Intersubunit proximity of residues in the RecA protein as shown by engineered disulfide cross-links.	Disulfides	78-87	RAD51 recombinase	Homo sapiens	42-46
7957076-6	1994	The two cysteines in the first periplasmic domain are in a Cys-X-Y-Cys configuration that is characteristic of the active site of other proteins involved in disulfide bond formation, including DsbA and protein disulfide isomerase.	Disulfides	157-166	protein-disulfide isomerase	Escherichia coli	202-229
10462449-14	1999	Specific alkylation of the selenocysteine residue of TrxR1 which completely inhibits the NADPH-dependent reduction of disulfides also destroyed peroxidase activity.	Disulfides	118-128	thioredoxin reductase 1	Homo sapiens	53-58
7929311-4	1994	Thioredoxin, in conjunction with thioredoxin reductase and NADPH, allows direct measurements of the rate and extent of disulfide bond reduction.	Disulfides	119-128	thioredoxin	Homo sapiens	0-11
10491120-5	1999	The peptide (abbreviated SP7) with the highest affinity to BCF2 (IC50 = 5.1 microM) was a synthetic heterodimer comprising the amino acid sequence from position 3-15 (amidated) of Cn2, bridged by disulfide to peptide from position 54-66, acetylated and amidated.	Disulfides	196-205	Sp7 transcription factor 7	Mus musculus	25-28
8425544-6	1993	Electrospray mass spectrometric analysis of the purified protein demonstrated that the recombinant product corresponds to the native human lipocortin 1, without the initial methionine and with a free N-terminal alanine; tryptic peptide mapping by fast-atom-bombardment mass spectrometry showed that the recombinant protein contains cysteine residues at positions 263 and 324 with free thiol groups, whereas Cys270 and Cys343 are probably involved in an intrachain disulfide bridge.	Disulfides	464-473	annexin A1	Homo sapiens	139-151
7929311-4	1994	Thioredoxin, in conjunction with thioredoxin reductase and NADPH, allows direct measurements of the rate and extent of disulfide bond reduction.	Disulfides	119-128	thioredoxin	Homo sapiens	33-44
7929311-6	1994	Moreover, those disulfide bonds that were resistant to reduction by thioredoxin in the presence of Ca2+, but were readily reduced in the absence of the metal ion, were located in the N-terminal EGF-like module and in the Gla module, whereas disulfide bonds in the C-terminal EGF-like module appeared to be equally accessible whether Ca2+ was present or not.	Disulfides	16-25	thioredoxin	Homo sapiens	68-79
7929311-6	1994	Moreover, those disulfide bonds that were resistant to reduction by thioredoxin in the presence of Ca2+, but were readily reduced in the absence of the metal ion, were located in the N-terminal EGF-like module and in the Gla module, whereas disulfide bonds in the C-terminal EGF-like module appeared to be equally accessible whether Ca2+ was present or not.	Disulfides	241-250	thioredoxin	Homo sapiens	68-79
7860698-1	1994	Triadin in skeletal muscle exists as a disulfide linked oligomer.	Disulfides	39-48	triadin	Oryctolagus cuniculus	0-7
8109324-6	1993	Binding of troponin I (TnI) to the disulfide form of TnC is weakened owing to the blocking of its interaction with the N-terminal domain; however incorporation of the mutant into TnC-extracted myofibrils is not abolished.	Disulfides	35-44	tenascin C	Homo sapiens	53-56
8109324-7	1993	Introduction of a Cys residue in the C-terminal domain of TnC leads to disulfide formation between it and the indigenous Cys-98, with accompanying inhibition of regulatory activity attributable to interference with binding to TnI and, consequently, incorporation into the thin filaments.	Disulfides	71-80	tenascin C	Homo sapiens	58-61
10450692-5	1999	Previous studies have shown that circulating soluble IL-2Ralpha (slL-2Ralpha) adversely affected the biodistribution of radiolabeled antiTac disulfide-stabilized (ds)Fv.	Disulfides	141-150	interleukin 2 receptor, alpha chain	Mus musculus	53-63
7520915-3	1994	The purified BN domain specifically and stoichiometrically bound G-CSF, with an apparent dissociation constant (Kd) of 3-8 x 10(-8) M. The CD spectrum of the mBN domain was similar to that of the extracellular region of the human growth hormone (GH) receptor, which is composed of turns and beta-sheets held together by disulfide bonds.	Disulfides	320-329	colony stimulating factor 3	Homo sapiens	65-70
10404975-2	1999	In this study, FCS was used to measure equilibrium binding constants of disulfide-reduced apo-alpha-lactalbumin (rLA), denatured pepsin, and apo-cytochrome c (apo-cyt c) bound by chaperonin GroEL at different salt concentrations.	Disulfides	72-81	heat shock protein family D (Hsp60) member 1	Homo sapiens	190-195
10527895-0	1999	Disulfide-cross-linked tau and MAP2 homodimers readily promote microtubule assembly.	Disulfides	0-9	microtubule associated protein 2	Homo sapiens	31-35
10527895-2	1999	Although Tau-MTBR is the principal component of pronase-treated Alzheimer paired helical filaments, both Tau and MAP2 form filaments in vitro from disulfide-linked homodimers.	Disulfides	147-156	microtubule associated protein 2	Homo sapiens	113-117
10527895-3	1999	That the critical thiol lies within a domain needed for MT binding raised the question: Does disulfide formation block Tau-Tau or MAP2-MAP2 dimer binding to microtubules, thereby acting to divert dimers toward filament formation?	Disulfides	93-102	microtubule associated protein 2	Homo sapiens	130-134
8109324-9	1993	Introduction of a disulfide bridge into calmodulin, another member of the super-family of Ca(2+)-binding proteins to which TnC belongs, abolishes its interaction with target enzymes.	Disulfides	18-27	tenascin C	Homo sapiens	123-126
8424457-6	1993	Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting of proteins in the lavage pellet with antibodies to the carbohydrate-binding domain of proteinosis human SP-D demonstrated covalently cross-linked multimers of SP-D monomers (43 kd, reduced) and multimers of trimeric components stabilized by disulfide and non-disulfide bonds.	Disulfides	335-344	surfactant protein D	Homo sapiens	198-202
8424457-6	1993	Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting of proteins in the lavage pellet with antibodies to the carbohydrate-binding domain of proteinosis human SP-D demonstrated covalently cross-linked multimers of SP-D monomers (43 kd, reduced) and multimers of trimeric components stabilized by disulfide and non-disulfide bonds.	Disulfides	353-362	surfactant protein D	Homo sapiens	198-202
10527895-3	1999	That the critical thiol lies within a domain needed for MT binding raised the question: Does disulfide formation block Tau-Tau or MAP2-MAP2 dimer binding to microtubules, thereby acting to divert dimers toward filament formation?	Disulfides	93-102	microtubule associated protein 2	Homo sapiens	135-139
7520915-8	1994	However, the third disulfide bond varied considerably between the G-CSF and GH receptors.	Disulfides	19-28	colony stimulating factor 3	Homo sapiens	66-71
7520915-9	1994	Disruption of these disulfide bonds in the BN domain of the G-CSF receptor suggested that all of them are critical for maintaining a stably folded protein.	Disulfides	20-29	colony stimulating factor 3	Homo sapiens	60-65
8062245-0	1994	Introduction of a disulfide bond in the alpha 1 domain of the H-2Kb molecule confers immunogenicity to the transfected RMA-S tumors.	Disulfides	18-27	histocompatibility 2, K1, K region	Mus musculus	62-67
10368949-11	1999	The results are discussed within the context of differences in the three-dimensional structures of the ions that result from the presence or absence of the three disulfide linkages found in native BPTI.	Disulfides	162-171	spleen trypsin inhibitor I	Bos taurus	197-201
10329650-0	1999	The N-terminal disulfide linkages of human insulin-like growth factor-binding protein-6 (hIGFBP-6) and hIGFBP-1 are different as determined by mass spectrometry.	Disulfides	15-24	insulin like growth factor binding protein 6	Homo sapiens	43-87
10329650-0	1999	The N-terminal disulfide linkages of human insulin-like growth factor-binding protein-6 (hIGFBP-6) and hIGFBP-1 are different as determined by mass spectrometry.	Disulfides	15-24	insulin like growth factor binding protein 6	Homo sapiens	89-97
10329650-4	1999	The complete disulfide linkages of IGFBP-6 were determined using electrospray ionization mass spectrometry of purified tryptic peptide complexes digested with combinations of chymotrypsin, thermolysin, and endoproteinase Glu-C.	Disulfides	13-22	insulin like growth factor binding protein 6	Homo sapiens	35-42
10329650-5	1999	Numbering IGFBP-6 cysteines sequentially from the N terminus, the first three disulfide linkages are Cys1-Cys2, Cys3-Cys4, and Cys5-Cys6.	Disulfides	78-87	insulin like growth factor binding protein 6	Homo sapiens	10-17
10329650-9	1999	Analogous with IGFBP-3, IGFBP-5, and IGFBP-6, Cys9-Cys11 and Cys10-Cys12 of IGFBP-1 are also disulfide-linked.	Disulfides	93-102	insulin like growth factor binding protein 6	Homo sapiens	37-44
8318253-10	1993	Within this complex the binding protein monomers can be chemically cross-linked to opposite arms of the disulfide-linked TGF-beta 2 homodimer.	Disulfides	104-113	transforming growth factor beta 2	Homo sapiens	121-131
1401917-0	1992	Human pre-B and B cell membrane mu-chains are noncovalently associated with a disulfide-linked complex containing a product of the B29 gene.	Disulfides	78-87	prolactin regulatory element binding	Homo sapiens	6-11
7914908-1	1994	Two-dimensional gel electrophoresis of in vitro phosphorylated proteins coprecipitated by CD2 monoclonal antibody (mAb) from Brij58 lysates of resting human T lymphocytes and natural killer (NK) cells resulted in the identification of a novel 29/30-kD disulfide-linked dimer (pp29/30).	Disulfides	252-261	CD2 molecule	Homo sapiens	90-93
10350489-4	1999	Treatment of PTP1B with diamide and reduced glutathione or with only glutathione disulfide (GSSG) results in a modification detected by mass spectrometry in which the cysteine residues are oxidized to mixed disulfides with glutathione.	Disulfides	207-217	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	13-18
10350608-2	1999	We have shown that p70 exists predominantly as p45 and p40 fragments which are linked by disulfide bonds.	Disulfides	89-98	caspase 1	Rattus norvegicus	47-50
8202493-2	1994	Addition of the disulfide-bonded dimeric form of S100 beta to primary neuronal and glial cultures and established cell lines induces axonal extension and alterations in astrocyte proliferation and phenotype, but evidence that S100 beta exerts the same effects in vivo has not been presented.	Disulfides	16-25	S100 protein, beta polypeptide, neural	Mus musculus	49-58
10371151-2	1999	Referred to as minimized agouti related protein, MARP is a 46 residue polypeptide containing 10 Cys residues involved in five disulfide bonds that retains the biological activity of full length AGRP.	Disulfides	126-135	agouti related neuropeptide	Homo sapiens	25-47
1376686-7	1992	In the case of anti-(tPA4-8) cleavage of one-chain tPA to two-chain tPA and reduction of disulfide bonds exposed this epitope.	Disulfides	89-98	chromosome 20 open reading frame 181	Homo sapiens	21-24
8202493-2	1994	Addition of the disulfide-bonded dimeric form of S100 beta to primary neuronal and glial cultures and established cell lines induces axonal extension and alterations in astrocyte proliferation and phenotype, but evidence that S100 beta exerts the same effects in vivo has not been presented.	Disulfides	16-25	S100 protein, beta polypeptide, neural	Mus musculus	226-235
1377029-0	1992	Complete determination of disulfide bonds localized within the short consensus repeat units of decay accelerating factor (CD55 antigen).	Disulfides	26-35	CD55 molecule (Cromer blood group)	Homo sapiens	95-120
7514405-6	1994	The slow thiol-disulfide exchange reaction that irreversibly stabilizes noncovalent growth factor-alpha 2M-methylamine complexes was completely inhibited by modification of Cys-949.	Disulfides	15-24	alpha-2-macroglobulin	Homo sapiens	98-106
1377029-0	1992	Complete determination of disulfide bonds localized within the short consensus repeat units of decay accelerating factor (CD55 antigen).	Disulfides	26-35	CD55 molecule (Cromer blood group)	Homo sapiens	122-126
1377029-4	1992	To determine the disulfide-bonding pattern, we used the urine form of DAF.	Disulfides	17-26	CD55 molecule (Cromer blood group)	Homo sapiens	70-73
1377029-6	1992	Because all of the cysteine residues are disulfide-bonded, DAF should contain eight disulfide bonds.	Disulfides	41-50	CD55 molecule (Cromer blood group)	Homo sapiens	59-62
1377029-6	1992	Because all of the cysteine residues are disulfide-bonded, DAF should contain eight disulfide bonds.	Disulfides	84-93	CD55 molecule (Cromer blood group)	Homo sapiens	59-62
1377029-8	1992	From sequence analyses of these peptides, we could identify all disulfide bonds in the 4 SCR units of DAF as being between the first and the third and between the second and the fourth half-cystines within each SCR unit.	Disulfides	64-73	CD55 molecule (Cromer blood group)	Homo sapiens	102-105
10320325-6	1999	Structural investigations with a HCC-2 mutant prove that a third additional disulfide bond present in wild-type HCC-2 is not necessary for maintaining the relative orientation of the helix and the beta-sheet.	Disulfides	76-85	C-C motif chemokine ligand 15	Homo sapiens	112-117
10225957-7	1999	Electronmicroscopic and electrophoretic analysis of a secreted form of the extracellular domain of Ten-m1 showed that Ten-m1 is a disulfide-linked dimer and that the dimerization is mediated by EGF-like modules 2 and 5 which contain an odd number of cysteines.	Disulfides	130-139	teneurin transmembrane protein 1	Mus musculus	99-105
7510283-1	1994	Site-specific incorporation of synthetic peptides that mimic the 64-74 disulfide loop of granulocyte colony-stimulating factor.	Disulfides	71-80	colony stimulating factor 3	Homo sapiens	89-126
10225957-7	1999	Electronmicroscopic and electrophoretic analysis of a secreted form of the extracellular domain of Ten-m1 showed that Ten-m1 is a disulfide-linked dimer and that the dimerization is mediated by EGF-like modules 2 and 5 which contain an odd number of cysteines.	Disulfides	130-139	teneurin transmembrane protein 1	Mus musculus	118-124
1618297-0	1992	A modified Kex2 enzyme retained in the endoplasmic reticulum prevents disulfide-linked dimerisation of recombinant human insulin-like growth factor-1 secreted from yeast.	Disulfides	70-79	kexin KEX2	Saccharomyces cerevisiae S288C	11-15
1618297-5	1992	We find that co-expression of a novel ER-retained Kex2p variant, soluble Kex2pHDEL, can prevent intermolecular disulfide bond formation between two IGF1 molecules, implying that the presence of the proregion during the folding of IGF1 in the ER could be a reason for disulfide-linked dimerisation.	Disulfides	111-120	kexin KEX2	Saccharomyces cerevisiae S288C	50-55
7510283-9	1994	We illustrate the particularity of this concept by the engineered modifications of the 64-74 disulfide loop region of human granulocyte colony-stimulating factor.	Disulfides	93-102	colony stimulating factor 3	Homo sapiens	124-161
1618297-5	1992	We find that co-expression of a novel ER-retained Kex2p variant, soluble Kex2pHDEL, can prevent intermolecular disulfide bond formation between two IGF1 molecules, implying that the presence of the proregion during the folding of IGF1 in the ER could be a reason for disulfide-linked dimerisation.	Disulfides	267-276	kexin KEX2	Saccharomyces cerevisiae S288C	50-55
10200021-2	1999	beta-Lactoglobulin has 2 intramolecular disulfide bonds that may be responsible for its allergic effects.	Disulfides	40-49	beta-lactoglobulin	Bos taurus	0-18
10200021-3	1999	OBJECTIVE: This study was carried out to assess the importance of disulfide bonds to the allergenicity and digestibility of beta-lactoglobulin.	Disulfides	66-75	beta-lactoglobulin	Bos taurus	124-142
8120034-7	1994	Mutants Ala184, Ala184,190, and Ala184,191 displayed high affinity and DTT sensitivity, indicating that a solvent-accessible disulfide bond(s) is present in these mutant receptors as in the wild-type beta 2-AR.	Disulfides	125-134	beta-2 adrenergic receptor	Cricetulus griseus	200-209
10200021-7	1999	RESULTS: As found for other proteins with intramolecular disulfide bonds, beta-lactoglobulin was reduced specifically by the thioredoxin system.	Disulfides	57-66	beta-lactoglobulin	Bos taurus	74-92
10200021-8	1999	After reduction of one or both of its disulfide bonds, beta-lactoglobulin became strikingly sensitive to pepsin and lost allergenicity as determined by skin test responses and gastrointestinal symptoms in the dog model.	Disulfides	38-47	beta-lactoglobulin	Bos taurus	55-73
8120034-9	1994	These studies indicate that the covalent linkage between loops 1 and 2 of the beta 2-AR extracellular domains involves the formation of disulfide bonds, uniquely between Cys106 and Cys191, and Cys184 and Cys190, and is, thus, distinct from that of other G-protein-coupled receptors.	Disulfides	136-145	beta-2 adrenergic receptor	Cricetulus griseus	78-87
7509297-3	1994	C949S alpha 2M behaves like methylamine-treated plasma alpha 2M, with correctly formed inter-subunit disulfide bridges, non-covalent association of covalent dimers to form tetramers, and exposure of the receptor binding domain, but an inability to inhibit proteinases, and inaccessibility of the bait regions to proteolysis.	Disulfides	101-110	alpha-2-macroglobulin	Homo sapiens	6-14
10068459-3	1999	Proteolytic cleavage of pro-MSP at a single site yields active MSP, a disulfide-linked alphabeta-chain heterodimer.	Disulfides	70-79	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	28-31
10068459-3	1999	Proteolytic cleavage of pro-MSP at a single site yields active MSP, a disulfide-linked alphabeta-chain heterodimer.	Disulfides	70-79	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	63-66
7909462-2	1994	The formation of disulfide bridges is facilitated by the thiol-disulfide oxidoreductases, protein disulfide isomerase (PDI) in eukaryotes and dsbA in prokaryotes.	Disulfides	17-26	protein-disulfide isomerase	Escherichia coli	90-117
10068459-4	1999	However cleavage of recombinant pro-MSP yielded not only the disulfide-linked heterodimer, but also free alpha- and beta-chains, indicating that some of the recombinant molecules lacked an alphabeta-chain disulfide.	Disulfides	61-70	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	36-39
10068459-4	1999	However cleavage of recombinant pro-MSP yielded not only the disulfide-linked heterodimer, but also free alpha- and beta-chains, indicating that some of the recombinant molecules lacked an alphabeta-chain disulfide.	Disulfides	205-214	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	36-39
10052357-2	1999	Its three components-GroEL minichaperone (191-345), which can prevent protein aggregation; DsbA, which catalyzes the shuffling and oxidative formation of disulfide bonds; and peptidyl-prolyl isomerase-were immobilized on an agarose gel.	Disulfides	154-163	heat shock protein family D (Hsp60) member 1	Homo sapiens	21-26
1577825-2	1992	These cells synthesized and expressed on the plasma membrane high amounts of CD8 in a homodimeric form stabilized by a disulfide bridge.	Disulfides	119-128	CD8a molecule	Homo sapiens	77-80
1578187-0	1992	Engineered disulfide bond greatly increases specific activity of recombinant murine interferon-beta.	Disulfides	11-20	interferon beta 1, fibroblast	Mus musculus	84-99
7909462-2	1994	The formation of disulfide bridges is facilitated by the thiol-disulfide oxidoreductases, protein disulfide isomerase (PDI) in eukaryotes and dsbA in prokaryotes.	Disulfides	17-26	protein-disulfide isomerase	Escherichia coli	119-122
7909462-5	1994	The analysis of structure-function relationships of PDI and dsbA have indicated that these thiol-disulfide oxidoreductases act as protein oxidants to facilitate the formation of disulfides during the folding process.	Disulfides	178-188	protein-disulfide isomerase	Escherichia coli	52-55
9878372-8	1998	In contrast with the wild-type protein, reducing the disulfide in Y35G BPTI significantly decreased the number of backbone amides displaying large R2 rates.	Disulfides	53-62	spleen trypsin inhibitor I	Bos taurus	71-75
7909462-6	1994	The ability of PDI and dsbA to catalyze the formation and/or isomerization of disulfide bridging establishes their usefulness in facilitating the in vitro and in vivo folding of proteins.	Disulfides	78-87	protein-disulfide isomerase	Escherichia coli	15-18
8011288-4	1994	Components of this disulfide linked heterodimeric complex, Ig-alpha and Ig-beta, contain an approximately 26 residue sequence motif termed ARH1, also known as TAM, which binds to cytoplasmic effectors, including src-family tyrosine kinases, and contains all structural information needed for signal transduction.	Disulfides	19-28	CD79b molecule	Homo sapiens	72-79
9826515-3	1998	Taking advantage of the high stability of the diselenide group toward reducing agents for disulfides a regioselective disulfide bridging of the second cysteine pair allowed for straightforward preparation of the [Sec3,Sec11, Nle7]-endothelin-1.	Disulfides	90-100	exocyst complex component 1	Homo sapiens	213-217
9826515-3	1998	Taking advantage of the high stability of the diselenide group toward reducing agents for disulfides a regioselective disulfide bridging of the second cysteine pair allowed for straightforward preparation of the [Sec3,Sec11, Nle7]-endothelin-1.	Disulfides	90-99	exocyst complex component 1	Homo sapiens	213-217
1409008-5	1992	[125I]-Rat ANF(99-126) binding was competitively displaced by unlabeled ANF analogues with an intact disulfide bridge showing a lower affinity than the iodinated ligand.	Disulfides	101-110	natriuretic peptide A	Rattus norvegicus	11-14
1409008-5	1992	[125I]-Rat ANF(99-126) binding was competitively displaced by unlabeled ANF analogues with an intact disulfide bridge showing a lower affinity than the iodinated ligand.	Disulfides	101-110	natriuretic peptide A	Rattus norvegicus	72-75
7508463-1	1994	BACKGROUND: The major cat allergen Fel d I is composed of two disulfide-linked polypeptide chains, chain 1 (70 amino acid residues) and chain 2 (92 amino acid residues).	Disulfides	62-71	major allergen I polypeptide chain 2	Felis catus	35-42
1737006-9	1992	The results suggest that in the folding of apamin, the one-disulfide intermediate containing the C-3 to C-15 disulfide bond, as in Apa-2, is favored slightly.	Disulfides	59-68	complement C3	Homo sapiens	97-100
1737006-9	1992	The results suggest that in the folding of apamin, the one-disulfide intermediate containing the C-3 to C-15 disulfide bond, as in Apa-2, is favored slightly.	Disulfides	109-118	complement C3	Homo sapiens	97-100
9836577-4	1998	The overall structure of NT-3 resembles that of the other neurotrophins, NGF and BDNF; each protomer forms a twisted four-stranded beta sheet, with three intertwined disulfide bonds.	Disulfides	166-175	neurotrophin 3	Homo sapiens	25-29
8309347-5	1994	TGF alpha-PE38, which has one of the two disulfide pairs of PE40, inhibited amino acid uptake with ED50 values of 3-50 ng/ml whereas TGF alpha-PE40Asp553, which lacks ADP ribosylation activity, had an ED50 &gt; 100 ng/ml.	Disulfides	41-50	transforming growth factor alpha	Mus musculus	0-9
9819197-5	1998	A nearly full-length form of AGRP (MKd5-AGRP) was expressed in the cytosolic or soluble fraction of Escherichia coli and appeared as large intermolecular disulfide-bonded aggregates.	Disulfides	154-163	agouti related neuropeptide	Homo sapiens	29-33
9819197-5	1998	A nearly full-length form of AGRP (MKd5-AGRP) was expressed in the cytosolic or soluble fraction of Escherichia coli and appeared as large intermolecular disulfide-bonded aggregates.	Disulfides	154-163	agouti related neuropeptide	Homo sapiens	40-44
9819197-9	1998	Mobility shifts observed using SDS-PAGE under reducing and nonreducing conditions for bacterially expressed and mammalian expressed AGRP were identical, an indication of a similar disulfide structure.	Disulfides	180-189	agouti related neuropeptide	Homo sapiens	132-136
1748641-6	1991	Cleavage of prothrombin within a disulfide loop at Arg323-Ile324 leads to formation of meizothrombin with no loss of peptide material but with formation of amidolytic activity.	Disulfides	33-42	coagulation factor II, thrombin	Bos taurus	12-23
7937349-7	1994	Ala analogues of the Et isomeric disulfide arrangement (Cys1,11 and Cys3,15) were always less active than the corresponding analogues with the native disulfide pairings (Cys1,15 and Cys3,11).	Disulfides	33-42	cystin 1	Homo sapiens	56-60
7937349-7	1994	Ala analogues of the Et isomeric disulfide arrangement (Cys1,11 and Cys3,15) were always less active than the corresponding analogues with the native disulfide pairings (Cys1,15 and Cys3,11).	Disulfides	33-42	cystin 1	Homo sapiens	170-174
7937349-7	1994	Ala analogues of the Et isomeric disulfide arrangement (Cys1,11 and Cys3,15) were always less active than the corresponding analogues with the native disulfide pairings (Cys1,15 and Cys3,11).	Disulfides	150-159	cystin 1	Homo sapiens	56-60
7903251-5	1993	These cysteine residues in the putative extracellular domain of the NR1 subunit may form a disulfide bridge important for agonist interaction.	Disulfides	91-100	glutamate ionotropic receptor NMDA type subunit 1 L homeolog	Xenopus laevis	68-71
7925487-1	1993	Glutaredoxin catalyzes glutathione-dependent disulfide oxidoreduction reactions in a coupled system with NADPH, GSH and glutathione reductase and has an active site disulfide/dithiol with the sequence -Cys-Pro-Tyr-Cys-.	Disulfides	45-54	glutaredoxin-1	Bos taurus	0-12
1747162-1	1991	Recent evidence indicates that the transmembrane form of IgM on murine and human B lymphocytes is physically associated with at least two proteins, forming a disulfide-linked dimer, which may control cell surface expression of IgM and also play a role in signal transduction after Ag binding (by analogy with the TCR-associated CD3 components in T lymphocytes).	Disulfides	158-167	immunoglobulin heavy constant mu	Mus musculus	57-60
1747162-1	1991	Recent evidence indicates that the transmembrane form of IgM on murine and human B lymphocytes is physically associated with at least two proteins, forming a disulfide-linked dimer, which may control cell surface expression of IgM and also play a role in signal transduction after Ag binding (by analogy with the TCR-associated CD3 components in T lymphocytes).	Disulfides	158-167	immunoglobulin heavy constant mu	Mus musculus	227-230
7925487-1	1993	Glutaredoxin catalyzes glutathione-dependent disulfide oxidoreduction reactions in a coupled system with NADPH, GSH and glutathione reductase and has an active site disulfide/dithiol with the sequence -Cys-Pro-Tyr-Cys-.	Disulfides	165-174	glutaredoxin-1	Bos taurus	0-12
8226834-1	1993	Multiple disulfide bonds form in recombinant myosin light chain-2 mutants that contain an engineered cysteine at positions 2, 73, or 94, in addition to the endogenous cysteines at residues 126 and 155 (Saraswat, L.D., and Lowey, S. (1991) J. Biol.	Disulfides	9-18	myosin light chain 2	Homo sapiens	45-65
1779967-1	1991	The most widely held model for the human TSH receptor is of holoreceptor of 80 kDa with two subunits of approximately 50 and 30 kDa linked by disulfide bridges, with the former subunit containing the major hormone-binding site.	Disulfides	142-151	thyroid stimulating hormone receptor	Homo sapiens	41-53
8226834-7	1993	When the reconstituted myosin was reacted with 5,5"-dithiobis(2-nitrobenzoic acid) in the absence of divalent cations, intramolecular disulfide bonds formed in the mutant and wild type LCs, but the LCs did not remain bound to the myosin heavy chains.	Disulfides	134-143	myosin heavy chain 14	Homo sapiens	23-29
8226834-9	1993	Instead, mutants containing cysteines in the NH2-terminal domain formed intermolecular disulfide bonds between the two heads of myosin.	Disulfides	87-96	myosin heavy chain 14	Homo sapiens	128-134
7506556-2	1993	The epitope of this HuMAb was destroyed by reduction of gp120 disulfide bonds, but not by removal of N-linked carbohydrates.	Disulfides	62-71	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	56-61
1717078-7	1991	Western blots indicate that the binding site of LYP22 on GPIIa is disulfide bridge-dependent.	Disulfides	66-75	integrin subunit beta 1	Homo sapiens	57-62
8412327-8	1993	Cell surface staining of these cells showed the presence of CD3 molecules and of a TCR-beta chain corresponding to the normal beta allele expressed in a disulfide-linked complex with a protein which is not TCR-alpha, gamma, or delta.	Disulfides	153-162	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	83-91
8395501-0	1993	Direct identification of the primary nucleophile of thioredoxin f. Thioredoxin, by virtue of the proximal active-site sulfhydryls (Trp-Cys-Gly-Pro-Cys), catalyzes thiol-disulfide exchange with specific target enzymes.	Disulfides	169-178	thioredoxin	Homo sapiens	52-63
1856193-7	1991	The specific disulfide bridges, Cys-5 to Cys-59, Cys-15 to Cys-39, and Cys-33 to Cys-55, are analogous to those in the prototype Kunitz-type inhibitor, bovine pancreatic trypsin inhibitor (BPTI).	Disulfides	13-22	spleen trypsin inhibitor I	Bos taurus	189-193
1856193-8	1991	While treatment of BPTI with dithiothreitol rapidly and specifically reduced one disulfide bond, the reduction of disulfide bonds in rTAP proceeded at a slower rate and appeared to be nonspecific, reaching a maximum of two disulfides reduced.	Disulfides	81-90	spleen trypsin inhibitor I	Bos taurus	19-23
8395501-0	1993	Direct identification of the primary nucleophile of thioredoxin f. Thioredoxin, by virtue of the proximal active-site sulfhydryls (Trp-Cys-Gly-Pro-Cys), catalyzes thiol-disulfide exchange with specific target enzymes.	Disulfides	169-178	thioredoxin	Homo sapiens	67-78
8395501-6	1993	Therefore, in the normal thioredoxin-catalyzed reduction pathway, Cys-46 is the nucleophile required to attack the disulfide of the substrate and Cys-49 serves to cleave the mixed disulfide intermediate, thus allowing for the release of oxidized thioredoxin and the reduced target enzyme.	Disulfides	115-124	thioredoxin	Homo sapiens	25-36
8262907-8	1993	Our study shows that the disulfide-bond pairings of [-32-153]M-CSF that is expressed and post-translationally modified in mammalian cells are identical to those of Escherichia coli-derived [3-153]M-CSF with only one intermolecular disulfide bond, namely, Cys31-Cys31.	Disulfides	25-34	colony stimulating factor 1	Homo sapiens	61-66
8338847-2	1993	Thereby, as is known from comparing the three-dimensional (3D) structures of thioredoxin and glutaredoxin in the reduced and oxidized state, reduction of the disulfide bond is accompanied by minimal perturbation of the backbone folding of the active sites.	Disulfides	158-167	thioredoxin	Homo sapiens	77-88
1904772-1	1991	Extracellular carbonic anhydrase from the unicellular green alga Chlamydomonas reinhardtii is an oligomeric protein containing subunits of 36 and 4 kDa which are joined by disulfide bonds to form higher molecular mass oligomers.	Disulfides	172-181	uncharacterized protein	Chlamydomonas reinhardtii	14-32
1904772-7	1991	These results indicate that disulfide bonds are essential for maintenance of the oligomeric structure of Chlamydomonas reinhardtii carbonic anhydrase, and that the small subunit may be necessary for enhancing catalysis, but not for the binding of sulfonamides to the enzyme.	Disulfides	28-37	uncharacterized protein	Chlamydomonas reinhardtii	131-149
8338847-3	1993	In order to estimate the sequence-dependent intrinsic free energy of formation of the active-site disulfide loops in oxidoreductases, synthetic fragments corresponding to the sequences 31-38, 10-17, 134-141, and 34-41 of thioredoxin, glutaredoxin, thioredoxin reductase, and protein disulfide isomerase (PDI), respectively, were analyzed for their tendency to form 14-membered rings.	Disulfides	98-107	thioredoxin	Homo sapiens	221-232
8329391-2	1993	Reduction of the two active-site disulfides in PDI by NADPH and bovine thioredoxin reductase was not reversible by addition of excess NADP+, consistent with a redox potential (E0") above -200 mV.	Disulfides	33-43	peroxiredoxin 5	Bos taurus	71-92
8392223-8	1993	gamma delta TCR utilizing the C gamma 1 gene segment are disulfide-linked, whereas those utilizing the C gamma 2 gene segment are non-disulfide-linked.	Disulfides	57-66	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	12-15
7687098-1	1993	The major cat allergen Fel d I is a homodimer of which each monomer consists of two disulfide-linked polypeptide chains: chain 1 (70 amino acid residues) and chain 2 (92 amino acid residues).	Disulfides	84-93	major allergen I polypeptide chain 2	Felis catus	23-30
1713731-1	1991	Tenascin is an extracellular matrix glycoprotein consisting of six disulfide linked subunits with molecular masses of 190-250 kDa.	Disulfides	67-76	tenascin C	Homo sapiens	0-8
8387210-3	1993	This suggested that the disulfides of both macromolecules might be cleaved by a thiol-disulfide interchange reaction, possibly mediated by protein disulfide-isomerase (PDI, EC 5.3.4.1).	Disulfides	24-34	protein disulfide-isomerase	Cricetulus griseus	139-166
1881870-4	1991	All two-disulfide mutants of BPTI investigated thus far have two very slow folding reactions which have characteristics of proline isomerization.	Disulfides	8-17	spleen trypsin inhibitor I	Bos taurus	29-33
8387210-3	1993	This suggested that the disulfides of both macromolecules might be cleaved by a thiol-disulfide interchange reaction, possibly mediated by protein disulfide-isomerase (PDI, EC 5.3.4.1).	Disulfides	24-34	protein disulfide-isomerase	Cricetulus griseus	168-171
8387210-3	1993	This suggested that the disulfides of both macromolecules might be cleaved by a thiol-disulfide interchange reaction, possibly mediated by protein disulfide-isomerase (PDI, EC 5.3.4.1).	Disulfides	24-33	protein disulfide-isomerase	Cricetulus griseus	139-166
2403360-0	1990	Disulfide isoforms of recombinant glia maturation factor beta.	Disulfides	0-9	glia maturation factor beta	Homo sapiens	34-61
8387210-3	1993	This suggested that the disulfides of both macromolecules might be cleaved by a thiol-disulfide interchange reaction, possibly mediated by protein disulfide-isomerase (PDI, EC 5.3.4.1).	Disulfides	24-33	protein disulfide-isomerase	Cricetulus griseus	168-171
8387210-6	1993	This strongly suggests that the disulfide cleavage in the two membrane-bound macromolecules is mediated by PDI and that this enzyme, besides its known retention in the endoplasmic reticulum, must also be exposed at the plasma membrane.	Disulfides	32-41	protein disulfide-isomerase	Cricetulus griseus	107-110
8387210-7	1993	This paper points to other potentially important disulfide reductions that might be catalyzed by surface-associated PDI.	Disulfides	49-58	protein disulfide-isomerase	Cricetulus griseus	116-119
8466909-7	1993	The native structure of alpha-lactalbumin appears to be split by selective disulfide bond cleavage into at least one subdomain, which retains the Ca(2+)-binding site.	Disulfides	75-84	lactalbumin alpha	Bos taurus	24-41
8450210-2	1993	The B29 gene is specifically expressed in all cells of the B lymphocyte lineage, and the B29 protein is disulfide-linked to the protein product of at least one other gene, known as mb-1.	Disulfides	104-113	histocompatibility 2, M region locus 1	Mus musculus	181-185
1696913-1	1990	In circulating blood, vitronectin occurs in two forms: a single-chain (75 kDa) and an endogenously clipped two-chain form (65 kDa and 10 kDa) held together by a disulfide bridge.	Disulfides	161-170	vitronectin	Homo sapiens	22-33
8382632-1	1993	Bovine seminal ribonuclease, a uniquely dimeric pancreatic-like RNase, with its dimeric structure stabilized by two intersubunit disulfides, and endowed with special, i.e. non-catalytic, actions (antitumor, immunosuppressive, antispermatogenic), was stably expressed in Chinese hamster ovary cells.	Disulfides	129-139	seminal ribonuclease	Bos taurus	7-27
2171044-1	1990	The influence of gastrin alpha-amidation of the heavy-metal chelator diethyldithiocarbamate and disulfiram, its disulfide dimer, was studied in rat gastric antrum.	Disulfides	112-121	gastrin	Rattus norvegicus	17-24
7679287-4	1993	The other three antibodies bound the heavy chain of protein C: PC13 bound activation peptide, PC04 recognized the activation site and PC09 bound the region close to a disulfide bond connecting light and heavy chains.	Disulfides	167-176	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	52-61
2162106-2	1990	Analyses of these glycoproteins by chemical crosslinking and nonreducing/reducing two-dimensional electrophoresis showed that both gp55 and gp65 exist as monomer and disulfide-bonded dimer and trimer.	Disulfides	166-175	neuroplastin	Homo sapiens	140-144
8443602-6	1993	Peptide mapping and electrospray ionization mass spectrometry revealed that a folded monomeric species of M-CSF contained three of the four native disulfide bridges, and this folded monomer also showed some biological activity in a cell-based assay.	Disulfides	147-156	colony stimulating factor 1	Homo sapiens	106-111
2332434-0	1990	The disulfide structure of mouse lysosome-associated membrane protein 1.	Disulfides	4-13	lysosomal-associated membrane protein 1	Mus musculus	33-71
8443604-11	1993	To demonstrate the use of this method in simulating structures of proteins with nonhomologous disulfides, we construct a model of murine interleukin (IL)-4 using the NMR structure of human IL-4 as the template.	Disulfides	94-104	interleukin 4	Mus musculus	137-155
2332434-1	1990	The disulfide structure of mouse lysosome-associated membrane protein 1 has been determined by reverse-phase isolation and sequence analysis of the cysteine-containing tryptic fragments of the reduced and non-reduced deglycosylated protein.	Disulfides	4-13	lysosomal-associated membrane protein 1	Mus musculus	33-71
8443604-12	1993	The resulting geometry of the nonhomologous disulfide in the model structure for murine IL-4 is consistent with standard disulfide geometry.	Disulfides	44-53	interleukin 4	Mus musculus	88-92
8443604-12	1993	The resulting geometry of the nonhomologous disulfide in the model structure for murine IL-4 is consistent with standard disulfide geometry.	Disulfides	121-130	interleukin 4	Mus musculus	88-92
8422244-0	1993	The disulfide bond arrangement of leukemia inhibitory factor: homology to oncostatin M and structural implications.	Disulfides	4-13	leukemia inhibitory factor	Mus musculus	34-60
2189497-7	1990	The conversion of the Cys135-Cys140 disulfide in wild-type enzyme to the monothiol Cys140 in ACAA and the elevated pKa of Cys140 (6.7 vs 5.0 in wild type) have permitted detection of these intermediates at low pH (5.0).	Disulfides	36-45	acetyl-CoA acyltransferase 1	Homo sapiens	93-97
8422244-5	1993	The spatial organization of the cysteine residues in the predicted four alpha-helical bundle structure of LIF (Bazan, Neuron 7,197;1991) is compatible with these disulfide assignments.	Disulfides	162-171	leukemia inhibitory factor	Mus musculus	106-109
2159799-1	1990	Evidence is presented for a role of disulfide bridging in forming the ligand binding site of the beta 2-adrenergic receptor (beta AR).	Disulfides	36-45	adrenoceptor beta 2	Homo sapiens	97-123
8424686-0	1993	Modulation of glutathione S-transferase activity by a thiol/disulfide exchange reaction and involvement of thioltransferase.	Disulfides	60-69	glutathione S-transferase kappa 1	Homo sapiens	14-39
8424686-1	1993	Low concentrations of cystamine and cystine inactivated human placenta glutathione S-transferase (GST-pi) in cytosolic fraction very effectively, as did the purified enzyme, through the thiol/disulfide exchange reaction.	Disulfides	192-201	glutathione S-transferase kappa 1	Homo sapiens	71-96
8274532-2	1993	The turbidimetric assay of thioredoxin with insulin as the disulfide substrate was optimized; by incorporation of the lag time (tau) into the calculations, linearity was maintained for a wider range of thioredoxin concentrations, and a distinction could be made between reduced and non-reduced forms.	Disulfides	59-68	insulin	Bos taurus	44-51
7834494-7	1993	Concerning the second point, we studied the role of the single, highly conserved disulfide bond in chromogranin B on its sorting to secretory granules.	Disulfides	81-90	chromogranin B	Rattus norvegicus	99-113
2159799-1	1990	Evidence is presented for a role of disulfide bridging in forming the ligand binding site of the beta 2-adrenergic receptor (beta AR).	Disulfides	36-45	adrenoceptor beta 2	Homo sapiens	125-132
7834494-8	1993	We showed that reduction of this disulfide bond by incubation of intact PC12 cells with the membrane permeable thiol reducing agent dithiothreitol (DTT) causes the missorting of chromogranin B to the constitutive secretory pathway.	Disulfides	33-42	chromogranin B	Rattus norvegicus	178-192
29261001-5	2018	Upon N-end rule interaction with the Nt-Arg of arginylated HSPA5 (R-HSPA5), SQSTM1 undergoes self-polymerization via disulfide bonds of Cys residues including Cys113, facilitating cargo collection.	Disulfides	117-126	sequestosome 1	Homo sapiens	76-82
7834494-10	1993	We found that the effect of DTT on chromogranin B, which was already known to prevent disulfide bond formation in the endoplasmic reticulum, occurred in the TGN.	Disulfides	86-95	chromogranin B	Rattus norvegicus	35-49
7834494-11	1993	We concluded that the sorting, in the TGN, of chromogranin B to secretory granules is dependent upon the integrity of its disulfide bond and that DTT treatment in vivo is as valuable tool to study the post-endoplasmic reticulum traffic of disulfide bond containing proteins.	Disulfides	122-131	chromogranin B	Rattus norvegicus	46-60
7834494-11	1993	We concluded that the sorting, in the TGN, of chromogranin B to secretory granules is dependent upon the integrity of its disulfide bond and that DTT treatment in vivo is as valuable tool to study the post-endoplasmic reticulum traffic of disulfide bond containing proteins.	Disulfides	239-248	chromogranin B	Rattus norvegicus	46-60
10343777-1	1998	OBJECTIVE: Cartilage oligomeric matrix protein (COMP) is a large disulfide-linked pentameric protein.	Disulfides	65-74	cartilage oligomeric matrix protein	Homo sapiens	11-46
8417119-5	1993	It has been shown that 1) the difference between these two types of the IgG2a proteins is whether the two L chains are linked by a disulfide bridge or not, and 2) C1q-binding and complement-activating activities are expressed only when the inter L chain disulfide bridge does not exist.	Disulfides	254-263	complement C1q A chain	Homo sapiens	163-166
10343777-1	1998	OBJECTIVE: Cartilage oligomeric matrix protein (COMP) is a large disulfide-linked pentameric protein.	Disulfides	65-74	cartilage oligomeric matrix protein	Homo sapiens	48-52
9842726-4	1998	Concerning the PPO tertiary structure, denaturing conditions (combinations of boiling and reducing agent) used on SDS-PAGE have shown (i) a compact tertiary structure and (ii) the presence of disulfide bonds in PPOr, accounting for the shift between 27 and 41 kDa, and 41 and 42 kDa, respectively.	Disulfides	192-201	polyphenol oxidase, chloroplastic	Malus domestica	15-18
34742736-8	2021	The WFA-ZAP70 interaction was disrupted by a disulfide reducing agent dithiothreitol, suggesting an involvement of cysteine covalent binding interface.	Disulfides	45-54	zeta chain of T cell receptor associated protein kinase 70	Homo sapiens	8-13
1282887-3	1992	[Arg33, Lys39]IGF II was expressed in NIH-3T3 cells as a processed two-chain peptide with a deletion of amino acid residues 37-40 and crosslinked by three disulfide bonds.	Disulfides	155-164	insulin-like growth factor 2	Mus musculus	14-20
34455077-3	2021	The thioredoxin system, comprised of TrxR Trx and NADPH, exerts its activities via a disulfide-dithiol exchange reaction.	Disulfides	85-94	2,4-dienoyl-CoA reductase 1	Homo sapiens	50-55
9820620-6	1998	This mRNA encodes a putative 25 K protein of 219 amino acids in length, having the first 124 amino acids and, thus, two and a half structural alpha-helices in common with hGH-V.hGH-Vdelta4 has lost the N-glycosylation site at Asn 140 of hGH-V, but acquires a novel site at position 148 as well as a cystein-rich domain in the 65 carboxyl-terminal amino acids, potentially involved in multiple disulfide-bridge formation.	Disulfides	393-402	growth hormone 2	Homo sapiens	177-182
1461372-7	1992	These results are compatible with the existence of a hydrophobic segment present both on salt-soluble and detergent-soluble 11 S AChE as well as on the minor forms 4 S and 7 S. This segment is not linked to the catalytic subunits by disulfide bounds in contrast to the 20 kD non-catalytic subunit described by Inestrosa et al.	Disulfides	233-242	acetylcholinesterase	Rattus norvegicus	129-133
9932650-0	1998	The sulfonylurea-inhibited NADH oxidase activity of HeLa cell plasma membranes has properties of a protein disulfide-thiol oxidoreductase with protein disulfide-thiol interchange activity.	Disulfides	107-116	thioredoxin reductase 1	Homo sapiens	123-137
34791819-4	2021	Our explanation for this behavior is that, when BST2 gets in contact with Zn bound to the orf7a Cys15 ligand, it has the ability of displacing the metal owing to the creation of a new disulfide bridge across the two proteins.	Disulfides	184-193	bone marrow stromal cell antigen 2	Homo sapiens	48-52
1455231-2	1992	The biologically active form of M-CSF is a disulfide-linked dimer that activates an intrinsic tyrosine kinase activity on the M-CSF receptor by inducing dimerization of the receptor molecules.	Disulfides	43-52	colony stimulating factor 1	Homo sapiens	32-37
34674683-9	2021	The N-SH2 domain of SHP-2 as a protein chaperone may be potentially favorable to produce other proteins with disulfide bonds.	Disulfides	109-118	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	20-25
9758748-0	1998	Recombinant human retinol-binding protein refolding, native disulfide formation, and characterization.	Disulfides	60-69	retinol binding protein 4	Homo sapiens	18-41
1455231-2	1992	The biologically active form of M-CSF is a disulfide-linked dimer that activates an intrinsic tyrosine kinase activity on the M-CSF receptor by inducing dimerization of the receptor molecules.	Disulfides	43-52	colony stimulating factor 1	Homo sapiens	126-131
34619770-2	2022	To date, only 6 variants causing PT-VWD have been described, 5 in the C-terminal disulfide loop of the VWF-binding domain of GPIbalpha and 1 in the macroglycopeptide.	Disulfides	81-90	glycoprotein Ib platelet subunit alpha	Homo sapiens	125-140
1455231-3	1992	The structure of a recombinant human M-CSF dimer, determined at 2.5 angstroms by x-ray crystallography, contains two bundles of four alpha helices laid end-to-end, with an interchain disulfide bond.	Disulfides	183-192	colony stimulating factor 1	Homo sapiens	37-42
34619770-3	2022	GoF GP1BA variants generate a high affinity conformation of the C-terminal disulfide loop with a consequent allosteric conformational change on another region of GPIbalpha, the leucine-rich-repeat (LRR) domain.	Disulfides	75-84	glycoprotein Ib platelet subunit alpha	Homo sapiens	4-9
34619770-3	2022	GoF GP1BA variants generate a high affinity conformation of the C-terminal disulfide loop with a consequent allosteric conformational change on another region of GPIbalpha, the leucine-rich-repeat (LRR) domain.	Disulfides	75-84	glycoprotein Ib platelet subunit alpha	Homo sapiens	162-171
9739164-2	1998	In previous studies we have shown that a disulfide stabilized multimeric form of vitronectin is endocytosed and degraded by fibroblast cells (T.S.	Disulfides	41-50	vitronectin	Homo sapiens	81-92
9739164-13	1998	The preparation of multimeric vitronectin used in these earlier studies was in the form of high molecular weight disulfide-bonded aggregates which were stable in sodium dodecyl sulfate (SDS).	Disulfides	113-122	vitronectin	Homo sapiens	30-41
9739164-15	1998	The resulting protein migrated as a 65/75 kDa protein on SDS gels in the absence of reducing agent, confirming that this form of vitronectin was no longer stabilized into disulfide-bonded aggregates.	Disulfides	171-180	vitronectin	Homo sapiens	129-140
1384932-1	1992	Two extracellular matrix proteins of brain tissue, neuronectin (NEC1) and cytotactin (CT), are disulfide-bonded multimers of M(r) 180,000-250,000 subunits.	Disulfides	95-104	proprotein convertase subtilisin/kexin type 1	Homo sapiens	64-68
1644829-11	1992	Native procathepsin E is a dimer, consisting of two monomers covalently bound by a disulfide bridge between 2 Cys37.	Disulfides	83-92	cathepsin E	Cavia porcellus	7-21
9751809-3	1998	MOX maintains many of the structural features of DBH, as evidenced by the retention of most of the disulfide linkages and all of the peptidyl ligands to the active site copper atoms.	Disulfides	99-108	monooxygenase, DBH-like 1	Mus musculus	0-3
9751237-1	1998	Protein disulfide isomerase (PDI) is an enzyme that participates in the formation of disulfide bonds.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	29-32
34619770-8	2022	Hydrogen-deuterium exchange mass spectrometryshowed that p.Arg127Gln of LRR, while having little effect on the dynamics of the LRR locally, enhances the conformational dynamics of the GPIbalpha C-terminal disulfide loop structure.	Disulfides	205-214	glycoprotein Ib platelet subunit alpha	Homo sapiens	184-193
34619770-9	2022	Our data demonstrate for the first time that GoF variants outside the GPIbalpha C-terminal disulfide loop may be pathogenic and that aminoacidic changes in the LRR may cause allosterically conformational changes in the C-terminal disulfide loop of GPIbalpha inducing a conformation with high affinity for VWF.	Disulfides	91-100	glycoprotein Ib platelet subunit alpha	Homo sapiens	70-79
34619770-9	2022	Our data demonstrate for the first time that GoF variants outside the GPIbalpha C-terminal disulfide loop may be pathogenic and that aminoacidic changes in the LRR may cause allosterically conformational changes in the C-terminal disulfide loop of GPIbalpha inducing a conformation with high affinity for VWF.	Disulfides	230-239	glycoprotein Ib platelet subunit alpha	Homo sapiens	248-257
1412217-8	1992	The 40 kDa form is a heterodimer of TFPI in covalent disulfide linkage to human apolipoprotein AII.	Disulfides	53-62	apolipoprotein A2	Homo sapiens	80-98
9712916-10	1998	Since UG is a homodimer in which the 70 amino acid subunits are connected by two disulfide bonds, we sought to determine whether UG monomers also interact with the 190-kDa UG-binding protein and if so, whether it has the same biological activity as the dimer.	Disulfides	81-90	secretoglobin, family 1A, member 1 (uteroglobin)	Mus musculus	6-8
1385238-8	1992	The results from immunoblots, enzyme digestions and DEAE-Sephacell binding studies suggest that the unreduced MT2 antigen is a large protein composed of subunits which are connected by disulfide bonds.	Disulfides	185-194	metallothionein 2A	Homo sapiens	110-113
34509915-0	2021	A thiol redox sensor in soluble epoxide hydrolase enables oxidative activation by intra-protein disulfide bond formation.	Disulfides	96-105	epoxide hydrolase 2, cytoplasmic	Mus musculus	24-49
9753780-9	1998	TCH4 is shown to have at least one disulfide bond as monitored by a mobility shift in SDS-PAGE in the presence of dithiothreitol (DTT).	Disulfides	35-44	Xyloglucan endotransglucosylase/hydrolase family protein	Arabidopsis thaliana	0-4
1632791-0	1992	The cysteine residues in the carboxy terminal domain of tropoelastin form an intrachain disulfide bond that stabilizes a loop structure and positively charged pocket.	Disulfides	88-97	elastin	Bos taurus	56-68
1632791-1	1992	Analysis of purified bovine tropoelastin with Ellman"s reagent and [14C]iodoacetamide demonstrated that the only two cysteine residues in the molecule form an intrachain disulfide bond.	Disulfides	170-179	elastin	Bos taurus	28-40
34403458-3	2021	Here we find that PTB presents as dimer and monomer in nucleus and cytoplasm respectively, and a disulfide bond involving Cysteine 23 is critical for the dimerization of PTB.	Disulfides	97-106	polypyrimidine tract binding protein 1	Homo sapiens	18-21
9624150-9	1998	These appeared to represent disulfide-bonded multimeric polypeptide forms that resolved upon reduction into 85-95-kDa bands that are likely to represent a mixture of splice forms of monomeric type XIII collagen chains.	Disulfides	28-37	collagen, type XIII, alpha 1	Mus musculus	192-210
1350784-9	1992	The data strongly suggest that hemin regulates eIF-2 alpha kinase activity by promoting formation of the inactive dimer HCI.p87 via disulfide bonds and direct binding of hemin.	Disulfides	132-141	eukaryotic translation initiation factor 2A	Oryctolagus cuniculus	47-58
9622502-2	1998	GCAP-II consists of 24 amino acid residues and contains two disulfide bridges.	Disulfides	60-69	guanylate cyclase activator 2B	Homo sapiens	0-7
9622502-3	1998	The correct disulfide paring of GCAP-II is an absolute requirement for its biological activity.	Disulfides	12-21	guanylate cyclase activator 2B	Homo sapiens	32-39
9603915-2	1998	Here, we examined and compared the disulfide linkage status of newly synthesized TCR proteins in murine CD4(+)CD8(+) thymocytes and splenic T cells.	Disulfides	35-44	CD4 antigen	Mus musculus	104-107
34403458-3	2021	Here we find that PTB presents as dimer and monomer in nucleus and cytoplasm respectively, and a disulfide bond involving Cysteine 23 is critical for the dimerization of PTB.	Disulfides	97-106	polypyrimidine tract binding protein 1	Homo sapiens	170-173
34573121-3	2021	Herein, we show that oxidation induces the disulfide bond formation between Cys252 and Cys255 in the CXXC motif, thus stimulating the H2S-producing activity of CSE.	Disulfides	43-52	cystathionine gamma-lyase	Homo sapiens	160-163
1316788-8	1992	These findings suggest that homocysteine directly inhibited the cofactor activity of thrombomodulin on endothelial cells by reducing the disulfide-bond rich epidermal growth factor-like structures of thrombomodulin.	Disulfides	137-146	thrombomodulin	Homo sapiens	85-99
34573121-5	2021	Molecular dynamics and molecular docking suggest that the disulfide bond formation induces the conformational change in the active site of CSE and consequently increases the affinity of the enzyme for the substrate L-cysteine.	Disulfides	58-67	cystathionine gamma-lyase	Homo sapiens	139-142
34341191-4	2021	Using fluorescence polarization, isothermal titration calorimetry and X-ray crystallography, it is shown that synthetic peptides containing either phosphorylated Thr869 or Ser542 can indeed interact with 14-3-3, with the latter capable of forming an interprotein disulfide bond with 14-3-3sigma: a hitherto unreported phenomenon.	Disulfides	263-272	tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein theta	Homo sapiens	204-210
9603915-3	1998	These studies demonstrate that CD3delta proteins exist as both monomeric and oligomeric (disulfide-linked) species that differentially assemble with CD3epsilon subunits in CD4(+)CD8(+) thymocytes and splenic T cells.	Disulfides	89-98	CD4 antigen	Mus musculus	172-175
9609684-13	1998	The presence of a disulfide bridge between the OBPp beta- and alpha-domains (cysteines 63 and 155) may lock the resulting fold in a nonswapped monomeric conformation.	Disulfides	18-27	odorant-binding protein	Bos taurus	47-51
9572875-0	1998	Identification of O-glycosylation sites and partial characterization of carbohydrate structure and disulfide linkages of human insulin-like growth factor binding protein 6.	Disulfides	99-108	insulin like growth factor binding protein 6	Homo sapiens	127-171
9572875-8	1998	Native disulfide bond positions in IGFBP-6 were localized by means of observed disulfide-linked tryptic fragments, revealing that there are two disulfide-linked subdomains within each of the N- and C-terminal regions and confirming a previous suggestion that the latter regions are not interconnected.	Disulfides	7-16	insulin like growth factor binding protein 6	Homo sapiens	35-42
1316788-8	1992	These findings suggest that homocysteine directly inhibited the cofactor activity of thrombomodulin on endothelial cells by reducing the disulfide-bond rich epidermal growth factor-like structures of thrombomodulin.	Disulfides	137-146	thrombomodulin	Homo sapiens	200-214
9572875-8	1998	Native disulfide bond positions in IGFBP-6 were localized by means of observed disulfide-linked tryptic fragments, revealing that there are two disulfide-linked subdomains within each of the N- and C-terminal regions and confirming a previous suggestion that the latter regions are not interconnected.	Disulfides	79-88	insulin like growth factor binding protein 6	Homo sapiens	35-42
1610568-5	1992	Although both rom-1 and peripherin form disulfide-linked dimers, they do not form heterodimers with each other, but appear to associate noncovalently.	Disulfides	40-49	peripherin	Homo sapiens	24-34
9572875-8	1998	Native disulfide bond positions in IGFBP-6 were localized by means of observed disulfide-linked tryptic fragments, revealing that there are two disulfide-linked subdomains within each of the N- and C-terminal regions and confirming a previous suggestion that the latter regions are not interconnected.	Disulfides	79-88	insulin like growth factor binding protein 6	Homo sapiens	35-42
1599934-3	1992	The antimicrobial sequence was found to consist mainly of a loop of 18 amino acid residues formed by a disulfide bond between cysteine residues 20 and 37 of human lactoferrin, or 19 and 36 of bovine lactoferrin.	Disulfides	103-112	lactotransferrin	Bos taurus	163-174
9585486-2	1998	Previous in vitro investigations have demonstrated the ability of CS2 to cross-link proteins through thiourea, dithiocarbamate ester, and disulfide structures.	Disulfides	138-147	calsyntenin 2	Rattus norvegicus	66-69
9535854-1	1998	Identification of a novel disulfide-cross-linked network of alpha3, alpha4, and alpha5 chains of type IV collagen and its implications for the pathogenesis of Alport syndrome.	Disulfides	26-35	immunoglobulin binding protein 1	Homo sapiens	60-86
34208101-4	2021	In vitro experiments with disulfide-HMGB1 in primary neuro-glial cell cultures of the area postrema (AP), a circumventricular organ with a leaky blood-brain barrier and direct access to circulating mediators like HMGB1 and LPS, were performed to determine the direct influence of HMGB1 on this pivotal brain structure for immune-to-brain communication.	Disulfides	26-35	high mobility group box 1	Rattus norvegicus	36-41
34208101-7	2021	Moreover, disulfide-HMGB1 stimulation induced nuclear factor (NF)-kappaB activation and a significant release of interleukin-6, but not tumor necrosis factor alpha, into AP culture supernatants.	Disulfides	10-19	high mobility group box 1	Rattus norvegicus	20-25
1581300-3	1992	This structure is stabilized by two disulfide bonds connecting Cys-1 to Cys-11 and Cys-3 to Cys-15.	Disulfides	36-45	cystin 1	Homo sapiens	63-68
35477858-11	2022	When inter-protein hydrogen bonds were disrupted under wet conditions, disulfide labelling occurred in the head domains of type II keratins, likely affecting keratin-KAP interactions, and tail domains of the type I keratins, likely affecting keratin-keratin interactions.	Disulfides	71-80	cyclin dependent kinase inhibitor 3	Homo sapiens	166-169
9602168-3	1998	Previous studies have shown that LTBP-1 binds the small latent TGF-beta 1 complex through a disulfide bond between an 8-cysteine structural motif of LTBP-1 (TGF-bp repeat) and the propeptide dimer of latent TGF-beta 1 (TGF-beta 1 latency associated peptide).	Disulfides	92-101	latent transforming growth factor beta binding protein 1	Mus musculus	33-39
9602168-3	1998	Previous studies have shown that LTBP-1 binds the small latent TGF-beta 1 complex through a disulfide bond between an 8-cysteine structural motif of LTBP-1 (TGF-bp repeat) and the propeptide dimer of latent TGF-beta 1 (TGF-beta 1 latency associated peptide).	Disulfides	92-101	latent transforming growth factor beta binding protein 1	Mus musculus	149-155
1374379-10	1992	Recombinant human granulocyte colony stimulating factor lacking either disulfide bond or both has overall secondary and tertiary structures different from those of the wild type molecule and exhibits lower biological activity.	Disulfides	71-80	colony stimulating factor 3	Homo sapiens	18-55
9790257-8	1998	The G370C mutation introduces an unpaired cysteine residue in the extracellular domain of FGFR3, which may result in formation of an intermolecular disulfide bond between two mutant FGFR3 monomers and their constitutive activation.	Disulfides	148-157	fibroblast growth factor receptor 3	Homo sapiens	90-95
9790257-8	1998	The G370C mutation introduces an unpaired cysteine residue in the extracellular domain of FGFR3, which may result in formation of an intermolecular disulfide bond between two mutant FGFR3 monomers and their constitutive activation.	Disulfides	148-157	fibroblast growth factor receptor 3	Homo sapiens	182-187
35430336-5	2022	Here, we designed a robust and CD44-specific GEM nanotherapeutics by encapsulating hydrophobic phosphorylated gemcitabine prodrug (HPG) into the core of A6 peptide-functionalized disulfide-crosslinked micelles (A6-mHPG), which exhibited reduction-triggered HPG release and specific targetability to CD44 overexpressing tumor cells.	Disulfides	179-188	CD44 molecule (Indian blood group)	Homo sapiens	31-35
35430336-5	2022	Here, we designed a robust and CD44-specific GEM nanotherapeutics by encapsulating hydrophobic phosphorylated gemcitabine prodrug (HPG) into the core of A6 peptide-functionalized disulfide-crosslinked micelles (A6-mHPG), which exhibited reduction-triggered HPG release and specific targetability to CD44 overexpressing tumor cells.	Disulfides	179-188	CD44 molecule (Indian blood group)	Homo sapiens	299-303
35430336-10	2022	Here, we report on CD44-targeting GEM nanotherapeutics obtained by encapsulating hydrophobic phosphorylated GEM prodrug (HPG), a single isomer of NUC-1031, into A6 peptide-functionalized disulfide-crosslinked micelles (A6-mHPG).	Disulfides	187-196	CD44 molecule (Indian blood group)	Homo sapiens	19-23
1532255-2	1992	We tested whether effective lysosomal targeting of the human enzyme beta-N-acetylhexosaminidase A (Hex A; beta-N-acetyl-D-hexosaminide N-acetylhexosaminohydrolase, EC 3.2.1.52) can be obtained by coupling it via disulfide linkage to the atoxic fragment C of tetanus toxin (TTC) that is bound avidly by neuronal membrane.	Disulfides	212-221	hexosaminidase subunit alpha	Homo sapiens	99-104
35613580-5	2022	We further demonstrate that Rad6 and its human homolog UBE2A are redox regulated by forming a reversible disulfide with the E1 ubiquitin-activating enzyme (Uba1).	Disulfides	105-114	ubiquitin conjugating enzyme E2 A	Homo sapiens	55-60
35587260-6	2022	We also observed that the disulfide of native PTPN22 can be directly reduced by the thioredoxin system, while the C129S mutant lacking this disulfide was less amenable to reductive reactivation.	Disulfides	26-35	thioredoxin 1	Mus musculus	84-95
35471205-0	2022	Structural and functional regulations by a disulfide bond designed in myoglobin like human neuroglobin.	Disulfides	43-52	neuroglobin	Homo sapiens	91-102
35471205-2	2022	This study shows the successful design of a disulfide bond with suitable positions in globins, conferring a structure and function like those of the native human neuroglobin.	Disulfides	44-53	neuroglobin	Homo sapiens	162-173
9497358-8	1998	In contrast to TPx, in which one of the two conserved cysteines is oxidized to Cys-SOH and then immediately reacts with the second conserved cysteine of the second subunit of the enzyme homodimer to form an intermolecular disulfide, the Cys-SOH of 1-Cys Prx does not form a disulfide.	Disulfides	222-231	thyroid peroxidase	Homo sapiens	15-18
9497358-8	1998	In contrast to TPx, in which one of the two conserved cysteines is oxidized to Cys-SOH and then immediately reacts with the second conserved cysteine of the second subunit of the enzyme homodimer to form an intermolecular disulfide, the Cys-SOH of 1-Cys Prx does not form a disulfide.	Disulfides	274-283	thyroid peroxidase	Homo sapiens	15-18
9490731-0	1998	The pattern of disulfide linkages in the extracellular loop regions of connexin 32 suggests a model for the docking interface of gap junctions.	Disulfides	15-24	gap junction protein beta 1	Homo sapiens	71-82
1368324-1	1992	Human epidermal growth factor (h-EGF) composed of 53 amino acids bearing three intramolecular disulfide bridges was synthesized by the maximum protecting solution method.	Disulfides	94-103	epidermal growth factor	Homo sapiens	6-29
9519413-10	1998	Cys84 is positioned at an exposed surface of S100B, surrounded by hydrophobic residues, and could form a disulfide bond to tau protein, one of the known target molecules thought to interact with S100B in this way.	Disulfides	105-114	S100 calcium binding protein B	Bos taurus	45-50
9519413-10	1998	Cys84 is positioned at an exposed surface of S100B, surrounded by hydrophobic residues, and could form a disulfide bond to tau protein, one of the known target molecules thought to interact with S100B in this way.	Disulfides	105-114	S100 calcium binding protein B	Bos taurus	195-200
9519413-13	1998	It is through hydrophobic interactions and possibly a Cys84-mediated disulfide bond that S100B is thought to bind its target molecules.	Disulfides	69-78	S100 calcium binding protein B	Bos taurus	89-94
1309791-0	1992	The reactivity of thiols and disulfides with different redox states of myoglobin.	Disulfides	29-39	myoglobin	Homo sapiens	71-80
9462726-7	1998	Essentially all cysteines are conserved between the human and the murine genes, suggesting conservation of the Trop2 disulfide bridges and of its overall structure.	Disulfides	117-126	tropomyosin 2, beta	Mus musculus	111-116
1730727-10	1992	The Cys216----Ser mutation destroys a conserved disulfide bridge that is apparently critical for maintaining LPL structure and function.	Disulfides	48-57	lipoprotein lipase	Homo sapiens	109-112
34982478-0	2022	The X-ray crystal structure of human A15C neuroglobin reveals both native/de novo disulfide bonds and unexpected ligand-binding sites.	Disulfides	82-91	neuroglobin	Homo sapiens	42-53
34982478-2	2022	By introducing an additional Cys at position 15, the X-ray structure of A15C Ngb mutant was solved at a high resolution of 1.35 A, which reveals the formation of both the native (C46-C55) and the engineered (C15-C120) disulfide bonds, likely playing a functional and structural role, respectively, according to the geometry analysis.	Disulfides	218-227	neuroglobin	Homo sapiens	77-80
1368125-7	1992	Refolded IGF II had an identical primary structure including disulfide bonds and showed identical thymidine uptake stimulation activity with human IGF II.	Disulfides	61-70	insulin like growth factor 2	Homo sapiens	9-15
35621952-5	2022	While DCD was first isolated from human skin and thought to be only an antimicrobial peptide, currently DCD has been also identified as a peptide associated with the survival of cancer cells, through what is believed to be a disulfide-based conjugation with proteins that would normally induce apoptosis.	Disulfides	225-234	dermcidin	Homo sapiens	104-107
1541337-11	1992	Whether the Cys 18/Cys 22 disulfide bond was present in native gamma II or was produced during isolation or enzymic digestion could not be determined from these studies.	Disulfides	26-35	G protein subunit gamma 7	Bos taurus	63-71
35167877-3	2022	However, mu-conotoxin KIIIA, the smallest and most studied mu-conotoxin with inhibitory activity on NaV1.7, forms two distinct disulfide bond isomers during thermodynamic oxidative folding, including Isomer 1 (CysI-CysV, CysII-CysIV, CysIII-CysVI) and Isomer 2 (CysI-CysVI, CysII-CysIV, CysIII-CysV), but not the native mu-conotoxin arrangement.	Disulfides	127-136	sodium voltage-gated channel alpha subunit 9	Homo sapiens	100-106
1721638-4	1991	We coupled [125I]tyrosine to 131I-alpha 2-macroglobulin or [131I] transferrin via a reducible disulfide linker.	Disulfides	94-103	alpha-2-macroglobulin	Homo sapiens	34-55
34985274-2	2022	(PtBr2(CN)4)2- can oxidatively deprotect two Acm groups or deprotect one Thz group and one Acm group to directly form an intramolecular disulfide bond in peptides.	Disulfides	136-145	translocator protein	Homo sapiens	1-5
34985274-6	2022	Apamin, alpha-conotoxin SI, and the parallel homodimer of oxytocin, all containing two disulfide bonds, were synthesized regioselectively through a one-pot method by the combined use of the above deprotection approach with oxidants l-methionine selenoxide and (PtBr2(CN)4)2-.	Disulfides	87-96	oxytocin/neurophysin I prepropeptide	Homo sapiens	58-66
1837811-4	1991	Furthermore, the TcR-gamma combinatorial repertoire appears to be even more limited by the fact that particular V gamma genes are preferentially used in TcR-gamma 1 or TcR-gamma 2 derived receptors, i.e. in disulfide-linked or non-disulfide-linked TcR-gamma delta receptors.	Disulfides	231-240	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	153-156
34609517-8	2022	Furthermore, AtPDI2/5 work synergistically with PDI-M/S members in relaying disulfide bonds from AtERO1 to substrates.	Disulfides	76-85	PDI-like 1-4	Arabidopsis thaliana	13-21
1837811-4	1991	Furthermore, the TcR-gamma combinatorial repertoire appears to be even more limited by the fact that particular V gamma genes are preferentially used in TcR-gamma 1 or TcR-gamma 2 derived receptors, i.e. in disulfide-linked or non-disulfide-linked TcR-gamma delta receptors.	Disulfides	231-240	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	153-156
1660140-5	1991	When expressed in transfected human cells, TNFR-IgG is secreted as a disulfide-bonded homodimer.	Disulfides	69-78	TNF receptor superfamily member 1A	Homo sapiens	43-47
1722112-3	1991	Both these cytoplasmic and surface mu are disulfide-linked to omega (lambda 5) surrogate light chains and are noncovalently associated with iota (Vpre-B) variable region-like proteins.	Disulfides	42-51	immunoglobulin lambda like polypeptide 1	Homo sapiens	69-77
1653704-7	1991	Reduction of both authentic and recombinant BM-40 decreased binding activity which indicates correct formation of disulfide bonds in the recombinant protein.	Disulfides	114-123	secreted protein acidic and cysteine rich	Homo sapiens	44-49
1716445-5	1991	Pretreatment of methylamine-activated serum or plasma by iodoacetamide substantially decreased the binding of HNP-1 to alpha 2M, suggesting that thiol groups in activated alpha 2M play a role in defensin binding, possibly by covalently trapping defensins via thiol-disulfide exchange.	Disulfides	265-274	HNP1	Homo sapiens	110-115
1905953-0	1991	Role of the hexapeptide disulfide loop present in the gamma-carboxyglutamic acid domain of human protein C in its activation properties and in the in vitro anticoagulant activity of activated protein C.	Disulfides	24-33	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	97-106
1905953-0	1991	Role of the hexapeptide disulfide loop present in the gamma-carboxyglutamic acid domain of human protein C in its activation properties and in the in vitro anticoagulant activity of activated protein C.	Disulfides	24-33	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	192-201
1905953-1	1991	In order to examine whether the structural integrity of the hexapeptide disulfide loop (residues 17-22), present in the gamma-carboxyglutamic acid (gamma) domain of human protein C (PC), and common to all vitamin K dependent coagulation proteins, is necessary for its anticoagulant properties, we employed recombinant (r) DNA technology to generate two important variants that would address this issue.	Disulfides	72-81	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	171-180
1917302-3	1991	The disulfide bond pairings in bTGF-alpha were determined to be homologous to those in the human and mouse TGF-alpha molecules.	Disulfides	4-13	transforming growth factor alpha	Mus musculus	32-41
1707981-0	1991	Homooligomerization of the hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3 occurs before the acquisition of correct intramolecular disulfide bonds and mature immunoreactivity.	Disulfides	160-169	hemagglutinin-neuraminidase	Human respirovirus 3	27-54
1850095-1	1991	The third disulfide loop (amino acids 33 to 42) of human epidermal growth factor (hEGF) encompasses the region of highest amino acid conservation among all of the EGF-like family of molecules.	Disulfides	10-19	epidermal growth factor	Homo sapiens	57-80
1850095-1	1991	The third disulfide loop (amino acids 33 to 42) of human epidermal growth factor (hEGF) encompasses the region of highest amino acid conservation among all of the EGF-like family of molecules.	Disulfides	10-19	epidermal growth factor	Homo sapiens	82-86
1850095-1	1991	The third disulfide loop (amino acids 33 to 42) of human epidermal growth factor (hEGF) encompasses the region of highest amino acid conservation among all of the EGF-like family of molecules.	Disulfides	10-19	epidermal growth factor	Homo sapiens	83-86
1707541-4	1991	mIgM is associated with the MB-1 protein, which is disulfide-linked to a protein designated Ig-beta.	Disulfides	51-60	CD79b molecule	Homo sapiens	92-99
1707541-5	1991	mIgD is not associated with MB-1 but is with IgD-alpha, which is also disulfide-linked to Ig-beta.	Disulfides	70-79	CD79b molecule	Homo sapiens	90-97
1848538-7	1991	Additional evidence was provided by affinity cross-linking of [125I]IGF-II to the same high-molecular-weight material which demonstrated a major specific band at 250 kDa after reduction of disulfide bonds.	Disulfides	189-198	insulin like growth factor 2	Homo sapiens	68-74
1705175-3	1991	This indicates that dgA or dgA-containing immunotoxins are bound to alpha 2M by disulfide bonds.	Disulfides	80-89	alpha-2-macroglobulin	Homo sapiens	68-76
1846021-1	1991	Activin, a disulfide-linked polypeptide dimer first isolated from gonadal tissue extracts, has amino acid sequence and structural homology with transforming growth factor beta (TGF beta).	Disulfides	11-20	inhibin subunit beta E	Homo sapiens	0-7
2090516-6	1990	PLP-A species isolated from placental cytosol or from serum of pregnant rats predominantly circulated as disulfide-linked high molecular weight complexes.	Disulfides	105-114	prolactin family 4, subfamily A, member 1	Rattus norvegicus	0-5
2261983-0	1990	Complete localization of the disulfide bridges and glycosylation sites in boar sperm acrosin.	Disulfides	29-38	acrosin	Homo sapiens	85-92
2261983-1	1990	Acrosin is a disulfide-bonded two-chain glycoprotein, which belongs to the serine proteinase family and which plays a central role in mammalian fertilization.	Disulfides	13-22	acrosin	Homo sapiens	0-7
2261983-3	1990	Boar sperm acrosin contains twelve cysteine residues forming two interchain and 4 intrachain disulfide bonds.	Disulfides	93-102	acrosin	Homo sapiens	11-18
2172979-4	1990	cDNA cloning of ADF demonstrated high homology with the prokaryotic disulfide reducing enzyme thioredoxin.	Disulfides	68-77	thioredoxin	Homo sapiens	16-19
2172979-4	1990	cDNA cloning of ADF demonstrated high homology with the prokaryotic disulfide reducing enzyme thioredoxin.	Disulfides	68-77	thioredoxin	Homo sapiens	94-105
1698779-10	1990	The sodium dodecyl sulfate-polyacrylamide gel electrophoresis pattern of the high molecular weight cross-linked species indicates that binding of a proteinase through two cross-links occurs not only within the 360-kDa disulfide-bridged alpha 2M dimer but also between the two dimers in the alpha 2M tetramer.	Disulfides	218-227	alpha-2-macroglobulin	Homo sapiens	236-244
1698779-10	1990	The sodium dodecyl sulfate-polyacrylamide gel electrophoresis pattern of the high molecular weight cross-linked species indicates that binding of a proteinase through two cross-links occurs not only within the 360-kDa disulfide-bridged alpha 2M dimer but also between the two dimers in the alpha 2M tetramer.	Disulfides	218-227	alpha-2-macroglobulin	Homo sapiens	290-298
2115173-2	1990	Sixteen cysteine residues exist in disulfide forms: Cys-1-Cys-3, Cys-2-Cys-4, Cys-5-Cys-6, Cys-7-Cys-8, Cys-9-Cys-10, Cys-11-Cys-12, Cys-13-Cys-14, and Cys-20-Cys-21.	Disulfides	35-44	cystin 1	Homo sapiens	52-63
2112541-8	1990	This disulfide-bonded pair of triple helices is termed C-1.	Disulfides	5-14	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	55-58
1698797-6	1990	The alpha 6 subunit consists of disulfide-linked heavy and light chains.	Disulfides	32-41	gamma-aminobutyric acid (GABA) A receptor, subunit alpha 6	Mus musculus	4-11
9877221-1	1998	Human adrenomedullin (ADM) is a 52-amino acid hypotensive peptide, which possesses a disulfide bridge-formed six-membered ring in 16-21 position.	Disulfides	85-94	adrenomedullin	Homo sapiens	6-20
9877221-1	1998	Human adrenomedullin (ADM) is a 52-amino acid hypotensive peptide, which possesses a disulfide bridge-formed six-membered ring in 16-21 position.	Disulfides	85-94	adrenomedullin	Homo sapiens	22-25
2201313-1	1990	We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51-found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin.	Disulfides	66-75	insulin	Bos taurus	142-149
1692828-4	1990	Both forms of hG-CSF have a free Cys-17 and two intramolecular disulfide linkages, between Cys-36 and Cys-42, and between Cys-64 and Cys-74.	Disulfides	63-72	colony stimulating factor 3	Homo sapiens	14-20
9388258-5	1997	Combining this method with Western blot analysis, disulfide cross-linking, and SDS-polyacrylamide gel electrophoresis in the second dimension showed that NFL readily forms significant amounts of heterodimer with NFH, NFM, alpha-internexin, or peripherin in the presence of 2 M urea.	Disulfides	50-59	neurofilament light chain	Homo sapiens	154-157
9388463-4	1997	We evaluated here the redox status and disulfide bond formation of Vif cysteines inside cells or in virions and tested the role of Vif cysteines in Vif distribution in cells and in virions.	Disulfides	39-48	Vif	Human immunodeficiency virus 1	67-70
2154371-0	1990	B lymphocyte antigen receptors (mIg) are non-covalently associated with a disulfide linked, inducibly phosphorylated glycoprotein complex.	Disulfides	74-83	chemokine (C-X-C motif) ligand 9	Mus musculus	32-35
9312147-7	1997	Disulfide linkages present in the first domain are necessary for BDNF binding, probably because of preservation of the native conformation.	Disulfides	0-9	brain derived neurotrophic factor	Homo sapiens	65-69
1690131-7	1990	Expression of distinct forms of the T cell receptor gamma/delta, disulfide-bonded N-glycosylated surface heterodimers of under reducing conditions 38/40 and 37/40 kDa, respectively, hallmarks the CD2-86D+ and CD2-86D- subsets both as T lymphocytes.	Disulfides	65-74	CD2 molecule	Sus scrofa	196-199
9300481-2	1997	APPI and BPTI belong to the Kunitz family of inhibitors, which is characterized by a distinctive tertiary fold with three conserved disulfide bonds.	Disulfides	132-141	spleen trypsin inhibitor I	Bos taurus	9-13
9265624-16	1997	The majority of the 14 residues are located in the vicinity of the Cys14(20)-Cys38(44) disulfide bond, suggesting the presence of a disulfide bond isomerization similar to the one observed in BPTI [Otting, G., Liepinsh, E., &amp; Wuthrich, K. (1993) Biochemistry 32, 3571-3582].	Disulfides	87-96	spleen trypsin inhibitor I	Bos taurus	192-196
9265624-16	1997	The majority of the 14 residues are located in the vicinity of the Cys14(20)-Cys38(44) disulfide bond, suggesting the presence of a disulfide bond isomerization similar to the one observed in BPTI [Otting, G., Liepinsh, E., &amp; Wuthrich, K. (1993) Biochemistry 32, 3571-3582].	Disulfides	132-141	spleen trypsin inhibitor I	Bos taurus	192-196
9305784-6	1997	Based on the results of molecular weight analysis and its reversion from methemoglobin, protein formed mixed disulfides with GSH were also regarded as hemoglobin.	Disulfides	109-119	hemoglobin subunit gamma 2	Homo sapiens	73-86
1690131-7	1990	Expression of distinct forms of the T cell receptor gamma/delta, disulfide-bonded N-glycosylated surface heterodimers of under reducing conditions 38/40 and 37/40 kDa, respectively, hallmarks the CD2-86D+ and CD2-86D- subsets both as T lymphocytes.	Disulfides	65-74	CD2 molecule	Sus scrofa	209-212
2162313-3	1990	Thioredoxin reductase (TR) is a widely distributed flavoenzyme that provides reduced thioredoxin, a dithiol hydrogen donor for protein disulfide reduction and for the reduction of ribonucleotides to deoxyribonucleotides, the first unique step of DNA synthesis.	Disulfides	135-144	peroxiredoxin 5	Homo sapiens	0-21
9232656-2	1997	The roles of aromatic residues in determining the folding pathway of bovine pancreatic trypsin inhibitor (BPTI) were analyzed mutationally by examining the distribution of disulfide-bonded intermediates that accumulated during the refolding of protein variants in which tyrosine or phenylalanine residues were individually replaced with leucine.	Disulfides	172-181	spleen trypsin inhibitor I	Bos taurus	69-104
2162313-3	1990	Thioredoxin reductase (TR) is a widely distributed flavoenzyme that provides reduced thioredoxin, a dithiol hydrogen donor for protein disulfide reduction and for the reduction of ribonucleotides to deoxyribonucleotides, the first unique step of DNA synthesis.	Disulfides	135-144	peroxiredoxin 5	Homo sapiens	23-25
2162313-3	1990	Thioredoxin reductase (TR) is a widely distributed flavoenzyme that provides reduced thioredoxin, a dithiol hydrogen donor for protein disulfide reduction and for the reduction of ribonucleotides to deoxyribonucleotides, the first unique step of DNA synthesis.	Disulfides	135-144	thioredoxin	Homo sapiens	85-96
33767592-7	2021	Physical interactions of AGR2 and FABP1 depended on the PDI motif in AGR2 and the formation of a disulfide bond between these two proteins.	Disulfides	97-106	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	56-59
9195930-0	1997	Close association of the first and fourth extracellular domains of the Duffy antigen/receptor for chemokines by a disulfide bond is required for ligand binding.	Disulfides	114-123	atypical chemokine receptor 1 (Duffy blood group)	Homo sapiens	71-108
9195930-6	1997	Analysis of red cells treated by sulfhydryl group-modifying reagents suggested that the chemokine receptor function of DARC required the integrity of disulfide bond(s) but not that of free sulfhydryl group(s).	Disulfides	150-159	atypical chemokine receptor 1 (Duffy blood group)	Homo sapiens	119-123
9195930-8	1997	Altogether, our results suggested that the chemokine binding pocket of DARC included sequences located in the first and fourth extracellular domains which are brought into close vicinity by a disulfide bridge.	Disulfides	192-201	atypical chemokine receptor 1 (Duffy blood group)	Homo sapiens	71-75
33767552-1	2020	CD38 is a disulfide-linked molecule present on red blood cells (RBCs) and daratumumab; an anti-CD38 monoclonal antibody is a novel agent for treating multiple myeloma patients.	Disulfides	10-19	CD38 molecule	Homo sapiens	0-4
9224699-2	1997	To define the cysteine residues forming a disulfide bond in Xenopus eIF-4E, each of the 3 cysteine residues was changed to serine by site-directed mutagenesis.	Disulfides	42-51	eukaryotic translation initiation factor 4E L homeolog	Xenopus laevis	68-74
33767552-1	2020	CD38 is a disulfide-linked molecule present on red blood cells (RBCs) and daratumumab; an anti-CD38 monoclonal antibody is a novel agent for treating multiple myeloma patients.	Disulfides	10-19	CD38 molecule	Homo sapiens	95-99
25880503-8	2015	While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding.	Disulfides	85-95	thioredoxin	Homo sapiens	6-17
25880503-8	2015	While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding.	Disulfides	85-94	thioredoxin	Homo sapiens	6-17
25880503-8	2015	While thioredoxin and glutaredoxin primarily act as antioxidants by reducing protein disulfides and mixed disulfide, another member of the superfamily, protein disulfide isomerase (PDI), can act as an oxidant by forming intrachain disulfide bonds that contribute to proper protein folding.	Disulfides	106-115	thioredoxin	Homo sapiens	6-17
9209005-6	1997	Electron microscopic analysis of actin polymers indicated that ISC actin generates a large amount of aggregates which we conclude are due to the structural modification caused by the disulfide bridge between cysteine284 and cysteine373 in beta-actin.	Disulfides	183-192	POTE ankyrin domain family member F	Homo sapiens	239-249
15050695-4	2004	Both AmGluRA and AmGluRB form homodimers independently on disulfide bonds, and bind [3H]glutamate with K(D) values of 156.7 and 80.7 nM, respectively.	Disulfides	58-67	metabotropic glutamate receptor 1	Apis mellifera	5-12
7925367-7	1994	Based on the knowledge of the location of the five disulfide bonds in the structure of pig pancreatic alpha-amylase, the possible disulfide bridges were established for each of these groups of homologous alpha-amylases.	Disulfides	130-139	amylase, alpha 2A (pancreatic)	Sus scrofa	91-115
9154914-0	1997	"Designing out" disulfide bonds: thermodynamic properties of 30-51 cystine substitution mutants of bovine pancreatic trypsin inhibitor.	Disulfides	16-25	spleen trypsin inhibitor I	Bos taurus	99-134
9154914-2	1997	Correctly folded, wild type BPTI contains a disulfide at the 30-51 positions, with the nonbackbone atoms of this cystine being relatively solvent inaccessible.	Disulfides	44-53	spleen trypsin inhibitor I	Bos taurus	28-32
2088576-0	1990	Location of disulfide bonds in antithrombin III.	Disulfides	12-21	serpin family C member 1	Homo sapiens	31-47
9154914-3	1997	Mutants missing this buried 30-51 disulfide adopt a conformation very similar to that of the native state of wild type BPTI (Eigenbrot et al., 1990, 1992), although they are severely destabilized relative to the wild type molecule (Hurle et al., 1990).	Disulfides	34-43	spleen trypsin inhibitor I	Bos taurus	119-123
9154914-4	1997	We have conducted a systematic effort to find the energetically most favorable substitution for this buried 30-51 disulfide in BPTI.	Disulfides	114-123	spleen trypsin inhibitor I	Bos taurus	127-131
9154914-9	1997	In the aggregate, our data provide insight into the residue-, position-, and context-dependent consequences on protein stability of "designing out" the buried 30-51 disulfide bond in the BPTI molecule.	Disulfides	165-174	spleen trypsin inhibitor I	Bos taurus	187-191
9191030-1	1997	Protein disulfide isomerase (PDI) is a protein of the endoplasmic reticulum (ER) that is essential for the unscrambling of nonnative disulfide bonds.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	29-32
2088576-1	1990	Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.	Disulfides	201-210	serpin family C member 1	Homo sapiens	29-45
2088576-1	1990	Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.	Disulfides	201-210	serpin family C member 1	Homo sapiens	47-52
9092537-6	1997	In addition, heparin serves as a template for the assembly of type 1 plasminogen activator inhibitor-induced disulfide-linked Vn multimers.	Disulfides	109-118	vitronectin	Homo sapiens	126-128
2088576-1	1990	Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.	Disulfides	201-210	serpin family C member 1	Homo sapiens	278-283
2088576-1	1990	Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.	Disulfides	256-265	serpin family C member 1	Homo sapiens	29-45
2088576-1	1990	Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.	Disulfides	256-265	serpin family C member 1	Homo sapiens	47-52
34904718-2	2022	Here, we report identification of a homozygous c.170G>A (p.Cys57Tyr or C57Y) mutation in the gene coding for protein disulfide isomerase A3 (PDIA3, also known as ERp57), an enzyme that catalyzes formation of disulfide bonds in the endoplasmic reticulum, to be associated with syndromic intellectual disability.	Disulfides	208-217	protein disulfide isomerase associated 3	Mus musculus	109-139
9242985-6	1997	Treatment of Vn with reducing agents abolished type 1 plasminogen activator inhibitor and antibody binding to the highly disulfide-linked N-terminal somatomedin B domain (amino acids 1 to 51), whereas epitopes located in the connecting region/first hemopexin-like repeat (amino acids 52 to 239) and the glycosaminoglycan binding domain (amino acids 343-379) were not affected.	Disulfides	121-130	vitronectin	Homo sapiens	13-15
9063871-1	1997	This paper reports a detailed conformational analysis by 1H NMR (DMSO-d6, 300 K) and molecular modeling of the octapeptide D-Phe1-Cys2-Phe3-D-Trp4-Lys5-Thr6-Cys7+ ++-Thr8-ol (disulfide bridged) known as sandostatin (or SMS 201-995 or octreotide) with both somatostatin-like and opioid-like bioactivities.	Disulfides	175-184	transient receptor potential cation channel subfamily C member 4	Homo sapiens	142-146
34904718-2	2022	Here, we report identification of a homozygous c.170G>A (p.Cys57Tyr or C57Y) mutation in the gene coding for protein disulfide isomerase A3 (PDIA3, also known as ERp57), an enzyme that catalyzes formation of disulfide bonds in the endoplasmic reticulum, to be associated with syndromic intellectual disability.	Disulfides	208-217	protein disulfide isomerase associated 3	Mus musculus	141-146
34904718-2	2022	Here, we report identification of a homozygous c.170G>A (p.Cys57Tyr or C57Y) mutation in the gene coding for protein disulfide isomerase A3 (PDIA3, also known as ERp57), an enzyme that catalyzes formation of disulfide bonds in the endoplasmic reticulum, to be associated with syndromic intellectual disability.	Disulfides	208-217	protein disulfide isomerase associated 3	Mus musculus	162-167
9002990-1	1997	To study the interaction of TSH receptor (TSHR) autoantibodies with receptor protein; it is necessary first to express the receptor in the proper conformation including the formation of correct disulfide bridges.	Disulfides	194-203	thyroid stimulating hormone receptor	Homo sapiens	42-46
34904718-6	2022	Biochemical studies show that PDIA3C57Y has decreased catalytic activity and forms disulfide-crosslinked aggregates that abnormally interact with chaperones in the endoplasmic reticulum.	Disulfides	83-92	protein disulfide isomerase associated 3	Mus musculus	30-35
9002990-3	1997	To circumvent these limitations, hTSHR complementary DNA encoding the extracellular domain (hTSHR-ecd; amino acids 21-415) was inserted into the vector pGEX-2TK by directional cloning and used to transform the thioredoxin reductase mutant strain of E. coli (Ad494), which allowed formation of disulfide bonds in the cytoplasm.	Disulfides	293-302	thyroid stimulating hormone receptor	Homo sapiens	33-38
34695570-0	2022	Effects of removing a highly conserved disulfide bond in ubiquitin-associated domain of human HOIP on biochemical characteristics.	Disulfides	39-48	ring finger protein 31	Homo sapiens	94-98
9002990-3	1997	To circumvent these limitations, hTSHR complementary DNA encoding the extracellular domain (hTSHR-ecd; amino acids 21-415) was inserted into the vector pGEX-2TK by directional cloning and used to transform the thioredoxin reductase mutant strain of E. coli (Ad494), which allowed formation of disulfide bonds in the cytoplasm.	Disulfides	293-302	thyroid stimulating hormone receptor	Homo sapiens	92-97
9002990-7	1997	Under nonreducing SDS-PAGE conditions, the soluble hTSHR-ecd migrated as refolded, disulfide bond-stabilized, multimeric species, whose formation was independent of fusion partner protein.	Disulfides	83-92	thyroid stimulating hormone receptor	Homo sapiens	51-56
34975517-3	2021	Here, we identified a leptin-a gene (lepa) in the cold-adapted and neutrally buoyant Antarctic toothfish Dissostichus mawsoni that encodes a polypeptide carrying four alpha-helices and two cysteine residues forming in-chain disulfide bonds, structures shared by most vertebrate leptins.	Disulfides	224-233	leptin a	Danio rerio	37-41
9111139-0	1997	Alteration of N-linked oligosaccharide structures of human chorionic gonadotropin beta-subunit by disruption of disulfide bonds.	Disulfides	112-121	chorionic gonadotropin subunit beta 3	Homo sapiens	59-94
9111139-1	1997	The human chorionic gonadotropin beta-subunit (hCGbeta) is a glycoprotein in which 12 cysteine residues pair to form six intramolecular disulfide bonds.	Disulfides	136-145	chorionic gonadotropin subunit beta 3	Homo sapiens	10-45
9111139-1	1997	The human chorionic gonadotropin beta-subunit (hCGbeta) is a glycoprotein in which 12 cysteine residues pair to form six intramolecular disulfide bonds.	Disulfides	136-145	chorionic gonadotropin subunit beta 3	Homo sapiens	47-54
9111139-5	1997	These results suggest that elimination of a specific disulfide bond, resulting in a change in the protein conformation, disturbs the normal assembly of the mature complex type oligosaccharides in the hCGbeta molecule.	Disulfides	53-62	chorionic gonadotropin subunit beta 3	Homo sapiens	200-207
34843209-3	2021	In-solution deglycosylation with peptide-N4-(N-acetyl-beta-d-glucosaminyl)-asparagine amidase A (PNGase A) or PNGase H+ combined with chemical reduction using tris-(2-carboxyethyl)phosphine (TCEP) has previously been used for HDX-MS analysis of disulfide-linked glycoproteins.	Disulfides	245-254	N-glycanase 1	Homo sapiens	110-116
9013852-5	1997	A 40 kDa form is revealed after treatment with a reducing agent, strongly suggesting that native mTWIK-1 subunits dimerize via a disulfide bridge.	Disulfides	129-138	potassium channel, subfamily K, member 1	Mus musculus	97-104
9013874-1	1997	beta-Lactamase, from which the disulfide bond was removed by two Cys--&gt;Ala mutations, forms stable complexes with GroEL only during the first 30 s of folding, while wild-type beta-lactamase forms no stable complex under these conditions.	Disulfides	31-40	heat shock protein family D (Hsp60) member 1	Homo sapiens	117-122
9015368-1	1997	Serine proteases of the chymotrypsin family contain three conserved disulfide bonds: C42-C58, C168-C182, and C191-C220.	Disulfides	68-77	CDK5 regulatory subunit associated protein 1	Homo sapiens	85-88
34773863-6	2021	We have reported that human GILT suppresses HIV-1 particle production by digestion of disulfide bonds on CD63.	Disulfides	86-95	CD63 molecule	Homo sapiens	105-109
8985427-6	1997	The viral counterpart of IL-6 (vIL-6) has conserved important features such as cysteine residues involved in disulfide bridging or an amino-terminal signal peptide.	Disulfides	109-118	K2	Human gammaherpesvirus 8	31-36
34943005-6	2021	Using ELISA, we demonstrate that the disulfide bridge between the enzymatic cysteines is required to allow improved TLR4-dependent IL-8 secretion.	Disulfides	37-46	toll like receptor 4	Homo sapiens	116-120
8988018-6	1996	The determined disulfide structure is highly homologous to that of transforming growth factor beta 2.	Disulfides	15-24	transforming growth factor beta 2	Homo sapiens	67-100
8988018-7	1996	Since one intramolecular disulfide points through a ring consisting of eight amino acid residues based on the similarity with transforming growth factor beta 2, the disulfide-linked peptides were not purified by conventional methods.	Disulfides	25-34	transforming growth factor beta 2	Homo sapiens	126-159
34943005-8	2021	Finally, flow cytometry binding assays show that disulfide PRDX5 has a higher propensity to bind to the surface of living TLR4-expressing cells than the mutant protein.	Disulfides	49-58	peroxiredoxin 5	Homo sapiens	59-64
8988018-7	1996	Since one intramolecular disulfide points through a ring consisting of eight amino acid residues based on the similarity with transforming growth factor beta 2, the disulfide-linked peptides were not purified by conventional methods.	Disulfides	165-174	transforming growth factor beta 2	Homo sapiens	126-159
34943005-8	2021	Finally, flow cytometry binding assays show that disulfide PRDX5 has a higher propensity to bind to the surface of living TLR4-expressing cells than the mutant protein.	Disulfides	49-58	toll like receptor 4	Homo sapiens	122-126
34411303-7	2021	PIGR/FCAMR/FCMR are members of a larger superfamily including TREM, CD300, and NKp44, which we name the "double-disulfide Ig superfamily" (ddIgSF).	Disulfides	112-121	polymeric immunoglobulin receptor	Homo sapiens	0-4
34656563-2	2021	In a recent issue, Weismiller et al showed that intramolecular disulfide links between cys291 and cys322 for a specific tau isoform containing 4 microtubule-binding repeats direct the formation of a structurally distinct amyloid polymorph.	Disulfides	63-72	microtubule associated protein tau	Homo sapiens	120-123
8980687-8	1996	(3) The circular dichroism spectra of beta-lactoglobulin and its disulfide-cleaved derivative in 4.0 M guanidine hydrochloride suggests the presence of the residual beta-structure in the unfolded state and the stabilization of the beta-structure by disulfide bonds.	Disulfides	65-74	beta-lactoglobulin	Bos taurus	38-56
8980687-8	1996	(3) The circular dichroism spectra of beta-lactoglobulin and its disulfide-cleaved derivative in 4.0 M guanidine hydrochloride suggests the presence of the residual beta-structure in the unfolded state and the stabilization of the beta-structure by disulfide bonds.	Disulfides	249-258	beta-lactoglobulin	Bos taurus	38-56
34679713-7	2021	Cysteine 277 is required for most of the disulfide-dependent interactions of p53, including those with 14-3-3theta and 53BP1.	Disulfides	41-50	tumor protein p53 binding protein 1	Homo sapiens	119-124
8972386-1	1996	Bovine pancreatic trypsin inhibitor (BPTI) is a 58-residue protein with three disulfide bonds that belongs to the Kunitz family of serine proteinase inhibitors.	Disulfides	78-87	spleen trypsin inhibitor I	Bos taurus	0-35
8972386-1	1996	Bovine pancreatic trypsin inhibitor (BPTI) is a 58-residue protein with three disulfide bonds that belongs to the Kunitz family of serine proteinase inhibitors.	Disulfides	78-87	spleen trypsin inhibitor I	Bos taurus	37-41
34339733-4	2021	Four-repeat tau contains two cysteines that can form an intramolecular disulfide bond, resulting in a structurally restrained compact monomer.	Disulfides	71-80	microtubule associated protein tau	Homo sapiens	12-15
8871643-0	1996	Residues critical for H-L disulfide bond formation in human IgA1 and IgA2.	Disulfides	26-35	immunoglobulin heavy constant alpha 1	Homo sapiens	60-64
8871643-3	1996	The variants of human IgA differ in their H and L chain disulfide-bonding pattern; in IgA1, IgA2(n), and IgA2 m(2), a disulfide bond connects a cysteine residue in CH1 of the H chain with the L chains while human IgA2 m(1) has been reported to lack a covalent bond between the H and L chains.	Disulfides	118-127	immunoglobulin heavy constant alpha 1	Homo sapiens	86-90
34260218-2	2021	We designed a trimeric, highly thermotolerant glycan engineered RBD by fusion to a heterologous, poorly immunogenic disulfide linked trimerization domain derived from cartilage matrix protein.	Disulfides	116-125	matrilin 1	Homo sapiens	167-191
8871643-4	1996	Here we have used site-directed mutagenesis to demonstrate that Cys133 is essential for the formation of the H-L disulfide bond in IgA1.	Disulfides	113-122	immunoglobulin heavy constant alpha 1	Homo sapiens	131-135
8917445-3	1996	We have developed such a procedure for the active N-terminal domain of tissue inhibitor of metalloproteinases-2 [TIMP-2-(1-127)], a small mammalian protein containing three disulfide bonds.	Disulfides	173-182	TIMP metallopeptidase inhibitor 2	Homo sapiens	71-111
8917445-3	1996	We have developed such a procedure for the active N-terminal domain of tissue inhibitor of metalloproteinases-2 [TIMP-2-(1-127)], a small mammalian protein containing three disulfide bonds.	Disulfides	173-182	TIMP metallopeptidase inhibitor 2	Homo sapiens	113-119
34389743-5	2021	To explore this interaction, we constructed disulfide-linked MHCI-peptide complexes using HLA-B*08 and a 12mer kinetically labile peptide, or a 16mer carrying a phosphinic transition-state analogue N-terminus with high-affinity for ERAP1.	Disulfides	44-53	major histocompatibility complex, class I, B	Homo sapiens	90-95
8816464-2	1996	The mature Ron protein is a heterodimer of disulfide-linked alpha and beta chains, originated by proteolytic cleavage of a single-chain precursor of 185 kDa.	Disulfides	43-52	macrophage stimulating 1 receptor	Homo sapiens	11-14
8816464-5	1996	The delta-Ron tyrosine kinase is constitutively activated by disulfide-linked intracellular oligomerization because it contains an uneven number of cysteine residues.	Disulfides	61-70	macrophage stimulating 1 receptor	Homo sapiens	10-13
34389743-5	2021	To explore this interaction, we constructed disulfide-linked MHCI-peptide complexes using HLA-B*08 and a 12mer kinetically labile peptide, or a 16mer carrying a phosphinic transition-state analogue N-terminus with high-affinity for ERAP1.	Disulfides	44-53	endoplasmic reticulum aminopeptidase 1	Homo sapiens	232-237
8816464-7	1996	Inhibition of thiol-mediated intermolecular disulfide bonding prevented delta-Ron oligomerization.	Disulfides	44-53	macrophage stimulating 1 receptor	Homo sapiens	78-81
34251012-5	2021	With the addition of GSH, the breakage of disulfide bonds was promoted, thereby enhancing the SERS signal of SPDP.	Disulfides	42-51	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	94-98
9047377-8	1996	rBLG shared the same molecular weight as the natural BLG (nBLG) and also possessed at least one intrachain disulfide bridge.	Disulfides	107-116	beta-lactoglobulin	Bos taurus	1-4
8889803-1	1996	We fused various polypeptide extensions to the C-termini of single chain Fv (scFv) and disulfide-stabilized Fv (dsFv) fragments to facilitate detection of bi-functional proteins or to add biological effector domains, which included the human metallothionein (HMT) motif and biotin mimetic sequence.	Disulfides	87-96	histamine N-methyltransferase	Homo sapiens	259-262
8812841-1	1996	Ricin, the highly toxic glycoprotein expressed in the endosperm of castor seeds, is composed of a galactose-binding lectin B chain (RTB) disulfide linked to a RNA N-glycosidase A chain (RTA).	Disulfides	137-146	ricin	Ricinus communis	0-5
34436011-8	2021	Network analysis showed significant difference in immune response and in disulfide bond formation, with EGR1/EGR2 and PDIA2 genes as regulators for immune response and disulfide bond formation, respectively.	Disulfides	73-82	early growth response 1	Homo sapiens	104-108
8679585-7	1996	Interestingly, under nonreducing conditions, the ecto-ATPase activity in rat and pig (unlike chicken and rabbit) was evident on Western blots as an immunoreactive band at approximately 200 kDa, proposed to be an intermolecularly disulfide-linked ecto-ATPase homotrimer.	Disulfides	229-238	CEA cell adhesion molecule 1	Rattus norvegicus	49-60
8679585-11	1996	Intermolecular disulfide bonds appear to be one of the species-specific ways to stabilize the native, active ecto-ATPase quaternary structure (the homotrimer).	Disulfides	15-24	CEA cell adhesion molecule 1	Rattus norvegicus	109-120
34436011-8	2021	Network analysis showed significant difference in immune response and in disulfide bond formation, with EGR1/EGR2 and PDIA2 genes as regulators for immune response and disulfide bond formation, respectively.	Disulfides	73-82	early growth response 2	Homo sapiens	109-113
34436011-8	2021	Network analysis showed significant difference in immune response and in disulfide bond formation, with EGR1/EGR2 and PDIA2 genes as regulators for immune response and disulfide bond formation, respectively.	Disulfides	168-177	early growth response 1	Homo sapiens	104-108
34436011-8	2021	Network analysis showed significant difference in immune response and in disulfide bond formation, with EGR1/EGR2 and PDIA2 genes as regulators for immune response and disulfide bond formation, respectively.	Disulfides	168-177	early growth response 2	Homo sapiens	109-113
8828574-1	1996	Adrenomedullin (ADM) is a hypotensive peptide with structural homology, including a ring structure linked by a disulfide bridge, to calcitonin gene-related peptide (CGRP), calcitonin and amylin.	Disulfides	111-120	adrenomedullin	Rattus norvegicus	0-14
8828574-1	1996	Adrenomedullin (ADM) is a hypotensive peptide with structural homology, including a ring structure linked by a disulfide bridge, to calcitonin gene-related peptide (CGRP), calcitonin and amylin.	Disulfides	111-120	adrenomedullin	Rattus norvegicus	16-19
34360542-6	2021	Cys-mutants of HspB6 and HspB8 containing a single-Cys residue in the central part of the beta7 strand in a position homologous to that of Cys137 in HspB1 can be crosslinked to the wild-type HspB7 through a disulfide bond.	Disulfides	207-216	immunoglobulin kappa variable 2D-24 (non-functional)	Homo sapiens	90-95
8663084-5	1996	Self-association was evaluated by equilibrium analytical ultracentrifugation which demonstrated that multimers form only during the refolding process after removal of denaturant, that multimeric vitronectin dissociates to constituent subunits readily upon treatment with chemical denaturant, and that intermolecular disulfide cross-linking occurs primarily at the dimer level among a subset of constituent vitronectin subunits within the multimer.	Disulfides	316-325	vitronectin	Homo sapiens	195-206
8663085-3	1996	Unfolding and refolding of plasma vitronectin appear irreversible under near physiological conditions, with rearrangements of disulfides and self-association to a multimeric form observed as prominent structural alterations which accompany denaturation.	Disulfides	126-136	vitronectin	Homo sapiens	34-45
34360542-6	2021	Cys-mutants of HspB6 and HspB8 containing a single-Cys residue in the central part of the beta7 strand in a position homologous to that of Cys137 in HspB1 can be crosslinked to the wild-type HspB7 through a disulfide bond.	Disulfides	207-216	heat shock protein family B (small) member 1	Homo sapiens	149-154
34336854-8	2021	GPIHBP1 is an atypical member of the LU (Ly6/uPAR) domain protein superfamily, containing an intrinsically disordered and highly acidic N-terminal extension and a disulfide bond-rich three-fingered LU domain.	Disulfides	163-172	plasminogen activator, urokinase receptor	Homo sapiens	45-49
8724363-10	1996	During the acrosome reaction, PH-20 undergoes endoproteolytic cleavage into two disulfide-linked fragments whereas the released sPH-20 is not cleaved, suggesting the possible activity of a membrane-bound endoprotease on PH-20.	Disulfides	80-89	hyaluronidase PH-20	Cavia porcellus	30-35
8626683-0	1996	Isolation and characterization of a disulfide-linked human stem cell factor dimer.	Disulfides	36-45	KIT ligand	Homo sapiens	59-75
34194623-1	2021	L-type amino acid transporter 1 (LAT1)/SLC7A5 is the first identified CD98 light chain disulfide linked to the CD98 heavy chain (CD98hc/SLC3A2).	Disulfides	87-96	solute carrier family 3 (activators of dibasic and neutral amino acid transport), member 2	Mus musculus	136-142
8819011-0	1996	Human neurotrophin-3: a one-step peptide mapping method and complete disulfide characterization of the recombinant protein.	Disulfides	69-78	neurotrophin 3	Homo sapiens	6-20
34194623-5	2021	We confirmed that endogenous mouse CD98hc forms a disulfide bond with exogenous human LAT1 in naLAT1/3T3, but not in muLAT1/3T3.	Disulfides	50-59	solute carrier family 7 member 5	Homo sapiens	86-90
8617749-15	1996	However, cellular thiol-disulfide redox status and formation of disulfide linked aggregates of cellular proteins are linked to HSF1 activation and hsp70 transcriptional activation.	Disulfides	24-33	heat shock protein family A (Hsp70) member 4	Homo sapiens	147-152
34095684-5	2021	Since hBD-3 in the analogue form in which all three pairs of disulfide bonds are broken has similar antibacterial activities to the wild-type, this project investigates the structure and dynamics of an hBD-3 analogue in monomer, dimer, and tetramer forms through both zwitterionic and negatively charged lipid bilayers using molecular dynamics (MD) simulations.	Disulfides	61-70	defensin beta 103B	Homo sapiens	6-11
8617749-15	1996	However, cellular thiol-disulfide redox status and formation of disulfide linked aggregates of cellular proteins are linked to HSF1 activation and hsp70 transcriptional activation.	Disulfides	64-73	heat shock protein family A (Hsp70) member 4	Homo sapiens	147-152
8576206-3	1996	When P35 is isolated from human serum, it forms a homopolymer by means of intermolecular disulfide bonding, as is the case with collectins.	Disulfides	89-98	ficolin 2	Homo sapiens	5-8
34211593-0	2021	Synthesis of Disulfide-Bridging Trehalose Polymers for Antibody and Fab Conjugation Using a Bis-Sulfone ATRP Initiator.	Disulfides	13-22	FA complementation group B	Homo sapiens	68-71
8907610-5	1996	In these cells which express both the endogenous gene and the mutant cDNA lys-gp45 was linked via disulfide bonds to the gp80 complex.	Disulfides	98-107	clusterin	Canis lupus familiaris	121-125
35587955-1	2022	N-Sulfenylimines (sulfenimines, thiooximes, N-alkylidenesulfenamides) were efficiently synthesized through the reaction of primary amines and disulfides with NBS or bromine.	Disulfides	142-152	nibrin	Homo sapiens	158-161
8576577-2	1996	We recently showed that secretion of non-chimeric disulfide-linked human gamma delta TCR ("soluble" TCR, sTCR) comprising V gamma 9 and V delta 2 regions could be achieved by simply introducing translational termination codons upstream from the sequences encoding TCR transmembrane region.	Disulfides	50-59	G protein subunit gamma 8	Homo sapiens	124-145
8883845-3	1996	The results suggest that the acute phase proteins alpha 1-PI and alpha 1-ACT undergo conformational changes following oxidative mixed-disulfide formation and that alpha 2-AP and angiotensinogen do not.	Disulfides	134-143	serpin family A member 3	Homo sapiens	65-76
8883845-7	1996	However, disulfide formation in alpha 1-PI and alpha 1-ACT was much slower than for any other serpin, e.g., alpha 2-AP and angiotensinogen.	Disulfides	9-18	serpin family A member 3	Homo sapiens	47-58
35596004-7	2022	Furthermore, when N-linked glycosylation and disulfide bond formation are blocked, the cleavage and fusogenic activity of syncytin-2 are inhibited.	Disulfides	45-54	endogenous retrovirus group FRD member 1, envelope	Homo sapiens	122-132
8746786-5	1995	Second, like the IFN-alpha subtype, all IFN-tau have a three-amino acid insertion in loop AB and a likely disulfide bridge between Cys29 and Cys139 that lead to marked conformational differences between them and MuIFN-beta in a region (Leu22 to Arg33 in IFN-tau) believed to interact with the receptor.	Disulfides	106-115	interferon-tau-like	Bos taurus	40-47
35393494-5	2022	Using gel electrophoresis, tandem MS/MS, and collision-induced unfolding, we find that NOTCH3 mutant proteins feature increased amounts of inappropriate disulfide bridges, reduced cysteines, and structural instability.	Disulfides	153-162	notch receptor 3	Homo sapiens	87-93
7592822-3	1995	TlpA possesses an active-site disulfide bond common to all members of the thiol:disulfide oxidoreductase family.	Disulfides	30-39	TlpA	Escherichia coli	0-4
7592822-8	1995	Here, we compare the far- and near-UV CD spectra of TlpA before and after reduction of both disulfides by dithiothreitol and show that the non-active-site disulfide bond is not required for the integrity of TlpA"s native conformation.	Disulfides	92-101	TlpA	Escherichia coli	52-56
7592822-10	1995	The selective reduction of the active-site disulfide bond leads to a 10-fold increase of the intrinsic tryptophan fluorescence of TlpA at 355 nm, which may be interpreted as a quenching of tryptophan fluorescence by the active-site disulfide bond.	Disulfides	43-52	TlpA	Escherichia coli	130-134
7592822-10	1995	The selective reduction of the active-site disulfide bond leads to a 10-fold increase of the intrinsic tryptophan fluorescence of TlpA at 355 nm, which may be interpreted as a quenching of tryptophan fluorescence by the active-site disulfide bond.	Disulfides	232-241	TlpA	Escherichia coli	130-134
35393494-6	2022	Presence of a second protein factor, an N-terminal fragment of NOTCH3 (NTF), is capable of further altering disulfide statuses of both wildtype and mutant proteins, leading to increased numbers of reduced cysteines and further destabilization of NOTCH3 structure.	Disulfides	108-117	notch receptor 3	Homo sapiens	63-69
35314356-7	2022	Apo-SOD1 in the disulfide-reduced state was monomeric and was found to bind only one zinc ion per monomer.	Disulfides	16-25	aminopeptidase O (putative)	Homo sapiens	0-3
35179864-3	2022	Intracellular antioxidant proteins, such as thioredoxin 1 (Trx1) and peroxiredoxin 1 (Prx1), could regulate redox homeostasis through thiol-disulfide exchange.	Disulfides	140-149	thioredoxin	Homo sapiens	44-57
7492694-8	1995	SDS-PAGE profiles revealed that the 120-kDa protein was bound to a 28-30-kDa protein by a disulfide bond; this was compatible with the reported characteristics of human integrin alpha 6.	Disulfides	90-99	integrin subunit alpha 6	Homo sapiens	169-185
35179864-3	2022	Intracellular antioxidant proteins, such as thioredoxin 1 (Trx1) and peroxiredoxin 1 (Prx1), could regulate redox homeostasis through thiol-disulfide exchange.	Disulfides	140-149	thioredoxin	Homo sapiens	59-63
35179864-3	2022	Intracellular antioxidant proteins, such as thioredoxin 1 (Trx1) and peroxiredoxin 1 (Prx1), could regulate redox homeostasis through thiol-disulfide exchange.	Disulfides	140-149	peroxiredoxin 1	Homo sapiens	69-84
35179864-3	2022	Intracellular antioxidant proteins, such as thioredoxin 1 (Trx1) and peroxiredoxin 1 (Prx1), could regulate redox homeostasis through thiol-disulfide exchange.	Disulfides	140-149	peroxiredoxin 1	Homo sapiens	86-90
7545113-4	1995	The epitopes recognized by both antibodies are dependent on disulfide bonding and map to the major extracellular region of CD53, requiring the presence of a single threonine residue at position 154.	Disulfides	60-69	CD53 antigen	Mus musculus	123-127
35210360-5	2022	COA7 interacts transiently with the copper metallochaperones SCO1 and SCO2 and catalyzes the reduction of disulfide bonds within these proteins, which are crucial for copper relay to COX2.	Disulfides	106-115	synthesis of cytochrome C oxidase 2	Homo sapiens	70-74
35233453-5	2022	To assist homogeneous orientations of the target, disulfide bonds are introduced at the target-apoferritin interface, resulting in a cryo-EM structure at 2.6 A resolution.	Disulfides	50-59	ferritin heavy chain 1	Homo sapiens	95-106
7542475-5	1995	The slower exchange of W122 indicates that the functionally active region of BPTI, near the Cys14-Cys38 disulfide bond, is less flexible than the central region of BPTI, where the other 3 buried waters are located.	Disulfides	104-113	spleen trypsin inhibitor I	Bos taurus	77-81
35204068-3	2022	Here we report that oxidized forms of EGT, EGT-disulfide (ESSE) and 5-oxo-EGT, can be reduced by the selenoenzyme mammalian thioredoxin reductase (Sec-TrxR).	Disulfides	47-56	peroxiredoxin 5	Homo sapiens	124-145
7606797-3	1995	IL-12 is a disulfide-linked heterodimer containing two chains (designated P35 and P40); however, bioactive cytokine production has been more closely linked with P40 expression.	Disulfides	11-20	interleukin 12b	Mus musculus	82-85
2605244-4	1989	In the absence of divalent metal ions at 25 degrees C, DTNB was shown to induce an intrachain disulfide bond between Cys-127 and Cys-156 of the RLC.	Disulfides	94-103	integrin subunit alpha 9	Homo sapiens	144-147
7558602-1	1995	The solution conformation of a synthetic cyclic decapeptide [with sequence mimicking the third disulfide loop of rat transforming growth factor-alpha (rTGF-alpha)] in deuterated dimethyl sulfoxide was studied by 2D NMR.	Disulfides	95-104	transforming growth factor alpha	Rattus norvegicus	117-149
7777520-7	1995	The different subunit assemblies in TGF-beta 2 dimer were characterized in terms of the intersubunit disulfide torsion.	Disulfides	101-110	transforming growth factor beta 2	Homo sapiens	36-46
7666952-2	1995	Sustained treatment with disulfiram (Antabuse), the disulfide dimer of diethyldithiocarbamate (DDC), inhibits PHM in vivo, causing tissue levels of alpha-amidated peptides to decrease.	Disulfides	52-61	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	110-113
7759498-0	1995	The ethylene response mediator ETR1 from Arabidopsis forms a disulfide-linked dimer.	Disulfides	61-70	Signal transduction histidine kinase, hybrid-type, ethylene sensor	Arabidopsis thaliana	31-35
7759498-6	1995	Site-directed mutagenesis of two cysteines near the amino terminus of ETR1 prevented formation of the covalently linked dimer in yeast, consistent with a role in disulfide bond formation.	Disulfides	162-171	enoyl-[acyl-carrier-protein] reductase	Saccharomyces cerevisiae S288C	70-74
7759498-7	1995	These data indicate that ETR1 may use a dimeric mechanism of signal transduction in a manner similar to its bacterial counterparts but with the additional feature of a disulfide bond between monomers.	Disulfides	168-177	Signal transduction histidine kinase, hybrid-type, ethylene sensor	Arabidopsis thaliana	25-29
7663350-3	1995	Complementing these techniques with quantitative sulfhydryl assays, we discovered that the four cysteines present in rCAS form two intramolecular disulfide bonds.	Disulfides	146-155	BCAR1 scaffold protein, Cas family member	Rattus norvegicus	117-121
7663350-5	1995	When reduced and denatured rCAS was allowed to refold and its disulfide bonding state monitored, it again adopted a conformation with two intramolecular disulfide bonds.	Disulfides	62-71	BCAR1 scaffold protein, Cas family member	Rattus norvegicus	27-31
7663350-5	1995	When reduced and denatured rCAS was allowed to refold and its disulfide bonding state monitored, it again adopted a conformation with two intramolecular disulfide bonds.	Disulfides	153-162	BCAR1 scaffold protein, Cas family member	Rattus norvegicus	27-31
7663350-6	1995	The inherent ability of rCAS to quantitatively form two intramolecular disulfide bonds may reflect a previously unknown feature of the in vivo silk proteins from which it is derived.	Disulfides	71-80	BCAR1 scaffold protein, Cas family member	Rattus norvegicus	24-28
7737114-2	1995	A 78 residue antimicrobial, basic peptide, NK-lysin, with three intrachain disulfide bonds was purified from pig small intestine and characterized.	Disulfides	75-84	granulysin	Sus scrofa	43-51
7852406-0	1995	Localization of the disulfide bond involved in post-translational processing of glycosylasparaginase and disrupted by a mutation in the Finnish-type aspartylglycosaminuria.	Disulfides	20-29	aspartylglucosaminidase	Homo sapiens	80-100
7663389-6	1995	The results show that the interchain disulfide bond of M-CSF is not essential for the natural folding of active M-CSF.	Disulfides	37-46	colony stimulating factor 1 (macrophage)	Mus musculus	55-60
7530646-1	1995	We have analyzed protein folding and disulfide bond formation in the extracellular domain of the human TSH receptor (hTSHR-ecd) expressed in Escherichia coli.	Disulfides	37-46	thyroid stimulating hormone receptor	Homo sapiens	103-115
7530646-1	1995	We have analyzed protein folding and disulfide bond formation in the extracellular domain of the human TSH receptor (hTSHR-ecd) expressed in Escherichia coli.	Disulfides	37-46	thyroid stimulating hormone receptor	Homo sapiens	117-122
7829492-2	1995	Although EGF and TGF alpha share similar secondary and tertiary structures imposed by three highly conserved intramolecular disulfide bonds, they have only 30-40% overall sequence identity.	Disulfides	124-133	epidermal growth factor	Gallus gallus	9-12
7829492-2	1995	Although EGF and TGF alpha share similar secondary and tertiary structures imposed by three highly conserved intramolecular disulfide bonds, they have only 30-40% overall sequence identity.	Disulfides	124-133	transforming growth factor alpha	Gallus gallus	17-26
7710103-1	1995	Bovine erythrocyte acetylcholinesterase was prepared for tryptic digestion by radiomethylating with [14C]HCHO and NaCNBH3, cleaving with purified bacterial phosphatidylinositol-specific phospholipase C to remove the lipid portion of the glycoinositol phospholipid anchor, and reducing and alkylating the intersubunit disulfide bonds.	Disulfides	317-326	acetylcholinesterase	Bos taurus	19-39
7929230-3	1994	Consistent with being the only SPC subunit with at least one intrachain disulfide bond, SPC 25 contains 4 Cys residues.	Disulfides	72-81	SPC25 component of NDC80 kinetochore complex	Canis lupus familiaris	88-94
7944388-4	1994	A peptide encompassing Lys266-Gly295 of kallikrein, conformationally constrained by a disulfide bond, displayed the lowest Kd value (approximately 67 microM).	Disulfides	86-95	kallikrein related peptidase 4	Homo sapiens	40-50
7883753-10	1994	These results indicate that most of the C3b on HUVEC was cleaved at its alpha" chain to yield iC3b, which consists of three disulfide-linked polypeptide chains and is a ligand of the complement receptor type 3 (CR3) of phagocytes.	Disulfides	124-133	complement C3	Homo sapiens	40-43
7520437-3	1994	In vivo, native BPTI formed with a half-life of 7 min which is 3-fold faster than the optimal in vitro folding rate in growth media supplemented with low molecular weight disulfides.	Disulfides	171-181	spleen trypsin inhibitor I	Bos taurus	16-20
7520437-6	1994	We found that the folding of BPTI in E. coli was absolutely dependent on DsbA, a protein which accelerates the formation of disulfide bonds in the periplasm.	Disulfides	124-133	spleen trypsin inhibitor I	Bos taurus	29-33
8034656-5	1994	Recombinant p9Ka forms multimers in vitro, which are not due to intermolecular disulfide bridges, it binds 2 mol of calcium ions/mol of protein, and the binding of calcium ions is strongly antagonized by monovalent and divalent cations tested.	Disulfides	79-88	S100 calcium-binding protein A4	Rattus norvegicus	12-16
8055901-4	1994	Pure TlpA was shown to be a monomer in solution and was active in reducing the disulfides of insulin and in reactivating reduced, denatured RNaseA.	Disulfides	79-89	TlpA	Escherichia coli	5-9
8013347-0	1994	Treatment of IM-9 cells with human growth hormone (GH) promotes rapid disulfide linkage of the GH receptor.	Disulfides	70-79	growth hormone receptor	Homo sapiens	95-106
8013347-7	1994	The disulfide-linked form of the hGHR accounted for a substantial fraction of the receptors that became tyrosine phosphorylated early into hGH treatment.	Disulfides	4-13	growth hormone receptor	Homo sapiens	33-37
8013347-8	1994	However, formation of the disulfide-linked hGHR was not blocked by attenuation of tyrosine kinase activation, in that pretreatment of cells with staurosporine (1.25 microM) prevented detectable hGH-induced tyrosine phosphorylation without preventing the appearance of p215-230.	Disulfides	26-35	growth hormone receptor	Homo sapiens	43-47
7919999-6	1994	After reduction, the TPO activity migrated as a smear of bands from 105 to 110 kDa, suggesting that the higher molecular weight form of the enzyme is a disulfide-linked dimer.	Disulfides	152-161	thyroid peroxidase	Homo sapiens	21-24
8195177-8	1994	The oligomeric organization of purified meprin A (EC 3.4.24.18), examined by sedimentation equilibrium analysis and native gradient gel electrophoresis, is that of disulfide-bridged dimers which aggregate noncovalently to form higher molecular weight complexes, predominantly tetramers.	Disulfides	164-173	meprin 1 alpha	Mus musculus	40-48
7514598-1	1994	Human serum macrophage-stimulating protein (MSP) is a disulfide-linked heterodimer that induces motile and phagocytic activity of mouse resident peritoneal macrophages.	Disulfides	54-63	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	12-42
7514598-1	1994	Human serum macrophage-stimulating protein (MSP) is a disulfide-linked heterodimer that induces motile and phagocytic activity of mouse resident peritoneal macrophages.	Disulfides	54-63	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	44-47
8058646-2	1994	Following tritiation, the BDNF was biotinylated via a disulfide linker and was coupled to a covalent conjugate of neutral avidin (NLA), which binds the biotinylated peptide with a high affinity, and the murine OX26 monoclonal antibody to the rat transferrin receptor.	Disulfides	54-63	brain-derived neurotrophic factor	Rattus norvegicus	26-30
8163539-6	1994	Another mutant, PDGF-B(C2,4S), in which just the 2 cysteines involved in interchain disulfides were converted to serine, ran as a monomer on SDS-polyacrylamide gels as expected.	Disulfides	84-94	platelet derived growth factor subunit B	Homo sapiens	16-22
7523290-0	1994	Novel heterogeneity of the leucocyte common antigen (CD45): disulfide-bound heterodimers between CD45 and an 80 kDa polypeptide.	Disulfides	60-69	protein tyrosine phosphatase receptor type C	Homo sapiens	53-57
7523290-0	1994	Novel heterogeneity of the leucocyte common antigen (CD45): disulfide-bound heterodimers between CD45 and an 80 kDa polypeptide.	Disulfides	60-69	protein tyrosine phosphatase receptor type C	Homo sapiens	97-101
7523290-3	1994	In this paper we report an additional basis for generation of heterogeneity by revealing that CD45 can form disulfide-bound heterodimers with an 80 kDa polypeptide.	Disulfides	108-117	protein tyrosine phosphatase receptor type C	Homo sapiens	94-98
8144590-6	1994	The overall structure of cholinesterases was conserved in ACE-1 as indicated by the conserved sequence positions of Ser-216, His-468, and Glu-346 (S200, H440, E327 in Torpedo (AChE) as components of the catalytic triad, of the six cysteines which form three intrachain disulfide bonds, and of Trp-99(84), a critical side chain in the choline binding site.	Disulfides	269-278	ACE1	Drosophila melanogaster	58-63
7907329-8	1994	These findings demonstrate that nascent unfolded p70 is tethered to calnexin during normal protein maturation, including the formation and editing of disulfide bonds and that ATP is required for the productive interaction of gp80 and calnexin.	Disulfides	150-159	calnexin	Canis lupus familiaris	68-76
7818854-0	1994	A nuclear magnetic resonance study of the DNA-binding affinity of Cro repressor protein stabilized by a disulfide bond.	Disulfides	104-113	cro	Escherichia virus Lambda	66-69
8167239-1	1994	Sulfated glycoprotein 2 (SGP 2) is a 73-kDa highly glycosylated disulfide-linked heterodimer.	Disulfides	64-73	clusterin	Rattus norvegicus	0-23
8167239-1	1994	Sulfated glycoprotein 2 (SGP 2) is a 73-kDa highly glycosylated disulfide-linked heterodimer.	Disulfides	64-73	clusterin	Rattus norvegicus	25-30
7509003-2	1994	The Env-Sea oncoprotein is synthesized as a precursor of 155 kDa which undergoes proteolytic processing to generate a disulfide-linked complex of the proteins gp85 and gp70.	Disulfides	118-127	endogenous retrovirus group K member 20	Homo sapiens	4-7
7508987-1	1994	Bovine pancreatic trypsin inhibitor (BPTI) unfolds upon reduction of its three disulfide bonds.	Disulfides	79-88	spleen trypsin inhibitor I	Bos taurus	0-35
7508987-1	1994	Bovine pancreatic trypsin inhibitor (BPTI) unfolds upon reduction of its three disulfide bonds.	Disulfides	79-88	spleen trypsin inhibitor I	Bos taurus	37-41
8300582-3	1994	To facilitate studies of structure-function relationships in HB-EGF, a bacterial recombinant expression system was established that produced biologically active HB-EGF with the expected disulfide bonding pattern.	Disulfides	186-195	proheparin-binding EGF-like growth factor	Cricetulus griseus	161-167
8305467-4	1994	The retinal oxidase is a metalloflavoenzyme containing 2 FADs as the coenzyme, and 8 irons, 2 molybdenums, 2 disulfide bonds and 8 inorganic sulfurs.	Disulfides	109-118	aldehyde oxidase 1	Oryctolagus cuniculus	4-19
7688428-1	1993	Herein we describe the results of molecular dynamics simulations of the bovine pancreatic trypsin inhibitor (BPTI) in solution at a variety of temperatures both with and without disulfide bonds.	Disulfides	178-187	spleen trypsin inhibitor I	Bos taurus	72-107
7688428-1	1993	Herein we describe the results of molecular dynamics simulations of the bovine pancreatic trypsin inhibitor (BPTI) in solution at a variety of temperatures both with and without disulfide bonds.	Disulfides	178-187	spleen trypsin inhibitor I	Bos taurus	109-113
7692879-1	1993	In a mouse/human chimeric IgG1 Ab with a deletion of the CH1 domain the disulfide bridges between H and L chain cannot be formed, although the corresponding cysteine residues are present.	Disulfides	72-81	LOC105243590	Mus musculus	26-30
7685018-0	1993	Disulfide bond mutations affect the folding of the human chorionic gonadotropin-beta subunit in transfected Chinese hamster ovary cells.	Disulfides	0-9	chorionic gonadotropin subunit beta 3	Homo sapiens	57-92
8349412-1	1993	Disulfide structure and characterization of BDNF expressed in CHO cells.	Disulfides	0-9	brain-derived neurotrophic factor	Cricetulus griseus	44-48
8349412-2	1993	Three disulfide linkages of recombinant human brain-derived neurotrophic factor (BDNF) were determined by peptide sequence analysis and characterized by mass spectrometry.	Disulfides	6-15	brain derived neurotrophic factor	Homo sapiens	46-79
8349412-2	1993	Three disulfide linkages of recombinant human brain-derived neurotrophic factor (BDNF) were determined by peptide sequence analysis and characterized by mass spectrometry.	Disulfides	6-15	brain derived neurotrophic factor	Homo sapiens	81-85
8349412-3	1993	The three disulfide bonds for BDNF expressed in Chinese hamster ovary cells include Cys-13-Cys-80, Cys-58-Cys-109 and Cys-68-Cys-111, and the disulfide structure was homologous to that of nerve growth factor.	Disulfides	10-19	brain-derived neurotrophic factor	Cricetulus griseus	30-34
7685111-6	1993	Consistent with the cell-autonomous nature of the Sb-sbd bristle phenotype, a disulfide bond between cysteine residues in the noncatalytic N-terminal fragment and the C-terminal catalytic fragment could tether the protease to the membrane after activation.	Disulfides	78-87	Stubble	Drosophila melanogaster	50-56
8387092-0	1993	Disulfide linkage between C3b and tetanus toxin on tetanus toxin-specific EBV-transformed B cells.	Disulfides	0-9	complement C3	Homo sapiens	26-29
8387092-4	1993	When C3b was incubated with the same cells coated with tetanus toxin bound to their specific membrane Ig, preferential formation of disulfide-bonded complexes between tetanus toxin and C3b was observed.	Disulfides	132-141	complement C3	Homo sapiens	5-8
8387092-4	1993	When C3b was incubated with the same cells coated with tetanus toxin bound to their specific membrane Ig, preferential formation of disulfide-bonded complexes between tetanus toxin and C3b was observed.	Disulfides	132-141	complement C3	Homo sapiens	185-188
8387092-7	1993	In the context of Ag processing and presentation by B cells, disulfide binding of chaperone C3b to Ag is likely to persist during transcytosis and to play a significant role in the modulation of the processing.	Disulfides	61-70	complement C3	Homo sapiens	92-95
8324198-2	1993	We replaced endogenous TnC in single skinned fibers from rabbit psoas muscle with a modified form of cardiac TnC (cTnC) which, unlike native cTnC, probably contains an intramolecular disulfide bond.	Disulfides	183-192	tenascin	Oryctolagus cuniculus	109-112
8474164-7	1993	Analogous to gp55, gp42 is processed inefficiently as a disulfide-bonded dimer to form cell surface gp42p.	Disulfides	56-65	neuroplastin	Homo sapiens	13-17
8474164-7	1993	Analogous to gp55, gp42 is processed inefficiently as a disulfide-bonded dimer to form cell surface gp42p.	Disulfides	56-65	basigin	Mus musculus	19-23
8454849-1	1993	The Fc gamma RIIIA, which is composed of a transmembrane IgG-binding glycoprotein and either a disulfide-linked homodimer (zeta zeta, gamma gamma) or heterodimer (zeta gamma), mediates the antibody-dependent cellular cytotoxicity in NK cells.	Disulfides	95-104	Fc gamma receptor IIIa	Homo sapiens	4-18
8429021-6	1993	Unlike all previously described members of this superfamily, both GDF-3 and GDF-9 lack the conserved cysteine residue that is believed to form the sole disulfide linkage between subunits in other family members.	Disulfides	152-161	LOC105378979	Homo sapiens	66-71
8429021-6	1993	Unlike all previously described members of this superfamily, both GDF-3 and GDF-9 lack the conserved cysteine residue that is believed to form the sole disulfide linkage between subunits in other family members.	Disulfides	152-161	growth differentiation factor 9	Homo sapiens	76-81
7679640-5	1993	According to the disulfide-bridge positions and the long-range NOE observed these secondary-structural elements fold in a similar manner to BPTI.	Disulfides	17-26	spleen trypsin inhibitor I	Bos taurus	140-144
8423792-5	1993	The third novel BGP isoform contains none of the extracellular disulfide-linked immunoglobulin-like domains typical of these molecules but retains N-terminal and intracellular domains, suggesting distinct functions for N-terminal versus other disulfide-linked domains.	Disulfides	63-72	CEA cell adhesion molecule 1	Homo sapiens	16-19
8423792-5	1993	The third novel BGP isoform contains none of the extracellular disulfide-linked immunoglobulin-like domains typical of these molecules but retains N-terminal and intracellular domains, suggesting distinct functions for N-terminal versus other disulfide-linked domains.	Disulfides	243-252	CEA cell adhesion molecule 1	Homo sapiens	16-19
8420975-3	1993	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis indicated that approximately 70% of CD8 alpha 161 was secreted as a disulfide-linked dimer, but CD8 alpha 114 was not disulfide-linked.	Disulfides	135-144	CD8a molecule	Homo sapiens	103-112
8416818-0	1993	Disulfide bridges in human complement component C3b.	Disulfides	0-9	complement C3	Homo sapiens	48-51
8416818-1	1993	The disulfide bridges of human complement component C3b, derived from C3 by removal of the 77-residue C3a, have been determined.	Disulfides	4-13	complement C3	Homo sapiens	52-55
8416941-0	1993	Oxidative inactivation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and subunit cross-linking involve different dithiol/disulfide centers.	Disulfides	126-135	3-hydroxy-3-methylglutaryl-CoA reductase	Rattus norvegicus	26-73
8374001-7	1993	Second, single cysteine substitutions in PRPs (Pa from PRH1 and G1 8 from PRB3) may lead to disulfide bonded homodimers as well as heterodimers with salivary peroxidase.	Disulfides	92-101	proline rich protein BstNI subfamily 3	Homo sapiens	74-78
8422543-2	1993	HGF, first purified to homogeneity from rat platelets in 1986, is a disulfide-linked heterodimer molecule composed of a 69 kDa alpha-subunit and a 34 kDa beta-subunit.	Disulfides	68-77	hepatocyte growth factor	Rattus norvegicus	0-3
1281423-0	1992	Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP.	Disulfides	60-69	proteolipid protein 1	Homo sapiens	0-19
1281423-0	1992	Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide-bonded, and fatty acid thioester-linked cysteine residues and implications for the membrane topology of PLP.	Disulfides	60-69	proteolipid protein 1	Homo sapiens	21-24
1465440-1	1992	A mutation in the Escherichia coli dsbA gene (coding for a periplasmic disulfide oxidoreductase) reduces the rate of disulfide bond formation in the enzyme pullulanase and also reduces the rate at which the enzyme is secreted to the cell surface, as measured by protease accessibility.	Disulfides	71-80	oxidoreductase	Escherichia coli	81-95
1447207-0	1992	Inactivation of ribonuclease inhibitor by thiol-disulfide exchange.	Disulfides	48-57	ribonuclease/angiogenin inhibitor 1	Homo sapiens	16-38
1447207-7	1992	All 1/2-cystinyl residues in the inactive, monomeric inhibitor had formed disulfide bridges, judged by the absence of either free thiol groups or mixed disulfides with 5-mercapto-2-nitrobenzoate.	Disulfides	74-83	ALL1	Homo sapiens	0-5
1429587-2	1992	Expression of the cDNA in COS cells showed that COMP is a homopolymer composed of five identical disulfide-linked subunits.	Disulfides	97-106	cartilage oligomeric matrix protein	Homo sapiens	48-52
1328198-2	1992	In the present study, we produced the recombinant human OP-1 (hOP-1) in mammalian cells as a processed mature disulfide-linked homodimer with an apparent molecular weight of 36,000.	Disulfides	110-119	bone morphogenetic protein 7	Homo sapiens	56-60
1328198-2	1992	In the present study, we produced the recombinant human OP-1 (hOP-1) in mammalian cells as a processed mature disulfide-linked homodimer with an apparent molecular weight of 36,000.	Disulfides	110-119	bone morphogenetic protein 7	Homo sapiens	62-67
1457207-7	1992	Our results indicate that the cysteines that form the V3 loop or the disulfide bond itself are important for proper envelope glycoprotein folding and processing.	Disulfides	69-78	endogenous retrovirus group K member 20	Homo sapiens	116-137
1382647-4	1992	For this purpose, we take a look at the formation and breaking of disulfide bonds during the folding process of BPTI.	Disulfides	66-75	spleen trypsin inhibitor I	Bos taurus	112-116
1384031-1	1992	The rates of folding and disulfide bond formation in reduced BPTI were measured in vitro in the presence and absence of total protein from the endoplasmic reticulum.	Disulfides	25-34	spleen trypsin inhibitor I	Bos taurus	61-65
1510914-2	1992	The crystal structure of pancreatic lipase suggests that it contains a trypsin-like Asp-His-Ser catalytic triad at the active center, which is shielded by a disulfide bridge-bounded surface loop that must be repositioned before the substrate can gain access to the catalytic residues.	Disulfides	157-166	pancreatic lipase	Homo sapiens	25-42
1495977-3	1992	We show here that TCR gamma-IgH and TCR delta-IgH chimeric chains are produced intracellularly in significant amounts, that the two chains can assemble correctly to form disulfide-linked, glycosylated heterodimers, and that a selective mechanism allows secretion of correctly paired receptor chains into the medium.	Disulfides	170-179	immunoglobulin heavy chain complex	Mus musculus	28-31
1495977-3	1992	We show here that TCR gamma-IgH and TCR delta-IgH chimeric chains are produced intracellularly in significant amounts, that the two chains can assemble correctly to form disulfide-linked, glycosylated heterodimers, and that a selective mechanism allows secretion of correctly paired receptor chains into the medium.	Disulfides	170-179	immunoglobulin heavy chain complex	Mus musculus	46-49
1629227-4	1992	Protein disulfide isomerase is an oxidoreductase which catalyzes the interconversion between the reduced and oxidized states of proteins which contain multiple sulfhydryl groups and disulfide bonds.	Disulfides	8-17	thioredoxin reductase 1	Homo sapiens	34-48
1380192-1	1992	Recent studies of the disulfide-bonded intermediates in the refolding of bovine pancreatic trypsin inhibitor (BPTI) indicate that the most stable intermediates can take on much or all of the structure of the fully folded protein.	Disulfides	22-31	spleen trypsin inhibitor I	Bos taurus	73-108
1380192-1	1992	Recent studies of the disulfide-bonded intermediates in the refolding of bovine pancreatic trypsin inhibitor (BPTI) indicate that the most stable intermediates can take on much or all of the structure of the fully folded protein.	Disulfides	22-31	spleen trypsin inhibitor I	Bos taurus	110-114
1317541-5	1992	Under non-reducing conditions both p170met and the alpha, beta-disulfide-linked protein are detected as a 185 kDa product (p185met), but only alpha-beta heterodimeric p185met is cross-linked and rendered resistant to disulfide reduction with membrane-impermeable 6.4 A linker length cross-linking reagents.	Disulfides	63-72	eukaryotic translation initiation factor 3 subunit A	Homo sapiens	123-127
1584784-2	1992	By using ribonuclease T1 as a model system, we show that these two processes can become linked in the oxidative folding of reduced proteins and that the formation of the correct disulfide bonds is facilitated in the presence of peptidyl-prolyl cis-trans isomerase.	Disulfides	178-187	peptidylprolyl isomerase like 1	Homo sapiens	228-263
1584784-3	1992	In particular, the efficiency of protein disulfide isomerase (EC 5.3.4.1) as a catalyst of disulfide bond formation in the course of oxidative folding is markedly improved when peptidyl-prolyl cis-trans isomerase is present simultaneously.	Disulfides	41-50	peptidylprolyl isomerase like 1	Homo sapiens	177-212
1368343-6	1992	These results and gene structure indicate that CA2 is a heterotetramer consisting of two large and two small subunits linked by disulfide bonds like CA1, which is the CAH1 gene product.	Disulfides	128-137	uncharacterized protein	Chlamydomonas reinhardtii	167-171
1547238-10	1992	The fluorescence quenching event observed upon Ca2+ ion binding is due to a disulfide-pi-electron interaction that causes a 100 degrees reorientation of Trp42 of the Gla domain.	Disulfides	76-85	galactosidase alpha	Homo sapiens	166-169
1547238-12	1992	The Gla domain and its trailing disulfide unit associate intimately and together give rise to a domain-like structure.	Disulfides	32-41	galactosidase alpha	Homo sapiens	4-7
1557043-0	1992	Effects of limited reduction on disulfide bonds in human IgA1 and IgA1 fragments.	Disulfides	32-41	immunoglobulin heavy constant alpha 1	Homo sapiens	57-61
1557043-0	1992	Effects of limited reduction on disulfide bonds in human IgA1 and IgA1 fragments.	Disulfides	32-41	immunoglobulin heavy constant alpha 1	Homo sapiens	66-70
1371875-1	1992	In the oxidative folding of bovine pancreatic trypsin inhibitor (BPTI) at neutral pH, only two one-disulfide intermediates accumulate to a significant extent, namely [5-55] and [30-51].	Disulfides	99-108	spleen trypsin inhibitor I	Bos taurus	65-69
1603807-3	1992	Reduction of disulfides caused large changes in the intrinsic fluorescence and abolished the gelatin-binding activity of 42-kDa GBF and two nonoverlapping gelatin-binding subfragments, 30-kDa GBF (I6-II1-II2-I7) and 21-kDa GBF (I8-I9).	Disulfides	13-23	Kruppel like factor 6	Homo sapiens	128-131
1603807-3	1992	Reduction of disulfides caused large changes in the intrinsic fluorescence and abolished the gelatin-binding activity of 42-kDa GBF and two nonoverlapping gelatin-binding subfragments, 30-kDa GBF (I6-II1-II2-I7) and 21-kDa GBF (I8-I9).	Disulfides	13-23	Kruppel like factor 6	Homo sapiens	192-195
1603807-3	1992	Reduction of disulfides caused large changes in the intrinsic fluorescence and abolished the gelatin-binding activity of 42-kDa GBF and two nonoverlapping gelatin-binding subfragments, 30-kDa GBF (I6-II1-II2-I7) and 21-kDa GBF (I8-I9).	Disulfides	13-23	Kruppel like factor 6	Homo sapiens	192-195
1319550-2	1992	In addition to the 180 kDa mGC, there exists another 120-130 kDa protein which is also bifunctional and a 120 kDa disulfide-linked dimeric cell surface protein that is an ANF receptor, but is not a part of guanylate cyclase.	Disulfides	114-123	natriuretic peptide A	Rattus norvegicus	171-174
1428397-3	1992	It has recently been shown that CD16 is associated with disulfide-linked dimers composed of 2 homologous sub-units, zeta and gamma.	Disulfides	56-65	Fc gamma receptor IIIa	Homo sapiens	32-36
1836994-4	1991	Competition studies with structural variants of ANP demonstrate that both the C terminus and the disulfide loop of the molecule are essential for high-affinity binding.	Disulfides	97-106	natriuretic peptide A	Rattus norvegicus	48-51
1663820-5	1991	The lead compound (Arg6,Cha8 ANF 6-15 Phe-Arg-Cys-NH2) is a tridecapeptide that integrates the C-terminal amino acids inside the disulfide ring.	Disulfides	129-138	natriuretic peptide A	Rattus norvegicus	29-32
1772437-2	1991	Purified gp 80 was found to have a disulfide-bonded dimeric structure, and appeared to exist in two molecular forms, a major (high-molecular weight) form consisting of a 46 KDa subunit and a 39 KDa subunit and a minor (low-molecular weight) form consisting of a 46 KDa subunit and a 33 KDa subunit.	Disulfides	35-44	clusterin	Canis lupus familiaris	9-14
1712728-2	1991	The extracellular-matrix glycoprotein, tenascin, consists of disulfide-linked subunits of 190, 200 and 230 kDa (the three splicing variants reported in chicken) and usually exists as a six-armed structure under the electron microscope.	Disulfides	61-70	avian tenascin X	Gallus gallus	39-47
1712728-6	1991	These fragments represent the thin proximal part of the tenascin arms and they are still partially linked to dimers and trimers via disulfide bridges.	Disulfides	132-141	avian tenascin X	Gallus gallus	56-64
1989985-0	1991	Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase.	Disulfides	20-29	acid phosphatase 3	Homo sapiens	112-138
1790669-14	1991	At the polypeptide level, comparisons of chymotryptic and endoproteinase-Arg-C peptide maps, as well as CNBr-cleavage products, suggested that tunicate and mouse Lyt-1 molecules are structurally similar and that each may contain at least one intra-chain disulfide bridge.	Disulfides	254-263	CD5 antigen	Mus musculus	162-167
1708670-11	1990	These data suggest that the predominant form of PAI-2 in placenta extract is heterogeneous and of high molecular mass, containing complexes in which vitronectin is covalently bound to PAI-2 by disulfide bridges.	Disulfides	193-202	vitronectin	Homo sapiens	149-160
2229039-4	1990	p18 appears to possess five disulfide bonds per molecule.	Disulfides	28-37	cyclin dependent kinase inhibitor 2C	Mus musculus	0-3
2171674-7	1990	The results of additional experiments using erythrocyte lysate and of kinetic experiments on solutions containing PSSG and/or GSH, NADPH and glutathione reductase suggest that the predominant mechanism for reduction of PSSG is by a thiol-disulfide exchange reaction with GSH to form PSH and GSSG, which in turn undergoes enzyme-catalyzed reduction by NADPH.	Disulfides	238-247	2,4-dienoyl-CoA reductase 1	Homo sapiens	131-136
2171674-7	1990	The results of additional experiments using erythrocyte lysate and of kinetic experiments on solutions containing PSSG and/or GSH, NADPH and glutathione reductase suggest that the predominant mechanism for reduction of PSSG is by a thiol-disulfide exchange reaction with GSH to form PSH and GSSG, which in turn undergoes enzyme-catalyzed reduction by NADPH.	Disulfides	238-247	2,4-dienoyl-CoA reductase 1	Homo sapiens	351-356
2171329-0	1990	Alleles at the PRB3 locus coding for a disulfide-bonded human salivary proline-rich glycoprotein (Gl 8) and a null in an Ashkenazi Jew.	Disulfides	39-48	proline rich protein BstNI subfamily 3	Homo sapiens	15-19
2171329-1	1990	From electrophoretic analysis, we identified in the saliva of an Ashkenazi Jew a disulfide-bonded major glycoprotein variant (Gl 8) that is a product of the proline-rich protein (PRP) locus PRB3.	Disulfides	81-90	proline rich protein BstNI subfamily 3	Homo sapiens	190-194
2171329-10	1990	It is interesting that products of different PRP genes, Gl 8 from PRB3 and Pa 1 from PRH1, are both disulfide bonded and probably modify salivary peroxidase (part of an important intraoral antibacterial system) through formation of disulfide-bonded heterodimers.	Disulfides	100-109	proline rich protein BstNI subfamily 3	Homo sapiens	66-70
2171329-10	1990	It is interesting that products of different PRP genes, Gl 8 from PRB3 and Pa 1 from PRH1, are both disulfide bonded and probably modify salivary peroxidase (part of an important intraoral antibacterial system) through formation of disulfide-bonded heterodimers.	Disulfides	100-109	proline rich protein HaeIII subfamily 1	Homo sapiens	85-89
2171329-10	1990	It is interesting that products of different PRP genes, Gl 8 from PRB3 and Pa 1 from PRH1, are both disulfide bonded and probably modify salivary peroxidase (part of an important intraoral antibacterial system) through formation of disulfide-bonded heterodimers.	Disulfides	232-241	proline rich protein BstNI subfamily 3	Homo sapiens	66-70
2171329-10	1990	It is interesting that products of different PRP genes, Gl 8 from PRB3 and Pa 1 from PRH1, are both disulfide bonded and probably modify salivary peroxidase (part of an important intraoral antibacterial system) through formation of disulfide-bonded heterodimers.	Disulfides	232-241	proline rich protein HaeIII subfamily 1	Homo sapiens	85-89
1697643-5	1990	Fragments generated by enzyme digest further suggest that the peptide recognized on beef insulin appears to involve A-chain loop residues A5-A12 and B-chain residues B7-B13 that are linked by the A7-B7 disulfide bridge.	Disulfides	202-211	LOC105613195	Ovis aries	89-96
2351656-3	1990	Mature platelet GPIIb is processed from a single precursor peptide into a disulfide-linked GPIIb alpha and GPIIb beta chain.	Disulfides	74-83	integrin subunit alpha 2b	Homo sapiens	16-21
2351656-3	1990	Mature platelet GPIIb is processed from a single precursor peptide into a disulfide-linked GPIIb alpha and GPIIb beta chain.	Disulfides	74-83	integrin subunit alpha 2b	Homo sapiens	91-96
2351656-3	1990	Mature platelet GPIIb is processed from a single precursor peptide into a disulfide-linked GPIIb alpha and GPIIb beta chain.	Disulfides	74-83	integrin subunit alpha 2b	Homo sapiens	91-96
2111326-5	1990	The molecule contains unstable intramolecular disulfide bonds that undergo disulfide exchange during solubilization, thereby covalently cross-linking neighboring synaptophysin molecules.	Disulfides	46-55	synaptophysin	Homo sapiens	162-175
2111326-5	1990	The molecule contains unstable intramolecular disulfide bonds that undergo disulfide exchange during solubilization, thereby covalently cross-linking neighboring synaptophysin molecules.	Disulfides	75-84	synaptophysin	Homo sapiens	162-175
2111326-6	1990	The locations of the intramolecular disulfide bonds in synaptophysin were determined, revealing that each of the two intravesicular loops of synaptophysin is circularized by a single disulfide bond.	Disulfides	36-45	synaptophysin	Homo sapiens	55-68
2111326-6	1990	The locations of the intramolecular disulfide bonds in synaptophysin were determined, revealing that each of the two intravesicular loops of synaptophysin is circularized by a single disulfide bond.	Disulfides	36-45	synaptophysin	Homo sapiens	141-154
2111326-6	1990	The locations of the intramolecular disulfide bonds in synaptophysin were determined, revealing that each of the two intravesicular loops of synaptophysin is circularized by a single disulfide bond.	Disulfides	183-192	synaptophysin	Homo sapiens	55-68
2111326-6	1990	The locations of the intramolecular disulfide bonds in synaptophysin were determined, revealing that each of the two intravesicular loops of synaptophysin is circularized by a single disulfide bond.	Disulfides	183-192	synaptophysin	Homo sapiens	141-154
2111326-7	1990	Cross-linking of synaptophysin by disulfide bonds can be triggered in synaptic vesicles and in intact cells by a cycle of reduction and oxidation, suggesting that native synaptophysin is a homomultimer in situ.	Disulfides	34-43	synaptophysin	Homo sapiens	17-30
2111326-7	1990	Cross-linking of synaptophysin by disulfide bonds can be triggered in synaptic vesicles and in intact cells by a cycle of reduction and oxidation, suggesting that native synaptophysin is a homomultimer in situ.	Disulfides	34-43	synaptophysin	Homo sapiens	170-183
2111326-8	1990	In addition, chemical cross-linking of native synaptophysin demonstrates that a low molecular weight protein is specifically associated with synaptophysin complexes and is lost upon reduction of the intramolecular disulfide bonds.	Disulfides	214-223	synaptophysin	Homo sapiens	46-59
2111326-9	1990	These data suggest that native synaptophysin forms a noncovalent homomultimeric complex whose structure and interaction with other proteins are dependent on the integrity of its intramolecular disulfide bonds and phospholipid environment.	Disulfides	193-202	synaptophysin	Homo sapiens	31-44
1693524-10	1990	The major unfolding/refolding phase for each of the 30-51 mutants was more than an order of magnitude slower than for Ala14/Ala38 or for BPTI in which the 14-38 disulfide bond was specifically reduced and blocked with iodoacetamide [Jullien, M., &amp; Baldwin, R. L. (1981) J. Mol.	Disulfides	161-170	spleen trypsin inhibitor I	Bos taurus	137-141
2327790-16	1990	A model is proposed suggesting that the 60-kDa fragment was generated by trypsin cleavage of native TPO at two internal sites within a disulfide loop (res approximately 300 and res 564) and at one further internal site (res 280).	Disulfides	135-144	thyroid peroxidase	Homo sapiens	100-103
1691184-12	1990	Gap b3 consists of two polypeptide chains (Mr = 110,000 and 30,000), which seem to be proteolytic cleavage products connected by disulfide bonds from a precursor protein.	Disulfides	129-138	integrin subunit alpha 3	Homo sapiens	0-6
2114044-5	1990	However, reduction of disulfide bonds unmasked the epitope on the heavy chain of tPA which became accessible to anti-tPA4-8 antibodies.	Disulfides	22-31	chromosome 20 open reading frame 181	Homo sapiens	81-84
2159799-0	1990	Role of extracellular disulfide-bonded cysteines in the ligand binding function of the beta 2-adrenergic receptor.	Disulfides	22-31	adrenoceptor beta 2	Homo sapiens	87-113
2318210-11	1990	Enzymatic digestion of non-reduced rCD4 generated disulfide-bonded fragments that demonstrated the presence of disulfide bonds between Cys-16 and Cys-84, Cys-130 and Cys-159, and between Cys-303 and Cys-345.	Disulfides	50-59	Cd4 molecule	Rattus norvegicus	35-39
2318210-11	1990	Enzymatic digestion of non-reduced rCD4 generated disulfide-bonded fragments that demonstrated the presence of disulfide bonds between Cys-16 and Cys-84, Cys-130 and Cys-159, and between Cys-303 and Cys-345.	Disulfides	111-120	Cd4 molecule	Rattus norvegicus	35-39
2139352-0	1990	The disulfide bonded ring of iso-rANP, unlike that of rANP, has potent cardiovascular activity.	Disulfides	4-13	natriuretic peptide A	Rattus norvegicus	33-37
2139352-1	1990	Iso-atrial natriuretic peptide (iso-rANP), a 45 amino acid peptide with a disulfide bond between residues 23 and 39, is a newly discovered second atrial hormone with considerable homology with rat atrial natriuretic peptide (rANP).	Disulfides	74-83	natriuretic peptide A	Rattus norvegicus	36-40
2584692-6	1989	We suggest that PDI catalyzes the formation of disulfide bonds of various secretory proteins, perhaps type II procollagen, in the cisternal space of the ER in epiphyseal chondrocytes.	Disulfides	47-56	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	16-19
34952470-4	2022	As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5.	Disulfides	26-35	PDI-like 1-4	Arabidopsis thaliana	165-171
34656934-4	2022	Herein, the purity assignment of a synthetic oxytocin containing a disulfide linkage was established based on a mass balance method, which had never been performed for a cross-linked peptide.	Disulfides	67-76	oxytocin/neurophysin I prepropeptide	Homo sapiens	45-53
34465218-5	2022	CRITICAL ISSUES: In addition to the predicted function of ER protein quality control, several independent studies have suggested the diverse roles of TMX family proteins in the regulation of cellular processes, including calcium homeostasis, bioenergetics, and thiol-disulfide exchange in the extracellular space.	Disulfides	267-276	thioredoxin related transmembrane protein 1	Homo sapiens	150-153
34428381-2	2021	The poly(t-butyl betaine carboxylate) (PCB-tBU) segment was conjugated to the poly(1, 3-dioxan-2-one)(PDI) moity with a disulfide bond to obtain the copolymer PCB-tBU-S-S-PDI.	Disulfides	120-129	pyruvate carboxylase	Rattus norvegicus	39-42
34077620-6	2021	Specifically, we demonstrate that the ZG16 cysteine thiols can be oxidized to a disulfide by QSOX1, which is a sulfhydryl oxidase present together with ZG16 in the Golgi apparatus and in mucus, as well as by protein disulfide isomerase.	Disulfides	80-89	quiescin sulfhydryl oxidase 1	Homo sapiens	93-98
33818502-0	2021	Exploring the contribution of the mitochondrial disulfide relay system to Parkinson"s disease: the PINK1/CHCHD4 interplay.	Disulfides	48-57	PTEN induced kinase 1	Homo sapiens	99-104
33818502-0	2021	Exploring the contribution of the mitochondrial disulfide relay system to Parkinson"s disease: the PINK1/CHCHD4 interplay.	Disulfides	48-57	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	105-111
34241972-4	2021	The complement proteins C7 and C6 share very high sequence homology and exhibit several conserved domains, disulfide bridges, and C-mannosylation sites.	Disulfides	107-116	complement C7	Homo sapiens	24-33
34647648-0	2022	Novel CACNA1A Variant p.Cys256Phe Disrupts Disulfide Bonds and Causes Spinocerebellar Ataxia.	Disulfides	43-52	calcium voltage-gated channel subunit alpha1 A	Homo sapiens	6-13
34509915-6	2021	C262S/264S sEH mutants were resistant to peroxide-induced activation, corroborating the disulfide-activation mechanism.	Disulfides	88-97	epoxide hydrolase 2, cytoplasmic	Mus musculus	11-14
34174313-0	2021	Generation of soluble, disulfide-rich JEV NS1 protein recognizable by anti-NS1 antibodies through a simplified, in vitro refolding approach.	Disulfides	23-32	influenza virus NS1A binding protein	Homo sapiens	42-45
34174313-0	2021	Generation of soluble, disulfide-rich JEV NS1 protein recognizable by anti-NS1 antibodies through a simplified, in vitro refolding approach.	Disulfides	23-32	influenza virus NS1A binding protein	Homo sapiens	75-78
2482292-1	1989	Tenascin is a large, disulfide-bonded glycoprotein of the extracellular matrix.	Disulfides	21-30	tenascin C	Homo sapiens	0-8
34360775-12	2021	The changes are exemplified by the thiamine enhancement of the SIRT2 correlations with metabolic enzymes and proteins of thiol-disulfide metabolism.	Disulfides	127-136	sirtuin 2	Rattus norvegicus	63-68
2482065-6	1989	alpha-Thrombin-serpin complexes but not Xa-serpin complexes formed disulfide-bonded complexes with vitronectin.	Disulfides	67-76	vitronectin	Homo sapiens	99-110
34116124-6	2021	Furthermore, we demonstrate that MPV17 forms oligomers in a lipid bilayer that are further stabilized by disulfide-bridges.	Disulfides	105-114	mitochondrial inner membrane protein MPV17	Homo sapiens	33-38
34116124-9	2021	These data suggest that, induced by oxidative stress, MPV17 can alter its oligomeric state from a properly folded monomer to a disulfide-stabilized oligomeric pore which might be required for the transport of metabolic DNA precursors into the mitochondrial matrix to compensate for the damage caused by reactive oxygen species.	Disulfides	127-136	mitochondrial inner membrane protein MPV17	Homo sapiens	54-59
34194623-1	2021	L-type amino acid transporter 1 (LAT1)/SLC7A5 is the first identified CD98 light chain disulfide linked to the CD98 heavy chain (CD98hc/SLC3A2).	Disulfides	87-96	solute carrier family 7 (cationic amino acid transporter, y+ system), member 5	Mus musculus	0-31
34194623-1	2021	L-type amino acid transporter 1 (LAT1)/SLC7A5 is the first identified CD98 light chain disulfide linked to the CD98 heavy chain (CD98hc/SLC3A2).	Disulfides	87-96	solute carrier family 7 (cationic amino acid transporter, y+ system), member 5	Mus musculus	33-37
2701945-2	1989	On thymocytes, CD1a forms noncovalent complexes with CD1b and CD1c, and a disulfide-linked heterodimer with CD8.	Disulfides	74-83	CD8a molecule	Homo sapiens	108-111
34194623-1	2021	L-type amino acid transporter 1 (LAT1)/SLC7A5 is the first identified CD98 light chain disulfide linked to the CD98 heavy chain (CD98hc/SLC3A2).	Disulfides	87-96	solute carrier family 7 (cationic amino acid transporter, y+ system), member 5	Mus musculus	39-45
2553632-8	1989	For DPDPE, however, this was only possible with a positive dihedral angle for the disulfide bond due to the presence of the beta-carbon methyls of Pen2.	Disulfides	82-91	presenilin enhancer, gamma-secretase subunit	Homo sapiens	147-151
35244730-4	2022	The current model consists of AS3MT methylating iAs in the presence of the cofactor S-adenosyl-L-methionine (SAM), and the formation of intramolecular disulfide bonds following the reduction of MAsV to MAsIII.	Disulfides	151-160	arsenite methyltransferase	Mus musculus	30-35
35398099-6	2022	Furthermore, our structure captured a fortuitous higher-order assembly between IL-18 and IL-18BP coordinated by a disulfide-bond distal to the binding surface connecting IL-18 and IL-18BP molecules from different complexes, resulting in a novel tetramer with 2:2 stoichiometry.	Disulfides	114-123	interleukin 18	Homo sapiens	79-84
35398099-6	2022	Furthermore, our structure captured a fortuitous higher-order assembly between IL-18 and IL-18BP coordinated by a disulfide-bond distal to the binding surface connecting IL-18 and IL-18BP molecules from different complexes, resulting in a novel tetramer with 2:2 stoichiometry.	Disulfides	114-123	interleukin 18	Homo sapiens	170-175
2722851-0	1989	Disulfide bond formation in the regulation of eIF-2 alpha kinase by heme.	Disulfides	0-9	eukaryotic translation initiation factor 2A	Homo sapiens	46-57
35514997-6	2022	Our analysis of 8 possible dimerization models, suggested that the most likely ERAP1/ERAP2 heterodimerization topology involves the exon 10 loop, a non-conserved loop previously implicated in interactions between ERAP1 and the disulfide-bond shuffling chaperone ERp44.	Disulfides	227-236	endoplasmic reticulum aminopeptidase 2	Homo sapiens	85-90
2539974-10	1989	This study demonstrates that 1) pancreatic acinar cells rapidly internalize [125I]secretin; 2) internalization of secretin does not enhance cAMP production; and 3) disulfide linkages are important for secretin receptor activity.	Disulfides	164-173	secretin	Homo sapiens	82-90
2522969-8	1989	After disulfide-linking to the mAb, the C3b became highly resistant to inactivation by factors H and I, probably due to its reduced factor H binding capacity.	Disulfides	6-15	complement C3	Homo sapiens	40-43
35112407-6	2022	These studies suggest that SELENOF may be responsible for reducing the non-native disulfide bonds of misfolded glycoproteins as part of the quality control system in the ER.	Disulfides	82-91	selenoprotein F	Bos taurus	27-34
2558637-5	1989	Altogether the results indicated that Cys402, probably by participating in a disulfide bridge, is essential for (i) the CD4-binding ability of env gene products and for (ii) the physical stability of gp 120.	Disulfides	77-86	endogenous retrovirus group K member 20	Homo sapiens	143-146
35151934-7	2022	When selectively targeting CD206 highly expressed on the surface of TAM, disulfide bond was cleaved by the glutathione enriched in the microenvironment, resulting in fluorescence recovery, thus achieving NIR fluorescence molecular imaging of TAM and diagnosis of tumor lymph node metastasis in mouse models.	Disulfides	73-82	mannose receptor, C type 1	Mus musculus	27-32
34609517-6	2022	PDI-L members AtPDI2/5/6 mainly serve as an isomerase, while PDI-M/S members AtPDI9/10/11 are more efficient in accepting oxidizing equivalents from AtERO1 and catalyzing disulfide bond formation.	Disulfides	171-180	PDI-like 1-4	Arabidopsis thaliana	14-24
2918254-3	1989	This IAAD inactivation is slowed down by pretreatment of the enzyme with disulfides, indicating that inactivation of HMG-CoA reductase occurs mainly through alkylation of specific cysteine residues in the protein.	Disulfides	73-83	3-hydroxy-3-methylglutaryl-CoA reductase	Rattus norvegicus	117-134
2972706-5	1988	To define the structural basis for high affinity IGF I binding, we have examined the effect of disulfide bond reduction on the binding parameters of the high affinity IGF I receptor.	Disulfides	95-104	insulin like growth factor 1 receptor	Homo sapiens	167-181
2972706-6	1988	We find that the disulfide bonds linking the two alpha beta dimers of the IGF I receptor heterotetramer are reduced by incubation at pH 8.75 with 2 mM dithiothreitol (DTT) for 5 min at room temperature.	Disulfides	17-26	insulin like growth factor 1 receptor	Homo sapiens	74-88
3419426-11	1988	It is concluded, therefore, that the mechanism of inhibition of glucokinase by alloxan is a reaction of alloxan with two adjacent SH groups in the depth of the sugar-binding site of the glucokinase, with formation of a disulfide bond and concomitant inactivation of the enzyme.	Disulfides	219-228	glucokinase	Homo sapiens	64-75
3419426-11	1988	It is concluded, therefore, that the mechanism of inhibition of glucokinase by alloxan is a reaction of alloxan with two adjacent SH groups in the depth of the sugar-binding site of the glucokinase, with formation of a disulfide bond and concomitant inactivation of the enzyme.	Disulfides	219-228	glucokinase	Homo sapiens	186-197
3413723-1	1988	The sulfhydryl group oxidizing agent azodicarboxylic acid-bis-dimethylamide (diamide) which causes disulfide-linked polymer formation of certain cytoskeletal proteins, the actin-polymerization inhibitor, cytochalasin B, and 2-mercaptopropionylglycine (2-MPG), a cell-permeable SH-reagent, completely abolish adhesion-induced platelet spreading and mural platelet aggregate formation on collagen-coated surfaces.	Disulfides	99-108	N-methylpurine DNA glycosylase	Homo sapiens	254-257
3173345-4	1988	Under non-reducing conditions the catalytic subunit possesses a molecular weight of 65 kDa, however this value increases to 68 kDa after reduction, suggesting that intrachain-disulfide bonds are important in the folding of the catalytic subunits of the AChE.	Disulfides	175-184	acetylcholinesterase	Bos taurus	253-257
2454656-1	1988	The kinetics of the disulfide-coupled unfolding-refolding transition of a mutant form of bovine pancreatic trypsin inhibitor (BPTI) lacking Cys-14 and -38 were measured and compared to previous results for the wild-type protein and other modified forms.	Disulfides	20-29	spleen trypsin inhibitor I	Bos taurus	126-130
2454656-9	1988	113, 275-293] that the energetically preferred pathway for folding and unfolding of BPTI includes intramolecular rearrangements of intermediates in which Cys-14 and -38 are paired in disulfides not present in the native protein.	Disulfides	183-193	spleen trypsin inhibitor I	Bos taurus	84-88
3131747-8	1988	These results suggest that the Mr 62,000 CCK binding protein in the toad retina contains an intramolecular disulfide bond(s).	Disulfides	107-116	cholecystokinin	Rattus norvegicus	41-44
3203406-0	1988	Covalent binding of 4-nitrobenzyl mercaptan S-sulfate to the sulfhydryl groups of hepatic cytosolic proteins and bovine serum albumin with mixed disulfide bond formation.	Disulfides	145-154	albumin	Rattus norvegicus	120-133
3203406-3	1988	Bovine serum albumin (BSA), a model protein with a single SH group, also reacted readily with radioactive NBM S-sulfate to form a disulfide bond in stoichiometric manner.	Disulfides	130-139	albumin	Rattus norvegicus	7-20
2456237-2	1988	Tenascin is a disulfide-linked oligomeric, extracellular matrix glycoprotein of subunit Mr 170,000, 190,000, 200,000, and 220,000, which has been proposed to promote epithelial cell proliferation.	Disulfides	14-23	tenascin C	Homo sapiens	0-8
2450560-6	1987	Translation of these sequences showed that the FNR alpha, the VnR alpha, and GP IIb are composed of disulfide-linked large (858-871 amino acids) and small (137-158 amino acids) chains that are posttranslationally processed from a single mRNA.	Disulfides	100-109	integrin subunit alpha V	Homo sapiens	62-71
2450560-6	1987	Translation of these sequences showed that the FNR alpha, the VnR alpha, and GP IIb are composed of disulfide-linked large (858-871 amino acids) and small (137-158 amino acids) chains that are posttranslationally processed from a single mRNA.	Disulfides	100-109	integrin subunit alpha 2b	Homo sapiens	77-83
3499438-6	1987	VCA-2 is composed of the same 1401-kDa polypeptide as VCA-1 and another 170-kDa species; this 170-kDa species consists of a second distinct 140-kDa (designated 140(2)) and a 30-kDa polypeptide which are disulfide-bonded.	Disulfides	203-212	integrin subunit alpha 3	Homo sapiens	0-5
3676486-3	1987	Reduction of disulfide bonds in residual chromatin protein with 5% mercaptoethanol linearized scc DNA, present in chromatin preparations as nuclear matrix subunits containing some loops of scc DNA on the protein globule.	Disulfides	13-22	SCC	Bos taurus	94-97
3676486-3	1987	Reduction of disulfide bonds in residual chromatin protein with 5% mercaptoethanol linearized scc DNA, present in chromatin preparations as nuclear matrix subunits containing some loops of scc DNA on the protein globule.	Disulfides	13-22	SCC	Bos taurus	189-192
3622999-3	1987	The view that the three-dimensional structure of AGP is closely similar to the published structures of RBP and LG is supported by its homology with these proteins, similarities in disulfide bond arrangements, and its secondary structure profile, predicted from the amino acid sequence.	Disulfides	180-189	retinol binding protein 4	Homo sapiens	103-106
2443162-4	1987	The temperature dependence of all thermodynamic parameters of BPTI is drastically altered in the absence of the third disulfide bridge.	Disulfides	118-127	spleen trypsin inhibitor I	Bos taurus	62-66
2443162-6	1987	The Gibbs energy of BPTI at pH 2, 25 degrees C, decreases by approximately 70% when the 14-38 disulfide bond is cleaved.	Disulfides	94-103	spleen trypsin inhibitor I	Bos taurus	20-24
3108266-2	1987	GPIIb is a two-chain protein containing disulfide-linked alpha and beta subunits.	Disulfides	40-49	integrin subunit alpha 2b	Homo sapiens	0-5
2435002-4	1987	Previous work with BPTI chemically modified at cysteines 14 and 38 indicated that transient disulfide bond formation by these residues contributed to efficient folding at 25 degrees C. In the present work, mutants of BPTI in which these cysteines were replaced by alanines or threonines were made and the mutant proteins were produced by a heterologous Escherichia coli expression system.	Disulfides	92-101	spleen trypsin inhibitor I	Bos taurus	217-221
2444024-1	1987	The complete amino acid sequence of human serum Retinol-binding protein (RBP) including the distribution of its three disulfide bridges, has been determined.	Disulfides	118-127	retinol binding protein 4	Homo sapiens	73-76
2427334-4	1986	All six cysteine residues were conserved in agreement with the previous finding that the biological activity of NGF is conformation-dependent requiring intact disulfide bridges.	Disulfides	159-168	nerve growth factor	Bos taurus	112-115
3748012-6	1986	In contrast, the anti-pre-S(2)/GP33-GP36 antibodies and the anti-pre-S(1)/P39-GP42 antibodies can be easily detected in WIBA, providing these antibodies recognize the disulfide-bond independent pre-S determinants on the denatured env proteins.	Disulfides	167-176	endogenous retrovirus group K member 20	Homo sapiens	230-233
2937786-2	1986	After thrombin cleavage the NH2-terminal region containing gamma-carboxyglutamic acid (Gla) is linked to the large COOH-terminal fragment by a disulfide bond.	Disulfides	143-152	coagulation factor II, thrombin	Bos taurus	6-14
3957910-4	1986	After mild treatment of spectrin with 2.5 microM diamide, with formation of an average of only one disulfide bond, we observed a 50% reduction in the ability of protein 4.1 to amplify spectrin-actin binding.	Disulfides	99-108	erythrocyte membrane protein band 4.1	Homo sapiens	161-172
3643720-2	1986	Kallikrein liberated bradykinin from HMW kininogen (Mr 114 kDa) and generated a two-chain molecule with a heavy chain of Mr 63 kDa and a light chain of Mr 58 kDa interconnected via a single disulfide bridge.	Disulfides	190-199	kallikrein related peptidase 4	Homo sapiens	0-10
3863143-11	1985	Our results indicate that a biological activity, neurite extension, which is critical for the development of the nervous system, is associated with a disulfide form of S100 beta.	Disulfides	150-159	S100 calcium binding protein B	Bos taurus	168-177
4073491-2	1985	The resultant compound, N,N"-bis(4-azidobenzoyl) cystine [(ABC)2], reacts with protein sulfhydryl groups through disulfide exchange to generate photoactive derivatives.	Disulfides	113-122	ATP binding cassette subfamily A member 2	Homo sapiens	59-64
2985702-1	1985	The plasma cell membrane antigen PC-1 and the receptor for the iron transport protein transferrin are high m.w., developmentally regulated proteins consisting of two similar or identical disulfide-bonded subunits.	Disulfides	187-196	minisatellite 6 hypermutable	Mus musculus	33-37
2985702-1	1985	The plasma cell membrane antigen PC-1 and the receptor for the iron transport protein transferrin are high m.w., developmentally regulated proteins consisting of two similar or identical disulfide-bonded subunits.	Disulfides	187-196	transferrin	Mus musculus	86-97
2985702-9	1985	Disulfide bonding between chains was conserved in both PC-1 and the transferrin receptor in all species examined, but transferrin receptors from mouse cells had a significantly higher apparent m.w.	Disulfides	0-9	minisatellite 6 hypermutable	Mus musculus	55-59
2985702-9	1985	Disulfide bonding between chains was conserved in both PC-1 and the transferrin receptor in all species examined, but transferrin receptors from mouse cells had a significantly higher apparent m.w.	Disulfides	0-9	transferrin	Mus musculus	68-79
3921621-2	1985	Some of these TL-like molecules are disulfide-bonded to CD8(Tp32), on which they form the thymus-specific 45 kilodalton (Kd) subunit of the CD8 complex.	Disulfides	36-45	CD8a molecule	Homo sapiens	56-59
3921621-2	1985	Some of these TL-like molecules are disulfide-bonded to CD8(Tp32), on which they form the thymus-specific 45 kilodalton (Kd) subunit of the CD8 complex.	Disulfides	36-45	CD8a molecule	Homo sapiens	140-143
4039728-6	1985	Whether CRBP contains a disulfide bond is not yet established.	Disulfides	24-33	retinol binding protein 1	Rattus norvegicus	8-12
3158361-2	1985	Six of the hybridomas secreted MoAbs that recognized epitopes on the 23,000-dalton, disulfide-linked subunit of GPIIb, GPIIb beta.	Disulfides	84-93	integrin subunit alpha 2b	Homo sapiens	112-117
3158361-2	1985	Six of the hybridomas secreted MoAbs that recognized epitopes on the 23,000-dalton, disulfide-linked subunit of GPIIb, GPIIb beta.	Disulfides	84-93	integrin subunit alpha 2b	Homo sapiens	119-124
3845123-6	1985	Proteolysis of ZP1 by chymotrypsin or reduction of intermolecular disulfides of ZP1 by dithiothreitol results in both solubilization of zonae pellucidae and disruption of interconnections between individual zona pellucida filaments.	Disulfides	66-76	zona pellucida glycoprotein 1	Mus musculus	80-83
4066774-4	1985	Polyacrylamide gel analysis of immunoprecipitated [3H]-leucine- and [3H]-glucosamine-labeled ECM from the human glioma cell line U-251MG has shown that GMEM is a high-molecular-weight macromolecule (Mr approximately 1,000,000) composed of Mr approximately 230,000 disulfide-bonded glycoprotein subunits.	Disulfides	264-273	tenascin C	Homo sapiens	152-156
6501279-4	1984	The dimeric inhibitor (TPI-D) with an intermolecular disulfide bridge was also inactive and was converted to the active monomeric inhibitor on addition of dithiothreitol.	Disulfides	53-62	triosephosphate isomerase 1	Rattus norvegicus	23-26
6501279-5	1984	TPI-2 is most likely a mixed disulfide with glutathione.	Disulfides	29-38	triosephosphate isomerase 1	Rattus norvegicus	0-3
6501279-6	1984	One (Cys-3) of two cysteine residues exposed on the surface of the molecule of TPI-2 is involved in the formation of a mixed disulfide, and the other cysteine residue (Cys-64) is buried in the molecule.	Disulfides	125-134	triosephosphate isomerase 1	Rattus norvegicus	79-82
6231955-3	1984	Affinity of toxin sites for agonists is altered by specific sulfhydryl/disulfide modification and by Ca2+, and sites may be labeled with the nicotinic acetylcholine receptor affinity reagent bromoacetylcholine.	Disulfides	71-80	cholinergic receptor nicotinic alpha 2 subunit	Rattus norvegicus	141-173
6693769-5	1984	Both native IgG and IgG modified by cleavage of its single-hinge disulfide bond formed similar complexes on interaction with SpA.	Disulfides	65-74	pulmonary surfactant-associated protein A	Oryctolagus cuniculus	125-128
6190801-5	1983	Renin was then hydrolyzed slowly to give two chains of Mr = 33,000 and 5,000 held together by disulfide bonds.	Disulfides	94-103	renin	Canis lupus familiaris	0-5
6217839-5	1982	However, when the disulfide bridges are reduced, followed either by reoxidation or alkylation, the structure of Factor H is modified so that it now exhibits conventional protein secondary structure as determined from its CD spectra in the far ultraviolet region.	Disulfides	18-27	complement factor H	Homo sapiens	112-120
6217839-6	1982	Factor H also fails to mediate its regulatory function of inhibiting the alternative pathway convertase once the disulfides have been ruptured and conformational rearrangement has occurred.	Disulfides	113-123	complement factor H	Homo sapiens	0-8
6807342-8	1982	Integration of predictive calculations from osteocalcin sequence has yielded a structural model for the protein, the dominant features of which include two opposing alpha-helical domains of 9-12 residues each, connected by a bea turn and stabilized by the Cys23-Cys29 disulfide bond.	Disulfides	268-277	bone gamma-carboxyglutamate protein	Gallus gallus	44-55
7330011-2	1981	Disulfide-linked polypeptide aggregates are found in membranes from fresh RBC of these G6PD mutants and from aerobically incubated normal erythrocytes.	Disulfides	0-9	glucose-6-phosphate dehydrogenase	Homo sapiens	87-91
7330011-5	1981	Thus, most of the disulfide bonds in the G6PD mutants were intramolecular.	Disulfides	18-27	glucose-6-phosphate dehydrogenase	Homo sapiens	41-45
7330011-11	1981	We conclude that in G6PD mutants with chronic hemolysis oxidative damage includes aggregate formation due to intermolecular disulfide bonds, and intramolecular disulfide bond formation associated with increased binding of non-hemoglobin cytoplasmic proteins to the membrane.	Disulfides	124-133	glucose-6-phosphate dehydrogenase	Homo sapiens	20-24
7330011-11	1981	We conclude that in G6PD mutants with chronic hemolysis oxidative damage includes aggregate formation due to intermolecular disulfide bonds, and intramolecular disulfide bond formation associated with increased binding of non-hemoglobin cytoplasmic proteins to the membrane.	Disulfides	160-169	glucose-6-phosphate dehydrogenase	Homo sapiens	20-24
7452679-1	1980	Condensation of (tert-butyloxycarbonyl)tocinoic acid with L-prolyl-L-tryptophylglycinamide produced the Boc derivative of a nonapeptide (disulfide) which on deprotection afforded [8-L-tryptophan]oxytocin.	Disulfides	137-146	BOC cell adhesion associated, oncogene regulated	Rattus norvegicus	104-107
6106638-2	1980	The results indicate that the CS-SC dihedral angles of somatostatin and of these analogues (except [Ala3,14]-SS, which has no disulfide bond) are within 20 degrees of +/- 85 degrees, and the SS-CC dihedral angles are predominantly in the range of 50 degrees-180 degrees.	Disulfides	126-135	somatostatin	Homo sapiens	55-67
500690-9	1979	This cleavage, which liberates kinin and gives a two-chain, disulfide-linked molecule, is dependent upon the presence of prekallikrein and Factor XII (Hageman factor) in plasma.	Disulfides	60-69	coagulation factor XII	Homo sapiens	151-165
393607-9	1979	Thus all the disulfide bridges of an IgA1 immunoglobulin could be established.	Disulfides	13-22	immunoglobulin heavy constant alpha 1	Homo sapiens	37-41
390060-2	1979	The major function of this protein is to act as a co-factor for C3b Inactivator (C3bINA) in the cleavage of C3b to an intermediate molecule, C3b", consisting of an intact beta-chain covalently bound by disulfide bridges to 2 alpha-chain fragments of 40,000 and 67,000 daltons.	Disulfides	202-211	complement factor I	Homo sapiens	64-79
390060-2	1979	The major function of this protein is to act as a co-factor for C3b Inactivator (C3bINA) in the cleavage of C3b to an intermediate molecule, C3b", consisting of an intact beta-chain covalently bound by disulfide bridges to 2 alpha-chain fragments of 40,000 and 67,000 daltons.	Disulfides	202-211	complement factor I	Homo sapiens	81-87
390060-2	1979	The major function of this protein is to act as a co-factor for C3b Inactivator (C3bINA) in the cleavage of C3b to an intermediate molecule, C3b", consisting of an intact beta-chain covalently bound by disulfide bridges to 2 alpha-chain fragments of 40,000 and 67,000 daltons.	Disulfides	202-211	complement C3	Homo sapiens	64-67
390060-2	1979	The major function of this protein is to act as a co-factor for C3b Inactivator (C3bINA) in the cleavage of C3b to an intermediate molecule, C3b", consisting of an intact beta-chain covalently bound by disulfide bridges to 2 alpha-chain fragments of 40,000 and 67,000 daltons.	Disulfides	202-211	complement C3	Homo sapiens	81-84
216697-8	1979	The specific retention of SJ protein kinase(s) activity during purification and their resistance to detergent solubilization was achieved by chemical treatments which produce interprotein cross-linking via disulfide bridges.	Disulfides	206-215	KIT proto-oncogene receptor tyrosine kinase	Rattus norvegicus	29-43
762110-3	1979	Utilizing methyl-5-bromovalerimidate, a disulfide cross-linked conjugate of hCGbeta and toxin subunit A was prepared in 30% yield relative to hCGbeta input.	Disulfides	40-49	chorionic gonadotropin subunit beta 3	Homo sapiens	76-83
762110-3	1979	Utilizing methyl-5-bromovalerimidate, a disulfide cross-linked conjugate of hCGbeta and toxin subunit A was prepared in 30% yield relative to hCGbeta input.	Disulfides	40-49	chorionic gonadotropin subunit beta 3	Homo sapiens	142-149
410452-1	1977	An IgA1 half-molecule, which is composed of a deleted alpha1 chain linked with a disulfide bond to an intact kappa chain, was detected in a patient (Cha).	Disulfides	81-90	immunoglobulin heavy constant alpha 1	Homo sapiens	3-7
864009-9	1977	The cleavage of the surface-bound Hageman factor molecule responsible for the formation of the 52,000-and 28,000-mol wt fragments occurred at two closely situated sites, one of which was within a disulfide loop.	Disulfides	196-205	coagulation factor XII	Homo sapiens	34-48
1002996-13	1976	Additional similarities between the C3a and C5a molecules include length of the polypeptide chain, number of disulfide bonds and an absence of tryptophan residues.	Disulfides	109-118	complement C3	Homo sapiens	36-39
1278162-7	1976	After reduction and carbamidomethylation of the disulfide bonds in thrombin modified ovine growth hormone, the two fragments (residues 1--133 and 134--191) were isolated.	Disulfides	48-57	coagulation factor II, thrombin	Bos taurus	67-75
4736435-2	1973	Effect of thiol and disulfide compounds on activities of thioldisulfide transhydrogenase, glutathione reductase and glucose-6-phosphate dehydrogenase].	Disulfides	20-29	glucose-6-phosphate dehydrogenase	Homo sapiens	116-149
4564211-7	1972	The high disulfide content reduces drastically the allowed number of biofunctional conformers of neurophysin-II.	Disulfides	9-18	arginine vasopressin	Bos taurus	97-111
5289004-2	1970	The ellipticities per disulfide bond of the unresolved bands in neurophysin-II are -2900 deg cm(2)/decimole and +2300 deg cm(2)/decimole at 280 nm and 248 nm, respectively.	Disulfides	22-31	arginine vasopressin	Bos taurus	64-78
13970458-11	1963	It is suggested that lipids serve as a framework for the developing keratin structure which acquires permanent stability through hydrogen bonds and disulfide cross-links.	Disulfides	148-157	keratin	Gallus gallus	68-75
34054871-6	2021	Since FH has 40 disulfide bonds, we created a P. pastoris strain containing a methanol-inducible codon-modified gene for protein-disulfide isomerase (PDI) and transformed this with codon-modified DNA encoding mFH under the same promoter.	Disulfides	16-25	ferritin heavy polypeptide 1	Mus musculus	6-8
33963564-13	2021	Disulfide-bonded KCNQ1/KCNE1 constructs reported preferential association after they had reached cell surface.	Disulfides	0-9	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	23-28
33530614-3	2021	Recently, it was found that the functional properties of Stx2a (binding to circulating cells and complement components) change according to modifications of the structure of the toxin, i.e., after a single cleavage of the A subunit resulting in two fragments, A1 and A2, linked by a disulfide bridge.	Disulfides	283-292	syntaxin 2	Homo sapiens	57-62
33196173-5	2020	We recently reported a mass spectrometry-based disulfide-trapping (tethering) approach for a cysteine residue in the hub protein 14-3-3, an important regulator of phosphorylated client proteins.	Disulfides	47-56	tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein theta	Homo sapiens	129-135
33196173-7	2020	Using the DNA-binding domain of the nuclear receptor Estrogen Related Receptor gamma (ERRgamma), we target a native cysteine positioned at the 14-3-3 PPI interface and identify several fragments that form a disulfide bond to ERRgamma and stabilize the complex up to 5-fold.	Disulfides	207-216	tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein theta	Homo sapiens	143-149
32698065-1	2020	Reteplase is a deleted variant of human tissue plasminogen activator with a complex structure containing nine disulfide bonds.	Disulfides	110-119	chromosome 20 open reading frame 181	Homo sapiens	40-68
33198886-6	2020	This was due to olanzapine"s impairment of proper disulfide bond formation in proinsulin, although direct targets of olanzapine remain undetermined.	Disulfides	50-59	insulin II	Mus musculus	78-88
33049718-2	2020	Cytosolic thioredoxin (Trx) is a multifunctional redox protein which has antioxidant and protein disulfide reducing properties.	Disulfides	97-106	thioredoxin 1	Mus musculus	10-21
33049718-2	2020	Cytosolic thioredoxin (Trx) is a multifunctional redox protein which has antioxidant and protein disulfide reducing properties.	Disulfides	97-106	thioredoxin 1	Mus musculus	23-26
32938661-4	2020	Crystal structures of Env-bound and unbound antibodies revealed heavy chain-mediated recognition of the glycan supersite with a unique angle of approach and a critical role of the intra-HCDR3 disulfide.	Disulfides	192-201	endogenous retrovirus group K member 20	Homo sapiens	22-25
32454156-3	2020	Protein disulfide isomerase a1 (PDIA1) can directly catalyze the formation, isomerization and reduction of disulfide bonds in proteins and may play an important role in the formation of TFF3 dimer.	Disulfides	8-17	trefoil factor 3	Rattus norvegicus	186-190
32454156-8	2020	Furthermore, we propose that the Cys24-Cys27 active site at the region a" of PDIA1 mediates disulfide bond formation between the Cys79 residues of each of the two TFF3 monomers via deprotonation and nucleophilic attack.	Disulfides	92-101	trefoil factor 3	Rattus norvegicus	163-167
32788374-4	2020	Using biochemical and immunomicroscopic approaches, we found that, like the corresponding poxviral proteins, pE199L localizes to the inner viral envelope and behaves as an integral transmembrane polypeptide with cytosolic intramolecular disulfide bonds.	Disulfides	237-246	pE199L	African swine fever virus	109-115
32592613-9	2020	We conclude that both deglycosylation and disulfide bond formation are important for CD44 to compete with IGFBP-3 for binding HA.	Disulfides	42-51	CD44 molecule (Indian blood group)	Homo sapiens	85-89
32601205-5	2020	We show the CRES monomer has a typical cystatin fold that assembles into highly branched amyloid matrices, comparable to those in vivo, by forming beta-sheet assemblies that our data suggest occur via two distinct mechanisms: a unique conformational switch of a highly flexible disulfide-anchored loop to a rigid beta-strand and by traditional cystatin domain swapping.	Disulfides	278-287	cystatin 8 (cystatin-related epididymal spermatogenic)	Mus musculus	12-16
32637036-10	2020	The usherin laminin epidermal growth factor repeats adopt a rod-shaped structure, which is maintained by disulfide bonds.	Disulfides	105-114	usherin	Homo sapiens	4-11
32142475-4	2020	After this reaction, MIA40 is reoxidized by the sulfhydryl oxidase ALR, which couples disulfide formation by this machinery to the activity of the respiratory chain.	Disulfides	86-95	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	21-26
32359542-6	2020	Sequence analysis revealed that the seven nAChR subunits of B. odoriphaga shared the typical structural features with Drosophila melanogaster nAChR alpha1 subunit, including an extracellular N-terminal domain containing six functional loops (loop A-F), a signature Cys-loop with two disulfide bond-forming cysteines separated by 13 amino acid residues, and four typical transmembrane helices (TM1-TM4) in the C-terminal region.	Disulfides	283-292	nicotinic Acetylcholine Receptor alpha1	Drosophila melanogaster	42-47
32174509-3	2020	Herein, by analyzing a set of ORF2 truncated proteins expressed in Escherichia coli, we found that the highly conserved C-terminal cysteines play a crucial role in the oligomerization of the truncated ORF2 proteins and in their assembly into VLPs, through the formation of dimer-dimer disulfide bonds; and the treatment of native HEV particles with dithiothreitol (DTT) induced the disassembly of the viral capsid, suggesting that the disulfide bonding is required for stabilizing the native HEV capsid.	Disulfides	285-294	hypothetical protein	Escherichia coli	30-34
32174509-3	2020	Herein, by analyzing a set of ORF2 truncated proteins expressed in Escherichia coli, we found that the highly conserved C-terminal cysteines play a crucial role in the oligomerization of the truncated ORF2 proteins and in their assembly into VLPs, through the formation of dimer-dimer disulfide bonds; and the treatment of native HEV particles with dithiothreitol (DTT) induced the disassembly of the viral capsid, suggesting that the disulfide bonding is required for stabilizing the native HEV capsid.	Disulfides	285-294	hypothetical protein	Escherichia coli	201-205
32174509-3	2020	Herein, by analyzing a set of ORF2 truncated proteins expressed in Escherichia coli, we found that the highly conserved C-terminal cysteines play a crucial role in the oligomerization of the truncated ORF2 proteins and in their assembly into VLPs, through the formation of dimer-dimer disulfide bonds; and the treatment of native HEV particles with dithiothreitol (DTT) induced the disassembly of the viral capsid, suggesting that the disulfide bonding is required for stabilizing the native HEV capsid.	Disulfides	435-444	hypothetical protein	Escherichia coli	30-34
32174509-3	2020	Herein, by analyzing a set of ORF2 truncated proteins expressed in Escherichia coli, we found that the highly conserved C-terminal cysteines play a crucial role in the oligomerization of the truncated ORF2 proteins and in their assembly into VLPs, through the formation of dimer-dimer disulfide bonds; and the treatment of native HEV particles with dithiothreitol (DTT) induced the disassembly of the viral capsid, suggesting that the disulfide bonding is required for stabilizing the native HEV capsid.	Disulfides	435-444	hypothetical protein	Escherichia coli	201-205
32151664-4	2020	Herein, a tumor targeted and stimuli responsive nano-delivery system for cisplatin was constructed using branched polyethyleneimine (BPEI) as the backbone, disulfide bond as the redox-responsive covalent linker and hyaluronic acid (HA) as targeting recognition unit which can bind selectively to the receptor of CD44, which is highly expressed on the A549 tumor cells.	Disulfides	156-165	CD44 molecule (Indian blood group)	Homo sapiens	312-316
32271748-6	2020	By comprehensive disulfide cross-linking, we establish the existence and the structure of a novel interface between the CXCR4 distal N-terminus and CXCL12 beta1-strand, while also recapitulating earlier findings from nuclear magnetic resonance, modeling and crystallography of homologous receptors.	Disulfides	17-26	C-X-C motif chemokine receptor 4	Homo sapiens	120-125
32103528-3	2020	However, several alternative models of ADAM17 regulation exist that do not involve the iRhoms, such as regulation through disulfide bond exchange or through interaction with charged phospholipids.	Disulfides	122-131	ADAM metallopeptidase domain 17	Homo sapiens	39-45
32197489-0	2020	PDI-Mediated Reduction of Disulfide Bond on PSD95 Increases Spontaneous Seizure Activity by Regulating NR2A-PSD95 Interaction in Epileptic Rats Independent of S-Nitrosylation.	Disulfides	26-35	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	0-3
32197489-3	2020	Protein disulfide isomerase (PDI) reduces disulfide bonds (S-S) to free thiol (-SH) on various proteins.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	29-32
31825724-7	2020	Surprisingly, the Erv46 cysteine mutants continued to bind cargo in cell free assays and produced an increased level of Erv46-cargo complexes in cell extracts suggesting that disulfide linkages in the cysteine-rich region perform a role in releasing bound cargo.	Disulfides	175-184	ERGIC and golgi 3	Homo sapiens	18-23
31825724-7	2020	Surprisingly, the Erv46 cysteine mutants continued to bind cargo in cell free assays and produced an increased level of Erv46-cargo complexes in cell extracts suggesting that disulfide linkages in the cysteine-rich region perform a role in releasing bound cargo.	Disulfides	175-184	ERGIC and golgi 3	Homo sapiens	120-125
33250972-6	2020	Presence of redox-active disulfides in the interacting parts of S-protein, ACE2, and a ferredoxin-like fold domain in the transmembrane part of ACE2, strongly indicate the role of redox in COVID-19 pathogenesis and severity.	Disulfides	25-35	vitronectin	Homo sapiens	64-73
33335361-3	2020	All ZP proteins have a zona pellucida domain (ZPD) that consists of  270 amino acids and has 8 conserved Cys residues present as four intramolecular disulfides.	Disulfides	149-159	hephaestin like 1	Homo sapiens	4-6
31831824-8	2019	In the modules studied, disulfide bridges play a protective role, probably making both selective binding and protease activity of reelin possible.	Disulfides	24-33	reelin	Homo sapiens	130-136
31704286-3	2019	Using molecular modeling, fluorescence resonance energy transfer experiments on living cells, biochemical and mutational analysis, we show that CD8 binding to pMHC in cis involves a different docking mode and is regulated by post-translational modifications including a membrane-distal inter-chain disulfide bond and negatively charged O-linked glycans near positively charged sequences on the CD8beta stalk.	Disulfides	298-307	CD8a molecule	Homo sapiens	144-147
29712536-2	2019	Quiescin sulfhydryl oxidase 1 (QSOX1) is upregulated in many types of cancer cells; it promotes disulfide bond formation as well as hydrogen peroxide (H2O2) production.	Disulfides	96-105	quiescin sulfhydryl oxidase 1	Homo sapiens	0-29
29712536-2	2019	Quiescin sulfhydryl oxidase 1 (QSOX1) is upregulated in many types of cancer cells; it promotes disulfide bond formation as well as hydrogen peroxide (H2O2) production.	Disulfides	96-105	quiescin sulfhydryl oxidase 1	Homo sapiens	31-36
31481523-6	2019	We found that the extreme amino-terminal residues of the chemokine XCL1 (Val1, Gly2, Ser3, and Glu4) contribute a large fraction of the binding energy to its receptor XCR1, whereas residues near the disulfide bond-forming residue Cys11 modulate XCR1 activation.	Disulfides	199-208	X-C motif chemokine ligand 1	Homo sapiens	67-71
31299423-0	2019	S-Glutathionylation of mouse selenoprotein W prevents oxidative stress-induced cell death by blocking the formation of an intramolecular disulfide bond.	Disulfides	137-146	selenoprotein W	Mus musculus	29-44
31361147-6	2019	We took advantage of the native disulfide bridge of the oxytocin for anchoring the peptide to the Au surface, while preserving the metal-ion binding properties.	Disulfides	32-41	oxytocin/neurophysin I prepropeptide	Homo sapiens	56-64
31087497-1	2019	Bovine beta-lactoglobulin (BLG) is a major whey protein with unique structural characteristics: it possesses a free Cys thiol (SH) and two disulfide (SS) bonds and consists of a beta-barrel core surrounded by one long and several short alpha helices.	Disulfides	139-148	beta-lactoglobulin	Bos taurus	7-25
31087497-1	2019	Bovine beta-lactoglobulin (BLG) is a major whey protein with unique structural characteristics: it possesses a free Cys thiol (SH) and two disulfide (SS) bonds and consists of a beta-barrel core surrounded by one long and several short alpha helices.	Disulfides	139-148	beta-lactoglobulin	Bos taurus	27-30
31366154-4	2019	Genetically programming sGFP and RFP with Cys-tag and His-tag, respectively, allowed tuning the protein spatial organization either across the porous structure of two microbeads with different functional groups (agarose-based materials activated with metal chelates and epoxy-methacrylate materials) or across the surface of a single microbead functionalized with both metal-chelates and disulfide groups.	Disulfides	388-397	tripartite motif containing 27	Homo sapiens	33-36
31315052-4	2019	Our analyses of multiple mutant mice lines, complemented by MEFs expressing a series of Keap1 mutants, reveal that Keap1 uses the cysteine residues redundantly to set up an elaborate fail-safe mechanism in which specific combinations of these four cysteine residues can form a disulfide bond to sense hydrogen peroxide.	Disulfides	277-286	kelch-like ECH-associated protein 1	Mus musculus	115-120
31196353-5	2019	Briefly, GQD-miR-150 linked by disulfide bonds was adopted to functionalize both the inner and outer TEBVs.	Disulfides	31-40	microRNA 150	Homo sapiens	13-20
31054990-5	2019	The sCT-Mal-Asp6 was synthesized via a disulfide re-bridge reaction with high specificity and purity.	Disulfides	39-48	secretin	Homo sapiens	4-16
31216687-3	2019	Ricin is a typical A-B toxin consisting of a single enzymatic A subunit (RTA) and a binding B subunit (RTB) joined by a single disulfide bond.	Disulfides	127-136	ricin	Ricinus communis	0-5
31184302-1	2019	Biosynthesis of insulin - critical to metabolic homeostasis - begins with folding of the proinsulin precursor, including formation of three evolutionarily conserved intramolecular disulfide bonds.	Disulfides	180-189	insulin II	Mus musculus	89-99
31184302-4	2019	In genetically obese mice with otherwise wild-type islets, disulfide-linked complexes of proinsulin are more abundant, and leptin receptor-deficient mice, the further increase of such complexes tracks with the onset of islet insulin deficiency and diabetes.	Disulfides	59-68	insulin II	Mus musculus	89-99
31184302-5	2019	Proinsulin-Cys(B19) and Cys(A20) are necessary and sufficient for the formation of proinsulin disulfide-linked complexes; indeed, proinsulin Cys(B19)-Cys(B19) covalent homodimers resist reductive dissociation, highlighting a structural basis for aberrant proinsulin complex formation.	Disulfides	94-103	insulin II	Mus musculus	0-10
31184302-5	2019	Proinsulin-Cys(B19) and Cys(A20) are necessary and sufficient for the formation of proinsulin disulfide-linked complexes; indeed, proinsulin Cys(B19)-Cys(B19) covalent homodimers resist reductive dissociation, highlighting a structural basis for aberrant proinsulin complex formation.	Disulfides	94-103	insulin II	Mus musculus	83-93
31184302-5	2019	Proinsulin-Cys(B19) and Cys(A20) are necessary and sufficient for the formation of proinsulin disulfide-linked complexes; indeed, proinsulin Cys(B19)-Cys(B19) covalent homodimers resist reductive dissociation, highlighting a structural basis for aberrant proinsulin complex formation.	Disulfides	94-103	insulin II	Mus musculus	130-140
31184302-5	2019	Proinsulin-Cys(B19) and Cys(A20) are necessary and sufficient for the formation of proinsulin disulfide-linked complexes; indeed, proinsulin Cys(B19)-Cys(B19) covalent homodimers resist reductive dissociation, highlighting a structural basis for aberrant proinsulin complex formation.	Disulfides	94-103	insulin II	Mus musculus	130-140
31184302-6	2019	We conclude that increased proinsulin misfolding via disulfide-linked complexes is an early event associated with prediabetes that worsens with ss-cell dysfunction in type two diabetes.	Disulfides	53-62	insulin II	Mus musculus	27-37
31184304-2	2019	In ss cells, protein disulfide isomerase A1 (PDIA1/P4HB), the most abundant ER oxidoreductase of over 17 members, can interact with proinsulin to influence disulfide maturation.	Disulfides	21-30	insulin II	Mus musculus	132-142
31184304-6	2019	Furthermore, Pdia1 deletion increased accumulation of disulfide-linked high molecular weight proinsulin complexes and islet vulnerability to oxidative stress.	Disulfides	54-63	insulin II	Mus musculus	93-103
31152503-0	2019	Does GPIbalpha prove the allosteric disulfide bond hypothesis?	Disulfides	36-45	glycoprotein Ib platelet subunit alpha	Homo sapiens	5-14
30853337-9	2019	Although the disulfide-bonded form of homocysteine (HSSH) modified PTP1B to form an inactive S-homocysteinylated PTP1B, HcySH-induced increase in the activities of cellular thioredoxin and thioredoxin reductase, components of thioredoxin system, could recover active PTP1B from S-homocysteinylated PTP1B.	Disulfides	13-22	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	67-72
30317562-4	2019	In this study, we first demonstrated that an intramolecular disulfide bond was formed between cysteine-102 and cysteine-121 in FGF21, implying that the oxidation of the cysteine to cysteic acid, which may interfere with the active conformation of FGF21, did not occur during the iodination procedures, and thus ruled out the possibility of the two conserved cysteine residues mediating the loss of FGF21 binding affinity to FGFR1-KLB upon iodination.	Disulfides	60-69	klotho beta	Homo sapiens	430-433
30608169-3	2019	We solved the crystal structure of the apo form of Kti11 to reveal two disulfide bonds at the metal-binding site, which seals off a cavity in the beta-barrel part of the protein.	Disulfides	71-80	diphthamide biosynthesis 3	Homo sapiens	51-56
30958660-4	2019	PDIs target disulfide bridges in the extracellular domains of proteins, such as integrins or A Disintegrin And Metalloprotease 17 (ADAM17) leading to changes in the structure and function of these molecules.	Disulfides	12-21	ADAM metallopeptidase domain 17	Homo sapiens	93-129
30958660-4	2019	PDIs target disulfide bridges in the extracellular domains of proteins, such as integrins or A Disintegrin And Metalloprotease 17 (ADAM17) leading to changes in the structure and function of these molecules.	Disulfides	12-21	ADAM metallopeptidase domain 17	Homo sapiens	131-137
30958660-5	2019	Integrins become activated and ADAM17 inactivated upon disulfide isomerization.	Disulfides	55-64	ADAM metallopeptidase domain 17	Homo sapiens	31-37
31376820-3	2019	LAT1 (also known as SLC7A5), is defined as a heteromeric amino acid transporter (HAT) interacting with the glycoprotein CD98 (SLC3A2) through a conserved disulfide to uptake not only large neutral amino acids, but also several pharmaceutical drugs to cells.	Disulfides	154-163	solute carrier family 3 member 2	Felis catus	126-132
29577955-1	2019	Adrenomedullin (AM), a peptide isolated from an extract of human pheochromocytoma, comprises 52 amino acids with an intramolecular disulfide bond and amidation at the carboxy-terminus.	Disulfides	131-140	adrenomedullin	Homo sapiens	0-14
30016556-5	2018	The digallanes reacted with 2 equiv of PhNCS in the presence of Na metal or at high temperatures through a unique reductive cleavage of the C=S bond to yield the disulfide-bridged digallium species [Na(THF)3 ]2 [L1 Ga(mu-S)2 GaL1 ] (5), [L2 Ga(mu-S)2 GaL2 ] (10), and [Na(DME)3 ][L2 Ga(mu-S)2 GaL2 ] (11).	Disulfides	162-171	galectin 2	Homo sapiens	251-255
30016556-5	2018	The digallanes reacted with 2 equiv of PhNCS in the presence of Na metal or at high temperatures through a unique reductive cleavage of the C=S bond to yield the disulfide-bridged digallium species [Na(THF)3 ]2 [L1 Ga(mu-S)2 GaL1 ] (5), [L2 Ga(mu-S)2 GaL2 ] (10), and [Na(DME)3 ][L2 Ga(mu-S)2 GaL2 ] (11).	Disulfides	162-171	galectin 2	Homo sapiens	293-297
29857171-5	2018	The oxidation of beta4-HbA is associated with the formation of a disulfide bridge between residues Cys112(G14) of beta1/beta4 and beta2/beta3 chains.	Disulfides	65-74	UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2	Homo sapiens	114-125
29845893-13	2018	CONCLUSION: An intermolecular disulfide bridge rather than an intramolecular disulfide bridge is important for both the trafficking and H2O2-generating activity of the DUOX1-DUOXA1 complex.	Disulfides	30-39	dual oxidase maturation factor 1	Homo sapiens	174-180
29900929-1	2018	BACKGROUND Whey acidic protein/four-disulfide core domain 21 (Wfdc21), also known as Lnc-DC, it has been reported to be correlated with immune response.	Disulfides	36-45	WAP four-disulfide core domain 21	Mus musculus	62-68
29789341-7	2018	Knockdown of Mia40, which introduces disulfide bonds into CHCH domain proteins, blocked mitochondrial import of CHCHD10.	Disulfides	37-46	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	13-18
29789341-8	2018	Overexpression of Mia40 rescued mitochondrial import of CHCHD10 Q108P by enhancing disulfide-bond formation.	Disulfides	83-92	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	18-23
29361137-0	2018	Homodimer formation by the ATP/UTP receptor P2Y2 via disulfide bridges.	Disulfides	53-62	purinergic receptor P2Y2	Homo sapiens	44-48
29910933-0	2018	BPTI folding revisited: switching a disulfide into methylene thioacetal reveals a previously hidden path.	Disulfides	36-45	spleen trypsin inhibitor I	Bos taurus	0-4
29910933-1	2018	Bovine pancreatic trypsin inhibitor (BPTI) is a 58-residue protein that is stabilized by three disulfide bonds at positions 5-55, 14-38 and 30-51.	Disulfides	95-104	spleen trypsin inhibitor I	Bos taurus	0-35
29910933-1	2018	Bovine pancreatic trypsin inhibitor (BPTI) is a 58-residue protein that is stabilized by three disulfide bonds at positions 5-55, 14-38 and 30-51.	Disulfides	95-104	spleen trypsin inhibitor I	Bos taurus	37-41
29910933-2	2018	Widely studied for about 50 years, BPTI represents a folding model for many disulfide-rich proteins.	Disulfides	76-85	spleen trypsin inhibitor I	Bos taurus	35-39
29410027-4	2018	Secreted AGR2 was defined to enhance VEGFR2 activity as evidenced by physical interaction of purified recombinant human AGR2 (rhAGR2) with rhVEGFA through the formation of a disulfide bond.	Disulfides	174-183	kinase insert domain receptor	Homo sapiens	37-43
29338251-1	2018	Oxytocin (OXT) is a cyclic nonapeptide, two amino acids of which are cysteine, forming an intramolecular disulfide bond.	Disulfides	105-114	oxytocin/neurophysin I prepropeptide	Homo sapiens	0-8
29338251-1	2018	Oxytocin (OXT) is a cyclic nonapeptide, two amino acids of which are cysteine, forming an intramolecular disulfide bond.	Disulfides	105-114	oxytocin/neurophysin I prepropeptide	Homo sapiens	10-13
29288085-5	2018	The presence of disulfide bonds in PAAs enables rapid disassembly of PAG micelles in response to reducing agents, inducing the release of loaded drugs (DTX, GA and MMP-9 shRNA).	Disulfides	16-25	phosphoprotein membrane anchor with glycosphingolipid microdomains 1	Homo sapiens	69-72
29288085-5	2018	The presence of disulfide bonds in PAAs enables rapid disassembly of PAG micelles in response to reducing agents, inducing the release of loaded drugs (DTX, GA and MMP-9 shRNA).	Disulfides	16-25	matrix metallopeptidase 9	Homo sapiens	164-169
29031766-8	2018	However, increasing the level to 200muM H2O2 results in a reversible intramolecular disulfide between Cys65-Cys110, which is substrate for glutaredoxin.	Disulfides	84-93	CAX interacting protein 1	Arabidopsis thaliana	139-151
29272095-0	2018	Hyaluronic Acid-Shelled Disulfide-Cross-Linked Nanopolymersomes for Ultrahigh-Efficiency Reactive Encapsulation and CD44-Targeted Delivery of Mertansine Toxin.	Disulfides	24-33	CD44 molecule (Indian blood group)	Homo sapiens	116-120
29272095-2	2018	Here, we report on novel hyaluronic acid-shelled disulfide-cross-linked biodegradable polymersomes (HA-XPS) self-assembled from hyaluronic acid-b-poly(trimethylene carbonate-co-dithiolane trimethylene carbonate) diblock copolymer for ultrahigh-efficiency reactive encapsulation and CD44-targeted delivery of mertansine (DM1) toxin, a highly potent warhead for clinically used antibody-drug conjugates.	Disulfides	49-58	CD44 molecule (Indian blood group)	Homo sapiens	282-286
30533490-3	2018	Through disulfide-cyclized method, we synthesized in this study, a new integrin alphavbeta6-targeted cyclic peptide (denoted as cHK), and radiolabeled it with 99mTc.	Disulfides	8-17	megakaryocyte-associated tyrosine kinase	Homo sapiens	128-131
28707588-1	2018	Prokineticin1 and prokineticin2 belong to a new family of chemokines identified in several species including mammals and characterized by the presence of five disulfide bridges.	Disulfides	159-168	prokineticin 1	Homo sapiens	0-13
28707588-1	2018	Prokineticin1 and prokineticin2 belong to a new family of chemokines identified in several species including mammals and characterized by the presence of five disulfide bridges.	Disulfides	159-168	prokineticin 2	Homo sapiens	18-31
29078150-0	2018	The influence of the Cys46/Cys55 disulfide bond on the redox and spectroscopic properties of human neuroglobin.	Disulfides	33-42	neuroglobin	Homo sapiens	99-110
29078150-2	2018	In the human protein (hNgb), Cys46 and Cys55 form an intramolecular disulfide bond under oxidizing conditions, whose cleavage induces a helix-to-strand rearrangement of the CD loop that strengthens the bond between the heme iron and the distal histidine.	Disulfides	68-77	neuroglobin	Homo sapiens	22-26
29078150-3	2018	Hence, it is conceivable that the intramolecular disulfide bridge modulates the functionality of human neuroglobin by controlling exogenous ligand binding.	Disulfides	49-58	neuroglobin	Homo sapiens	103-114
29078150-4	2018	In this work, we investigated the influence of the Cys46/Cys55 disulfide bond on the redox properties and on the pH-dependent conformational equilibria of hNgb, using UV-vis spectroelectrochemistry, cyclic voltammetry, electronic absorption spectroscopy and magnetic circular dichroism (MCD).	Disulfides	63-72	neuroglobin	Homo sapiens	155-159
29033317-2	2017	Here, we utilize disulfide tethering of a non-natural cysteine (K-Ras(M72C)) to identify a new switch-II pocket (S-IIP) binding ligand (2C07) that engages the active GTP state.	Disulfides	17-26	KRAS proto-oncogene, GTPase	Homo sapiens	64-69
28972175-9	2017	This is the first report of a bacterial GDP-regulated thioesterase and of covalent linkage of thioesterase domains through a disulfide bond, revealing structural similarities with ADP regulation in the human ACOT12 thioesterase.	Disulfides	125-134	acyl-CoA thioesterase 12	Homo sapiens	208-214
29241459-3	2017	However, the other essential protein, Mia40, was found to be absent or not required in some organisms, raising questions about how the disulfide relay functions in these organisms.	Disulfides	135-144	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	38-43
29212041-4	2017	We used a 96-well expression-screening format to assess the ability of artificial disulfides and Ile559Pro substitution (DS-SOSIP) to produce soluble cleaved-Env trimers; from 180 Env strains, 20 yielded prefusion closed trimers.	Disulfides	82-92	endogenous retrovirus group K member 20	Homo sapiens	158-161
29208936-5	2017	Using an integrated real-time approach, including chromatography, fluorescence, CD, FTIR, SAXS, NMR, and MS analysis, we demonstrate that in this mitochondrial protein, the conformational switch between disordered and folded states is controlled by the formation of a single disulfide bond, both in the presence and in the absence of Mia40.	Disulfides	275-284	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	334-339
28978648-6	2017	We generated a linker-less recombinant protein possessing a STAT1ND:STAT2ND heterodimeric structure via an artificial disulfide bond.	Disulfides	118-127	signal transducer and activator of transcription 1	Homo sapiens	60-67
28978648-6	2017	We generated a linker-less recombinant protein possessing a STAT1ND:STAT2ND heterodimeric structure via an artificial disulfide bond.	Disulfides	118-127	signal transducer and activator of transcription 2	Homo sapiens	68-73
29214238-10	2017	The structure shows that the catalytic Cys459 residue forms a disulfide bond with Cys367, which confirms that Cys367 functions as the "backdoor" cysteine in SHP2.	Disulfides	62-71	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	157-161
29117860-2	2017	In fungi and animals, the sulfhydryl oxidase Erv1 "generates" disulfide bonds that are passed on to the oxidoreductase Mia40, which oxidizes substrate proteins.	Disulfides	62-71	Mia40p	Saccharomyces cerevisiae S288C	119-124
29117860-9	2017	In accordance to the absence of Mia40 in many protists, our study suggests that the mitochondrial disulfide relay evolved in a stepwise reaction from an Erv1-only system to which Mia40 was added in order to improve substrate specificity.	Disulfides	98-107	Mia40p	Saccharomyces cerevisiae S288C	32-37
29117860-9	2017	In accordance to the absence of Mia40 in many protists, our study suggests that the mitochondrial disulfide relay evolved in a stepwise reaction from an Erv1-only system to which Mia40 was added in order to improve substrate specificity.	Disulfides	98-107	Mia40p	Saccharomyces cerevisiae S288C	179-184
28878015-3	2017	Specifically, RIPK3-dependent MLKL phosphorylation promotes the assembly of disulfide bond-dependent MLKL polymers that drive the execution of necroptosis.	Disulfides	76-85	receptor interacting serine/threonine kinase 3	Homo sapiens	14-19
28814504-6	2017	In reconstitution studies with reduced Tim13, Mia40, and Erv1, the addition of Osm1 and fumarate completes the disulfide exchange pathway that results in Tim13 oxidation.	Disulfides	111-120	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	46-51
28837266-5	2017	Using mutational analysis and pulse-chase experiments, we found that the four ILEI cysteines, conserved throughout the FAM3 family and involved in disulfide bond formation were essential for extracellular ILEI accumulation in cultured cells.	Disulfides	147-156	FAM3 metabolism regulating signaling molecule C	Mus musculus	78-82
28837266-5	2017	Using mutational analysis and pulse-chase experiments, we found that the four ILEI cysteines, conserved throughout the FAM3 family and involved in disulfide bond formation were essential for extracellular ILEI accumulation in cultured cells.	Disulfides	147-156	FAM3 metabolism regulating signaling molecule C	Mus musculus	205-209
28774960-3	2017	Endoplasmic reticulum oxidase 1alpha (ERO1alpha) functions as an oxidative enzyme of protein disulfide isomerase, which forms intramolecular disulfide bonds of membrane and secreted proteins.	Disulfides	93-102	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	38-47
28774960-8	2017	Silencing of ERO1alpha expression induced impaired disulfide bond formation and inhibited autophagy via activation of the Akt/mammalian target of rapamycin signaling pathway, resulting in intracellular accumulation of collagen type 1 in HSCs.	Disulfides	51-60	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	13-22
28751379-8	2017	However, more surprisingly, the ILEI dimer structure was found to feature a trans-linked domain swap, converting an intramolecular disulfide to intermolecular.	Disulfides	131-140	FAM3 metabolism regulating signaling molecule C	Homo sapiens	32-36
28716990-3	2017	Oxidants induce an interprotein disulfide in PKG Ialpha (protein kinase G Ialpha) at C42, which is associated with its targeting and activation, resulting in vasodilation and blood pressure lowering.	Disulfides	32-41	CDK5 regulatory subunit associated protein 1	Homo sapiens	85-88
28373131-9	2017	The close proximity of the non-covalent and disulfide binding domains on lubricin suggest a two-step mechanism to strongly bind lubricin to COMP.	Disulfides	44-53	cartilage oligomeric matrix protein	Homo sapiens	140-144
28369693-2	2017	Scalable high titer production of native NTN is particularly challenging because of the cystine knot structure which consists of an embedded ring comprised of at least three disulfide bonds.	Disulfides	174-183	neurturin	Homo sapiens	41-44
28790822-7	2017	OPSS forms a disulfide bond with activated complement C3, which then targets liposomes for uptake by dendritic cells, macrophages, B cells, MDSCs, and neutrophils in human blood.	Disulfides	13-22	complement C3	Homo sapiens	43-56
28601997-6	2017	Analysis of amino acid composition showed a severe damage to the disulfide bonds in keratin during the extraction procedure.	Disulfides	65-74	keratin	Gallus gallus	84-91
28464519-1	2017	BACKGROUND: Extra-corpuscular haemoglobin is an endogenous factor enhancing inflammatory tissue damage, a process counteracted by the haemoglobin-binding plasma protein haptoglobin composed of alpha and beta subunits connected by disulfide bridges.	Disulfides	230-239	haptoglobin	Mus musculus	169-180
28566233-11	2017	Based on the crystal structure we predict that the exchange of glutamate-113 against lysine should induce a strong destabilization of the secondary structure, possibly affecting the folding for correct disulfide bridging between C235-C346 as well as distortion of the active site groove that could affect both the intracellular stability as well as the activity of FGE.	Disulfides	202-211	sulfatase modifying factor 1	Homo sapiens	365-368
32263974-2	2017	In this work, the GSH responsive porphyrin molecule (TPP 1) was synthesized, which is amphiphilic and linked by a disulfide bond.	Disulfides	114-123	tripeptidyl peptidase 1	Homo sapiens	53-58
28389559-9	2017	Furthermore, we also show that whereas STEP and PTPRR stabilize their reversibly oxidized state by forming an intramolecular disulfide bond, HePTP uses an unexpected mechanism, namely, formation of a reversible intermolecular disulfide bond.	Disulfides	125-134	protein tyrosine phosphatase receptor type R	Homo sapiens	48-53
28283570-7	2017	Moreover, introduction of a disulfide bond in the bridging sheet region further stabilized the closed conformation of the Env.	Disulfides	28-37	endogenous retrovirus group K member 20	Homo sapiens	122-125
28394477-2	2017	The replacement of the interchain disulfide with a diselenide bridge, which is more resistant to reduction and internal bond rotation, can enhance the lifetime of insulin in the presence of the insulin-degrading enzyme (IDE) without impairing the hormonal function.	Disulfides	34-43	insulin degrading enzyme	Homo sapiens	194-218
28394477-2	2017	The replacement of the interchain disulfide with a diselenide bridge, which is more resistant to reduction and internal bond rotation, can enhance the lifetime of insulin in the presence of the insulin-degrading enzyme (IDE) without impairing the hormonal function.	Disulfides	34-43	insulin degrading enzyme	Homo sapiens	220-223
28300660-4	2017	Here we report that these so-called Cys-capping modifications take place outside mammalian cells, not in the endoplasmic reticulum (ER) where oxidoreductase-mediated protein disulfide formation occurs.	Disulfides	174-183	thioredoxin reductase 1	Homo sapiens	142-156
27733423-2	2017	In a previous study, we found that immunization with a recombinant disulfide-bridged dimeric form of OspC (D-OspC) stimulates increased antibody responses relative to immunization with commonly employed monomeric OspC.	Disulfides	67-76	OspC	Borreliella burgdorferi	109-113
27554421-3	2017	Through an analysis of the mode of disulfide formation among cysteines inserted at the N- or C-terminus of these peptide segments, EF3 and EF4 peptides were suggested to form a heterodimer with a topology similar to that in the wild-type protein.	Disulfides	35-44	GTP binding elongation factor GUF1	Homo sapiens	139-142
28063498-4	2017	High-resolution mass spectrometry and enzymatic assays were, respectively, used to show that all disulfides are formed and that the enzymes are active, strongly suggesting that each sPLA2 was prepared in the structurally native form.	Disulfides	97-107	phospholipase A2 group IIA	Homo sapiens	182-187
27992223-3	2016	However, the reports on the mechanistic pathway of irreversible proton pump inhibitors (PPIs) on the acid activation and formation of disulfide complex are scarce in the literature.	Disulfides	134-143	ATPase H+/K+ transporting subunit alpha	Homo sapiens	64-75
27992223-5	2016	The proton pump inhibitor is a prodrug and activated in the acidic canaliculi of the gastric pump H+,K+-ATPase to sulfenic acid which can either form another acid activate intermediate sulfenamide or a disulfide complex with cysteine amino acid of H+,K+-ATPase.	Disulfides	202-211	ATPase H+/K+ transporting subunit alpha	Homo sapiens	4-15
28031247-0	2016	Thioredoxin-dependent disulfide bond reduction is required for protamine eviction from sperm chromatin.	Disulfides	22-31	Thioredoxin-like	Drosophila melanogaster	0-11
28031247-2	2016	Here we identify the Drosophila thioredoxin Deadhead (DHD) as the factor responsible for the reduction of intermolecular disulfide bonds in protamines and their eviction from sperm during fertilization.	Disulfides	121-130	Thioredoxin-like	Drosophila melanogaster	32-43
27777122-1	2016	Fibulin-3 (F3) is an important, disulfide-rich, extracellular matrix glycoprotein that has been associated with a number of diseases ranging from cancer to retinal degeneration.	Disulfides	32-41	EGF containing fibulin extracellular matrix protein 1	Homo sapiens	0-13
27703014-1	2016	In the mammalian endoplasmic reticulum, oxidoreductin-1alpha (Ero1alpha) generates protein disulfide bonds and transfers them specifically to canonical protein-disulfide isomerase (PDI) to sustain oxidative protein folding.	Disulfides	91-100	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	62-71
27642162-4	2016	Our data reveal that ERp44 binds the oxidized form of peroxiredoxin 4 via thiol-disulfide interchange reactions.	Disulfides	80-89	peroxiredoxin 4	Homo sapiens	54-69
27480846-4	2016	Proteomics analysis showed that UNG1 bound to eight proteins in the mitochondria, including PAPSS2, CD70 antigen, and AGR2 under normal growth conditions, whereas UNG1 mainly bound to Peroxiredoxin 3 (PRDX3) via a disulfide linkage under oxidative stress.	Disulfides	214-223	peroxiredoxin 3	Homo sapiens	201-206
27264910-4	2016	These studies demonstrated that bis(3-propionic acid methyl ester) phenylphosphine-borane complex (PB1) and (3-propionic acid methyl ester) diphenylphosphine-borane complex (PB2) are potent intracellular disulfide reducing agents which are cell permeable.	Disulfides	204-213	submaxillary gland androgen regulated protein 3A	Homo sapiens	99-102
27233821-1	2016	The chloroplast ATP synthase is known to be regulated by redox modulation of a disulfide bridge on the gamma-subunit through the ferredoxin-thioredoxin regulatory system.	Disulfides	79-88	ATP synthase	Arabidopsis thaliana	16-28
27495374-10	2016	Importantly, we have discovered that a class of compounds termed Disulfide bond Disrupting Agents (DDAs) blocks CDCP1/EGFR/Src ternary complex formation and downstream signaling.	Disulfides	65-74	CUB domain containing protein 1	Homo sapiens	112-117
26946085-5	2016	Recombinant mMDH protein formed intramolecular disulfide bonds under oxidative conditions, but these bonds did not have a considerable effect on mMDH activity.	Disulfides	47-56	malate dehydrogenase 2, NAD (mitochondrial)	Mus musculus	12-16
27100727-1	2016	BACKGROUND: Endoplasmic reticulum disulfide oxidase 1-alpha (ERO1-alpha) is an oxidase that exists in the endoplasmic reticulum and has a role in the formation of disulfide bonds of secreted proteins and cell-surface proteins.	Disulfides	34-43	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	61-71
27041594-3	2016	Through structure-based design, we developed ID2, which consists of the ID expressed independently of the outer domain and stabilized in the CD4-bound conformation by an inter-layer disulfide bond.	Disulfides	182-191	inhibitor of DNA binding 2	Homo sapiens	45-48
26195288-3	2016	Our previous results show that the MED10a, MED28, and MED32 Mediator subunits form various types of covalent oligomers linked by intermolecular disulfide bonds in vitro.	Disulfides	144-153	Mediator complex, subunit Med10	Arabidopsis thaliana	35-41
26724416-0	2016	Improving the soluble expression and purification of recombinant human stem cell factor (SCF) in endotoxin-free Escherichia coli by disulfide shuffling with persulfide.	Disulfides	132-141	KIT ligand	Homo sapiens	71-87
26724416-0	2016	Improving the soluble expression and purification of recombinant human stem cell factor (SCF) in endotoxin-free Escherichia coli by disulfide shuffling with persulfide.	Disulfides	132-141	KIT ligand	Homo sapiens	89-92
26748070-2	2016	Oxidation of the enzyme causes its inactivation and the formation of intermolecular disulfide bonds, and leads to the accumulation of GAPDH aggregates and ultimately to cell death.	Disulfides	84-93	glyceraldehyde-3-phosphate dehydrogenase	Rattus norvegicus	134-139
26609676-0	2016	Redox-dependent disulfide bond formation in SAP30L corepressor protein: Implications for structure and function.	Disulfides	16-25	SAP30 like	Homo sapiens	44-50
26609676-5	2016	By using high-resolution mass spectrometry, we studied a redox-dependent disulfide bond formation in SAP30L ZnF as a regulatory mechanism for its structure and function.	Disulfides	73-82	SAP30 like	Homo sapiens	101-107
26609676-6	2016	We showed that upon oxidative stress SAP30L undergoes the formation of two specific disulfide bonds, a vicinal Cys29-Cys30 and Cys38-Cys74, with a concomitant release of the coordinated zinc ion.	Disulfides	84-93	SAP30 like	Homo sapiens	37-43
26555263-6	2016	The structures reveal the presence of a disulfide bond between conserved cysteines that is positioned at the nucleotide-binding loop of eukaryotic ADPGK.	Disulfides	40-49	ADP dependent glucokinase	Homo sapiens	147-152
26555263-7	2016	The AMP-bound ADPGK structure defines the nucleotide-binding site with one of the disulfide bond cysteines coordinating the AMP with its main chain atoms, a nucleotide-binding motif that appears unique to eukaryotic ADPGKs.	Disulfides	82-91	ADP dependent glucokinase	Homo sapiens	14-19
26537754-2	2016	It is made up of two disulfide-linked membrane subunits: the carrier, b(0,+)AT and the helper, rBAT (related to b(0,+) amino acid transporter).	Disulfides	21-30	solute carrier family 7 member 9	Homo sapiens	70-78
26537754-2	2016	It is made up of two disulfide-linked membrane subunits: the carrier, b(0,+)AT and the helper, rBAT (related to b(0,+) amino acid transporter).	Disulfides	21-30	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	95-99
26537754-10	2016	Deletion of the rBAT C-terminal disulfide loop (residues 673-685) prevented maturation and prompted degradation of the transporter.	Disulfides	32-41	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	16-20
26537754-13	2016	These data highlight the important role of the N-glycan Asn(575) and the C-terminal disulfide loop of rBAT in biogenesis of the rBAT-b(0,+)AT heterodimer.	Disulfides	84-93	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	102-106
26537754-13	2016	These data highlight the important role of the N-glycan Asn(575) and the C-terminal disulfide loop of rBAT in biogenesis of the rBAT-b(0,+)AT heterodimer.	Disulfides	84-93	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	128-132
26537754-13	2016	These data highlight the important role of the N-glycan Asn(575) and the C-terminal disulfide loop of rBAT in biogenesis of the rBAT-b(0,+)AT heterodimer.	Disulfides	84-93	solute carrier family 7 member 9	Homo sapiens	133-141
26638778-4	2016	In addition, owing to their cellular redox-responsiveness at the cleavable disulfide linker, the PEG-SS-Ce6-MMP2 nanoparticles were able to release Ce6 rapidly.	Disulfides	75-84	matrix metallopeptidase 2	Mus musculus	108-112
26913555-3	2016	Pig CD90 cDNA contained an open reading frame (486 bp) encoding 161 amino acids with three putative N-glycosylation sites and four well-conserved cysteine residues, which form a possible disulfide bond within the extracellular domain among mammalian species.	Disulfides	187-196	Thy-1 cell surface antigen	Sus scrofa	4-8
26719247-2	2015	We used a mass spectrometry (MS)-based method to map the disulfide bonds present in nonnative uncleaved gp140 proteins and native-like SOSIP.664 trimers based on the BG505 env gene.	Disulfides	57-66	endogenous retrovirus group K member 20	Homo sapiens	172-175
26719247-5	2015	We also observed that the purification method could influence the proportion of an Env protein population that contained aberrant disulfide bonds.	Disulfides	130-139	endogenous retrovirus group K member 20	Homo sapiens	83-86
26719247-11	2015	Moreover, some soluble recombinant Env proteins contain aberrant disulfide bonds that are not expected to be present in the native trimer.	Disulfides	65-74	endogenous retrovirus group K member 20	Homo sapiens	35-38
26719252-9	2015	Coupling the TD-based design with the engineered disulfide linkage, CC, increased the propensity of Env to form soluble highly stable spike mimics that are resistant to CD4-induced changes.	Disulfides	49-58	endogenous retrovirus group K member 20	Homo sapiens	100-103
26719270-9	2015	In parallel, the disulfide bonds of CP Env were identified using mass spectrometry.	Disulfides	17-26	endogenous retrovirus group K member 20	Homo sapiens	39-42
26729099-1	2015	Human leukocytic antigen-B27 heavy chain (HLA-B27 HC) has the tendency to fold slowly, in turn gradually forming a homodimer, (B27-HC)2 via a disulfide linkage to activate killer cells and T-helper 17 cells and inducing endoplasmic reticulum (ER) stress to trigger the IL-23/IL-17 axis for pro-inflammatory reactions.	Disulfides	142-151	interleukin 17A	Homo sapiens	275-280
26458166-8	2015	Overall, the results are consistent with the view that the binding of PTT positions the peptide SH group to interfere with conserved disulfides clustered proximal to the CD4 binding site in gp120, leading to disulfide exchange in gp120 and possibly gp41, rearrangement of the Env spike, and ultimately disruption of the viral membrane.	Disulfides	133-143	endogenous retrovirus group K member 20	Homo sapiens	276-279
26458166-8	2015	Overall, the results are consistent with the view that the binding of PTT positions the peptide SH group to interfere with conserved disulfides clustered proximal to the CD4 binding site in gp120, leading to disulfide exchange in gp120 and possibly gp41, rearrangement of the Env spike, and ultimately disruption of the viral membrane.	Disulfides	133-142	endogenous retrovirus group K member 20	Homo sapiens	276-279
26410624-1	2015	Thioredoxin 1 (Trx1) is a antioxidant protein that regulates protein disulfide bond reduction, transnitrosylation, denitrosylation and other redox post-translational modifications.	Disulfides	69-78	thioredoxin 1	Mus musculus	0-13
26410624-1	2015	Thioredoxin 1 (Trx1) is a antioxidant protein that regulates protein disulfide bond reduction, transnitrosylation, denitrosylation and other redox post-translational modifications.	Disulfides	69-78	thioredoxin 1	Mus musculus	15-19
26410624-3	2015	Although previous redox post-translational modifications proteomics studies found that several cellular protein networks are regulated by Trx1-mediated disulfide reduction and transnitrosylation, we found that Trx1 regulates the expression of a limited number of proteins.	Disulfides	152-161	thioredoxin 1	Mus musculus	138-142
26410624-6	2015	The results presented here suggest for the first time that, in addition to being a master redox regulator of protein disulfide bonds and nitrosation, Trx1 may also modulate lysine methylation, a non-redox post-translational modification, via the regulation of SMYD1 expression.	Disulfides	117-126	thioredoxin 1	Mus musculus	150-154
26456799-2	2015	As potential candidates we assessed thioredoxin-fold proteins, called redoxins, which maintain redox homeostasis by reduction of hydrogen peroxide or protein dithiol-disulfide exchange.	Disulfides	166-175	thioredoxin 1	Mus musculus	36-47
26483203-3	2015	JX06 forms a disulfide bond with the thiol group of a conserved cysteine residue (C240) based on recognition of a hydrophobic pocket adjacent to the ATP pocket of the PDK1 enzyme.	Disulfides	13-22	pyruvate dehydrogenase kinase 1	Homo sapiens	167-171
26523116-5	2015	Determining the disulfide bond connectivity between the cysteines of a protein is desirable as a previous step of the 3D PSP, as the protein conformational search space is highly reduced.	Disulfides	16-25	microseminoprotein beta	Homo sapiens	121-124
26371297-6	2015	Our new assignments include two CHCH-domain containing subunits that contain disulfide bridges between CX9C motifs; they are processed by the Mia40 oxidative-folding pathway in the intermembrane space and probably stabilize the membrane domain.	Disulfides	77-86	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	142-147
25761904-0	2015	When an Intramolecular Disulfide Bridge Governs the Interaction of DUOX2 with Its Partner DUOXA2.	Disulfides	23-32	dual oxidase maturation factor 2	Homo sapiens	90-96
26379032-0	2015	CD44 Binding to Hyaluronic Acid Is Redox Regulated by a Labile Disulfide Bond in the Hyaluronic Acid Binding Site.	Disulfides	63-72	CD44 molecule (Indian blood group)	Homo sapiens	0-4
26379032-3	2015	We have identified one such disulfide bond in CD44 formed by Cys77 and Cys97 that stabilises the HA binding groove.	Disulfides	28-37	CD44 molecule (Indian blood group)	Homo sapiens	46-50
26379032-5	2015	Analysis of CD44 crystal structures reveal the disulfide bond to be solvent accessible and in the-LH hook configuration characteristic of labile disulfide bonds.	Disulfides	47-56	CD44 molecule (Indian blood group)	Homo sapiens	12-16
26379032-5	2015	Analysis of CD44 crystal structures reveal the disulfide bond to be solvent accessible and in the-LH hook configuration characteristic of labile disulfide bonds.	Disulfides	145-154	CD44 molecule (Indian blood group)	Homo sapiens	12-16
26379032-6	2015	Kinetic trapping and binding experiments on CD44-Fc chimeric proteins show the bond is preferentially reduced over the other disulfide bonds in CD44 and reduction inhibits the CD44-HA interaction.	Disulfides	125-134	CD44 molecule (Indian blood group)	Homo sapiens	44-48
26379032-6	2015	Kinetic trapping and binding experiments on CD44-Fc chimeric proteins show the bond is preferentially reduced over the other disulfide bonds in CD44 and reduction inhibits the CD44-HA interaction.	Disulfides	125-134	CD44 molecule (Indian blood group)	Homo sapiens	144-148
26379032-6	2015	Kinetic trapping and binding experiments on CD44-Fc chimeric proteins show the bond is preferentially reduced over the other disulfide bonds in CD44 and reduction inhibits the CD44-HA interaction.	Disulfides	125-134	CD44 molecule (Indian blood group)	Homo sapiens	144-148
26203189-6	2015	Thus, our data demonstrate that the bundle of GP Ibbeta and GP IX TMDs instead of their individual CTs is the structural element that mediates the beta/IX complex localization to the membrane GEMs, which through the alpha/beta disulfide linkage brings GP Ibalpha into the GEMs.	Disulfides	227-236	glycoprotein Ib platelet subunit beta	Homo sapiens	46-55
26203189-6	2015	Thus, our data demonstrate that the bundle of GP Ibbeta and GP IX TMDs instead of their individual CTs is the structural element that mediates the beta/IX complex localization to the membrane GEMs, which through the alpha/beta disulfide linkage brings GP Ibalpha into the GEMs.	Disulfides	227-236	glycoprotein Ib platelet subunit alpha	Homo sapiens	252-262
26214018-8	2015	The introduction of disulfides in the IMS is catalyzed by Mia40 that functions as a chaperone inducing their folding.	Disulfides	20-30	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	58-63
26214018-10	2015	The solution NMR structure of Mia40 (and supporting biochemical experiments) showed that Mia40 is a novel type of disulfide donor whose recognition capacity for its substrates relies on a hydrophobic binding cleft found adjacent to a thiol active CPC motif.	Disulfides	114-123	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	30-35
26214018-10	2015	The solution NMR structure of Mia40 (and supporting biochemical experiments) showed that Mia40 is a novel type of disulfide donor whose recognition capacity for its substrates relies on a hydrophobic binding cleft found adjacent to a thiol active CPC motif.	Disulfides	114-123	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	89-94
26086102-5	2015	Exogenous expression of wild-type as well as pathogenic mutant SOD1 fused with a fluorescent protein in C. elegans resulted in the accumulation of disulfide-reduced SOD1 and retarded the worm"s motility.	Disulfides	147-156	Superoxide dismutase [Cu-Zn]	Caenorhabditis elegans	63-67
26086102-5	2015	Exogenous expression of wild-type as well as pathogenic mutant SOD1 fused with a fluorescent protein in C. elegans resulted in the accumulation of disulfide-reduced SOD1 and retarded the worm"s motility.	Disulfides	147-156	Superoxide dismutase [Cu-Zn]	Caenorhabditis elegans	165-169
26035642-7	2015	We find that linking the anti-parallel coiled-coils of the adjacent Orai1 C-termini through disulfide cross-links diminishes STIM1-Orai1 interaction, as assessed by FRET.	Disulfides	92-101	ORAI calcium release-activated calcium modulator 1	Homo sapiens	68-73
26035642-7	2015	We find that linking the anti-parallel coiled-coils of the adjacent Orai1 C-termini through disulfide cross-links diminishes STIM1-Orai1 interaction, as assessed by FRET.	Disulfides	92-101	ORAI calcium release-activated calcium modulator 1	Homo sapiens	131-136
25866208-0	2015	Structures of the Ets Protein DNA-binding Domains of Transcription Factors Etv1, Etv4, Etv5, and Fev: DETERMINANTS OF DNA BINDING AND REDOX REGULATION BY DISULFIDE BOND FORMATION.	Disulfides	154-163	ETS variant transcription factor 4	Homo sapiens	81-85
25892205-2	2015	The employed anti-miR-peptide conjugates are based on peptide nucleic acids (PNAs), which are connected with the membrane translocation peptide pHLIP through a disulfide bond.	Disulfides	160-169	membrane associated ring-CH-type finger 8	Homo sapiens	18-21
25825250-1	2015	Reactive oxygen species (ROS) in plants, arising from various environmental stresses, impair the thiol-contained proteins that are susceptible to irregular oxidative formation of disulfide bonds, which might be alleviated by a relatively specific modifier called protein disulfide isomerase (PDI).	Disulfides	179-188	protein disulfide-isomerase	Jatropha curcas	263-290
25825250-1	2015	Reactive oxygen species (ROS) in plants, arising from various environmental stresses, impair the thiol-contained proteins that are susceptible to irregular oxidative formation of disulfide bonds, which might be alleviated by a relatively specific modifier called protein disulfide isomerase (PDI).	Disulfides	179-188	protein disulfide-isomerase	Jatropha curcas	292-295
25727886-2	2015	In this study, a disulfide-linked alpha-helix-containing peptide, apamin, was used to mimic the extracellular, structured N-terminal part of the protein p32 and then serve as an imprinting template for generating a sub-40 nm-sized polymeric nanoparticle that potently binds to the target protein, recognizes p32-positive tumor cells, and successfully mediates targeted photodynamic therapy in vivo.	Disulfides	17-26	CD8a molecule	Homo sapiens	153-156
25727886-2	2015	In this study, a disulfide-linked alpha-helix-containing peptide, apamin, was used to mimic the extracellular, structured N-terminal part of the protein p32 and then serve as an imprinting template for generating a sub-40 nm-sized polymeric nanoparticle that potently binds to the target protein, recognizes p32-positive tumor cells, and successfully mediates targeted photodynamic therapy in vivo.	Disulfides	17-26	CD8a molecule	Homo sapiens	308-311
25559993-3	2015	The dynamic aggregation of TRAP protein in the presence of gold nanoparticles was observed, including oligomeric rearrangements, consistent with a role for gold in mediating intermolecular disulfide bond formation.	Disulfides	189-198	TRAP	Homo sapiens	27-31
25559993-5	2015	A potential role for inter-ring disulfide bonds in forming the TRAP-cage was shown by the fact that ring-ring interactions were reversed upon the addition of reducing agent dithiothreitol.	Disulfides	32-41	TRAP	Homo sapiens	63-67
25434589-3	2015	Prokineticins (PKs), which include PK1 and PK2, represent a novel family of chemokines characterized by a unique structural motif comprising five disulfide bonds.	Disulfides	146-155	pyruvate kinase liver and red blood cell	Mus musculus	35-38
26447598-0	2015	Recombinant expression, in vitro refolding and characterizing disulfide bonds of a mouse inhibitory C-type lectin-like receptor Nkrp1b.	Disulfides	62-71	killer cell lectin-like receptor subfamily B member 1B	Mus musculus	128-134
26447598-6	2015	Nkrp1b identity and folding was confirmed using mass spectrometry (accurate mass of the intact protein and evaluation of disulfide bonds) and one-dimensional nuclear magnetic resonance spectroscopy.	Disulfides	121-130	killer cell lectin-like receptor subfamily B member 1B	Mus musculus	0-6
25185155-2	2014	Typically, these receptors form a seven-transmembrane helix bundle, which is stabilized by a disulfide bond bridging the top of the third transmembrane segment (TM3) and the second extracellular loop (ECL2).	Disulfides	93-102	tropomyosin 3	Homo sapiens	161-164
25185155-3	2014	Resolution of the three-dimensional structures of the chemokine receptors CXCR1, CXCR4, and CCR5 revealed the existence of a second disulfide bridge that links the N terminus of the receptor to the top of the seventh transmembrane segment (TM7), thereby closing the receptor into a ring.	Disulfides	132-141	C-X-C motif chemokine receptor 1	Homo sapiens	74-79
25185155-3	2014	Resolution of the three-dimensional structures of the chemokine receptors CXCR1, CXCR4, and CCR5 revealed the existence of a second disulfide bridge that links the N terminus of the receptor to the top of the seventh transmembrane segment (TM7), thereby closing the receptor into a ring.	Disulfides	132-141	C-X-C motif chemokine receptor 4	Homo sapiens	81-86
25185155-3	2014	Resolution of the three-dimensional structures of the chemokine receptors CXCR1, CXCR4, and CCR5 revealed the existence of a second disulfide bridge that links the N terminus of the receptor to the top of the seventh transmembrane segment (TM7), thereby closing the receptor into a ring.	Disulfides	132-141	C-C motif chemokine receptor 5	Homo sapiens	92-96
25015885-3	2014	In this study, employing Saccharomyces cerevisiae display and secretion systems, it was found that BDNF was poorly expressed and partially inactive on the yeast surface and that BDNF was secreted at low levels in the form of disulfide-bonded aggregates.	Disulfides	225-234	brain-derived neurotrophic factor	Rattus norvegicus	178-182
24920800-6	2014	In the context of cell surface-expressed JRFL Env, introduction of a previously reported additional disulfide between residues A501 and T605 perturbs the native conformation, though this effect is partially alleviated by furin coexpression.	Disulfides	100-109	endogenous retrovirus group K member 20	Homo sapiens	46-49
24633508-1	2014	Ricin is a toxic protein derived from castor beans and composed of a cytotoxic A chain and a galactose-binding B chain linked by a disulfide bond, which can inhibit protein synthesis and cause cell death.	Disulfides	131-140	ricin	Ricinus communis	0-5
24855999-5	2014	We postulate that the strand-to-helix mechanics of the CD loop allows hNgb to utilize the lability of Cys46/Cys55 disulfide bonding and of the Tyr44/His64/heme propionate interaction network for redox-controlled functioning of hNgb.	Disulfides	114-123	neuroglobin	Homo sapiens	70-74
24758166-2	2014	In mammalian cells, the major pathway for de novo disulfide formation involves the enzyme Ero1alpha (endoplasmic reticulum oxidase 1alpha) which couples oxidation of thiols to the reduction of molecular oxygen to form hydrogen peroxide (H2O2).	Disulfides	50-59	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	90-99
24758166-3	2014	Ero1alpha activity is tightly regulated by a mechanism that requires the formation of regulatory disulfides.	Disulfides	97-107	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	0-9
24758166-8	2014	Further studies showed that both active sites of PDI contribute to the formation of regulatory disulfides in Ero1alpha and that the PDI substrate-binding domain is crucial to allow electron transfer between the two enzymes.	Disulfides	95-105	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	109-118
24787654-0	2014	Characterization and bioactivity of hepcidin-2 in zebrafish: dependence of antibacterial activity upon disulfide bridges.	Disulfides	103-112	hepcidin antimicrobial peptide	Danio rerio	36-46
24787654-6	2014	The data also show that the antibacterial activity of hepcidin-2 depends upon the disulfide bridges.	Disulfides	82-91	hepcidin antimicrobial peptide	Danio rerio	54-64
24625320-3	2014	Erv1 a FAD-dependent thiol oxidase, in turn reoxidizes Mia40 via its N-terminal Cys30-Cys33 shuttle disulfide.	Disulfides	100-109	Mia40p	Saccharomyces cerevisiae S288C	55-60
24625320-8	2014	Although Cys33 is essential for forming the intermediate disulfide Cys33-Cys130" and transferring electrons to the redox active-site directly, Cys30 plays two important roles: (i) dominantly interacts and receives electrons from the Mia40 CPC motif; and (ii) resolves the Erv1 Cys33-Cys130 intermediate disulfide.	Disulfides	57-66	Mia40p	Saccharomyces cerevisiae S288C	233-238
24625320-8	2014	Although Cys33 is essential for forming the intermediate disulfide Cys33-Cys130" and transferring electrons to the redox active-site directly, Cys30 plays two important roles: (i) dominantly interacts and receives electrons from the Mia40 CPC motif; and (ii) resolves the Erv1 Cys33-Cys130 intermediate disulfide.	Disulfides	303-312	Mia40p	Saccharomyces cerevisiae S288C	233-238
24855952-0	2014	Interaction of circadian clock proteins CRY1 and PER2 is modulated by zinc binding and disulfide bond formation.	Disulfides	87-96	period circadian regulator 2	Homo sapiens	49-53
24855952-6	2014	We provide evidence that mCRY1/mPER2 complex formation is modulated by an interplay of zinc binding and mCRY1 disulfide bond formation, which may be influenced by the redox state of the cell.	Disulfides	110-119	cryptochrome 1 (photolyase-like)	Mus musculus	25-30
24855952-6	2014	We provide evidence that mCRY1/mPER2 complex formation is modulated by an interplay of zinc binding and mCRY1 disulfide bond formation, which may be influenced by the redox state of the cell.	Disulfides	110-119	cryptochrome 1 (photolyase-like)	Mus musculus	104-109
24699645-0	2014	The crystal structure of wild-type human brain neuroglobin reveals flexibility of the disulfide bond that regulates oxygen affinity.	Disulfides	86-95	neuroglobin	Homo sapiens	47-58
24699645-2	2014	In human neuroglobin, a cysteine at position 46 in the loop connecting the C and D helices of the globin fold is presumed to form an intramolecular disulfide bond with Cys55.	Disulfides	148-157	neuroglobin	Homo sapiens	9-20
24038029-5	2014	We observed that hemichromes, following their binding to the cytoplasmic domain of band 3, induce the formation of disulfide band 3 dimers that are subsequently phosphorylated by p72Syk kinase.	Disulfides	115-124	spleen associated tyrosine kinase	Homo sapiens	179-185
24881668-9	2014	As a consequence, we concluded that redox changes of the heme iron and the disulfide bond could regulate neuroprotective functions of hNgb, and it suggests that hNgb can afford protection against hypoxic and ischemic stress in the brain.	Disulfides	75-84	neuroglobin	Homo sapiens	134-138
24176819-5	2014	The structural model of grouper IL-12 heterodimer revealed NC(141)F three amino acid patch of grouper p35, which is present in teleost p35 but absent in mammalian and avian p35, and is spatially nearby the conserved cysteine residue located at A-helix of p35 to form a disulfide bond when the 14aa peptide located at loop 1 of grouper p35 was aligned with human corresponding exon 4, instead of exon 5.	Disulfides	269-278	interleukin 12A	Homo sapiens	102-105
24176819-5	2014	The structural model of grouper IL-12 heterodimer revealed NC(141)F three amino acid patch of grouper p35, which is present in teleost p35 but absent in mammalian and avian p35, and is spatially nearby the conserved cysteine residue located at A-helix of p35 to form a disulfide bond when the 14aa peptide located at loop 1 of grouper p35 was aligned with human corresponding exon 4, instead of exon 5.	Disulfides	269-278	interleukin 12A	Homo sapiens	135-138
24176819-5	2014	The structural model of grouper IL-12 heterodimer revealed NC(141)F three amino acid patch of grouper p35, which is present in teleost p35 but absent in mammalian and avian p35, and is spatially nearby the conserved cysteine residue located at A-helix of p35 to form a disulfide bond when the 14aa peptide located at loop 1 of grouper p35 was aligned with human corresponding exon 4, instead of exon 5.	Disulfides	269-278	interleukin 12A	Homo sapiens	135-138
24176819-5	2014	The structural model of grouper IL-12 heterodimer revealed NC(141)F three amino acid patch of grouper p35, which is present in teleost p35 but absent in mammalian and avian p35, and is spatially nearby the conserved cysteine residue located at A-helix of p35 to form a disulfide bond when the 14aa peptide located at loop 1 of grouper p35 was aligned with human corresponding exon 4, instead of exon 5.	Disulfides	269-278	interleukin 12A	Homo sapiens	135-138
24176819-5	2014	The structural model of grouper IL-12 heterodimer revealed NC(141)F three amino acid patch of grouper p35, which is present in teleost p35 but absent in mammalian and avian p35, and is spatially nearby the conserved cysteine residue located at A-helix of p35 to form a disulfide bond when the 14aa peptide located at loop 1 of grouper p35 was aligned with human corresponding exon 4, instead of exon 5.	Disulfides	269-278	interleukin 12A	Homo sapiens	135-138
23968404-3	2014	STh is a 19-amino acid peptide containing three disulfide bonds that stimulates fluid secretion in the bowel by binding to the receptor domain of intestinal guanylyl cyclase C (GC-C).	Disulfides	48-57	saitohin	Homo sapiens	0-3
23968404-5	2014	Here, we present a strategy for recombinant expression of STh that relies on the use of the prosequence of human uroguanylin to support proper folding and disulfide bond formation.	Disulfides	155-164	saitohin	Homo sapiens	58-61
23968404-5	2014	Here, we present a strategy for recombinant expression of STh that relies on the use of the prosequence of human uroguanylin to support proper folding and disulfide bond formation.	Disulfides	155-164	guanylate cyclase activator 2B	Homo sapiens	113-124
24253198-8	2014	Nevertheless, both NRX1 and NRX2 have disulfide reduction capacities, although NRX1 alone can be reduced by the thioredoxin reductase NTRA.	Disulfides	38-47	DC1 domain-containing protein	Arabidopsis thaliana	19-23
23867277-0	2013	An inhibitory antibody blocks the first step in the dithiol/disulfide relay mechanism of the enzyme QSOX1.	Disulfides	60-69	quiescin sulfhydryl oxidase 1	Homo sapiens	100-105
23867277-1	2013	Quiescin sulfhydryl oxidase 1 (QSOX1) is a catalyst of disulfide bond formation that undergoes regulated secretion from fibroblasts and is over-produced in adenocarcinomas and other cancers.	Disulfides	55-64	quiescin sulfhydryl oxidase 1	Homo sapiens	0-29
23867277-1	2013	Quiescin sulfhydryl oxidase 1 (QSOX1) is a catalyst of disulfide bond formation that undergoes regulated secretion from fibroblasts and is over-produced in adenocarcinomas and other cancers.	Disulfides	55-64	quiescin sulfhydryl oxidase 1	Homo sapiens	31-36
24022479-7	2013	Indeed, using three different variants of Ero1alpha, we find that expression of either wild-type or an Ero1alpha variant lacking regulatory disulfides can rescue mutant proinsulin-G(B23)V, in parallel with its ability to provide an oxidizing environment in the ER lumen, whereas beneficial effects were less apparent for a redox-inactive form of Ero1.	Disulfides	140-150	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	103-112
23897465-0	2013	Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond.	Disulfides	144-153	carbonic anhydrase 2	Homo sapiens	97-118
23081913-2	2013	Relaxin-2 (RLX-2), a heteromeric polypeptide consisting of an A-chain (24 amino acids) and a B-chain (29 amino acids) linked together by two inter-chain disulfide bonds, is the main circulating RLX hormone in human.	Disulfides	153-162	relaxin 2	Homo sapiens	0-9
23081913-2	2013	Relaxin-2 (RLX-2), a heteromeric polypeptide consisting of an A-chain (24 amino acids) and a B-chain (29 amino acids) linked together by two inter-chain disulfide bonds, is the main circulating RLX hormone in human.	Disulfides	153-162	relaxin 2	Homo sapiens	11-16
23896616-7	2013	In addition to similar secondary and tertiary structure, NACI might possess similar types of protein conformational fluctuations as reported in BPTI, such as Cys14-Cys38 disulfide bond isomerization, based on line broadening of resonances from residues which are mainly confined to a region around the Cys14-Cys38 disulfide bond.	Disulfides	170-179	spleen trypsin inhibitor I	Bos taurus	144-148
23896616-7	2013	In addition to similar secondary and tertiary structure, NACI might possess similar types of protein conformational fluctuations as reported in BPTI, such as Cys14-Cys38 disulfide bond isomerization, based on line broadening of resonances from residues which are mainly confined to a region around the Cys14-Cys38 disulfide bond.	Disulfides	314-323	spleen trypsin inhibitor I	Bos taurus	144-148
23764395-0	2013	Cleavage of the interchain disulfide bonds in rituximab increases its affinity for FcgammaRIIIA.	Disulfides	27-36	Fc gamma receptor IIIa	Homo sapiens	83-95
23571001-3	2013	Recently, we reported a comb-shaped vector (DPD) consisting of a dextran backbone and disulfide-linked cationic poly((2-dimethyl amino)ethyl methacrylate) side chains for efficient gene delivery.	Disulfides	86-95	dihydropyrimidine dehydrogenase	Homo sapiens	44-47
23868209-1	2013	Oxytocin (OT) is a cyclic nonapeptide containing one internal disulfide bond between its Cys(1) and Cys(6) residues.	Disulfides	62-71	oxytocin/neurophysin I prepropeptide	Homo sapiens	0-8
23868209-1	2013	Oxytocin (OT) is a cyclic nonapeptide containing one internal disulfide bond between its Cys(1) and Cys(6) residues.	Disulfides	62-71	oxytocin/neurophysin I prepropeptide	Homo sapiens	10-12
23776472-6	2013	We show that CLEC2L-encoded CTLRs are expressed as non-glycosylated, disulfide-linked homodimers at the cell surface.	Disulfides	69-78	C-type lectin domain family 2 member L	Homo sapiens	13-19
23464809-7	2013	In the present study we have mapped the disulfide bonds in mouse HJV/RGMc using a proteomics strategy combining sequential MS steps composed of ETD (electron transfer dissociation) and CID (collision-induced dissociation), in which ETD induces cleavage of disulfide linkages, and CID establishes disulfide bond assignments between liberated peptides.	Disulfides	40-49	hemojuvelin BMP co-receptor	Mus musculus	65-68
23464809-7	2013	In the present study we have mapped the disulfide bonds in mouse HJV/RGMc using a proteomics strategy combining sequential MS steps composed of ETD (electron transfer dissociation) and CID (collision-induced dissociation), in which ETD induces cleavage of disulfide linkages, and CID establishes disulfide bond assignments between liberated peptides.	Disulfides	40-49	hemojuvelin BMP co-receptor	Mus musculus	69-73
23464809-7	2013	In the present study we have mapped the disulfide bonds in mouse HJV/RGMc using a proteomics strategy combining sequential MS steps composed of ETD (electron transfer dissociation) and CID (collision-induced dissociation), in which ETD induces cleavage of disulfide linkages, and CID establishes disulfide bond assignments between liberated peptides.	Disulfides	256-265	hemojuvelin BMP co-receptor	Mus musculus	65-68
23464809-7	2013	In the present study we have mapped the disulfide bonds in mouse HJV/RGMc using a proteomics strategy combining sequential MS steps composed of ETD (electron transfer dissociation) and CID (collision-induced dissociation), in which ETD induces cleavage of disulfide linkages, and CID establishes disulfide bond assignments between liberated peptides.	Disulfides	256-265	hemojuvelin BMP co-receptor	Mus musculus	65-68
23592195-2	2013	The reported major disulfide (S-S) linkages in mature human G-CSF are C36 -C42 and C64 -C74 , leaving C17 as a free cysteine, which could potentially result in S-S scrambling.	Disulfides	19-28	CDK5 regulatory subunit associated protein 1	Homo sapiens	75-78
23418776-3	2013	Whereas the eag/PAS domain is necessary for disulfide bridging, plus the cysteine residues introduced at positions 3 and 542 of the HERG sequence, the presence of the proximal domain seems to be dispensable.	Disulfides	44-53	potassium voltage-gated channel subfamily H member 1	Homo sapiens	12-15
23375721-7	2013	A disulfide bond between the two domains of PSP94 (C(37)A-C(73)A) was also important for this interaction.	Disulfides	2-11	microseminoprotein beta	Homo sapiens	44-49
23276819-0	2013	The long-term immunosuppressive effects of disulfide-linked HLA-G dimer in mice with collagen-induced arthritis.	Disulfides	43-52	major histocompatibility complex, class I, G	Homo sapiens	60-65
23276819-3	2013	HLA-G forms disulfide-linked dimers by natural oxidation, and the dimer associates with LILRB1/B2 much more strongly than the monomer.	Disulfides	12-21	major histocompatibility complex, class I, G	Homo sapiens	0-5
23506863-6	2013	The latter are the light or catalytic subunits of the heteromeric amino acid transporters (HATs), which are associated by a disulfide bridge with the heavy subunits 4F2hc or rBAT.	Disulfides	124-133	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	174-178
23362256-9	2013	These results support a role for the cysteine residues in intermolecular disulfide bond formation with the DUOX maturation factor DUOXA1.	Disulfides	73-82	dual oxidase maturation factor 1	Homo sapiens	130-136
23283984-2	2013	The oxidoreductase Mia40 is a central component of the pathway responsible for the transfer of disulfide bonds to intermembrane space precursor proteins, causing their oxidative folding.	Disulfides	95-104	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	19-24
23283984-6	2013	Tim22 forms a disulfide-bonded intermediate with Mia40 upon import into mitochondria.	Disulfides	14-23	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	49-54
23283984-8	2013	We propose that Mia40 not only is responsible for disulfide bond formation, but also assists the Tim22 protein in its integration into the inner membrane of mitochondria.	Disulfides	50-59	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	16-21
23186364-0	2013	Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40.	Disulfides	0-9	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	92-97
23122227-1	2013	XK is a putative transporter of unknown function that is ubiquitously expressed and linked through disulfide bonds to Kell protein, an endothelin-3 (ET-3)-converting enzyme.	Disulfides	99-108	Kell blood group	Mus musculus	118-130
23340690-1	2013	The purpose of this work is to characterize the interactions of two disulfide-constrained cyclic tetrapeptides [c(Ac-Cys-Pro-Phe-Cys-NH(2)), SS1; c(Ac-Cys-Pro-Gly-Cys-NH(2)), SS2] with Cu(2+) ions in order to facilitate the design of cyclic peptides as sensors for metal ions.	Disulfides	68-77	butyrophilin like 2	Homo sapiens	175-178
23302472-3	2013	BoHV-4 Open Reading Frame 8 (ORF8) codifies for glycoprotein B (gB) that shows a heterodimeric structure, composed of two subunits and covalently linked by disulfide bonds and responsible for host cell adhesion through binding to heparan sulfates associated with cellular proteoglycans.	Disulfides	156-165	glycoprotein B	Bovine gammaherpesvirus 4	48-62
25206370-2	2013	Based on peptide aptamers, the present study inserted ABAD-DP into the disulfide bond of human thioredoxin (TRX) using molecular cloning technique to construct a fusion gene that can express the TRX1-ABAD-DP-TRX2 aptamer.	Disulfides	71-80	hydroxysteroid 17-beta dehydrogenase 10	Homo sapiens	54-58
23537207-2	2013	Disulfide-rich peptides that antagonize the growth factor receptors neuropilin-1 and neuropilin-2 were developed using bacterial display libraries.	Disulfides	0-9	neuropilin 2	Homo sapiens	85-97
23451353-4	2013	From circular dichroism and non-reducing SDS-PAGE, we characterized the conformational properties of rLcn11 as a typical lipocalin scaffold with the conserved disulfide bridge.	Disulfides	159-168	progestagen associated endometrial protein	Rattus norvegicus	101-107
22966073-1	2013	Cysteines are thought integral to conformational epitopes of islet antigen-2 (IA-2) autoantibodies (IA-2A), possibly through disulfide bond formation.	Disulfides	125-134	protein tyrosine phosphatase receptor type N	Homo sapiens	61-76
22966073-1	2013	Cysteines are thought integral to conformational epitopes of islet antigen-2 (IA-2) autoantibodies (IA-2A), possibly through disulfide bond formation.	Disulfides	125-134	protein tyrosine phosphatase receptor type N	Homo sapiens	78-82
23135388-3	2013	Another distinctive feature of most mammalian Ngb is their ability to form an internal disulfide bridge that increases ligand affinity.	Disulfides	87-96	neuroglobin	Homo sapiens	46-49
22996269-7	2013	Mutational analysis revealed a novel, homozygous missense mutation in the C3 gene (c. C4554G, p. Cys1518Trp), substituting a highly conserved amino acid in the C345C domain of C3 and interrupting one of its disulfide bonds.	Disulfides	207-216	complement C3	Homo sapiens	74-76
22996269-7	2013	Mutational analysis revealed a novel, homozygous missense mutation in the C3 gene (c. C4554G, p. Cys1518Trp), substituting a highly conserved amino acid in the C345C domain of C3 and interrupting one of its disulfide bonds.	Disulfides	207-216	complement C3	Homo sapiens	160-162
23174349-0	2013	New analogs of the CART peptide with anorexigenic potency: the importance of individual disulfide bridges.	Disulfides	88-97	CART prepropeptide	Rattus norvegicus	19-23
23174349-4	2013	Two biologically active forms, CART(55-102) and CART(61-102), with equal biological activity, contain three disulfide bridges.	Disulfides	108-117	CART prepropeptide	Rattus norvegicus	31-35
23174349-4	2013	Two biologically active forms, CART(55-102) and CART(61-102), with equal biological activity, contain three disulfide bridges.	Disulfides	108-117	CART prepropeptide	Rattus norvegicus	48-52
23019327-4	2012	The CHCH domain proteins are traditionally imported and trapped in the IMS by using a disulfide relay system mediated by Mia40 and Erv1.	Disulfides	86-95	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	121-126
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Disulfides	14-23	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	49-54
23019327-8	2012	The transient disulfide-bonded intermediate with Mia40 is formed preferentially between the second cysteine in helix 1, Cys(193), and the active site cysteine in Mia40, Cys(55).	Disulfides	14-23	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	162-167
22801553-4	2012	The recently determined crystal structure of the N-terminal domain of Gpc-1 has revealed that all the evolutionary conserved cysteines form intramolecular disulfide bonds.	Disulfides	155-164	glypican 1	Homo sapiens	70-75
22872415-1	2012	Replacing the catalytic serine in trypsin with threonine (S195T variant) leads to a nearly complete loss of catalytic activity, which can be partially restored by eliminating the C42-C58 disulfide bond.	Disulfides	187-196	CDK5 regulatory subunit associated protein 1	Homo sapiens	179-182
22974285-2	2012	Disulfide-cross-linked polypeptide nanogel with near-infrared fluorescence property (NIRF nanogel) was first synthesized, then the anticancer drug doxorubicin was encapsulated into polypeptide core of the NIRF nanogel to prepare a drug carrier with near-infrared fluorescence (NIRF prodrug).	Disulfides	0-9	ubiquitin-like, containing PHD and RING finger domains 2	Mus musculus	85-89
22974285-2	2012	Disulfide-cross-linked polypeptide nanogel with near-infrared fluorescence property (NIRF nanogel) was first synthesized, then the anticancer drug doxorubicin was encapsulated into polypeptide core of the NIRF nanogel to prepare a drug carrier with near-infrared fluorescence (NIRF prodrug).	Disulfides	0-9	ubiquitin-like, containing PHD and RING finger domains 2	Mus musculus	205-209
22974285-2	2012	Disulfide-cross-linked polypeptide nanogel with near-infrared fluorescence property (NIRF nanogel) was first synthesized, then the anticancer drug doxorubicin was encapsulated into polypeptide core of the NIRF nanogel to prepare a drug carrier with near-infrared fluorescence (NIRF prodrug).	Disulfides	0-9	ubiquitin-like, containing PHD and RING finger domains 2	Mus musculus	205-209
22910915-2	2012	This process requires disulfide bond transfer from oxidized Mia40 to a substrate protein.	Disulfides	22-31	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	60-65
22988105-2	2012	Human meprin beta is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.	Disulfides	31-40	meprin A subunit beta	Homo sapiens	6-17
22743349-8	2012	Incubation of CaMKP with H(2)O(2) led to formation of disulfide bond between Cys-359 and Cys-259/Cys-315, resulting in the inactivation of the enzyme.	Disulfides	54-63	protein phosphatase, Mg2+/Mn2+ dependent 1F	Homo sapiens	14-19
22648419-4	2012	GSSG oxidizes copper-coordinating cysteines of Atox1 with the formation of an intramolecular disulfide.	Disulfides	93-102	antioxidant 1 copper chaperone	Homo sapiens	47-52
22648419-5	2012	GSH alone is sufficient to reduce the disulfide, restoring the ability of Atox1 to bind copper; glutaredoxin 1 facilitates this reaction when GSH is low.	Disulfides	38-47	antioxidant 1 copper chaperone	Homo sapiens	74-79
22429838-0	2012	Synthetic disulfide-bridged cyclic peptides mimic the anti-angiogenic actions of chondromodulin-I.	Disulfides	10-19	chondromodulin	Homo sapiens	81-97
22429838-4	2012	Site-directed mutagenesis experiments revealed that the cyclic structure formed by the disulfide bridge between Cys(83) and Cys(99) in human ChM-I is indispensable for its anti-angiogenic function.	Disulfides	87-96	chondromodulin	Homo sapiens	141-146
22577145-4	2012	Several antioxidant proteins were identified that exhibited changes in disulfide bonding unique to Htt-103Q expressing cells.	Disulfides	71-80	huntingtin	Rattus norvegicus	99-102
22451649-1	2012	In heterologous and endogenous expression systems, we studied the role of ERp44 and its complex partner endoplasmic reticulum (ER) oxidase 1-alpha (Ero1-Lalpha) in mechanisms regulating disulfide bond formation for serotonin transporter (SERT), an oligomeric glycoprotein.	Disulfides	186-195	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	148-159
22451649-13	2012	Based on these collective findings, we hypothesize that ERp44 together with Ero1-Lalpha plays an important role in disulfide formation of SERT, which may be a prerequisite step for the assembly of SERT molecules in oligomeric form.	Disulfides	115-124	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	76-87
22220984-6	2012	A specific protein-protein interaction between either isoform and protein disulfide isomerase (PDI) facilitates the propagation of disulfides from Ero1 via PDI to nascent polypeptides, and inbuilt oxidative shutdown mechanisms in Ero1alpha and Ero1beta prevent excessive oxidation of PDI.	Disulfides	131-141	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	230-239
22220984-7	2012	CRITICAL ISSUES: Besides disulfide-bond generation, Ero1alpha also regulates calcium release from the ER and the secretion of disulfide-linked oligomers through its reversible association with the chaperone ERp44.	Disulfides	25-34	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	52-61
22406264-0	2012	Protein disulfide isomerase-mediated disulfide bonds regulate the gelatinolytic activity and secretion of matrix metalloproteinase-9.	Disulfides	8-17	matrix metallopeptidase 9	Homo sapiens	106-132
22406264-6	2012	Mass spectrometric analysis of post-translational modification in MMP-9 confirmed six disulfide bonds in the catalytic domain and one disulfide bond in the hemopexin domain of MMP-9.	Disulfides	86-95	matrix metallopeptidase 9	Homo sapiens	66-71
22406264-6	2012	Mass spectrometric analysis of post-translational modification in MMP-9 confirmed six disulfide bonds in the catalytic domain and one disulfide bond in the hemopexin domain of MMP-9.	Disulfides	134-143	matrix metallopeptidase 9	Homo sapiens	66-71
22406264-7	2012	Establishment of cells that overexpressed wild-type and mutant forms of MMP-9 revealed that "cysteine-switch" and disulfide bonds within the catalytic domain are necessary for the secretion and intracellular trafficking of MMP-9.	Disulfides	114-123	matrix metallopeptidase 9	Homo sapiens	72-77
22406264-7	2012	Establishment of cells that overexpressed wild-type and mutant forms of MMP-9 revealed that "cysteine-switch" and disulfide bonds within the catalytic domain are necessary for the secretion and intracellular trafficking of MMP-9.	Disulfides	114-123	matrix metallopeptidase 9	Homo sapiens	223-228
22401853-6	2012	PDI is a converging hub for pathways of disulfide bond introduction into ER-processed proteins, via hydrogen peroxide-generating mechanisms involving the oxidase Ero1alpha, as well as hydrogen peroxide-consuming reactions involving peroxiredoxin IV and the novel peroxidases Gpx7/8.	Disulfides	40-49	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	162-171
22408268-5	2012	To explore this further, the in vitro and in vivo activity, PK, and target cell activation of T-DM1 and the disulfide-linked T-SPP-DM1 were examined.	Disulfides	108-117	DM1 protein kinase	Homo sapiens	131-134
22411627-3	2012	Using complementary approaches, we provide evidence here that endogenous SHP-2 can dimerize through the formation of disulfide bonds that may also involve the catalytic cysteine.	Disulfides	117-126	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	73-78
22351761-9	2012	The crystal structure of N-glycosylated human glypican-1 core protein at 2.5 A, the first crystal structure of a vertebrate glypican, reveals the complete disulfide bond arrangement of the conserved Cys residues, and it also extends the structural knowledge of glypicans for one alpha-helix and two long loops.	Disulfides	155-164	glypican 1	Homo sapiens	46-56
22342029-7	2012	Steady state anisotropy results showed successfully the break-down of dimer to monomer form of beta-lg within 50 C temperature range and augmentation in anisotropy up on further thermal stress reflected the reorganization of tryptophan residues into more restricted and rigid micro-environment as well as irreversible disulfide-linked dimer formation.	Disulfides	318-327	beta-lactoglobulin	Bos taurus	95-102
22234497-12	2012	We hypothesize that initial decreases in disulfide formation rates could allow adiponectin subunits to associate before becoming locked in fully oxidized conformations incapable of further oligomerization.	Disulfides	41-50	adiponectin, C1Q and collagen domain containing	Rattus norvegicus	79-90
22234497-13	2012	These data demonstrate that zinc stimulates oligomerization of HMW adiponectin and possibly other disulfide-dependent protein assembly processes.	Disulfides	98-107	adiponectin, C1Q and collagen domain containing	Rattus norvegicus	67-78
22278231-9	2012	Thus, only one disulfide from each of the three predicted domains, C429-C552 (DI), C503-C508 (DII), and C607-C644 (DIII), is essential for the assembly of the E2(661) CD81-binding site.	Disulfides	15-24	CD81 molecule	Homo sapiens	167-171
21850520-0	2012	SNAP-25 contains non-acylated thiol pairs that can form intrachain disulfide bonds: possible sites for redox modulation of neurotransmission.	Disulfides	67-76	synaptosome associated protein 25	Rattus norvegicus	0-7
21850520-1	2012	Intrachain disulfide bond formation among the cysteine thiols of SNAP-25, a component of the SNARE protein complex required for neurotransmitter release, has been hypothesized to link oxidative stress and inhibition of synaptic transmission.	Disulfides	11-20	synaptosome associated protein 25	Rattus norvegicus	65-72
21850520-4	2012	The results show for the first time that a substantial fraction of soluble and, to a lesser extent, particulate SNAP-25 contain non-acylated PAO-binding thiol pairs and that these thiols in soluble SNAP-25 in particular have a high propensity toward disulfide bond formation.	Disulfides	250-259	synaptosome associated protein 25	Rattus norvegicus	198-205
21850520-5	2012	Indeed, disulfide bonds were detected in a small fraction of soluble SNAP-25 even under conditions designed to prevent or greatly limit protein thiol oxidation during experimental procedures.	Disulfides	8-17	synaptosome associated protein 25	Rattus norvegicus	69-76
22250012-9	2012	The differential dependence on KCNE1 can be correlated with the physical proximity between these positions and KCNE1 as shown by disulfide cross-linking studies: V141C forms disulfide bonds with cysteine-substituted KCNE1 residues, whereas S140C does not.	Disulfides	129-138	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	31-36
22250012-9	2012	The differential dependence on KCNE1 can be correlated with the physical proximity between these positions and KCNE1 as shown by disulfide cross-linking studies: V141C forms disulfide bonds with cysteine-substituted KCNE1 residues, whereas S140C does not.	Disulfides	129-138	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	111-116
22250012-9	2012	The differential dependence on KCNE1 can be correlated with the physical proximity between these positions and KCNE1 as shown by disulfide cross-linking studies: V141C forms disulfide bonds with cysteine-substituted KCNE1 residues, whereas S140C does not.	Disulfides	129-138	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	111-116
22250012-9	2012	The differential dependence on KCNE1 can be correlated with the physical proximity between these positions and KCNE1 as shown by disulfide cross-linking studies: V141C forms disulfide bonds with cysteine-substituted KCNE1 residues, whereas S140C does not.	Disulfides	174-183	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	31-36
22250012-9	2012	The differential dependence on KCNE1 can be correlated with the physical proximity between these positions and KCNE1 as shown by disulfide cross-linking studies: V141C forms disulfide bonds with cysteine-substituted KCNE1 residues, whereas S140C does not.	Disulfides	174-183	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	111-116
22250012-9	2012	The differential dependence on KCNE1 can be correlated with the physical proximity between these positions and KCNE1 as shown by disulfide cross-linking studies: V141C forms disulfide bonds with cysteine-substituted KCNE1 residues, whereas S140C does not.	Disulfides	174-183	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	111-116
22286025-4	2012	A single free cysteine thiol group in TTR possesses the ability to form mixed disulfides potentially related to diseases such as TTR amyloidosis and Alzheimer"s disease (AD).	Disulfides	78-88	transthyretin	Homo sapiens	38-41
22286025-4	2012	A single free cysteine thiol group in TTR possesses the ability to form mixed disulfides potentially related to diseases such as TTR amyloidosis and Alzheimer"s disease (AD).	Disulfides	78-88	transthyretin	Homo sapiens	129-132
22210900-3	2012	According to this view, under oxidizing conditions occurring during the night the two AGP small subunits (APS1) are covalently linked via an intermolecular disulfide bridge that inactivates the protein, whereas under reducing conditions occurring during the day NADP-thioredoxin reductase C (NTRC)-dependent reductive monomerization of APS1 activates the enzyme.	Disulfides	156-165	ATP sulfurylase 1	Arabidopsis thaliana	106-110
22210900-6	2012	We also characterized aps1 plants expressing a redox-insensitive, mutated APS1 (APS1mut) form in which the highly conserved Cys81 residue involved in the formation of the intermolecular disulfide bridge has been replaced by serine.	Disulfides	186-195	ATP sulfurylase 1	Arabidopsis thaliana	22-26
22210900-6	2012	We also characterized aps1 plants expressing a redox-insensitive, mutated APS1 (APS1mut) form in which the highly conserved Cys81 residue involved in the formation of the intermolecular disulfide bridge has been replaced by serine.	Disulfides	186-195	ATP sulfurylase 1	Arabidopsis thaliana	74-78
22878205-0	2012	Interdomain disulfide bridge in the rice granule bound starch synthase I catalytic domain as elucidated by X-ray structure analysis.	Disulfides	12-21	soluble starch synthase 1, chloroplastic/amyloplastic	Oryza sativa Japonica Group	55-72
22645657-4	2012	The Cys(183)-Cys(232) disulfide bond in mouse CD132 is susceptible to reduction by enzymes such as thioredoxin (TRX), gamma interferon-inducible lysosomal thiolreductase and protein disulfide isomerase, which are commonly secreted during immune activation.	Disulfides	22-31	thioredoxin 1	Mus musculus	99-110
22645657-4	2012	The Cys(183)-Cys(232) disulfide bond in mouse CD132 is susceptible to reduction by enzymes such as thioredoxin (TRX), gamma interferon-inducible lysosomal thiolreductase and protein disulfide isomerase, which are commonly secreted during immune activation.	Disulfides	22-31	thioredoxin 1	Mus musculus	112-115
23284645-0	2012	Disulfide bonds within the C2 domain of RAGE play key roles in its dimerization and biogenesis.	Disulfides	0-9	advanced glycosylation end-product specific receptor	Homo sapiens	40-44
23284645-7	2012	CONCLUSION: Disulfide bond-mediated RAGE dimerization in the ER is the critical step of RAGE biogenesis.	Disulfides	12-21	advanced glycosylation end-product specific receptor	Homo sapiens	36-40
23284645-7	2012	CONCLUSION: Disulfide bond-mediated RAGE dimerization in the ER is the critical step of RAGE biogenesis.	Disulfides	12-21	advanced glycosylation end-product specific receptor	Homo sapiens	88-92
23284645-8	2012	Without formation of intermolecular disulfide bonds in the C2 region, RAGE fails to reach cell surface.	Disulfides	36-45	advanced glycosylation end-product specific receptor	Homo sapiens	70-74
23284645-9	2012	SIGNIFICANCE: This is the first report of RAGE intermolecular disulfide bond.	Disulfides	62-71	advanced glycosylation end-product specific receptor	Homo sapiens	42-46
23185254-2	2012	The CRES protein possesses four highly conserved cysteine residues which govern the overall conformation of the cystatins through the formation of two disulfide bonds.	Disulfides	151-160	cystatin 8 (cystatin-related epididymal spermatogenic)	Mus musculus	4-8
22911720-1	2012	Human quiescin-sulfhydryl oxidase 1 isoform b (HsQSOX1b) is a highly efficient, multiple-domain enzyme that directly inserts disulfide bonds into client protein.	Disulfides	125-134	quiescin sulfhydryl oxidase 1	Homo sapiens	6-35
22911720-7	2012	This study will help address the roles of different HsQSOX1b domains in de novo disulfide formation and encourage the engineering of more efficient QSOX variants for the in vitro folding of disulfide-containing proteins.	Disulfides	80-89	quiescin sulfhydryl oxidase 1	Homo sapiens	54-58
22080626-10	2011	Cys coordination is unlikely because all Cys residues in PHM are engaged in disulfide cross-links.	Disulfides	76-85	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	57-60
22050912-9	2011	These results suggest that the HMP is a disulfide-linked protein complex involving mtMGST1, ANT, CypD and function as a MPT pore in PON-induced swelling, in which the Ca(2+) released by PON might play an important role in the complex formation.	Disulfides	40-49	inner membrane mitochondrial protein	Homo sapiens	31-34
21994946-5	2011	Unlike other mammalian typical 2-Cys peroxiredoxins, we show that human PrxIV forms a stable decameric structure even in its disulfide-bonded state.	Disulfides	125-134	peroxiredoxin 4	Homo sapiens	72-77
22045566-6	2011	We identified specific hydrophobic/aromatic residues required for hepcidin-ferroportin binding and obtained evidence in vitro that a thiol-disulfide interaction between ferroportin C326 and the hepcidin disulfide cage may stabilize binding.	Disulfides	139-148	hepcidin antimicrobial peptide	Mus musculus	194-202
22045566-6	2011	We identified specific hydrophobic/aromatic residues required for hepcidin-ferroportin binding and obtained evidence in vitro that a thiol-disulfide interaction between ferroportin C326 and the hepcidin disulfide cage may stabilize binding.	Disulfides	203-212	hepcidin antimicrobial peptide	Mus musculus	194-202
21989104-1	2011	Quiescin sulfhydryl oxidase 1 (QSOX1) oxidizes sulfhydryl groups to form disulfide bonds in proteins.	Disulfides	73-82	quiescin sulfhydryl oxidase 1	Homo sapiens	0-29
21989104-1	2011	Quiescin sulfhydryl oxidase 1 (QSOX1) oxidizes sulfhydryl groups to form disulfide bonds in proteins.	Disulfides	73-82	quiescin sulfhydryl oxidase 1	Homo sapiens	31-36
21987804-4	2011	Treatment with diamide, a thiol-oxidizing agent, induced formation of disulfide bonds between R91C residues in adjacent Orai1 subunits and rapidly blocked STIM1-operated Ca(2+) current.	Disulfides	70-79	ORAI calcium release-activated calcium modulator 1	Homo sapiens	120-125
21939639-7	2011	We designated the cysteine-rich peptide "trissin" (it means for triple S-S bonds) and characterized the structure of intrachain disulfide bonds formation in a synthetic trissin peptide.	Disulfides	128-137	Drosomycin	Drosophila melanogaster	18-39
21844191-2	2011	Although it is known that functional reelin protein exists as multimer formed by interchain disulfide bond(s) as well as through non-covalent interactions, the chemical nature of the multimer assembly has been elusive.	Disulfides	92-101	reelin	Homo sapiens	37-43
21844191-4	2011	C2101A mutant reelin failed to assemble into disulfide-bonded multimers, whereas it still exhibited non-covalently associated high molecular weight oligomeric states in solution.	Disulfides	45-54	reelin	Homo sapiens	14-20
21865594-7	2011	In this study we detail the import and folding pathway of Ccs1 and characterize its interaction with the oxidoreductase of the mitochondrial disulfide relay Mia40.	Disulfides	141-150	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	157-162
21865594-9	2011	On interaction with Mia40, these cysteines form a structural disulfide bond that stabilizes the overall fold of domain I.	Disulfides	61-70	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	20-25
21636124-5	2011	Two bisazide cross-linkers that contain a disulfide bond, termed PEG8 (poly(ethylene glycol)) and PEG(16), were employed to stabilize the multilayer films, and used to tune the degradation and cargo release behavior of the capsules in simulated cytoplasmic conditions.	Disulfides	42-51	IGF2 antisense RNA	Homo sapiens	65-69
21873995-3	2011	Here our systematic evaluation of transient receptor potential (TRP) cation channels using reactive disulfides with different redox potentials reveals the capability of TRPA1 to sense O(2).	Disulfides	100-110	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	169-174
21755988-0	2011	Heme-dependent activation of neuronal nitric oxide synthase by cytosol is due to an Hsp70-dependent, thioredoxin-mediated thiol-disulfide interchange in the heme/substrate binding cleft.	Disulfides	128-137	heat shock protein family A (Hsp70) member 4	Homo sapiens	84-89
21675794-0	2011	Extracellular disulfide bonds support scavenger receptor class B type I-mediated cholesterol transport.	Disulfides	14-23	scavenger receptor class B member 1	Homo sapiens	38-71
21675794-3	2011	Using sulfhydryl labeling strategies, we report the novel finding that all six cysteine (Cys) residues in the extracellular domain of SR-BI are involved in disulfide bond formation that is intramolecular by nature.	Disulfides	156-165	scavenger receptor class B member 1	Homo sapiens	134-139
21675794-4	2011	We hypothesized that an SR-BI conformation stabilized by extracellular disulfide bonds is a prerequisite for SR-BI-mediated cholesterol transport.	Disulfides	71-80	scavenger receptor class B member 1	Homo sapiens	24-29
21675794-4	2011	We hypothesized that an SR-BI conformation stabilized by extracellular disulfide bonds is a prerequisite for SR-BI-mediated cholesterol transport.	Disulfides	71-80	scavenger receptor class B member 1	Homo sapiens	109-114
21675794-9	2011	Taken together, the intramolecular disulfide bonds in the extracellular domain of SR-BI appear to maintain the receptor in a conformation integral to its cholesterol transport functions.	Disulfides	35-44	scavenger receptor class B member 1	Homo sapiens	82-87
20849374-3	2011	Pathways that form disulfide bonds have now been unraveled in the bacterial periplasm (disulfide bond protein A [DsbA], DsbB, DsbC, DsbG, and DsbD), the endoplasmic reticulum (protein disulfide isomerase and Ero1), and the mitochondrial intermembrane space (Mia40 and Erv1).	Disulfides	19-28	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	258-263
21410328-1	2011	The insulin superfamily is composed of a diverse group of proteins that share a common structural design whose most notable feature is a set of disulfide bonds.	Disulfides	144-153	insulin	Xenopus tropicalis	4-11
21398518-0	2011	Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI).	Disulfides	39-48	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	75-84
21398518-5	2011	ERO1alpha associated preferentially with reduced PDI, explaining the stepwise disulfide shuttle mechanism, first from ERO1alpha to PDI and then from oxidized PDI to an unfolded polypeptide bound to its hydrophobic pocket.	Disulfides	78-87	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	0-9
21398518-5	2011	ERO1alpha associated preferentially with reduced PDI, explaining the stepwise disulfide shuttle mechanism, first from ERO1alpha to PDI and then from oxidized PDI to an unfolded polypeptide bound to its hydrophobic pocket.	Disulfides	78-87	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	118-127
21315357-5	2011	RESULTS: Homozygosity for a mutation in LCAT resulted in the exchange of cysteine to tyrosine at position 337, disrupting the second disulfide bond in LCAT.	Disulfides	133-142	lecithin-cholesterol acyltransferase	Homo sapiens	40-44
21315357-5	2011	RESULTS: Homozygosity for a mutation in LCAT resulted in the exchange of cysteine to tyrosine at position 337, disrupting the second disulfide bond in LCAT.	Disulfides	133-142	lecithin-cholesterol acyltransferase	Homo sapiens	151-155
21544205-3	2011	Here we studied the organization of the amino terminal domain (ATD) of the rat GluN1/GluN2A and GluN1/GluN2B NMDA receptors by cysteine-directed, disulfide bond-mediated cross-linking.	Disulfides	146-155	glutamate ionotropic receptor NMDA type subunit 2B	Rattus norvegicus	102-108
21544205-4	2011	We found that GluN1 ATDs and GluN2 ATDs spontaneously formed disulfide bond-mediated dimers after introducing cysteines into the L1 interface of GluN2A or GluN2B ATD.	Disulfides	61-70	glutamate ionotropic receptor NMDA type subunit 2B	Rattus norvegicus	155-161
21383180-5	2011	ERp57 disulfide linked to the class I-specific chaperone tapasin and CRT were the minimal PLC components required for MHC class I association and peptide loading.	Disulfides	6-15	Calreticulin	Drosophila melanogaster	69-72
21261298-5	2011	Here we present disulfide cross-linking experiments with DOR constructs with cysteines substituted at the extracellular ends of TM4 or TM5 that confirm the formation of DOR complexes involving these helices.	Disulfides	16-25	opioid receptor, delta 1	Mus musculus	57-60
21261298-5	2011	Here we present disulfide cross-linking experiments with DOR constructs with cysteines substituted at the extracellular ends of TM4 or TM5 that confirm the formation of DOR complexes involving these helices.	Disulfides	16-25	opioid receptor, delta 1	Mus musculus	169-172
21353161-7	2011	ZER was directly inserted between the disulfide bond in the HSP27 dimer and modified normal HSP27 dimerization.	Disulfides	38-47	heat shock protein 1	Mus musculus	60-65
21353161-7	2011	ZER was directly inserted between the disulfide bond in the HSP27 dimer and modified normal HSP27 dimerization.	Disulfides	38-47	heat shock protein 1	Mus musculus	92-97
21152909-5	2011	We investigate the interactions between the KCNE1 loop (positions 36-47) and KCNQ1 S1-S2 linker (positions 140-148) by means of disulfide trapping and voltage clamp techniques.	Disulfides	128-137	potassium voltage-gated channel subfamily E regulatory subunit 1	Homo sapiens	44-49
20138936-1	2011	Disulfide crosslinked polyplex micelles with RGD peptides were formed through ion complexation of thiolated c(RGDfK)-poly(ethylene glycol)-block-poly(L-lysine) (c(RGDfK)-PEG-P(Lys-SH)) and plasmid DNA encoding sFlt-1 and tested for their therapeutic effect in BxPC3 pancreatic adenocarcinoma tumor bearing mice.	Disulfides	0-9	FMS-like tyrosine kinase 1	Mus musculus	210-216
20486767-4	2011	AuIB is a unique member of the alpha-conotoxin family because the nonnative "ribbon" disulfide isomer exhibits enhanced activity at the nAChR in rat parasympathetic neurons compared with the native "globular" isomer.	Disulfides	85-94	cholinergic receptor nicotinic beta 1 subunit	Rattus norvegicus	136-141
21297336-1	2011	Protein disulfide isomerase (PDI) is a multifunctional protein that catalyzes disulfide bond formation and assists protein folding, as well as being a structural subunit of microsomal triglyceride transfer protein (MTP) and prolyl 4-hydroxylase (P4HD), and an estrogen and thyroid hormone-binding protein.	Disulfides	8-17	microsomal triglyceride transfer protein	Homo sapiens	215-218
20723574-3	2010	PLA(2), EcTx-I was 13,861.72 molecular weight as estimated by MALDI-TOF (15 kD by SDS-PAGE), and consisted of 121 amino acid residues cross-linked by seven disulfide bonds.	Disulfides	156-165	phospholipase A2 group IIA	Homo sapiens	0-6
21314614-3	2010	Potential GAPDH inhibitors were screened in silico, and three compounds with high affinity to the NAD-binding site and theoretically capable of forming a disulfide bond with amino acid residue Cys149 were found among cysteine and glutathione derivatives.	Disulfides	154-163	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	10-15
21314614-5	2010	As a result of experimental screening, we selected two compounds that inhibit GAPDH by forming disulfide bonds with the Cys149 residue in the enzyme active site.	Disulfides	95-104	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	78-83
21079601-3	2010	Here, we report a cell death pathway involving protein disulfide isomerase (PDI), a protein chaperone that catalyzes isomerization, reduction and oxidation of disulfides.	Disulfides	159-169	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	47-74
21079601-3	2010	Here, we report a cell death pathway involving protein disulfide isomerase (PDI), a protein chaperone that catalyzes isomerization, reduction and oxidation of disulfides.	Disulfides	159-169	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	76-79
20831872-7	2010	Further analysis of binding and functional data suggests that the ASIP C-terminal loop (a six-amino-acid segment closed by the final disulfide bond) is essential for high-affinity MC1R binding and inverse agonism.	Disulfides	133-142	agouti signaling protein	Homo sapiens	66-70
20136511-4	2010	Tim40/Mia40 transfers disulfide bonds to newly imported IMS proteins by dithiol/disulfide exchange reactions involving mixed disulfide intermediates.	Disulfides	22-31	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	6-11
20136511-4	2010	Tim40/Mia40 transfers disulfide bonds to newly imported IMS proteins by dithiol/disulfide exchange reactions involving mixed disulfide intermediates.	Disulfides	80-89	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	6-11
20136511-4	2010	Tim40/Mia40 transfers disulfide bonds to newly imported IMS proteins by dithiol/disulfide exchange reactions involving mixed disulfide intermediates.	Disulfides	80-89	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	6-11
20136511-6	2010	After disulfide transfer from Tim40/Mia40 to substrate proteins, Tim40/Mia40 is reoxidized again by Erv1, which is then oxidized by electron transfer to either cytochrome c or molecular oxygen.	Disulfides	6-15	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	36-41
20136511-6	2010	After disulfide transfer from Tim40/Mia40 to substrate proteins, Tim40/Mia40 is reoxidized again by Erv1, which is then oxidized by electron transfer to either cytochrome c or molecular oxygen.	Disulfides	6-15	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	71-76
20880831-7	2010	Hydrodynamic data demonstrated that BST2 formed a stable tetramer under reducing conditions and a dimer when oxidized to form disulfide bonds.	Disulfides	126-135	bone marrow stromal cell antigen 2	Homo sapiens	36-40
20880831-9	2010	Our data raise the possibility that BST2 may function as a tetramer at some stage, such as during trafficking, and strongly support a model in which the primary functional state of BST2 is a parallel disulfide-bound coiled coil that displays flexibility toward its N terminus.	Disulfides	200-209	bone marrow stromal cell antigen 2	Homo sapiens	36-40
20880831-9	2010	Our data raise the possibility that BST2 may function as a tetramer at some stage, such as during trafficking, and strongly support a model in which the primary functional state of BST2 is a parallel disulfide-bound coiled coil that displays flexibility toward its N terminus.	Disulfides	200-209	bone marrow stromal cell antigen 2	Homo sapiens	181-185
20392170-3	2010	SIRT1 formed mixed disulfides with GSNO-Sepharose, and mass spectrometry identified several cysteines that are modified by GSNO, including Cys-67 which was S-glutathiolated.	Disulfides	19-29	sirtuin 1	Homo sapiens	0-5
20621156-12	2010	GSH should combine with the hAS3MT after the methylation to reduce the disulfide bond formed during the catalytic cycle in the hAS3MT to resume the active form of the enzyme.	Disulfides	71-80	arsenite methyltransferase	Homo sapiens	28-34
20506311-2	2010	Previously, we reported that overexpression of protein disulfide isomerase (PDI), which catalyzes disulfide bond exchanges and assists in protein folding of newly synthesized proteins, enhanced q(Ab) of rCHO cells by about 27% (Mohan et al., 2007, Biotechnol Bioeng 98:611-615) .	Disulfides	55-64	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	76-79
20506311-3	2010	Since the rate limiting step in disulfide bond formation is found to be the regeneration of oxidized PDI, the oxidation state of PDI, as well as the amount of PDI, might be important.	Disulfides	32-41	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	101-104
20506311-3	2010	Since the rate limiting step in disulfide bond formation is found to be the regeneration of oxidized PDI, the oxidation state of PDI, as well as the amount of PDI, might be important.	Disulfides	32-41	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	129-132
20506311-3	2010	Since the rate limiting step in disulfide bond formation is found to be the regeneration of oxidized PDI, the oxidation state of PDI, as well as the amount of PDI, might be important.	Disulfides	32-41	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	129-132
20506311-4	2010	Endoplasmic reticulum oxidoreductase (ERO1L) maintains PDI in an oxidized state so that disulfide bond formation occurs.	Disulfides	88-97	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	55-58
20506311-5	2010	Here, PDI and its helper protein, ERO1L were overexpressed in rCHO cells producing an Ab in an attempt to ease the bottleneck in disulfide bond formation, and hence, Ab folding and secretion.	Disulfides	129-138	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	6-9
20518739-2	2010	In these analogues disulfide bridge Cys3 - Cys11 present in native inhibitor was replaced by different-sized carbonyl bridges formed by the amino groups of the side chain of Lys, Orn, Dab or Dap located in positions 3 and/or 11.	Disulfides	19-28	death associated protein	Bos taurus	191-194
20540164-6	2010	Various non-native intra-A (A20 with A6, A7, or A11), intra-B (between B7 and B19), and inter-A-B disulfide bonds were observed in the intermediates with two disulfide bonds.	Disulfides	158-167	immunoglobulin kappa variable 1-27	Homo sapiens	28-31
20566629-3	2010	GRX1 is a thiol oxidoreductase that catalyzes the reversible reduction of GSH-mixed disulfides to their respective sulfhydryls (deglutathionylation).	Disulfides	84-94	thioredoxin reductase 1	Homo sapiens	16-30
21567549-4	2010	In accord with the aminolysis results on CTAs, hydrazine aminolyzed RAFT polymers in an impressively short time and, more importantly, it significantly suppressed the formation of disulfides as comfirmed with GPC.	Disulfides	180-190	glycophorin C (Gerbich blood group)	Homo sapiens	209-212
20704729-8	2010	Finally, we show that protein dimerisation via disulfide bond is involved in the interaction of alphaS1-casein with membranes.	Disulfides	47-56	casein alpha s1	Rattus norvegicus	96-110
20643048-0	2010	Probing the role of the internal disulfide bond in regulating conformational dynamics in neuroglobin.	Disulfides	33-42	neuroglobin	Homo sapiens	89-100
20498052-5	2010	We also show that NOX2 activity significantly compromises the phagosome"s ability to reduce disulfides.	Disulfides	92-102	cytochrome b-245 beta chain	Homo sapiens	18-22
20152940-8	2010	SDS-PAGE and Western blotting analysis suggested that disulfide cross-linked and non-productively folded lysozyme was responsible for the anti-chaperone activity of PDI-P5.	Disulfides	54-63	protein disulfide isomerase family A member 6	Homo sapiens	165-171
20345372-5	2010	On the basis of ELISA binding studies with novel fragment antibodies against ADAM17 we propose that isomerization of the disulfide bonds in ADAM17, and the subsequent conformational changes, form the basis for the modulation of ADAM17 activity.	Disulfides	121-130	ADAM metallopeptidase domain 17	Homo sapiens	77-83
20345372-5	2010	On the basis of ELISA binding studies with novel fragment antibodies against ADAM17 we propose that isomerization of the disulfide bonds in ADAM17, and the subsequent conformational changes, form the basis for the modulation of ADAM17 activity.	Disulfides	121-130	ADAM metallopeptidase domain 17	Homo sapiens	140-146
20345372-5	2010	On the basis of ELISA binding studies with novel fragment antibodies against ADAM17 we propose that isomerization of the disulfide bonds in ADAM17, and the subsequent conformational changes, form the basis for the modulation of ADAM17 activity.	Disulfides	121-130	ADAM metallopeptidase domain 17	Homo sapiens	140-146
20504280-7	2010	This activation is accompanied by changes in disulfide bonds in the ADAM17 ectodomain.	Disulfides	45-54	ADAM metallopeptidase domain 17	Homo sapiens	68-74
20399176-2	2010	The 2.77 A crystal structure of the BST-2/tetherin extracellular core presented here reveals a parallel 90 A long disulfide-linked coiled-coil domain, while the complete extracellular domain forms an extended 170 A long rod-like structure based on small-angle X-ray scattering data.	Disulfides	114-123	bone marrow stromal cell antigen 2	Homo sapiens	36-41
20399176-2	2010	The 2.77 A crystal structure of the BST-2/tetherin extracellular core presented here reveals a parallel 90 A long disulfide-linked coiled-coil domain, while the complete extracellular domain forms an extended 170 A long rod-like structure based on small-angle X-ray scattering data.	Disulfides	114-123	bone marrow stromal cell antigen 2	Homo sapiens	42-50
20067811-2	2010	However, previous versions of cyclic NGR used a liable disulfide bridge between cysteine residues that may be problematic for liposome targeting due to disulfide bond formation between adjacent peptides on the liposomal surface.	Disulfides	55-64	reticulon 4 receptor	Homo sapiens	37-40
20067811-2	2010	However, previous versions of cyclic NGR used a liable disulfide bridge between cysteine residues that may be problematic for liposome targeting due to disulfide bond formation between adjacent peptides on the liposomal surface.	Disulfides	152-161	reticulon 4 receptor	Homo sapiens	37-40
20211621-1	2010	Quiescin sulfhydryl oxidase (QSOX) catalyzes formation of disulfide bonds between cysteine residues in substrate proteins.	Disulfides	58-67	quiescin sulfhydryl oxidase 1	Homo sapiens	0-27
20211621-1	2010	Quiescin sulfhydryl oxidase (QSOX) catalyzes formation of disulfide bonds between cysteine residues in substrate proteins.	Disulfides	58-67	quiescin sulfhydryl oxidase 1	Homo sapiens	29-33
20211621-5	2010	In QSOX evolution, a further concatenation to a member of the protein disulfide isomerase family resulted in an enzyme capable of both disulfide formation and efficient transfer to substrate proteins.	Disulfides	70-79	quiescin sulfhydryl oxidase 1	Homo sapiens	3-7
20018245-4	2010	In our study we show that when co-expressed with the signal-sequence-less disulfide bond isomerase (Delta ssDsbC) in the dual expression vector, pETDUET-1, both BLG A and BLG B can be reproducibly produced in a soluble form.	Disulfides	74-83	beta-lactoglobulin	Bos taurus	161-164
20018245-4	2010	In our study we show that when co-expressed with the signal-sequence-less disulfide bond isomerase (Delta ssDsbC) in the dual expression vector, pETDUET-1, both BLG A and BLG B can be reproducibly produced in a soluble form.	Disulfides	74-83	beta-lactoglobulin	Bos taurus	171-174
19857203-6	2009	Reversible conjugation by a disulfide bond of a carrier peptide bearing a penetration accelerating sequence to PRL, facilitated the cellular uptake of this peptide and significantly inhibited phosphorylation of tau by PKN1 at the PKN1-specific phosphorylation site in vivo.	Disulfides	28-37	protein kinase N1	Homo sapiens	218-222
19857203-6	2009	Reversible conjugation by a disulfide bond of a carrier peptide bearing a penetration accelerating sequence to PRL, facilitated the cellular uptake of this peptide and significantly inhibited phosphorylation of tau by PKN1 at the PKN1-specific phosphorylation site in vivo.	Disulfides	28-37	protein kinase N1	Homo sapiens	230-234
19835883-7	2009	The IL-17A is a disulfide-linked homodimer that is similar in structure to IL-17F, adopting a cystine-knot fold.	Disulfides	16-25	interleukin 17A	Homo sapiens	4-10
19919085-3	2009	Another important specific feature of human Ngb is the presence of two cysteine residues (Cys46 and Cys55), which are known to form an intramolecular disulfide bridge.	Disulfides	150-159	neuroglobin	Homo sapiens	44-47
19766098-1	2009	Human Ero1-Lalpha catalyzes the formation of disulfide bond and hence plays an essential role in protein folding.	Disulfides	45-54	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	6-17
19782948-5	2009	Interestingly, specific anti-CD146 mAb AA98, which bound a conformational epitope depending on C452-C499 disulfide bond, could abrogate NF kappaB activation and tumor angiogenesis, whereas another anti-CD146 mAb AA1 recognizing a linear epitope containing aa50-54 did not have such effects.	Disulfides	105-114	melanoma cell adhesion molecule	Homo sapiens	29-34
19703468-1	2009	The Mia40-Erv1 disulfide relay system is of high importance for mitochondrial biogenesis.	Disulfides	15-24	Mia40p	Saccharomyces cerevisiae S288C	4-9
19703468-6	2009	Among these, three represent novel proteins, which we named Cmc2 to 4 (for Cx(9)C motif-containing protein) and which we demonstrated to be dependent for import on the Mia40-Erv1 disulfide relay.	Disulfides	179-188	Mia40p	Saccharomyces cerevisiae S288C	168-173
20641539-9	2004	Three isoforms of ET (ET-1, ET-2, and ET-3) exist in mammalian tissues, each of which has 21 amino acids with two disulfide bonds.	Disulfides	114-123	endothelin 3	Homo sapiens	38-42
20103838-0	2009	Identification and assignment of three disulfide bonds in mammalian leukocyte cell-derived chemotaxin 2 by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.	Disulfides	39-48	leukocyte cell derived chemotaxin 2	Homo sapiens	68-103
20103838-4	2009	The analysis showed that murine and human LECT2 have three intramolecular disulfide bonds (Cys25-Cys60; Cys36-Cys41; Cys99-Cys142) and no free cysteine residues.	Disulfides	74-83	leukocyte cell derived chemotaxin 2	Homo sapiens	42-47
19564543-6	2009	Thioredoxin activity was assessed by the insulin disulfide reduction assay.	Disulfides	49-58	uncharacterized protein	Drosophila melanogaster	0-11
19489627-3	2009	This structure is stabilized by two disulfide bonds and can be altered by heating above 65 degrees C. beta-LG is also one of the major allergens in milk.	Disulfides	36-45	beta-lactoglobulin	Bos taurus	102-109
19366703-4	2009	However, the mature form of VEGF-D (VEGF-D(DeltaNDeltaC)) is predominantly a non-covalent dimer even though the cysteine residues (Cys-44 and Cys-53) forming the intersubunit disulfide bridges in the other members of the VEGF family are also conserved in VEGF-D.	Disulfides	175-184	vascular endothelial growth factor D	Homo sapiens	28-34
19366703-4	2009	However, the mature form of VEGF-D (VEGF-D(DeltaNDeltaC)) is predominantly a non-covalent dimer even though the cysteine residues (Cys-44 and Cys-53) forming the intersubunit disulfide bridges in the other members of the VEGF family are also conserved in VEGF-D.	Disulfides	175-184	vascular endothelial growth factor D	Homo sapiens	36-56
19366703-4	2009	However, the mature form of VEGF-D (VEGF-D(DeltaNDeltaC)) is predominantly a non-covalent dimer even though the cysteine residues (Cys-44 and Cys-53) forming the intersubunit disulfide bridges in the other members of the VEGF family are also conserved in VEGF-D.	Disulfides	175-184	vascular endothelial growth factor D	Homo sapiens	36-42
19362581-2	2009	However, compared to other textbook proteins, progress in the study of beta LG has been slow because of obstacles such as a low reversibility from denaturation linked with thiol-disulfide exchange or monomer-dimer equilibrium preventing a detailed NMR analysis.	Disulfides	178-187	beta-lactoglobulin	Bos taurus	71-78
19349280-6	2009	Thiol modification with polyethylene glycol-maleimide showed disulfide bond formation at the active site of TRP32 in cells exposed to As(III).	Disulfides	61-70	thioredoxin like 1	Homo sapiens	108-113
19409522-1	2009	A disulfide relay system (DRS) was recently identified in the yeast mitochondrial intermembrane space (IMS) that consists of two essential components: the sulfhydryl oxidase Erv1 and the redox-regulated import receptor Mia40.	Disulfides	2-11	Mia40p	Saccharomyces cerevisiae S288C	219-224
19254950-6	2009	Consistent with this finding, GPx-1 overexpression decreased global protein disulfide bond formation, which is dependent on mitochondrially produced oxidants.	Disulfides	76-85	glutathione peroxidase 1	Homo sapiens	30-35
19206074-2	2009	To investigate the effect of dimerization of Tat (48-60) analog, [Tat(W): GRKKRRQRRRPWQ-NH(2)], on antimicrobial activity and mechanism of bactericidal action, its dimeric peptides, di-Tat(W)-C and di-Tat(W)-K, were synthesized by a disulfide bond linkage and lysine linkage of monomeric Tat(W), respectively.	Disulfides	233-242	Tat	Human immunodeficiency virus 1	45-48
19258317-0	2009	Formation of two intramolecular disulfide bonds is necessary for ApoA-I-dependent cholesterol efflux mediated by ABCA1.	Disulfides	32-41	ATP binding cassette subfamily A member 1	Homo sapiens	113-118
19258317-2	2009	ABCA1 contains disulfide bond(s) between its N- and C-terminal halves, but it remains unclear whether disulfide bond formation is important for the functions of ABCA1 and which cysteines are involved in disulfide bond formation.	Disulfides	15-24	ATP binding cassette subfamily A member 1	Homo sapiens	0-5
19852088-6	2009	In this Account, we describe our studies of AlkB, ABH2, and ABH3, including our development of a general strategy to trap homogeneous protein-DNA complexes through active-site disulfide cross-linking.	Disulfides	176-185	alkB homolog 1, histone H2A dioxygenase	Homo sapiens	44-48
19336037-6	2009	We propose that Vanabin2 forms a possible electron transfer cascade from the electron donor, NADPH, via glutathione reductase, glutathione, and Vanabin2 to the acceptor, and vanadium ions conjugated through thiol-disulfide exchange reactions.	Disulfides	213-222	2,4-dienoyl-CoA reductase 1	Homo sapiens	93-98
19243140-3	2009	Here, we generated the first anti-PTPN22 20-mer antisense oligonucleotides (ASOs) and tethered them to PNTs through a cleavable disulfide bond.	Disulfides	128-137	protein tyrosine phosphatase non-receptor type 22	Homo sapiens	34-40
19136576-4	2009	Digestion of purified VEGF(165) with NE generated a partially degraded disulfide-linked fragment of VEGF.	Disulfides	71-80	vascular endothelial growth factor A	Mus musculus	22-26
19136576-4	2009	Digestion of purified VEGF(165) with NE generated a partially degraded disulfide-linked fragment of VEGF.	Disulfides	71-80	vascular endothelial growth factor A	Mus musculus	100-104
19037098-4	2009	Like the human counterparts, each Tim9 and Tim10 subunit contains a central loop flanked by disulfide bonds that separate two extended N- and C-terminal tentacle-like helices.	Disulfides	92-101	translocase of inner mitochondrial membrane 10	Homo sapiens	43-48
19182799-3	2009	MIA40 has a 66-residue folded domain made of an alpha-helical hairpin core stabilized by two structural disulfides and a rigid N-terminal lid, with a characteristic CPC motif that can donate its disulfide bond to substrates.	Disulfides	104-114	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
19182799-3	2009	MIA40 has a 66-residue folded domain made of an alpha-helical hairpin core stabilized by two structural disulfides and a rigid N-terminal lid, with a characteristic CPC motif that can donate its disulfide bond to substrates.	Disulfides	104-113	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	0-5
19038268-2	2009	We used a truncated form of the Agouti-related protein (AgRP), a 4-kDa cystine-knot peptide with four disulfide bonds and four solvent-exposed loops, as a scaffold for engineering peptides that bound to alpha(v)beta(3) integrins with high affinity and specificity.	Disulfides	102-111	agouti related neuropeptide	Homo sapiens	32-54
19038268-2	2009	We used a truncated form of the Agouti-related protein (AgRP), a 4-kDa cystine-knot peptide with four disulfide bonds and four solvent-exposed loops, as a scaffold for engineering peptides that bound to alpha(v)beta(3) integrins with high affinity and specificity.	Disulfides	102-111	agouti related neuropeptide	Homo sapiens	56-60
19011240-2	2009	This import pathway employs a disulfide relay system whose key components are the redox-regulated import receptor Mia40 and the thiol oxidase Erv1.	Disulfides	30-39	Mia40p	Saccharomyces cerevisiae S288C	114-119
19011240-7	2009	It is required for the interaction of Mia40 with Erv1 in a disulfide intermediate and forms a redox-sensitive disulfide bond with the first cysteine residue.	Disulfides	59-68	Mia40p	Saccharomyces cerevisiae S288C	38-43
19011240-7	2009	It is required for the interaction of Mia40 with Erv1 in a disulfide intermediate and forms a redox-sensitive disulfide bond with the first cysteine residue.	Disulfides	110-119	Mia40p	Saccharomyces cerevisiae S288C	38-43
19011240-12	2009	In particular, the disulfide bond formed by the third and sixth cysteine residues apparently supports a conformation crucial for the function of Mia40.	Disulfides	19-28	Mia40p	Saccharomyces cerevisiae S288C	145-150
19001419-4	2009	Oxygen consumption assays with purified recombinant Ero1-Lalpha revealed that it utilizes oxygen as a terminal electron acceptor producing one disulfide bond and one molecule of hydrogen peroxide per dioxygen molecule consumed.	Disulfides	143-152	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	52-63
19109142-3	2009	Although the stalk-swapped CD8beta was expressed on the cell surface as a disulfide-bonded heterodimer at equivalent levels of expression to an endogenous CD8beta molecule, it failed to restore selection of CD8(+) class I MHC-restricted T cells and it altered the response of peripheral T cells.	Disulfides	74-83	CD8 antigen, beta chain 1	Mus musculus	27-34
18937031-3	2008	In addition, we successfully expressed bovine pancreatic trypsin inhibitor (BPTI), which contains three pairs of disulfide bonds, as the soluble form.	Disulfides	113-122	spleen trypsin inhibitor I	Bos taurus	76-80
18815280-5	2008	Our results show that of the three intramolecular disulfides present in RBP (4-160, 70-174, and 120-129) the smallest loop (120-129) was most critical for RBP to fold.	Disulfides	50-60	retinol binding protein 4	Homo sapiens	72-75
18815280-5	2008	Our results show that of the three intramolecular disulfides present in RBP (4-160, 70-174, and 120-129) the smallest loop (120-129) was most critical for RBP to fold.	Disulfides	50-60	retinol binding protein 4	Homo sapiens	155-158
18815280-6	2008	Its absence caused RBP to aggregate into an intermolecular disulfide-linked structure.	Disulfides	59-68	retinol binding protein 4	Homo sapiens	19-22
18815280-7	2008	After acquisition of the small loop, formation of one of the two big disulfides (4-160 or 70-174) was sufficient for RBP to acquire a folded state.	Disulfides	69-79	retinol binding protein 4	Homo sapiens	117-120
18815280-10	2008	RBP dissociated from this complex coincident with the formation of one of the two big disulfide loops, whereas RBP mutant lacking both the large disulfides showed persistent association.	Disulfides	86-95	retinol binding protein 4	Homo sapiens	0-3
18815280-10	2008	RBP dissociated from this complex coincident with the formation of one of the two big disulfide loops, whereas RBP mutant lacking both the large disulfides showed persistent association.	Disulfides	145-155	retinol binding protein 4	Homo sapiens	111-114
18976165-1	2008	BACKGROUND: Cysteine (Cys) residues pair to form disulfide bonds that are important in maintaining structure and function of the thyrotropin receptor (TSHR).	Disulfides	49-58	thyroid stimulating hormone receptor	Homo sapiens	129-149
18976165-1	2008	BACKGROUND: Cysteine (Cys) residues pair to form disulfide bonds that are important in maintaining structure and function of the thyrotropin receptor (TSHR).	Disulfides	49-58	thyroid stimulating hormone receptor	Homo sapiens	151-155
18824154-3	2008	In this study, the strategy of cloning, overexpression, and purification of ECRG2 for obtaining a properly folded ECRG2 with accurately formed disulfide bonds was established.	Disulfides	143-152	serine peptidase inhibitor Kazal type 7	Homo sapiens	76-81
18824154-3	2008	In this study, the strategy of cloning, overexpression, and purification of ECRG2 for obtaining a properly folded ECRG2 with accurately formed disulfide bonds was established.	Disulfides	143-152	serine peptidase inhibitor Kazal type 7	Homo sapiens	114-119
18544680-2	2008	Platelets contain 40 times as much TGF-beta1 as other cells and secrete it as an inactive (latent) form in complex with latency-associated peptide (LAP), which is disulfide bonded via Cys33 to latent TGF-beta binding protein 1 (LTBP-1).	Disulfides	163-172	centromere protein J	Mus musculus	120-146
18544680-2	2008	Platelets contain 40 times as much TGF-beta1 as other cells and secrete it as an inactive (latent) form in complex with latency-associated peptide (LAP), which is disulfide bonded via Cys33 to latent TGF-beta binding protein 1 (LTBP-1).	Disulfides	163-172	centromere protein J	Mus musculus	148-151
18544680-2	2008	Platelets contain 40 times as much TGF-beta1 as other cells and secrete it as an inactive (latent) form in complex with latency-associated peptide (LAP), which is disulfide bonded via Cys33 to latent TGF-beta binding protein 1 (LTBP-1).	Disulfides	163-172	latent transforming growth factor beta binding protein 1	Mus musculus	193-226
18816062-4	2008	We therefore engineered a more stable version of cAb-HuL22 by adding a disulfide bridge between the two beta-sheets in the hydrophobic core of the protein.	Disulfides	71-80	neural proliferation, differentiation and control 1	Homo sapiens	49-52
18577522-2	2008	Previous work has demonstrated that the basic functional unit for the ethylene receptor, ETR1, is a disulfide-linked homodimer.	Disulfides	100-109	Signal transduction histidine kinase, hybrid-type, ethylene sensor	Arabidopsis thaliana	89-93
18577522-6	2008	When transgenically expressed in yeast, ETR1 and ERS2 can form disulfide-linked heterodimers.	Disulfides	63-72	enoyl-[acyl-carrier-protein] reductase	Saccharomyces cerevisiae S288C	40-44
18650385-1	2008	ERp57 is an oxidoreductase that, in conjunction with calnexin and calreticulin, assists disulfide bond formation in folding glycoproteins.	Disulfides	88-97	thioredoxin reductase 1	Homo sapiens	12-26
18465840-0	2008	Disulfide-linked bovine beta-lactoglobulin dimers fold slowly, navigating a glassy folding landscape.	Disulfides	0-9	beta-lactoglobulin	Bos taurus	24-42
18465840-2	2008	In the mutant, a free thiol group of wild-type beta-lg at Cys121 was removed and two beta-lg molecules were linked by a disulfide bridge through Cys34 created at the dimer"s interface.	Disulfides	120-129	beta-lactoglobulin	Bos taurus	85-92
18393506-8	2008	The majority of myosin heavy chain (MHC) was demonstrated to be cross-linked through intermolecular disulfide bonding 1 h after initiation of oxidation.	Disulfides	100-109	major histocompatibility complex, class I, C	Homo sapiens	16-34
18393506-8	2008	The majority of myosin heavy chain (MHC) was demonstrated to be cross-linked through intermolecular disulfide bonding 1 h after initiation of oxidation.	Disulfides	100-109	major histocompatibility complex, class I, C	Homo sapiens	36-39
18326041-7	2008	It has been suggested that amyloidogenicity may be conferred to wild-type TTR (the form deposited in SSA) by chemical modification of the lone cysteine residue (Cys(10)) through mixed disulfide bonds.	Disulfides	184-193	transthyretin	Homo sapiens	74-77
18380788-1	2008	Secretory leukocyte peptidase inhibitor (SLPI) belongs to the whey acidic protein four-disulfide core family of proteins, and has antimicrobial and antiprotease functions.	Disulfides	87-96	secretory leukocyte peptidase inhibitor	Mus musculus	0-39
18380788-1	2008	Secretory leukocyte peptidase inhibitor (SLPI) belongs to the whey acidic protein four-disulfide core family of proteins, and has antimicrobial and antiprotease functions.	Disulfides	87-96	secretory leukocyte peptidase inhibitor	Mus musculus	41-45
17926344-4	2008	While disulfide linkage patterns of four Cys residues in the N-terminal halves of the ZP domains of ZP3 and ZP4 were identical to those previously reported for mice, rats, humans, and fish, the disulfide linkage patterns of six Cys residues in the C-terminal half of the ZP domain in ZP4, as well as eight Cys residues in the C-terminal region of the ZP domain and a following region unique to ZP3, were different from those previously reported.	Disulfides	6-15	zona pellucida glycoprotein 3	Mus musculus	100-103
18413607-4	2008	Here, we show that the p66(Shc) N terminus forms a redox module responsible for apoptosis initiation, and that this module can be activated through reversible tetramerization by forming two disulfide bonds.	Disulfides	190-199	SHC adaptor protein 1	Homo sapiens	27-30
18179776-3	2008	Recently, a disulfide relay system in the IMS has been identified which consists of two essential components, the sulfhydryl oxidase Erv1 and the redox-regulated import receptor Mia40/Tim40.	Disulfides	12-21	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	178-183
18179776-5	2008	In order to enable Mia40 to perform the oxidation of substrate proteins, the sulfhydryl oxidase Erv1 mediates the oxidation of Mia40 in a disulfide transfer reaction.	Disulfides	138-147	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	19-24
18179776-5	2008	In order to enable Mia40 to perform the oxidation of substrate proteins, the sulfhydryl oxidase Erv1 mediates the oxidation of Mia40 in a disulfide transfer reaction.	Disulfides	138-147	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	127-132
18096690-12	2008	As expected, GH and GH-GH, but not G120R, induced GHR disulfide linkage, as assessed by anti-GHR blotting of cell extracts resolved by SDS-PAGE under nonreducing conditions.	Disulfides	54-63	growth hormone receptor	Homo sapiens	50-53
18093982-6	2008	Redox properties of the disulfides of human Cox17, here investigated, strongly support the current hypothesis that the unstructured fully reduced Cox17 protein is present in the cytoplasm and enters the intermembrane space (IMS) where is then oxidized by Mia40 to Cox17(2S-S), thus becoming partially structured and trapped into the IMS.	Disulfides	24-34	cytochrome c oxidase copper chaperone COX17	Homo sapiens	44-49
18093982-6	2008	Redox properties of the disulfides of human Cox17, here investigated, strongly support the current hypothesis that the unstructured fully reduced Cox17 protein is present in the cytoplasm and enters the intermembrane space (IMS) where is then oxidized by Mia40 to Cox17(2S-S), thus becoming partially structured and trapped into the IMS.	Disulfides	24-34	cytochrome c oxidase copper chaperone COX17	Homo sapiens	146-151
18093982-6	2008	Redox properties of the disulfides of human Cox17, here investigated, strongly support the current hypothesis that the unstructured fully reduced Cox17 protein is present in the cytoplasm and enters the intermembrane space (IMS) where is then oxidized by Mia40 to Cox17(2S-S), thus becoming partially structured and trapped into the IMS.	Disulfides	24-34	cytochrome c oxidase copper chaperone COX17	Homo sapiens	146-151
18322014-1	2008	Thioredoxin-interacting protein (Txnip) inhibits thioredoxin NADPH-dependent reduction of protein disulfides.	Disulfides	98-108	thioredoxin 1	Mus musculus	49-60
18258178-8	2008	The intersubunit disulfide bond formation also decreases the rate of stigmatellin induced reduction of ISP in the fully oxidized complex, suggesting that an endogenous electron donor comes from the vicinity of the b position in the cytochrome b.	Disulfides	17-26	mitochondrially encoded cytochrome b	Homo sapiens	232-244
18094169-4	2008	Activation of Mo-MLV Env is controlled by isomerization of its intersubunit disulfide.	Disulfides	76-85	endogenous retrovirus group K member 20	Homo sapiens	21-24
18054043-2	2008	The BPTI analogue termed [14-38](Abu) retains only the disulfide bond between Cys14 and Cys38, while Cys5, Cys30, Cys51, and Cys55 are replaced by isosteric alpha-amino-n-butyric acid residues.	Disulfides	55-64	spleen trypsin inhibitor I	Bos taurus	4-8
18423212-5	2008	The yield of disulfides formed by peroxynitrite anion is quantitated by monitoring the oxidation of NADPH, a cofactor required by the thioredoxin reductase system.	Disulfides	13-23	2,4-dienoyl-CoA reductase 1	Homo sapiens	100-105
17959605-0	2007	Functional characterization of Mia40p, the central component of the disulfide relay system of the mitochondrial intermembrane space.	Disulfides	68-77	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	31-37
17959605-2	2007	We have characterized the redox behavior of Mia40p and reconstituted the disulfide transfer system of Mia40p by using recombinant functional C-terminal fragment of Mia40p, Mia40C, and Erv1p.	Disulfides	73-82	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	102-108
17959605-2	2007	We have characterized the redox behavior of Mia40p and reconstituted the disulfide transfer system of Mia40p by using recombinant functional C-terminal fragment of Mia40p, Mia40C, and Erv1p.	Disulfides	73-82	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	102-108
17959605-3	2007	Oxidized Mia40p contains three intramolecular disulfide bonds.	Disulfides	46-55	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	9-15
17997984-4	2007	Here, we apply direct chemical mapping to determine the complete set of disulfide linkages in ASIP.	Disulfides	72-81	agouti signaling protein	Homo sapiens	94-98
17703232-5	2007	Notably, disulfide-bonded fusion proteins of the THD of mTRAIL and mCD95L with a subdomain of the tenascin-C (TNC) oligomerization domain, which still assembled into trimers, efficiently interacted with their cognate cellular receptors and robustly stimulated CD95 and TRAILR2 signaling after secondary cross-linking.	Disulfides	9-18	tumor necrosis factor (ligand) superfamily, member 10	Mus musculus	56-62
17703232-5	2007	Notably, disulfide-bonded fusion proteins of the THD of mTRAIL and mCD95L with a subdomain of the tenascin-C (TNC) oligomerization domain, which still assembled into trimers, efficiently interacted with their cognate cellular receptors and robustly stimulated CD95 and TRAILR2 signaling after secondary cross-linking.	Disulfides	9-18	tenascin C	Homo sapiens	98-108
17703232-5	2007	Notably, disulfide-bonded fusion proteins of the THD of mTRAIL and mCD95L with a subdomain of the tenascin-C (TNC) oligomerization domain, which still assembled into trimers, efficiently interacted with their cognate cellular receptors and robustly stimulated CD95 and TRAILR2 signaling after secondary cross-linking.	Disulfides	9-18	tenascin C	Homo sapiens	110-113
17541952-1	2007	Whey acidic protein (WAP) is a major whey protein in milk that has structural similarity to the family of serine protease inhibitors with WAP motif domains characterized by a four-disulfide core.	Disulfides	180-189	whey acidic protein	Mus musculus	0-19
17541952-1	2007	Whey acidic protein (WAP) is a major whey protein in milk that has structural similarity to the family of serine protease inhibitors with WAP motif domains characterized by a four-disulfide core.	Disulfides	180-189	whey acidic protein	Mus musculus	21-24
17541952-1	2007	Whey acidic protein (WAP) is a major whey protein in milk that has structural similarity to the family of serine protease inhibitors with WAP motif domains characterized by a four-disulfide core.	Disulfides	180-189	complement component 1, s subcomponent 1	Mus musculus	106-121
17541952-1	2007	Whey acidic protein (WAP) is a major whey protein in milk that has structural similarity to the family of serine protease inhibitors with WAP motif domains characterized by a four-disulfide core.	Disulfides	180-189	whey acidic protein	Mus musculus	138-141
17945253-3	2007	In contrast to the previously characterized CLIC1 protein, which forms a possibly functionally important disulfide-induced dimer under oxidizing conditions, we show that CLIC2 possesses an intramolecular disulfide and that the protein remains monomeric irrespective of redox conditions.	Disulfides	105-114	chloride intracellular channel 1	Homo sapiens	44-49
17962415-2	2007	Here we show that a major subgroup of PMD mutations that map into the extracellular loop region of PLP/DM20 leads to the failure of oligodendrocytes to form the correct intramolecular disulfide bridges.	Disulfides	184-193	proteolipid protein 1	Homo sapiens	99-107
17967948-3	2007	Both factors form a disulfide relay system in which Mia40 functions as a receptor that transiently interacts with incoming polypeptides via disulfide bonds.	Disulfides	20-29	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	52-57
17967948-3	2007	Both factors form a disulfide relay system in which Mia40 functions as a receptor that transiently interacts with incoming polypeptides via disulfide bonds.	Disulfides	140-149	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	52-57
17692543-1	2007	Oxytocin (OT; Cys-Tyr-Ile-Gln-Asn-Cys-Pro-leu-Gly), a posterior pituitary peptide hormone, is characterized by a Cys1-Cys6 disulfide bond in its stable, isolated state.	Disulfides	123-132	oxytocin/neurophysin I prepropeptide	Homo sapiens	0-8
17692543-1	2007	Oxytocin (OT; Cys-Tyr-Ile-Gln-Asn-Cys-Pro-leu-Gly), a posterior pituitary peptide hormone, is characterized by a Cys1-Cys6 disulfide bond in its stable, isolated state.	Disulfides	123-132	oxytocin/neurophysin I prepropeptide	Homo sapiens	10-12
17692543-4	2007	It was found that OT dithiol has a half-life of 1.8h with respect to reformation of OT disulfide at 37 degrees C and pH 6.9 in the presence of the copper chelators, DTPA and neocuproine.	Disulfides	87-96	oxytocin/neurophysin I prepropeptide	Homo sapiens	18-20
17692543-4	2007	It was found that OT dithiol has a half-life of 1.8h with respect to reformation of OT disulfide at 37 degrees C and pH 6.9 in the presence of the copper chelators, DTPA and neocuproine.	Disulfides	87-96	oxytocin/neurophysin I prepropeptide	Homo sapiens	84-86
17331072-0	2007	Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1.	Disulfides	27-36	quiescin sulfhydryl oxidase 1	Homo sapiens	85-90
17503775-7	2007	By analogy to thioredoxin, Rdx proteins can use catalytic cysteine (or Sec) to form transient mixed disulfides with substrate proteins.	Disulfides	100-110	radixin	Homo sapiens	27-30
17303807-2	2007	These mice exhibit a T--&gt;A transversion in the insulin 2 (Ins2) gene at nucleotide position 1903 in exon 3, which leads to the amino acid exchange C95S and loss of the A6-A11 intrachain disulfide bond.	Disulfides	189-198	insulin II	Mus musculus	50-59
17303807-2	2007	These mice exhibit a T--&gt;A transversion in the insulin 2 (Ins2) gene at nucleotide position 1903 in exon 3, which leads to the amino acid exchange C95S and loss of the A6-A11 intrachain disulfide bond.	Disulfides	189-198	insulin II	Mus musculus	61-65
17131045-0	2007	Direct evidence that two cysteines in the dopamine transporter form a disulfide bond.	Disulfides	70-79	solute carrier family 6 member 3	Homo sapiens	42-62
17131045-7	2007	Our results and previous results are consistent with the notion that the disulfide bond between EL2 cysteines is required for DAT biosynthesis and/or its delivery to the cell surface.	Disulfides	73-82	solute carrier family 6 member 3	Homo sapiens	126-129
17261023-12	2007	We also determined that the deposits in all samples contained Cys10 disulfide-linkedhomodimers composed of full-length TTR monomers.	Disulfides	68-77	transthyretin	Homo sapiens	119-122
17098255-7	2007	Furthermore, LC-MS/MS analysis of oxidized DmGPx exposed to a reduced Trx C35S mutant yielded a dead-end intermediate containing a disulfide between Trx C32 and DmGPx C91.	Disulfides	131-140	uncharacterized protein	Drosophila melanogaster	70-73
17098255-7	2007	Furthermore, LC-MS/MS analysis of oxidized DmGPx exposed to a reduced Trx C35S mutant yielded a dead-end intermediate containing a disulfide between Trx C32 and DmGPx C91.	Disulfides	131-140	uncharacterized protein	Drosophila melanogaster	149-152
17098255-8	2007	Thus, the catalytic mechanism of DmGPx, unlike that of selenocysteine (Sec)GPxs, involves formation of an internal disulfide that is pivotal to the interaction with Trx.	Disulfides	115-124	uncharacterized protein	Drosophila melanogaster	165-168
17071656-2	2007	In sharp contrast, two SGLT1 mutants (C255A and C511A) that lack a recently identified disulfide bridge express the pre-steady-state currents in the presence of alphaMG.	Disulfides	87-96	solute carrier family 5 (sodium/glucose cotransporter), member 1, gene 2 L homeolog	Xenopus laevis	23-28
17376729-2	2007	The most common mutation, C282Y, disrupts the disulfide bond necessary for the association of HFE with beta-2-microglobulin and abrogates cell surface HFE expression.	Disulfides	46-55	homeostatic iron regulator	Mus musculus	94-97
17376729-2	2007	The most common mutation, C282Y, disrupts the disulfide bond necessary for the association of HFE with beta-2-microglobulin and abrogates cell surface HFE expression.	Disulfides	46-55	homeostatic iron regulator	Mus musculus	151-154
17136616-5	2007	The disulfide bond locations are conserved among human MBP1, MBP2 and C-type lectins.	Disulfides	4-13	proteoglycan 3, pro eosinophil major basic protein 2	Homo sapiens	61-65
16916795-7	2006	These included the protocadherin-specific disulfide-bonded Cys-X(5)-Cys motif, which showed Ca(2+)-induced chemical shifts, and the RGD motif, which has been suggested to be involved in heterophilic cell adhesion via the active form of beta1 integrin.	Disulfides	42-51	integrin subunit beta 1	Homo sapiens	236-250
16930550-3	2006	Four of the proteins were found to belong to the Kazal protease inhibitor family and were named SPINK8, SPINK10, SPINK11, and SPINK12, whereas one of the proteins, WFDC10, contained the WAP four-disulfide core domain structure.	Disulfides	195-204	serine peptidase inhibitor, Kazal type 8	Mus musculus	96-102
16930550-3	2006	Four of the proteins were found to belong to the Kazal protease inhibitor family and were named SPINK8, SPINK10, SPINK11, and SPINK12, whereas one of the proteins, WFDC10, contained the WAP four-disulfide core domain structure.	Disulfides	195-204	serine peptidase inhibitor, Kazal type 10	Mus musculus	104-111
16893552-5	2006	We have determined by X-ray crystallography the structure of AtErv1, an ERV/ALR enzyme that contains a Cys-X4-Cys shuttle disulfide and oxidizes thioredoxin in vitro, and compared it to ScErv2, which has a Cys-X-Cys shuttle and does not oxidize thioredoxin at an appreciable rate.	Disulfides	122-131	Erv1/Alr family protein	Arabidopsis thaliana	61-67
16893552-6	2006	The AtErv1 shuttle disulfide is in a region of the structure that is disordered and thus apparently mobile and exposed.	Disulfides	19-28	Erv1/Alr family protein	Arabidopsis thaliana	4-10
16893552-9	2006	We found that the AtErv1 shuttle disulfide region could indeed confer thioredoxin oxidase activity on the ScErv2 core.	Disulfides	33-42	Erv1/Alr family protein	Arabidopsis thaliana	18-24
16820415-0	2006	Disulfide bonds determine growth hormone receptor folding, dimerisation and ligand binding.	Disulfides	0-9	growth hormone receptor	Homo sapiens	26-49
16820415-6	2006	Disulfide bond C38-C48 is important for efficient maturation.	Disulfides	0-9	CDK5 regulatory subunit associated protein 2	Homo sapiens	19-22
16497802-1	2006	The prevailing concept is that, in human thyroid tissue in vivo, all cell-surface TSH receptors (TSHR) cleave into disulfide linked A and B subunits.	Disulfides	115-124	thyroid stimulating hormone receptor	Homo sapiens	97-101
16704259-4	2006	With other substituents (CH(3)O, CH(3), H, Cl, and F), both the alpha (CH(2)-S) and the beta (S-CN) bonds could be cleaved as a result of an electrochemical reduction leading to the formation of the corresponding substituted monosulfides, disulfides, and toluenes.	Disulfides	239-249	sorcin	Homo sapiens	88-98
16531413-12	2006	These results support the presence of functionally important disulfide bonds in the motilin receptor ectodomain and demonstrate that the structural determinants for binding and biological activity of peptide and non-peptidyl agonist ligands are distinct, with a broad extracellular perimembranous base contributing to normal motilin binding.	Disulfides	61-70	motilin	Homo sapiens	84-91
16771672-5	2006	A redox pathway (Mia40p and Erv1p) mediates the import of intermembrane space proteins such as the small Tim proteins, Cox17p, and Cox19p, which have disulfide bonds.	Disulfides	150-159	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	17-23
16771672-5	2006	A redox pathway (Mia40p and Erv1p) mediates the import of intermembrane space proteins such as the small Tim proteins, Cox17p, and Cox19p, which have disulfide bonds.	Disulfides	150-159	cytochrome c oxidase copper chaperone COX17	Homo sapiens	119-125
16771672-5	2006	A redox pathway (Mia40p and Erv1p) mediates the import of intermembrane space proteins such as the small Tim proteins, Cox17p, and Cox19p, which have disulfide bonds.	Disulfides	150-159	cytochrome c oxidase assembly factor COX19	Homo sapiens	131-137
16446016-1	2006	The two major membrane-associated proteins of porcine reproductive and respiratory syndrome virus (PRRSV), GP5 and M (encoded by ORF5 and ORF6 genes, respectively), are associated as disulfide-linked heterodimers (GP5/M) in the virus particle.	Disulfides	183-192	glycoprotein 5 (platelet)	Mus musculus	107-110
16446016-1	2006	The two major membrane-associated proteins of porcine reproductive and respiratory syndrome virus (PRRSV), GP5 and M (encoded by ORF5 and ORF6 genes, respectively), are associated as disulfide-linked heterodimers (GP5/M) in the virus particle.	Disulfides	183-192	CWC15 spliceosome associated protein homolog	Homo sapiens	129-133
16446016-1	2006	The two major membrane-associated proteins of porcine reproductive and respiratory syndrome virus (PRRSV), GP5 and M (encoded by ORF5 and ORF6 genes, respectively), are associated as disulfide-linked heterodimers (GP5/M) in the virus particle.	Disulfides	183-192	glycoprotein 5 (platelet)	Mus musculus	214-217
16354652-2	2006	We report that human peptidoglycan recognition proteins 3 and 4 (PGLYRP3 and PGLYRP4) are secreted as 89-115-kDa disulfide-linked homo- and heterodimers and are bactericidal against several pathogenic and nonpathogenic transient, but not normal flora, Gram-positive bacteria.	Disulfides	113-122	peptidoglycan recognition protein 4	Homo sapiens	77-84
16179963-1	2006	In prokaryotes, protein disulfide bond oxidation, reduction and isomerization are catalyzed by members of the thioredoxin superfamily, characterized by the conserved C-X-X-C motif in their active site.	Disulfides	24-33	PSHA_RS00575	Pseudoalteromonas haloplanktis TAC125	110-121
16161151-4	2006	CD47 has multiple sites of glycosylation and a core disulfide bond.	Disulfides	52-61	CD47 molecule	Homo sapiens	0-4
17427151-10	2006	It is thought, that the character of the immunological response evoked by different cytokines of IL-17 family depends on the differences between the spatial structure of their fragments including disulfide bridges and that these differences determine their receptor interactions and biological functions.	Disulfides	196-205	interleukin 17A	Homo sapiens	97-102
16251189-9	2005	Alanine scanning of cysteine residues of Gpx2 revealed that an intramolecular disulfide bond was formed between Cys37 and Cys83 in vivo.	Disulfides	78-87	glutathione peroxidase GPX2	Saccharomyces cerevisiae S288C	41-45
16185709-7	2005	Studies on the in vivo redox state of human MIA40 demonstrated that it contains intramolecular disulfide bonds.	Disulfides	95-104	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	44-49
16143128-10	2005	Mutations that introduced disulfide bonds (keratin 8 G61C or R453C) decreased keratin solubility, particularly after oxidative stress, whereas others decreased keratin 8 phosphorylation (keratin 8 G433S).	Disulfides	26-35	keratin 8	Homo sapiens	43-52
16111437-6	2005	A computational search for proteins matching this target phylogenetic profile singles out a specific protein, known as protein disulfide oxidoreductase, as a potential key player in thermophilic intracellular disulfide-bond formation.	Disulfides	127-136	thioredoxin reductase 1	Homo sapiens	137-151
15989955-3	2005	After passage through the TOM channel, these proteins are covalently trapped by Mia40 via disulfide bridges.	Disulfides	90-99	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	80-85
15989955-6	2005	We propose that Erv1 and Mia40 function as a disulfide relay system that catalyzes the import of proteins into the IMS by an oxidative folding mechanism.	Disulfides	45-54	coiled-coil-helix-coiled-coil-helix domain containing 4	Homo sapiens	25-30
15980188-3	2005	AChE was identified as a mixture of disulfide- and noncovalently linked 88-kD homodimers consisting of 42- to 44-kD polypeptides.	Disulfides	36-45	GDSL esterase/lipase ACHE	Zea mays	0-4
15897295-6	2005	In addition, two MTSES-sensitive residues, on different helices and in close proximity in the prokaryotic structures, can form a disulfide bond in ClC-0.	Disulfides	129-138	Charcot-Leyden crystal galectin	Homo sapiens	147-150
15923321-10	2005	This feature of MsrB1 could result from the lack of the catalytical cysteine (Cys) corresponding to Cys-63 in Escherichia coli MsrB that is involved in the regeneration of Cys-117 through the formation of an intramolecular disulfide bridge followed by thioredoxin reduction.	Disulfides	223-232	methionine sulfoxide reductase B 1	Arabidopsis thaliana	16-21
15934996-1	2005	BACKGROUND: Kell and XK, two distinct red blood cell membrane proteins, are linked by a disulfide bond and form the Kell blood group complex.	Disulfides	88-97	Kell blood group	Mus musculus	116-132
15909993-0	2005	Site-directed disulfide mapping of residues contributing to the Ca2+ and K+ binding pocket of the NCKX2 Na+/Ca2+-K+ exchanger.	Disulfides	14-23	solute carrier family 24 member 2	Homo sapiens	98-103
15789064-2	2005	In contrast to other fragments described to date, K1-5 includes cysteine residues at positions 543, 555 and 560 allowing the formation of the three disulfide bonds lying within K5.	Disulfides	148-157	keratin 15	Homo sapiens	50-54
15713716-7	2005	These results demonstrate that the absence of the disulfide bridge Cys-53 to Cys-165 affects the binding affinity of GH for the GHR and subsequently the potency of GH to activate the Jak2/Stat5 signaling pathway.	Disulfides	50-59	growth hormone receptor	Homo sapiens	128-131
15826078-1	2005	Heat treatment of bovine beta-lactoglobulin B (beta-LG) causes it to partially unfold and aggregate via hydrophobic association and intra- and interprotein disulfide bonds.	Disulfides	156-165	beta-lactoglobulin	Bos taurus	25-45
15826078-1	2005	Heat treatment of bovine beta-lactoglobulin B (beta-LG) causes it to partially unfold and aggregate via hydrophobic association and intra- and interprotein disulfide bonds.	Disulfides	156-165	beta-lactoglobulin	Bos taurus	47-54
15826192-5	2005	Herein, we report a method to tether one fibril formation inhibitor to TTR by disulfide bond formation.	Disulfides	78-87	transthyretin	Homo sapiens	71-74
15761664-1	2005	Purple acid phosphatase (PAP), also known as tartrate-resistant acid phosphatase (TRAP), uteroferrin or type 5 acid phosphatase (Acp5) is synthesized as an N-glycosylated monomeric latent precursor, which can be processed by limited proteolysis to a disulfide-linked two-subunit form with increased enzyme activity.	Disulfides	250-259	acid phosphatase 5, tartrate resistant	Rattus norvegicus	45-80
15761664-1	2005	Purple acid phosphatase (PAP), also known as tartrate-resistant acid phosphatase (TRAP), uteroferrin or type 5 acid phosphatase (Acp5) is synthesized as an N-glycosylated monomeric latent precursor, which can be processed by limited proteolysis to a disulfide-linked two-subunit form with increased enzyme activity.	Disulfides	250-259	acid phosphatase 5, tartrate resistant	Rattus norvegicus	82-86
15761664-1	2005	Purple acid phosphatase (PAP), also known as tartrate-resistant acid phosphatase (TRAP), uteroferrin or type 5 acid phosphatase (Acp5) is synthesized as an N-glycosylated monomeric latent precursor, which can be processed by limited proteolysis to a disulfide-linked two-subunit form with increased enzyme activity.	Disulfides	250-259	acid phosphatase 5, tartrate resistant	Rattus norvegicus	104-127
15761664-1	2005	Purple acid phosphatase (PAP), also known as tartrate-resistant acid phosphatase (TRAP), uteroferrin or type 5 acid phosphatase (Acp5) is synthesized as an N-glycosylated monomeric latent precursor, which can be processed by limited proteolysis to a disulfide-linked two-subunit form with increased enzyme activity.	Disulfides	250-259	acid phosphatase 5, tartrate resistant	Rattus norvegicus	129-133
15736958-1	2005	The engineered disulfide bridge A23C/L203C in human carbonic anhydrase II, inserted from homology modeling of Neisseria gonorrhoeae carbonic anhydrase, significantly stabilizes the native state of the protein.	Disulfides	15-24	carbonic anhydrase 2	Homo sapiens	52-73
15718280-6	2005	The structural data suggest a head-to-tail mode of dimerization, mediated by an intermolecular disulfide bond, that is consistent with the observation of HLA-G dimers on the cell surface.	Disulfides	95-104	major histocompatibility complex, class I, G	Homo sapiens	154-159
15592500-0	2005	Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond formation and VEGF secretion under hypoxia: implication for cancer.	Disulfides	69-78	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	0-12
15385412-3	2005	The present study demonstrates the capacitation-dependent tyrosine-phosphorylation of phospholipid hydroperoxide glutathione peroxidase (PHGPx), the disulfide cross-linked, major structural protein of the sperm mitochondrial capsule.	Disulfides	149-158	glutathione peroxidase 4	Bos taurus	137-142
16399380-7	2005	A cysteine residue in place of the catalytic tyrosine or serine residues found in other GSTs was shown to form a mixed disulfide with glutathione.	Disulfides	119-128	glutathione S-transferase omega 1	Homo sapiens	88-92
16909016-11	2005	Cleavage of the disulfide linkage renders the well-folded WTL mutants vulnerable to metal loss and monomerization such that they may resemble the destabilized and locally misfolded MBR mutant species.	Disulfides	16-25	translocator protein	Homo sapiens	181-184
15610032-7	2004	Approximately 60% of TGFBIp was covalently associated with insoluble components of the extracellular matrix in both human and porcine corneas through a disulfide bridge.	Disulfides	152-161	transforming growth factor beta induced	Homo sapiens	21-27
15345746-8	2004	In signaling experiments, brief pretreatment of GH-responsive human fibrosarcoma cells with anti-GHR(ext-mAb) dramatically inhibited GH-induced Janus kinase 2 and signal transducer and activator of transcription 5 tyrosine phosphorylation and prevented GH-induced GHR disulfide linkage (a reflection of GH-induced conformational changes).	Disulfides	268-277	growth hormone receptor	Homo sapiens	97-100
15345746-11	2004	A Fab fragment of anti-GHR(ext-mAb) inhibited GH-induced GHR disulfide linkage and signaling, as well as phorbol ester-induced GHR proteolysis, in a fashion similar to the intact antibody.	Disulfides	61-70	growth hormone receptor	Homo sapiens	23-26
15345746-11	2004	A Fab fragment of anti-GHR(ext-mAb) inhibited GH-induced GHR disulfide linkage and signaling, as well as phorbol ester-induced GHR proteolysis, in a fashion similar to the intact antibody.	Disulfides	61-70	growth hormone receptor	Homo sapiens	57-60
15345746-11	2004	A Fab fragment of anti-GHR(ext-mAb) inhibited GH-induced GHR disulfide linkage and signaling, as well as phorbol ester-induced GHR proteolysis, in a fashion similar to the intact antibody.	Disulfides	61-70	growth hormone receptor	Homo sapiens	57-60
15509165-4	2004	The human AGRP protein is 132 amino acids and contains five disulfide bridges in the C-terminal domain.	Disulfides	60-69	agouti related neuropeptide	Homo sapiens	10-14
15575700-4	2004	Since there are two disulfide bonds in the native structure of GM-CSF, an oxidizing redox potential of the reaction mixture was required.	Disulfides	20-29	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	63-69
15317846-5	2004	The conformational stability and the ability to stimulate Hsp70 are dependent on a disulfide bridge within the loop region of the J-domain, suggesting a redox-regulated activation of the chaperone.	Disulfides	83-92	heat shock protein family A (Hsp70) member 4	Homo sapiens	58-63
15351709-2	2004	We report that peroxynitrite and H2O2-induced disulfides in the porcine brain microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH.	Disulfides	46-56	microtubule associated protein 2	Homo sapiens	118-150
15588374-1	2004	The thyrotropin receptor (TSHR) cleaves to a variable extent within the ectodomain into a ligand-binding A subunit linked by disulfide bonds to the largely transmembrane B subunit.	Disulfides	125-134	thyroid stimulating hormone receptor	Homo sapiens	4-24
15588374-1	2004	The thyrotropin receptor (TSHR) cleaves to a variable extent within the ectodomain into a ligand-binding A subunit linked by disulfide bonds to the largely transmembrane B subunit.	Disulfides	125-134	thyroid stimulating hormone receptor	Homo sapiens	26-30
15379542-3	2004	Here, we report (2)H and (17)O MRD data at three temperatures for wild-type BPTI and two BPTI variants where the 14-38 disulfide bond has been cleaved by a double Cys --&gt; Ser mutation or by disulfide reduction and carboxamidomethylation.	Disulfides	119-128	spleen trypsin inhibitor I	Bos taurus	89-93
15379542-3	2004	Here, we report (2)H and (17)O MRD data at three temperatures for wild-type BPTI and two BPTI variants where the 14-38 disulfide bond has been cleaved by a double Cys --&gt; Ser mutation or by disulfide reduction and carboxamidomethylation.	Disulfides	193-202	spleen trypsin inhibitor I	Bos taurus	89-93
15292166-5	2004	Denaturation of Muclin with reducing agents to break the numerous intrachain disulfide bonds in Muclin"s scavenger receptor cysteine-rich and CUB domains did not interfere with binding.	Disulfides	77-86	deleted in malignant brain tumors 1	Homo sapiens	16-22
15292166-5	2004	Denaturation of Muclin with reducing agents to break the numerous intrachain disulfide bonds in Muclin"s scavenger receptor cysteine-rich and CUB domains did not interfere with binding.	Disulfides	77-86	deleted in malignant brain tumors 1	Homo sapiens	96-102
15342244-3	2004	Cathepsin E is the only A1 aspartic protease that exists as a homodimer with a disulfide bridge linking the two monomers.	Disulfides	79-88	cathepsin E	Homo sapiens	0-11
15473697-5	2004	Although the overall structural topology between BACE1 and BACE2 protease domains is quite similar, the former contains 3 disulfide bonds but the latter only two.	Disulfides	122-131	beta-secretase 2	Homo sapiens	59-64
15315367-3	2004	The molecular mass of purified AChE was 116 kDa for its native protein (nonreduced form) and 61 kDa for its subunits (reduced form) as revealed on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), suggesting that the homodimer of AChE linked with disulfide bonds.	Disulfides	267-276	LOW QUALITY PROTEIN: acetylcholinesterase	Bactrocera dorsalis	31-35
15187079-3	2004	By contrast, the evolutionarily related meprin beta subunit retains the COOH-terminal domains during biosynthesis and travels to the plasma membrane as a disulfide-linked integral membrane dimer.	Disulfides	154-163	meprin A subunit beta	Homo sapiens	40-51
15242783-0	2004	Evidence for disulfide involvement in the regulation of intramolecular autolytic processing by human adamalysin19/ADAM19.	Disulfides	13-22	ADAM metallopeptidase domain 19	Homo sapiens	114-120
15242783-1	2004	Human adamalysin 19 (a disintegrin and metalloproteinase 19, hADAM19) is activated by furin-mediated cleavage of the prodomain followed by an autolytic processing within the cysteine-rich domain at Glu586-Ser587, which occurs intramolecularly, producing an NH2 terminal fragment (N-fragment) associated with its COOH-terminal fragment (C-fragment), most likely through disulfide bonds.	Disulfides	369-378	ADAM metallopeptidase domain 19	Homo sapiens	61-68
15242783-8	2004	The cysteine-rich domain likely forms disulfide bonds to regulate the autolytic processing and shedding of hADAM19.	Disulfides	38-47	ADAM metallopeptidase domain 19	Homo sapiens	107-114
15233797-3	2004	The NMR structure-based model reveals the structural features of the eLPs, in which the second extracellular loop (eLP(2)) and the disulfide bond between the first extracellular loop (eLP(1)) and eLP(2) play a major role in forming the ligand recognition pocket.	Disulfides	131-140	elongator acetyltransferase complex subunit 2	Homo sapiens	196-202
15233797-4	2004	The eLP(2) conformation is dynamic and regulated by the oxidation and reduction of the disulfide bond, which affects ligand docking in the initial recognition.	Disulfides	87-96	elongator acetyltransferase complex subunit 2	Homo sapiens	4-10
15233797-6	2004	The ligand-bound receptor was, however, resistant to the reduction inactivation because the ligand covered the disulfide bond and stabilized the eLP(2) conformation.	Disulfides	111-120	elongator acetyltransferase complex subunit 2	Homo sapiens	145-151
15231784-3	2004	We introduced pairs of cysteine mutations into the receptor binding domain of colicin E9 (ColE9) that resulted in the formation of a disulfide bond located near the middle or the top of the R domain.	Disulfides	133-142	colicin E9	Escherichia coli	78-88
15231784-3	2004	We introduced pairs of cysteine mutations into the receptor binding domain of colicin E9 (ColE9) that resulted in the formation of a disulfide bond located near the middle or the top of the R domain.	Disulfides	133-142	colicin E9	Escherichia coli	90-95
15196038-8	2004	Our results appear to rule out a critical importance of an intramolecular disulfide linkage in NCKX2 protein synthesis and folding as had been reported before.	Disulfides	74-83	solute carrier family 24 member 2	Homo sapiens	95-100
15075410-5	2004	Combined with other published data, these results indicate that heating induces at least two molten globule-like states of beta-lg, a highly reactive Mcys121 that returns to native state after cooling, and a less-reactive Mcys119 that is trapped and stabilized in a molten globule-like state by nonnative disulfide bond.	Disulfides	305-314	beta-lactoglobulin	Bos taurus	123-130
15096625-0	2004	Alteration of the disulfide-coupled folding pathway of BPTI by circular permutation.	Disulfides	18-27	spleen trypsin inhibitor I	Bos taurus	55-59
15096625-1	2004	The kinetics of disulfide-coupled folding and unfolding of four circularly permuted forms of bovine pancreatic trypsin inhibitor (BPTI) were studied and compared with previously published results for both wild-type BPTI and a cyclized form.	Disulfides	16-25	spleen trypsin inhibitor I	Bos taurus	93-128
15096625-1	2004	The kinetics of disulfide-coupled folding and unfolding of four circularly permuted forms of bovine pancreatic trypsin inhibitor (BPTI) were studied and compared with previously published results for both wild-type BPTI and a cyclized form.	Disulfides	16-25	spleen trypsin inhibitor I	Bos taurus	130-134
15096625-1	2004	The kinetics of disulfide-coupled folding and unfolding of four circularly permuted forms of bovine pancreatic trypsin inhibitor (BPTI) were studied and compared with previously published results for both wild-type BPTI and a cyclized form.	Disulfides	16-25	spleen trypsin inhibitor I	Bos taurus	215-219
15070359-0	2004	Structural change of the heme pocket due to disulfide bridge formation is significantly larger for neuroglobin than for cytoglobin.	Disulfides	44-53	neuroglobin	Homo sapiens	99-110
15070359-1	2004	Human neuroglobin (hNgb) and human cytoglobin (hCygb), two recently discovered members of the vertebrate globin family, are known to be able to form an intramolecular disulfide bridge.	Disulfides	167-176	neuroglobin	Homo sapiens	6-17
15070359-1	2004	Human neuroglobin (hNgb) and human cytoglobin (hCygb), two recently discovered members of the vertebrate globin family, are known to be able to form an intramolecular disulfide bridge.	Disulfides	167-176	neuroglobin	Homo sapiens	19-23
15070359-2	2004	Using electron paramagnetic resonance (EPR), we show that formation of a disulfide bridge in ferric hNgb causes a considerable change in the heme pocket structure, whereas this is not so clear for ferric hCygb.	Disulfides	73-82	neuroglobin	Homo sapiens	100-104
15001354-3	2004	Cofilin inhibited several-fold the rate of interstrand disulfide cross-linking between Cys265 and Cys374 in yeast S265C mutant F-actin, but enhanced excimer formation between pyrene probes attached to these cysteine residues.	Disulfides	55-64	cofilin	Saccharomyces cerevisiae S288C	0-7
15001354-7	2004	Disulfide cross-linking of S265C yeast F-actin inhibited strongly and reversibly the release of rhodamine phalloidin by cofilin.	Disulfides	0-9	cofilin	Saccharomyces cerevisiae S288C	120-127
14613939-4	2004	In this study we show that on oxidation CLIC1 undergoes a reversible transition from a monomeric to a non-covalent dimeric state due to the formation of an intramolecular disulfide bond (Cys-24-Cys-59).	Disulfides	171-180	chloride intracellular channel 1	Homo sapiens	40-45
14769035-1	2004	Partially folded conformational ensembles of bovine pancreatic trypsin inhibitor (BPTI) are accessed by replacing Cys 5, 30, 51, and 55 by alpha-amino-n-butyric acid (Abu) while retaining the disulfide between Cys 14 and 38; the resultant variant is termed [14-38](Abu).	Disulfides	192-201	spleen trypsin inhibitor I	Bos taurus	82-86
14597639-3	2004	RON is a trans-membrane heterodimer comprised of one alpha- and one beta-chain originating from a single-chain precursor and held together by several disulfide bonds.	Disulfides	150-159	macrophage stimulating 1 receptor	Homo sapiens	0-3
14999006-0	2004	Effects of deletion and shift of the A20-B19 disulfide bond on the structure, activity, and refolding of proinsulin.	Disulfides	45-54	immunoglobulin kappa variable 1-27	Homo sapiens	37-40
14999006-2	2004	This mutant, together with another proinsulin mutant previously constructed with an A19Tyr deletion, which can also be taken as shifted mutant of the A20-B19 disulfide bond, were studied for their in vitro refolding, oxidation of free thiol groups, circular dichroism spectra, antibody and receptor binding activities and sensitivity to trypsin digestion in comparison with native proinsulin.	Disulfides	158-167	immunoglobulin kappa variable 1-27	Homo sapiens	150-153
14999006-3	2004	The results indicate that deletion of the A20-B19 disulfide bond results in a large decrease in the alpha-helix content of the molecule and higher sensitivity to tryptic digestion.	Disulfides	50-59	immunoglobulin kappa variable 1-27	Homo sapiens	42-45
14999006-7	2004	These results suggest that the A20-B19 disulfide bond plays an important role in the structural stabilization and folding of the insulin precursor.	Disulfides	39-48	immunoglobulin kappa variable 1-27	Homo sapiens	31-34
15507277-4	2004	The binding site for GPIbalpha on vWF resides in the conserved A1 domain, encompassing the disulfide bond at Cys509-Cys695.	Disulfides	91-100	glycoprotein Ib platelet subunit alpha	Homo sapiens	21-30
14530264-3	2003	There are three cysteine residues in human neuroglobin; those at positions CD7 and D5 are sufficiently close to form an internal disulfide bond.	Disulfides	129-138	neuroglobin	Homo sapiens	43-54
14530264-4	2003	Both cysteine residues in cytoglobin, although localized in other positions than in human neuroglobin, may form a disulfide bond as well.	Disulfides	114-123	neuroglobin	Homo sapiens	90-101
14675190-4	2003	Differential extraction experiments demonstrated that efficient recovery of p200 from the dermis was strongly dependent on the presence of reducing agents, suggesting that it forms highly insoluble oligomers and/or is extensively cross-linked to other extracellular matrix components by disulfide bonding.	Disulfides	287-296	AT-rich interaction domain 2	Homo sapiens	76-80
14645556-6	2003	The GP(2b), GP(3), and GP(4) proteins occur as a heterotrimeric complex in which disulfide bonds play an important role.	Disulfides	81-90	integrin subunit alpha 2b	Homo sapiens	4-9
12963719-8	2003	Kinetics of the formation of the irreversibly unfolded species of wild-type beta-lg in 8 M urea at pH 7.0 indicated that, first, an intramolecular thiol-disulfide exchange occurs to produce a mixture of species with non-native disulfide bonds followed by the intermolecular thiol-disulfide exchange producing the oligomers.	Disulfides	153-162	beta-lactoglobulin	Bos taurus	76-83
12963719-8	2003	Kinetics of the formation of the irreversibly unfolded species of wild-type beta-lg in 8 M urea at pH 7.0 indicated that, first, an intramolecular thiol-disulfide exchange occurs to produce a mixture of species with non-native disulfide bonds followed by the intermolecular thiol-disulfide exchange producing the oligomers.	Disulfides	227-236	beta-lactoglobulin	Bos taurus	76-83
12963719-8	2003	Kinetics of the formation of the irreversibly unfolded species of wild-type beta-lg in 8 M urea at pH 7.0 indicated that, first, an intramolecular thiol-disulfide exchange occurs to produce a mixture of species with non-native disulfide bonds followed by the intermolecular thiol-disulfide exchange producing the oligomers.	Disulfides	227-236	beta-lactoglobulin	Bos taurus	76-83
12963719-9	2003	These results indicate that intramolecular and intermolecular thiol-disulfide exchange reactions cause the low reversibility of wild-type beta-lg especially at neutral pH and that the mutation of Cys-121 improves the reversibility, enabling us to study the folding of beta-lg more exactly under various conditions.	Disulfides	68-77	beta-lactoglobulin	Bos taurus	138-145
14607111-4	2003	The S.cerevisiae eIF2alpha lacks a disulfide bridge that is present in the homologous protein in humans and some of the other higher eukaryotes.	Disulfides	35-44	eukaryotic translation initiation factor 2A	Homo sapiens	17-26
12967471-5	2003	Transgenic mice expressing VEGF-E(NZ-7) showed a dramatic increase in angiogenesis with very few side effects (such as edema and hemorrhagic spots), suggesting strong angiogenic signaling and a potential clinical utility of VEGF-E. VEGF family members bear three loops produced via three intramolecular disulfide bonds, and cooperation between loop-1 and loop-3 is necessary for the specific binding and activation of VEGFR-2 for angiogenesis.	Disulfides	303-312	platelet-derived growth factor, C polypeptide	Mus musculus	27-33
12953119-7	2003	An intramolecular disulfide bridge in TGA1 precludes interaction with NPR1, and NPR1 can only stimulate the DNA binding activity of the reduced form of TGA1.	Disulfides	18-27	regulatory protein (NPR1)	Arabidopsis thaliana	70-74
12958615-7	2003	Substitution of either Cys5 or Cys7 by Ala failed to show surface expression of GPIb-IX, suggesting that the Cys5- Cys7 disulfide loop in GPIbbeta is essential for the efficient processing and trafficking of GPIb-IX complexes toward the plasma membrane.	Disulfides	120-129	glycoprotein Ib platelet subunit beta	Homo sapiens	138-146
12781781-4	2003	In this study, a peptide with the sequence of the third extracellular loop (eLP3, residues 271-289) of the TP receptor was synthesized, and its termini were constrained by the formation of a disulfide bond between the additional homocysteines located at both ends.	Disulfides	191-200	elongator acetyltransferase complex subunit 3	Homo sapiens	76-80
12787673-7	2003	In order to ensure the correct formation of the protein"s eight conserved disulfide bridges we expressed Mal d 2 in Nicotiana benthamiana plants by the use of a tobacco mosaic viral vector.	Disulfides	74-83	mal d 2	Malus domestica	105-112
12774022-9	2003	In conclusion, these findings suggest that extramitochondrial glutathione depletion alters the thiol-disulfide redox state, leading to inhibition of NF-kappaB transactivation of survival genes and to sustained activation of JNK, both of which contribute to the sensitization to TNF-induced apoptosis.	Disulfides	101-110	mitogen-activated protein kinase 8	Mus musculus	224-227
12743278-0	2003	Formation of disulfide-linked complexes between the three minor envelope glycoproteins (GP2b, GP3, and GP4) of equine arteritis virus.	Disulfides	13-22	glycoprotein 4 (GP4)	Equine arteritis virus	103-106
12743278-3	2003	Shortly after their release from infected cells, virions contained mainly cystine-linked GP(2b)/GP(4) heterodimers, which were subsequently converted into disulfide-bonded GP(2b)/GP(3)/GP(4) trimers through the covalent recruitment of GP(3).	Disulfides	155-164	integrin subunit alpha 2b	Homo sapiens	172-177
12743278-5	2003	In contrast, the sulfhydryl-modifying agent N-ethylmaleimide inhibited the formation of disulfide-bonded GP(2b)/GP(3)/GP(4) trimers.	Disulfides	88-97	integrin subunit alpha 2b	Homo sapiens	105-110
12743278-7	2003	Nevertheless, the instantaneous diamide-induced formation of disulfide-bonded GP(2b)/GP(3)/GP(4) heterotrimers at 4 degrees C suggests that the three minor glycoproteins of EAV are assembled as trimeric complexes.	Disulfides	61-70	integrin subunit alpha 2b	Homo sapiens	78-83
12743278-8	2003	The existence of a noncovalent interaction between the cystine-linked GP(2b)/GP(4) dimer and GP(3) was also inferred from coexpression experiments showing that the presence of GP(3) increased the electrophoretic mobility of the disulfide-bonded GP(2b)/GP(4) dimers.	Disulfides	228-237	integrin subunit alpha 2b	Homo sapiens	70-75
12743278-8	2003	The existence of a noncovalent interaction between the cystine-linked GP(2b)/GP(4) dimer and GP(3) was also inferred from coexpression experiments showing that the presence of GP(3) increased the electrophoretic mobility of the disulfide-bonded GP(2b)/GP(4) dimers.	Disulfides	228-237	integrin subunit alpha 2b	Homo sapiens	245-250
12611895-7	2003	The ECD1-CRFR2beta possesses a disulfide arrangement identical to that of the ECD1 of CRFR1, namely Cys(45)-Cys(70), Cys(60)-Cys(103), and Cys(84)-Cys(118).	Disulfides	31-40	corticotropin releasing hormone receptor 2	Mus musculus	9-18
12814263-1	2003	A human plasma retinol-binding protein (RBP) mutant, named RBP-S, has been designed and produced in which the six native cysteine residues, involved in the formation of three disulfide bonds, have been replaced with serine.	Disulfides	175-184	retinol binding protein 4	Homo sapiens	40-43
12814263-1	2003	A human plasma retinol-binding protein (RBP) mutant, named RBP-S, has been designed and produced in which the six native cysteine residues, involved in the formation of three disulfide bonds, have been replaced with serine.	Disulfides	175-184	retinol binding protein 4	Homo sapiens	59-62
12814263-3	2003	The removal of the disulfide bonds led to a decrease in the affinity of RBP for all trans-retinol.	Disulfides	19-28	retinol binding protein 4	Homo sapiens	72-75
12814263-5	2003	Circular dichroism in the far-UV shows that there is a relaxation of the RBP structure upon the removal of its disulfide bonds.	Disulfides	111-120	retinol binding protein 4	Homo sapiens	73-76
12814263-6	2003	Circular dichroism in the near-UV shows that in the absence of the disulfide bonds, the optical activity of RBP is higher in the 310-330 nm than in the 280-290 nm range.	Disulfides	67-76	retinol binding protein 4	Homo sapiens	108-111
12814263-7	2003	This work suggests that the three native disulfide bonds aid in the folding of RBP but are not essential to produce a soluble, active protein.	Disulfides	41-50	retinol binding protein 4	Homo sapiens	79-82
12695123-0	2003	Rat J chain is disulfide-linked to alpha-chains in rat polymeric (pIgA) and secretory IgA (SIgA).	Disulfides	15-24	phosphatidylinositol glycan anchor biosynthesis, class A	Rattus norvegicus	66-70
12540615-1	2003	Autosomal dominant diabetes in the Akita mouse is caused by mutation of the insulin 2 gene, whose product replaces a cysteine residue that is engaged in the formation of an intramolecular disulfide bond.	Disulfides	188-197	insulin II	Mus musculus	76-85
12533475-8	2003	SrgA efficiently oxidizes the disulfide bond of PefA, while the S. enterica serovar Typhimurium chromosomally encoded disulfide oxidoreductase DsbA does not.	Disulfides	30-39	plasmid-encoded major fimbrial subunit	Salmonella enterica subsp. enterica serovar Typhimurium	48-52
12533475-10	2003	SrgA therefore appears to be a substrate-specific disulfide oxidoreductase, thus explaining the requirement for an additional catalyst of disulfide bond formation in addition to DsbA of S. enterica serovar Typhimurium.	Disulfides	50-59	putative thiol-disulfide isomerase or thioredoxin	Salmonella enterica subsp. enterica serovar Typhimurium	0-4
12568924-2	2003	and disulfide bridge depleted (C3A/C26A) azurin has been investigated by differential scanning calorimetry (DSC) and fluorescence techniques.	Disulfides	4-13	complement C3	Homo sapiens	31-39
12568924-11	2003	as the reference state, for both Cu and Zn C3A/C26A azurin the unfolding free energy is decreased by about 28 kJ/mol, indicating that metal substitution is not able to compensate the destabilising effect induced by the disulfide bridge depletion.	Disulfides	219-228	complement C3	Homo sapiens	43-46
15969027-7	2003	This is not necessarily incompatible with the importance of the non-native disulfide intermediates in the bovine pancreatic trypsin inhibitor (BPTI) pathway, which are just a chemical necessity in the intramolecular arrangement to facilitate native disulfide formation.	Disulfides	75-84	spleen trypsin inhibitor I	Bos taurus	106-141
15969027-7	2003	This is not necessarily incompatible with the importance of the non-native disulfide intermediates in the bovine pancreatic trypsin inhibitor (BPTI) pathway, which are just a chemical necessity in the intramolecular arrangement to facilitate native disulfide formation.	Disulfides	75-84	spleen trypsin inhibitor I	Bos taurus	143-147
15969027-7	2003	This is not necessarily incompatible with the importance of the non-native disulfide intermediates in the bovine pancreatic trypsin inhibitor (BPTI) pathway, which are just a chemical necessity in the intramolecular arrangement to facilitate native disulfide formation.	Disulfides	249-258	spleen trypsin inhibitor I	Bos taurus	106-141
15969027-7	2003	This is not necessarily incompatible with the importance of the non-native disulfide intermediates in the bovine pancreatic trypsin inhibitor (BPTI) pathway, which are just a chemical necessity in the intramolecular arrangement to facilitate native disulfide formation.	Disulfides	249-258	spleen trypsin inhibitor I	Bos taurus	143-147
15969027-9	2003	Based on the BPTI refolding it was suggested that disulfide bonds have a stabilizing effect on the native state without determining either the folding pathway or the final three-dimensional structure of the protein.	Disulfides	50-59	spleen trypsin inhibitor I	Bos taurus	13-17
12501217-0	2002	Dramatic stabilization of the native state of human carbonic anhydrase II by an engineered disulfide bond.	Disulfides	91-100	carbonic anhydrase 2	Homo sapiens	52-73
12501217-1	2002	To find a disulfide pair that could stabilize the enzyme human carbonic anhydrase II (HCA II), we grafted the disulfide bridge from the related and unusually stable carbonic anhydrase form from Neisseria gonorrhoeae (NGCA) into the human enzyme.	Disulfides	10-19	carbonic anhydrase 2	Homo sapiens	63-84
12501217-1	2002	To find a disulfide pair that could stabilize the enzyme human carbonic anhydrase II (HCA II), we grafted the disulfide bridge from the related and unusually stable carbonic anhydrase form from Neisseria gonorrhoeae (NGCA) into the human enzyme.	Disulfides	110-119	carbonic anhydrase 2	Homo sapiens	63-84
12393867-0	2002	Screening for stable mutants with amino acid pairs substituted for the disulfide bond between residues 14 and 38 of bovine pancreatic trypsin inhibitor (BPTI).	Disulfides	71-80	spleen trypsin inhibitor I	Bos taurus	153-157
12377762-11	2002	These results suggest that NCKX2 associates as a dimer, an interaction that does not require, but may be stabilized by, a disulfide linkage through Cys-395.	Disulfides	122-131	solute carrier family 24 member 2	Rattus norvegicus	27-32
12454284-4	2002	Mutation of Cys-42 to a serine completely abrogated dimerization of HLA-G, suggesting that the disulfide linkage formed exclusively through this residue.	Disulfides	95-104	major histocompatibility complex, class I, G	Homo sapiens	68-73
12441378-3	2002	The reduction by dithiothreitol of the three intramolecular disulfide bonds of the fifth domain was accelerated in the presence of stoichiometric amounts of GroEL, indicating that the fifth domain was destabilized upon interaction with GroEL.	Disulfides	60-69	heat shock protein family D (Hsp60) member 1	Homo sapiens	157-162
12387870-3	2002	In gel filtration chromatography human Sptrx-1 eluates as a 400 kDa protein consistent with either an oligomeric form, not maintained by intermolecular disulfide bonding, and/or a highly asymmetrical structure.	Disulfides	152-161	thioredoxin domain containing 2	Homo sapiens	39-46
12387870-6	2002	This oxidizing enzymatic activity suggests that Sptrx-1 might govern the stabilization (by disulfide cross-linking) of the different structures in the developing tail of spermatids and spermatozoa.	Disulfides	91-100	thioredoxin domain containing 2	Homo sapiens	48-55
12167606-2	2002	The disulfide-linked rBAT-b(0,+)AT heterodimer mediates high-affinity transport of cystine and dibasic amino acids (b(0,+)-like activity) in heterologous cell systems.	Disulfides	4-13	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	21-25
12167606-2	2002	The disulfide-linked rBAT-b(0,+)AT heterodimer mediates high-affinity transport of cystine and dibasic amino acids (b(0,+)-like activity) in heterologous cell systems.	Disulfides	4-13	solute carrier family 7 member 9	Homo sapiens	26-34
12019263-0	2002	Identification of the disulfide bonds in the recombinant somatomedin B domain of human vitronectin.	Disulfides	22-31	vitronectin	Homo sapiens	57-70
12019263-0	2002	Identification of the disulfide bonds in the recombinant somatomedin B domain of human vitronectin.	Disulfides	22-31	vitronectin	Homo sapiens	87-98
12019263-1	2002	The NH(2)-terminal somatomedin B (SMB) domain (residues 1-44) of human vitronectin contains eight Cys residues organized into four disulfide bonds and is required for the binding of type 1 plasminogen activator inhibitor (PAI-1).	Disulfides	131-140	vitronectin	Homo sapiens	19-32
12019263-1	2002	The NH(2)-terminal somatomedin B (SMB) domain (residues 1-44) of human vitronectin contains eight Cys residues organized into four disulfide bonds and is required for the binding of type 1 plasminogen activator inhibitor (PAI-1).	Disulfides	131-140	vitronectin	Homo sapiens	71-82
12019263-2	2002	In the present study, we map the four disulfide bonds in recombinant SMB (rSMB) and evaluate their functional importance.	Disulfides	38-47	vitronectin	Homo sapiens	69-72
11877442-4	2002	In its disulfide form, the 13-kDa protein thioredoxin-2 is a substrate of thioredoxin reductase-1 (K(m) = 5.2 microm, k(cat) = 14.5 s(-1)) and in its dithiol form, an electron donor for TPx-1 (K(m) = 9 microm, k(cat) = 5.4 s(-1)).	Disulfides	7-16	thioredoxin reductase 1	Homo sapiens	74-97
11834744-7	2002	X-ray crystallographic structures of CLC protein in complex with the inhibitors showed that p-chloromercuribenzenesulfonate bound CLC protein via disulfide bonds with Cys(29) and with Cys(57) near the carbohydrate recognition domain (CRD), whereas N-ethylmaleimide bound to the galectin-10 CRD via ring stacking interactions with Trp(72), in a manner highly analogous to mannose binding to this CRD.	Disulfides	146-155	Charcot-Leyden crystal galectin	Homo sapiens	37-40
11834744-7	2002	X-ray crystallographic structures of CLC protein in complex with the inhibitors showed that p-chloromercuribenzenesulfonate bound CLC protein via disulfide bonds with Cys(29) and with Cys(57) near the carbohydrate recognition domain (CRD), whereas N-ethylmaleimide bound to the galectin-10 CRD via ring stacking interactions with Trp(72), in a manner highly analogous to mannose binding to this CRD.	Disulfides	146-155	Charcot-Leyden crystal galectin	Homo sapiens	130-133
11834744-7	2002	X-ray crystallographic structures of CLC protein in complex with the inhibitors showed that p-chloromercuribenzenesulfonate bound CLC protein via disulfide bonds with Cys(29) and with Cys(57) near the carbohydrate recognition domain (CRD), whereas N-ethylmaleimide bound to the galectin-10 CRD via ring stacking interactions with Trp(72), in a manner highly analogous to mannose binding to this CRD.	Disulfides	146-155	Charcot-Leyden crystal galectin	Homo sapiens	278-289
11698394-10	2002	In accordance with this, DmGCLC and DmGCLM have the ability to form reversible intermolecular disulfide bridges.	Disulfides	94-103	Glutamate-cysteine ligase catalytic subunit	Drosophila melanogaster	25-31
11772028-1	2002	We have previously demonstrated that an oxidative change, the formation of a disulfide bridge between two cysteine residues, in the membrane protein beta-actin is primarily responsible for locking the irreversibly sickled red blood cells (ISCs) of sickle cell anemic patients into the sickle shape.	Disulfides	77-86	POTE ankyrin domain family member F	Homo sapiens	149-159
11752136-2	2002	Repression of E10R prevented the formation of intramolecular disulfide bonds of the G4L glutaredoxin, the L1R membrane protein, and the structurally related F9L protein.	Disulfides	61-70	sulfhydryl oxidase	Vaccinia virus	14-18
11766986-4	2001	The members of heterodimeric amino acid transporter family are linked via a disulfide bond to single membrane spanning type II membrane glycoproteins such as 4F2hc (4F2 heavy chain) and rBAT (related to b(0,+)-amino acid transporter).	Disulfides	76-85	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	186-190
11581259-9	2001	These results indicate that (a) cubilin contains two distinct regions that bind both IF-Cbl and albumin and that (b) binding of both IF-Cbl and albumin to each of these regions can be distinguished and is regulated by the nonassisted formation of local disulfide bonds.	Disulfides	253-262	cubilin	Homo sapiens	32-39
11578775-3	2001	Although it is known that S100B"s neurotrophic activity requires a disulfide-linked dimeric form of the protein, the structural features of S100B that are important for glial activation have not been defined.	Disulfides	67-76	S100 calcium binding protein B	Rattus norvegicus	26-31
11568092-4	2001	Disulfides and protein-bound aminothiols were reduced by either tri-n-butylphosphine (the TBP method) or tris(2-carboxyethyl)phosphine (the TCEP method); the effects of temperature, time of reduction, and concentration of reductants were evaluated.	Disulfides	0-10	TATA-box binding protein	Homo sapiens	90-93
11533296-5	2001	Na(+)-independent glutamine transporter genes encoding for System L (LAT1, LAT2) and System b(0,+) (b(0,+)AT) have also been recently isolated, and similar to y(+)L, have been shown to function as disulfide-linked heterodimers with the 4F2 heavy chain (CD98) or rBAT (related to b(0,+) amino acid transporter).	Disulfides	197-206	solute carrier family 7 member 9	Homo sapiens	100-108
11297544-1	2001	Peripherin-2 and Rom-1 are homologous tetraspanning membrane proteins that assemble into noncovalent tetramers and higher order disulfide-linked oligomers implicated in photoreceptor disc morphogenesis.	Disulfides	128-137	peripherin 2	Homo sapiens	0-12
11297544-1	2001	Peripherin-2 and Rom-1 are homologous tetraspanning membrane proteins that assemble into noncovalent tetramers and higher order disulfide-linked oligomers implicated in photoreceptor disc morphogenesis.	Disulfides	128-137	retinal outer segment membrane protein 1	Homo sapiens	17-22
11297544-3	2001	We examined the expression, subunit assembly, and disulfide-mediated oligomerization of L185P and L185A peripherin-2 and L188P Rom-1 by velocity sedimentation, co-immunoprecipitation, and cross-linking.	Disulfides	50-59	peripherin 2	Homo sapiens	104-116
11297544-3	2001	We examined the expression, subunit assembly, and disulfide-mediated oligomerization of L185P and L185A peripherin-2 and L188P Rom-1 by velocity sedimentation, co-immunoprecipitation, and cross-linking.	Disulfides	50-59	retinal outer segment membrane protein 1	Homo sapiens	127-132
11297544-9	2001	Peripherin-2-containing tetramers are required for higher order disulfide-linked oligomer formation.	Disulfides	64-73	peripherin 2	Homo sapiens	0-12
11353828-6	2001	Locking the I domain open resulted in a 9,000-fold increase in affinity to intercellular adhesion molecule-1 (ICAM-1), which was reversed by disulfide reduction.	Disulfides	141-150	intercellular adhesion molecule 1	Homo sapiens	75-108
11353828-6	2001	Locking the I domain open resulted in a 9,000-fold increase in affinity to intercellular adhesion molecule-1 (ICAM-1), which was reversed by disulfide reduction.	Disulfides	141-150	intercellular adhesion molecule 1	Homo sapiens	110-116
11278376-0	2001	A full biological response to autoantibodies in Graves" disease requires a disulfide-bonded loop in the thyrotropin receptor N terminus homologous to a laminin epidermal growth factor-like domain.	Disulfides	75-84	thyroid stimulating hormone receptor	Homo sapiens	104-124
11292751-8	2001	The inhibitory antibodies targeted both conserved and strain-specific epitopes within the ectodomain of AMA1; however, it appears that the majority of these antibodies reacted with strain-specific epitopes in domain I, the N-terminal disulfide-bonded domain, which is the most polymorphic region of AMA1.	Disulfides	234-243	apical membrane antigen 1	Plasmodium falciparum 3D7	104-108
11152479-5	2001	Using recombinant proteins expressed in Escherichia coli, we demonstrated the activity of the Trx domain of TMX to cleave the interchain disulfide bridges in insulin in vitro.	Disulfides	137-146	thioredoxin related transmembrane protein 1	Homo sapiens	108-111
11170206-0	2001	Thermodynamics of the helix-coil transition: Binding of S15 and a hybrid sequence, disulfide stabilized peptide to the S-protein.	Disulfides	83-92	vitronectin	Homo sapiens	119-128
11170206-5	2001	A hybrid sequence, disulfide-stabilized peptide (ApaS-25), designed to stabilize the helical structure of the S-peptide in solution, also combines with the S-protein to yield a catalytically active complex.	Disulfides	19-28	vitronectin	Homo sapiens	156-165
11342054-3	2001	This reaction gives rise to a disulfide-bonded, two-chain form of vitronectin.	Disulfides	30-39	vitronectin	Homo sapiens	66-77
11288979-1	2001	Cleavage of thyrotropin receptors (TSHR) on the cell surface into disulfide-linked A and B subunits involves deletion of an intervening region that corresponds approximately to a 50 amino acid "insertion" in the TSHR relative to the noncleaving luteinizing hormone/choriogonadotropin receptor (LH/CGR).	Disulfides	66-75	thyroid stimulating hormone receptor	Homo sapiens	35-39
11288979-1	2001	Cleavage of thyrotropin receptors (TSHR) on the cell surface into disulfide-linked A and B subunits involves deletion of an intervening region that corresponds approximately to a 50 amino acid "insertion" in the TSHR relative to the noncleaving luteinizing hormone/choriogonadotropin receptor (LH/CGR).	Disulfides	66-75	thyroid stimulating hormone receptor	Homo sapiens	212-216
12016338-3	2001	However, S-glutahionylation, the formation of a mixed disulfide between glutathione and the redox-sensitive cysteine residues, has been shown to occur under NO exposure and pro-oxidative conditions in c-Jun, one of the AP-1 constituents.	Disulfides	54-63	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	201-206
11169440-4	2001	CD4(+) T cell hybridomas took longer to recognize an epitope derived from the disulfide-bonded region whether native parasite or recombinant MSP-1 antigen was used.	Disulfides	78-87	CD4 antigen	Mus musculus	0-3
11168891-3	2001	Insulin-like 4 was generated by solid-phase peptide synthesis of the two chains followed by the sequential synthesis of the three disulfide bonds.	Disulfides	130-139	insulin like 4	Homo sapiens	0-14
10964926-9	2000	Based on the results of competition experiments with various putrescine analogues and the disulfide cross-linking of PotE between cytoplasmic loops and the COOH terminus, a model of the putrescine recognition site on PotE consisting of the identified amino acids is presented.	Disulfides	90-99	POTE ankyrin domain family member D	Homo sapiens	117-121
10964926-9	2000	Based on the results of competition experiments with various putrescine analogues and the disulfide cross-linking of PotE between cytoplasmic loops and the COOH terminus, a model of the putrescine recognition site on PotE consisting of the identified amino acids is presented.	Disulfides	90-99	POTE ankyrin domain family member D	Homo sapiens	217-221
11035794-5	2000	When cells were infected with a mutant vaccinia virus in which the E10R gene encoding an ERV1/ALR family protein was repressed, the disulfide bonds of three other viral proteins-namely, the L1R and F9L proteins and the G4L glutaredoxin-were completely reduced.	Disulfides	132-141	sulfhydryl oxidase	Vaccinia virus	67-71
11035794-9	2000	These data indicated a viral pathway of disulfide bond formation in which the E10R protein has a central role.	Disulfides	40-49	sulfhydryl oxidase	Vaccinia virus	78-82
10915799-0	2000	Folding and maturation of tyrosinase-related protein-1 are regulated by the post-translational formation of disulfide bonds and by N-glycan processing.	Disulfides	108-117	tyrosinase-related protein 1	Mus musculus	26-54
10915799-2	2000	We show that TRP-1 folding process occurs much more rapidly than for tyrosinase, a highly homologous protein, being completed post-translationally by the formation of critical disulfide bonds.	Disulfides	176-185	tyrosinase-related protein 1	Mus musculus	13-18
10915799-9	2000	We conclude that disulfide bridge burring is crucial for the TRP-1 export.	Disulfides	17-26	tyrosinase-related protein 1	Mus musculus	61-66
11200939-7	2000	This finding indicated that hCGbeta-subunit rescued the a half-Cys mutants from the formation of intermolecular disulfide-linked homodimer by preferentially combining with the alpha mutants.	Disulfides	112-121	chorionic gonadotropin subunit beta 3	Homo sapiens	28-35
11083061-9	2000	Comparison of the biological activities of native and the disulfide bond isomer of human IGF-I highlight the importance of Tyr24, Phe25, Phe49-Cys52 and Phe16 in binding to the IGF-I receptor or specific IGFBPs.	Disulfides	58-67	insulin like growth factor 1 receptor	Homo sapiens	177-191
10964401-4	2000	The LC-MS analysis of the extracted cTnI samples provided evidence of posttranslational modification by phosphorylation, acetylation, proteolytic cleavage, and intrachain disulfide bond formation.	Disulfides	171-180	troponin I3, cardiac type	Homo sapiens	36-40
10783391-6	2000	Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.	Disulfides	94-103	glutathione S-transferase omega 1	Homo sapiens	29-37
10910937-4	2000	This modification produced an intermolecular disulfide bridge, resulting in a bivalent, rather than a monovalent IT, termed SS2, that selectively inhibited T-cell proliferation in vitro.	Disulfides	45-54	butyrophilin like 2	Homo sapiens	124-127
10938361-4	2000	ERS1, like ETR1, forms a membrane-associated, disulfide-linked dimer.	Disulfides	46-55	ethylene response sensor 1	Arabidopsis thaliana	0-4
10938361-4	2000	ERS1, like ETR1, forms a membrane-associated, disulfide-linked dimer.	Disulfides	46-55	enoyl-[acyl-carrier-protein] reductase	Saccharomyces cerevisiae S288C	11-15
10899108-1	2000	Human interleukin-12 (IL-12, p70) is an early pro-inflammatory cytokine, comprising two disulfide-linked subunits, p35 and p40.	Disulfides	88-97	interleukin 12A	Homo sapiens	115-118
10880522-1	2000	The B cell antigen receptor (BCR) is a large complex that consists of a disulfide-linked tetramer of two transmembrane heavy (mu) chains and two light (lambda or kappa) chains in association with a heterodimer of Igalpha and Igbeta.	Disulfides	72-81	BCR activator of RhoGEF and GTPase	Homo sapiens	4-27
10880522-1	2000	The B cell antigen receptor (BCR) is a large complex that consists of a disulfide-linked tetramer of two transmembrane heavy (mu) chains and two light (lambda or kappa) chains in association with a heterodimer of Igalpha and Igbeta.	Disulfides	72-81	BCR activator of RhoGEF and GTPase	Homo sapiens	29-32
10812071-1	2000	In the presence of denaturant and thiol initiator, the native bovine pancreatic trypsin inhibitor (BPTI) denatures by shuffling its native disulfide bonds and converts to a mixture of scrambled isomers.	Disulfides	139-148	spleen trypsin inhibitor I	Bos taurus	99-103
11043935-12	2000	However, the folding pathway of TAP differs from that of BPTI by (a) a higher degree of heterogeneity of one- and two-disulfide intermediates and (b) the presence of three-disulfide scrambled isomers as folding intermediates.	Disulfides	118-127	spleen trypsin inhibitor I	Bos taurus	57-61
11043935-12	2000	However, the folding pathway of TAP differs from that of BPTI by (a) a higher degree of heterogeneity of one- and two-disulfide intermediates and (b) the presence of three-disulfide scrambled isomers as folding intermediates.	Disulfides	172-181	spleen trypsin inhibitor I	Bos taurus	57-61
10794421-0	2000	Novel disulfide engineering in human carbonic anhydrase II using the PAIRWISE side-chain geometry database.	Disulfides	6-15	carbonic anhydrase 2	Homo sapiens	37-58
10794421-2	2000	A potential function was generated from these observations and used to evaluate models for novel disulfide bonds in human carbonic anhydrase II (HCAII).	Disulfides	97-106	carbonic anhydrase 2	Homo sapiens	122-143
10716634-6	2000	Further, the model suggested that cathepsin W could exist as a dimer with the Cys 5 of each monomer forming a disulfide bond and the Arg 40 Phe 46 loop (RISFWDF) forming part of the dimeric interface.	Disulfides	110-119	cathepsin W	Homo sapiens	34-45
10727107-0	2000	Maurotoxin and the Kv1.1 channel: voltage-dependent binding upon enantiomerization of the scorpion toxin disulfide bridge Cys31-Cys34.	Disulfides	105-114	potassium voltage-gated channel subfamily A member 1	Rattus norvegicus	19-24
10671517-0	2000	ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum.	Disulfides	36-45	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	0-6
10671517-5	2000	ERO1-L is able to complement several phenotypic traits of the yeast thermosensitive mutant ero1-1, including temperature and dithiothreitol sensitivity, and intrachain disulfide bond formation in carboxypeptidase Y.	Disulfides	168-177	endoplasmic reticulum oxidoreductase 1 alpha	Homo sapiens	0-6
10694815-2	2000	A chimeric protein consisting of a scFv of mAb 145.2C11, the hinge-CH2-CH3 region of human IgG1, and the transmembrane and cytosolic domains of murine CD80 formed disulfide-linked dimers on the plasma membrane of cells and specifically bound lymphocytes.	Disulfides	163-172	LOC105243590	Mus musculus	91-95
10644727-3	2000	A unique characteristic of MMP-9 is its ability to exist in a monomeric and a disulfide-bonded dimeric form.	Disulfides	78-87	matrix metallopeptidase 9	Homo sapiens	27-32
10667587-2	2000	Here, we present evidence indicating that subsequent reduction of surface protein disulfides with N-acetyl-L-cysteine (NAC) further augments the immunogenic potential of PCL-modified tumor cells both in vitro and in vivo.	Disulfides	82-92	X-linked Kx blood group	Homo sapiens	119-122
10604596-1	1999	We have assigned the disulfide structure of Md-65 agouti-related protein (Md65-AGRP) using differential reduction and alkylation followed by direct sequencing analysis.	Disulfides	21-30	agouti related neuropeptide	Homo sapiens	50-72
10604596-1	1999	We have assigned the disulfide structure of Md-65 agouti-related protein (Md65-AGRP) using differential reduction and alkylation followed by direct sequencing analysis.	Disulfides	21-30	agouti related neuropeptide	Homo sapiens	79-83
10604596-4	1999	The disulfide bonds in the cystine knot structure of Md65-AGRP were partially reduced using tris(2-carboxyethyl) phosphine (TCEP) under acidic conditions, followed by alkylation with N-ethylmaleimide (NEM).	Disulfides	4-13	agouti related neuropeptide	Homo sapiens	58-62
10604596-8	1999	The results confirmed that Md65-AGRP contained the same disulfide structure as that of Md5-AGRP reported previously [Bures, E. J., Hui, J. O., Young, Y. et al.	Disulfides	56-65	agouti related neuropeptide	Homo sapiens	32-36
10555972-5	1999	In contrast, although the starting affinity was lower for the disulfide elastin-turn mutant, it exhibited a 21-fold improvement in affinity over the same temperature range.	Disulfides	62-71	elastin	Homo sapiens	72-79
10581002-9	1999	In vitro dissociation tests of the purified PSP94-bound complexes showed that the binding of serum PSP94-complexes is probably via disulfide bonds and is chemically stable.	Disulfides	131-140	microseminoprotein beta	Homo sapiens	44-49
10581002-9	1999	In vitro dissociation tests of the purified PSP94-bound complexes showed that the binding of serum PSP94-complexes is probably via disulfide bonds and is chemically stable.	Disulfides	131-140	microseminoprotein beta	Homo sapiens	99-104
10571063-0	1999	Engineering an unnatural Nalpha-anchored disulfide into BPTI by total chemical synthesis: structural and functional consequences.	Disulfides	41-50	spleen trypsin inhibitor I	Bos taurus	56-60
10571063-1	1999	A disulfide-engineered analogue of bovine pancreatic trypsin inhibitor (BPTI), ((N(alpha)-(CH2)2S-)Gly38)BPTI, has been prepared using a thioester-mediated auxiliary functional group chemical ligation of a N(alpha)-ethanethiol-containing peptide segment with a peptide-alphaCOSR segment.	Disulfides	2-11	spleen trypsin inhibitor I	Bos taurus	35-70
10571063-1	1999	A disulfide-engineered analogue of bovine pancreatic trypsin inhibitor (BPTI), ((N(alpha)-(CH2)2S-)Gly38)BPTI, has been prepared using a thioester-mediated auxiliary functional group chemical ligation of a N(alpha)-ethanethiol-containing peptide segment with a peptide-alphaCOSR segment.	Disulfides	2-11	spleen trypsin inhibitor I	Bos taurus	72-76
10571063-1	1999	A disulfide-engineered analogue of bovine pancreatic trypsin inhibitor (BPTI), ((N(alpha)-(CH2)2S-)Gly38)BPTI, has been prepared using a thioester-mediated auxiliary functional group chemical ligation of a N(alpha)-ethanethiol-containing peptide segment with a peptide-alphaCOSR segment.	Disulfides	2-11	spleen trypsin inhibitor I	Bos taurus	105-109
10463938-4	1999	We show that changes in the ratio of reduced to oxidized glutathione provide the potential to oxidize c-Jun sulfhydryls by mechanisms that include both protein disulfide formation and S-glutathiolation.	Disulfides	160-169	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	102-107
10493584-0	1999	Early events in the disulfide-coupled folding of BPTI.	Disulfides	20-29	spleen trypsin inhibitor I	Bos taurus	49-53
10493584-1	1999	Recent studies of the refolding of reduced bovine pancreatic trypsin inhibitor (BPTI) have shown that a previously unidentified intermediate with a single disulfide is formed much more rapidly than any other one-disulfide species.	Disulfides	155-164	spleen trypsin inhibitor I	Bos taurus	80-84
10493584-1	1999	Recent studies of the refolding of reduced bovine pancreatic trypsin inhibitor (BPTI) have shown that a previously unidentified intermediate with a single disulfide is formed much more rapidly than any other one-disulfide species.	Disulfides	212-221	spleen trypsin inhibitor I	Bos taurus	80-84
10383387-9	1999	These results indicate that both disulfide bonds of CCR5 are necessary for maintaining the structural integrity of the receptor necessary for ligand binding and signaling.	Disulfides	33-42	C-C motif chemokine receptor 5	Homo sapiens	52-56
10369668-1	1999	The thiol/disulfide oxidoreductase DsbA is the strongest oxidant of the thioredoxin superfamily and is required for efficient disulfide bond formation in the periplasm of Escherichia coli.	Disulfides	10-19	oxidoreductase	Escherichia coli	20-34
10336646-3	1999	The peptide, containing residues 71-93 of transthyretin with its termini linked via a disulfide bond, was found to possess the same helix-turn motif as in the corresponding region of the crystallographically derived structure of transthyretin in 20% trifluoroethanol (TFE) solution.	Disulfides	86-95	transthyretin	Homo sapiens	42-55
10336646-3	1999	The peptide, containing residues 71-93 of transthyretin with its termini linked via a disulfide bond, was found to possess the same helix-turn motif as in the corresponding region of the crystallographically derived structure of transthyretin in 20% trifluoroethanol (TFE) solution.	Disulfides	86-95	transthyretin	Homo sapiens	229-242
10336489-3	1999	Although nitric oxide induced the formation of an intermolecular disulfide bridge between cysteine residues in the leucine zipper site of c-Jun monomers, this same radical directed the covalent incorporation of stoichiometric amounts of glutathione to a single conserved cysteine residue in the DNA-binding site of the protein.	Disulfides	65-74	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	138-143
10336489-6	1999	In conclusion, our results support the reversible formation of a mixed disulfide between glutathione and c-Jun as a potential mechanism by which nitrosative stress may be transduced into a functional response at the level of transcription.	Disulfides	71-80	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	105-110
10329657-6	1999	Surface enzyme-linked immunosorbent assay detection of both mutant receptors showed &lt;10% expression, suggesting that a critical disulfide bridge between EL2 and the upper part of transmembrane 3, as found in many other G protein-coupled receptors, is required for proper trafficking of the P2Y1 receptor to the cell surface.	Disulfides	131-140	spectrin alpha, erythrocytic 1	Homo sapiens	156-159
10350478-2	1999	Using a simple increase in pH to promote disulfide bond formation, three cross-links between residues on the extracellular side of TM5 (at positions 198, 200, and 204) and TM6 (at position 276) have been identified and characterized.	Disulfides	41-50	tropomyosin 3	Homo sapiens	131-134
10350478-4	1999	Rhodopsin mutants containing these disulfides demonstrate nativelike absorption spectra and light-dependent activation of transducin, suggesting that large movements on the extracellular side of TM5 with respect to TM6 are not required for receptor activation.	Disulfides	35-45	tropomyosin 3	Homo sapiens	195-198
10231542-2	1999	Short-term treatment of intact cells expressing large numbers of IR with GSH or NAC led to a rapid and reversible reduction of IR alpha-subunit disulfides, without affecting the receptor beta-subunit thiol reactivity.	Disulfides	144-154	X-linked Kx blood group	Homo sapiens	80-83
10231542-8	1999	Our results provide the first evidence that the IR alpha-subunit contains a select group of disulfides whose redox status can be rapidly altered by the reducing agents GSH and NAC.	Disulfides	92-102	X-linked Kx blood group	Homo sapiens	176-179
10206995-10	1999	These data indicate that impaired secretion of the naturally occurring C518R and C941Y mutant factor H proteins is due to disruption of framework-specific disulfide bonds in factor H short consensus repeat modules.	Disulfides	155-164	complement factor H	Homo sapiens	94-102
10206995-10	1999	These data indicate that impaired secretion of the naturally occurring C518R and C941Y mutant factor H proteins is due to disruption of framework-specific disulfide bonds in factor H short consensus repeat modules.	Disulfides	155-164	complement factor H	Homo sapiens	174-182
10090736-2	1999	Site-directed mutagenesis of the three extracellular loops (ELs) of the human P2Y1 receptor indicates the existence of two essential disulfide bridges (Cys124 in EL1 and Cys202 in EL2; Cys42 in the N-terminal segment and Cys296 in EL3) and several specific ionic and H-bonding interactions (involving Glu209 and Arg287).	Disulfides	133-142	erythrocyte membrane protein band 4.1	Homo sapiens	162-165
10090736-2	1999	Site-directed mutagenesis of the three extracellular loops (ELs) of the human P2Y1 receptor indicates the existence of two essential disulfide bridges (Cys124 in EL1 and Cys202 in EL2; Cys42 in the N-terminal segment and Cys296 in EL3) and several specific ionic and H-bonding interactions (involving Glu209 and Arg287).	Disulfides	133-142	spectrin alpha, erythrocytic 1	Homo sapiens	180-183
10049680-14	1999	Native mMRP14 contains one intramolecular disulfide bond between Cys79 and Cys90.	Disulfides	42-51	S100 calcium binding protein A9 (calgranulin B)	Mus musculus	7-13
10022822-2	1999	The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges.	Disulfides	110-119	erythrocyte membrane protein band 4.1	Homo sapiens	21-24
10024473-6	1999	Thus, the yield of active ATP N peroxidase can be increased 50-fold by using thioredoxin reductase negative strains, which facilitate the formation of disulfide bonds in inclusion body protein.	Disulfides	151-160	prx7	Hordeum vulgare	32-42
9916711-6	1999	The TCR signaling efficacy was dramatically reduced during peptide/MHC engagement in the zeta mutants containing the displaced disulfide bond.	Disulfides	127-136	major histocompatibility complex, class I, C	Homo sapiens	67-70
9886834-1	1999	The human GH receptor (hGHR) contains nine intracellular and seven extracellular cysteines, of which six are linked by disulfide bonds and one, at position 241 proximal to the membrane, is free.	Disulfides	119-128	growth hormone receptor	Homo sapiens	10-21
9886834-1	1999	The human GH receptor (hGHR) contains nine intracellular and seven extracellular cysteines, of which six are linked by disulfide bonds and one, at position 241 proximal to the membrane, is free.	Disulfides	119-128	growth hormone receptor	Homo sapiens	23-27
9886240-2	1999	MIC-1 is synthesized as a 62-kDa intracellular protein, which, after cleavage by a furin like protease, is secreted as a 25-kDa disulfide-linked dimeric protein.	Disulfides	128-137	growth differentiation factor 15	Homo sapiens	0-5
10195446-2	1999	It has been found that charcoal effectively, selectively and rapidly removes iodine by solid phase extraction from reaction mixtures in which it is used to convert the acetamidomethyl protected precursors of oxytocin or a peptide from the Pre-S1 region of hepatitis B virus into their intramolecularly disulfide-bonded products.	Disulfides	302-311	large envelope protein;middle envelope protein;small envelope protein	Hepatitis B virus	239-245
9852069-4	1998	We previously characterized KARAP (killer cell activating receptor-associated protein), a novel disulfide-linked tyrosine-phosphorylated dimer that selectively associates with the activating NKR isoforms.	Disulfides	96-105	TYRO protein tyrosine kinase binding protein	Mus musculus	28-33
9852069-4	1998	We previously characterized KARAP (killer cell activating receptor-associated protein), a novel disulfide-linked tyrosine-phosphorylated dimer that selectively associates with the activating NKR isoforms.	Disulfides	96-105	TYRO protein tyrosine kinase binding protein	Mus musculus	35-85
9851830-7	1998	Peroxynitrite-inactivated GAPDH was resistant to arsenite reduction and only 15% recovered by 20 mM dithiothreitol, suggesting that GAPDH-SH has been mainly oxidized to sulfinic or sulfonic acid, with a minor proportion yielding a disulfide.	Disulfides	231-240	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	26-31
9851830-7	1998	Peroxynitrite-inactivated GAPDH was resistant to arsenite reduction and only 15% recovered by 20 mM dithiothreitol, suggesting that GAPDH-SH has been mainly oxidized to sulfinic or sulfonic acid, with a minor proportion yielding a disulfide.	Disulfides	231-240	glyceraldehyde-3-phosphate dehydrogenase	Oryctolagus cuniculus	132-137
9876928-1	1998	Mixed disulfide derivatives of bovine beta-lactoglobulin (BLG) were studied by circular dichroism (CD), gel-permeation HPLC and high-sensitivity differential scanning calorimetry (HS-DSC).	Disulfides	6-15	beta-lactoglobulin	Bos taurus	38-56
9876928-1	1998	Mixed disulfide derivatives of bovine beta-lactoglobulin (BLG) were studied by circular dichroism (CD), gel-permeation HPLC and high-sensitivity differential scanning calorimetry (HS-DSC).	Disulfides	6-15	beta-lactoglobulin	Bos taurus	58-61
9774716-0	1998	Thiol/disulfide exchange between small heat shock protein 25 and glutathione.	Disulfides	6-15	heat shock protein 1	Mus musculus	39-60
9774716-2	1998	In glutathione redox buffers, Hsp25 equilibrates between reduced protein (PSH), mixed disulfide (PSSG) and protein dimer (PSSP) forms.	Disulfides	86-95	heat shock protein 1	Mus musculus	30-35
9774716-8	1998	At a constant R, the fractions of PSSG and PSH species depend similarly on GSH concentration, being approximately equal in glutathione redox buffers with low R. It is concluded that in oligomeric complexes, Hsp25 subunits in vitro form stable dimers, in which the reacting -SH groups are in a proximity to form intersubunit disulfide bonds.	Disulfides	324-333	heat shock protein 1	Mus musculus	207-212
9724530-0	1998	Determination of disulfide structure in agouti-related protein (AGRP) by stepwise reduction and alkylation.	Disulfides	17-26	agouti related neuropeptide	Homo sapiens	40-62
9724530-0	1998	Determination of disulfide structure in agouti-related protein (AGRP) by stepwise reduction and alkylation.	Disulfides	17-26	agouti related neuropeptide	Homo sapiens	64-68
9724530-3	1998	The disulfide structure of recombinant human AGRP was determined by chemical methods using partial reduction with tris(2-carboxyethyl)phosphine under acidic conditions, followed by direct alkylation with N-ethylmaleimide or fluorescein-5-maleimide.	Disulfides	4-13	agouti related neuropeptide	Homo sapiens	45-49
9724530-5	1998	The resulting proteins were characterized by peptide mapping, sequence analysis, and mass spectrometry, showing that AGRP contained a highly reducible disulfide bond, C85-C109, followed by less reactive ones, C90-C97, C74-C88, C67-C82, and C81-C99, respectively.	Disulfides	151-160	agouti related neuropeptide	Homo sapiens	117-121
9724530-6	1998	The chemically defined disulfide connectivity of the recombinant human AGRP was homologous to that of omega-agatoxin IVB except for an additional disulfide bond, C85-C109.	Disulfides	23-32	agouti related neuropeptide	Homo sapiens	71-75
9724530-6	1998	The chemically defined disulfide connectivity of the recombinant human AGRP was homologous to that of omega-agatoxin IVB except for an additional disulfide bond, C85-C109.	Disulfides	146-155	agouti related neuropeptide	Homo sapiens	71-75
9668102-4	1998	The thioredoxin domain of TRP32 has thioredoxin-like reducing activity, which can reduce the interchain disulfide bridges of insulin in vitro.	Disulfides	104-113	thioredoxin like 1	Homo sapiens	26-31
9660815-10	1998	Immunoblotting analysis indicated that LTBP-4 was secreted from cultured human lung fibroblasts both in a free form and in a disulfide bound complex with a TGF-beta.	Disulfides	125-134	latent transforming growth factor beta binding protein 4	Homo sapiens	39-45
9713325-6	1998	Clusterin expressed in the pancreas was shown by Western blot analysis to be a disulfide-linked heterodimer of 70 kDa with an alpha-subunit of 32 kDa.	Disulfides	79-88	clusterin	Rattus norvegicus	0-9
9684891-3	1998	To illustrate our strategy, we synthesized the naturally occurring circulin B and cyclopsychotride (CPT), both consisting of 31 amino acid residues tightly packed in a cystine-knot motif with three disulfide bonds and an end-to-end cyclic form.	Disulfides	198-207	choline phosphotransferase 1	Homo sapiens	100-103
9603903-4	1998	The experiments reported here show that both MAO A and MAO B contain a redox-active disulfide at the catalytic center.	Disulfides	84-93	monoamine oxidase B	Homo sapiens	55-60
9601043-1	1998	A single-disulfide variant of bovine pancreatic trypsin inhibitor (BPTI), [14-38]Abu, is a partially folded ensemble which includes two, and in one case three, conformations that interconvert slowly enough to exhibit separate cross-peaks in the amide region of homonuclear and heteronuclear NMR spectra.	Disulfides	9-18	spleen trypsin inhibitor I	Bos taurus	67-71
12014113-4	1998	The results of SDS-PAGE silver staining and western blotting showed that hCG beta-oLH alpha single peptide chain had apparent molecular weights of 40.5 kD and 38.0 kD under non-reducing and reducing conditions respectively, indicating the occurrence of disulfide bonds and significant tertiary structure in the single peptide chain.	Disulfides	253-262	chorionic gonadotropin subunit beta 3	Homo sapiens	73-81
9442046-3	1998	Disulfide bonding among tenascin subunits mediates intracellular assembly into hexamers.	Disulfides	0-9	tenascin C	Homo sapiens	24-32
9374679-4	1997	The detergent-insoluble receptor pool was progressively enriched in an apparent disulfide-linked form of the hGHR.	Disulfides	80-89	growth hormone receptor	Homo sapiens	109-113
9374679-5	1997	Exposure to hGH at 4 degrees C allowed hGH-induced hGHR disulfide linkage but did not promote changes in receptor detergent solubility, indicating that hGHR detergent insolubility cannot be explained solely by the formation of that linkage.	Disulfides	56-65	growth hormone receptor	Homo sapiens	51-55
9346903-7	1997	We therefore hypothesized that the small subunit of MTP, protein-disulfide isomerase (PDI), plays a role in apoB secretion by facilitating correct disulfide bond formation.	Disulfides	65-74	microsomal triglyceride transfer protein	Homo sapiens	52-55
9326233-1	1997	The platelet glycoprotein Ib (GpIb) complex is composed of four polypeptides: the disulfide-linked GpIb alpha and GpIb beta and the noncovalently associated GpIX and GpV.	Disulfides	82-91	glycoprotein Ib platelet subunit alpha	Homo sapiens	99-109
9326233-9	1997	HUVEC GpIb beta, in contrast to its platelet counterpart, has a molecular weight of 50 kD and forms a correspondingly larger disulfide-bonded complex with EC GpIb alpha.	Disulfides	125-134	glycoprotein Ib platelet subunit beta	Homo sapiens	6-15
9326233-9	1997	HUVEC GpIb beta, in contrast to its platelet counterpart, has a molecular weight of 50 kD and forms a correspondingly larger disulfide-bonded complex with EC GpIb alpha.	Disulfides	125-134	glycoprotein Ib platelet subunit alpha	Homo sapiens	158-168
9283080-0	1997	Peptidylglycine alpha-hydroxylating monooxygenase: active site residues, disulfide linkages, and a two-domain model of the catalytic core.	Disulfides	73-82	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	0-49
9299449-2	1997	Since Lp(a) is produced by a disulfide linkage between apolipoprotein(a) [apo(a)] and apolipoproteinB-100 (apoB-100) of low density lipoprotein (LDL) on the hepatocyte surface, modulation of either particle may be useful in lowering Lp(a).	Disulfides	29-38	apolipoprotein(a)	Macaca fascicularis	6-11
9299449-2	1997	Since Lp(a) is produced by a disulfide linkage between apolipoprotein(a) [apo(a)] and apolipoproteinB-100 (apoB-100) of low density lipoprotein (LDL) on the hepatocyte surface, modulation of either particle may be useful in lowering Lp(a).	Disulfides	29-38	apolipoprotein(a)	Macaca fascicularis	233-238
9299452-3	1997	rHDL containing apolipoprotein A-I (apoA-I), the disulfide-linked form of the apoA-IMilano variant, or apoA-II, were all effective in inhibiting the expression of vascular cell adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 in TNF alpha- or LPS-stimulated HUVEC.	Disulfides	49-58	intercellular adhesion molecule 1	Homo sapiens	210-243
9327340-2	1997	Complement C3 was detected as a molecule composed of a 115-kDa alpha-chain linked to a 70-kDa beta chain by disulfide bonds, and C3 levels ranged from 0.52 to 15.0 micrograms/ml (n = 15).	Disulfides	108-117	complement C3	Homo sapiens	0-13
9257722-0	1997	Disulfide-bonding between Drosophila laminin beta and gamma chains is essential for alpha chain to form alpha betagamma trimer.	Disulfides	0-9	LanB1	Drosophila melanogaster	37-49
9430198-2	1997	wt protein with two redox-active cysteine residues, together with thioredoxin reductase and NADPH, may reduce protein disulfides and thereby act as a molecular probe of their structure and reactivity.	Disulfides	118-128	2,4-dienoyl-CoA reductase 1	Homo sapiens	92-97
9430198-10	1997	A small but significant NADPH consumption by IgG2 myeloma proteins suggested reduction of a labile interchain or surface-exposed mixed disulfide.	Disulfides	135-144	2,4-dienoyl-CoA reductase 1	Homo sapiens	24-29
9332831-5	1997	The 2-benzisothiazolones are formed from the disulfides both chemically and in vivo and their SAR mimics that of the 2,2"-dithiobisbenzamides.	Disulfides	45-55	sarcosine dehydrogenase	Homo sapiens	94-97
9154151-13	1997	However, the disulfide bridge in this region of SPARC was found to be critical, as injection of peptide 4.2AA, a mutant lacking the cystine, generated no axial defects.	Disulfides	13-22	secreted protein, acidic, cysteine-rich (osteonectin) S homeolog	Xenopus laevis	48-53
9154151-15	1997	Moreover, we have identified at least one bioactive region of SPARC as the C-terminal disulfide-bonded, Ca(2+)-binding loop that was previously shown to be both counteradhesive and growth-inhibitory.	Disulfides	86-95	secreted protein, acidic, cysteine-rich (osteonectin) S homeolog	Xenopus laevis	62-67
9092579-8	1997	We conclude that: 1) folding of the amino-terminal disulfide bonded domain of apoB is achieved prior to the completion of translation and is independent of MTP and events associated with buoyant lipoprotein formation and 2) domain-specific folding of apoBs amino-terminal region is required to initiate MTP-dependent lipid transfer to nascent apoB in the hepatic endoplasmic reticulum.	Disulfides	51-60	apolipoprotein B-100	Cricetulus griseus	78-82
9092579-8	1997	We conclude that: 1) folding of the amino-terminal disulfide bonded domain of apoB is achieved prior to the completion of translation and is independent of MTP and events associated with buoyant lipoprotein formation and 2) domain-specific folding of apoBs amino-terminal region is required to initiate MTP-dependent lipid transfer to nascent apoB in the hepatic endoplasmic reticulum.	Disulfides	51-60	apolipoprotein B-100	Cricetulus griseus	251-255
9092584-0	1997	Role of glycosylation and disulfide bond formation in the beta subunit in the folding and functional expression of Na,K-ATPase.	Disulfides	26-35	ATPase Na+/K+ transporting subunit beta 1 L homeolog	Xenopus laevis	115-126
9242985-3	1997	In addition, combined treatment of disulfide-linked Vn multimers with L-Arg, urea, and reducing agent results in the formation of disperse oligomers with reduced expression of denaturation-sensitive epitopes.	Disulfides	35-44	vitronectin	Homo sapiens	52-54
9132026-1	1997	The native-like two-disulfide intermediate of bovine pancreatic trypsin inhibitor (BPTI), with the disulfide between Cys14 and Cys38 reduced, plays a particularly important role in the disulfide-coupled folding pathway of BPTI because of its participation in the rate-determining step of the reaction [Creighton &amp; Goldenberg (1984) J. Mol.	Disulfides	20-29	spleen trypsin inhibitor I	Bos taurus	46-81
9132026-1	1997	The native-like two-disulfide intermediate of bovine pancreatic trypsin inhibitor (BPTI), with the disulfide between Cys14 and Cys38 reduced, plays a particularly important role in the disulfide-coupled folding pathway of BPTI because of its participation in the rate-determining step of the reaction [Creighton &amp; Goldenberg (1984) J. Mol.	Disulfides	20-29	spleen trypsin inhibitor I	Bos taurus	83-87
9132026-1	1997	The native-like two-disulfide intermediate of bovine pancreatic trypsin inhibitor (BPTI), with the disulfide between Cys14 and Cys38 reduced, plays a particularly important role in the disulfide-coupled folding pathway of BPTI because of its participation in the rate-determining step of the reaction [Creighton &amp; Goldenberg (1984) J. Mol.	Disulfides	20-29	spleen trypsin inhibitor I	Bos taurus	222-226
9132026-1	1997	The native-like two-disulfide intermediate of bovine pancreatic trypsin inhibitor (BPTI), with the disulfide between Cys14 and Cys38 reduced, plays a particularly important role in the disulfide-coupled folding pathway of BPTI because of its participation in the rate-determining step of the reaction [Creighton &amp; Goldenberg (1984) J. Mol.	Disulfides	99-108	spleen trypsin inhibitor I	Bos taurus	46-81
9132026-1	1997	The native-like two-disulfide intermediate of bovine pancreatic trypsin inhibitor (BPTI), with the disulfide between Cys14 and Cys38 reduced, plays a particularly important role in the disulfide-coupled folding pathway of BPTI because of its participation in the rate-determining step of the reaction [Creighton &amp; Goldenberg (1984) J. Mol.	Disulfides	99-108	spleen trypsin inhibitor I	Bos taurus	83-87
9132026-1	1997	The native-like two-disulfide intermediate of bovine pancreatic trypsin inhibitor (BPTI), with the disulfide between Cys14 and Cys38 reduced, plays a particularly important role in the disulfide-coupled folding pathway of BPTI because of its participation in the rate-determining step of the reaction [Creighton &amp; Goldenberg (1984) J. Mol.	Disulfides	99-108	spleen trypsin inhibitor I	Bos taurus	222-226
9132026-4	1997	In order to study directly the relationship between conformational stability and reductive unfolding kinetics, and to gain insight concerning the rate-limiting transition state in the thiol/disulfide-mediated folding/unfolding reaction of BPTI, BPTI variants based on a native-like two-disulfide analog of this intermediate, BPTI(Ala14)Ala38, were examined.	Disulfides	190-199	spleen trypsin inhibitor I	Bos taurus	239-243
9132026-4	1997	In order to study directly the relationship between conformational stability and reductive unfolding kinetics, and to gain insight concerning the rate-limiting transition state in the thiol/disulfide-mediated folding/unfolding reaction of BPTI, BPTI variants based on a native-like two-disulfide analog of this intermediate, BPTI(Ala14)Ala38, were examined.	Disulfides	190-199	spleen trypsin inhibitor I	Bos taurus	245-249
9132026-4	1997	In order to study directly the relationship between conformational stability and reductive unfolding kinetics, and to gain insight concerning the rate-limiting transition state in the thiol/disulfide-mediated folding/unfolding reaction of BPTI, BPTI variants based on a native-like two-disulfide analog of this intermediate, BPTI(Ala14)Ala38, were examined.	Disulfides	190-199	spleen trypsin inhibitor I	Bos taurus	245-249
9132026-6	1997	The kinetic stability, with respect to reduction by dithiothreitol, of the disulfides in these BPTI(Ala14)Ala38 variants was also decreased by the substitutions.	Disulfides	75-85	spleen trypsin inhibitor I	Bos taurus	95-99
9054363-1	1997	Disrupting disulfide loops in the human chorionic gonadotropin beta subunit (CGbeta) inhibits combination with the alpha subunit.	Disulfides	11-20	chorionic gonadotropin subunit beta 3	Homo sapiens	40-75
9054363-1	1997	Disrupting disulfide loops in the human chorionic gonadotropin beta subunit (CGbeta) inhibits combination with the alpha subunit.	Disulfides	11-20	chorionic gonadotropin subunit beta 3	Homo sapiens	77-83
9133623-1	1997	alpha-Lactalbumin in which all the disulfide bonds are fully reduced (RLA) is known to bind strongly to the chaperonin GroEL.	Disulfides	35-44	heat shock protein family D (Hsp60) member 1	Homo sapiens	119-124
9032072-9	1997	CONCLUSIONS: The crystal structure of the kallikrein-hirustasin complex reveals that hirustasin differs from other serine protease inhibitors in its conformation and its disulfide bond connectivity, making it the prototype for a new class of inhibitor.	Disulfides	170-179	kallikrein related peptidase 4	Homo sapiens	42-52
9048894-9	1997	The enzyme inhibition by alloxan was accompanied by a change in the electrophoretic mobility with a second lower molecular 49 kDa glucokinase band which can be interpreted as a compact glucokinase molecule locked by disulfide bonds.	Disulfides	216-225	glucokinase	Homo sapiens	130-141
9048894-9	1997	The enzyme inhibition by alloxan was accompanied by a change in the electrophoretic mobility with a second lower molecular 49 kDa glucokinase band which can be interpreted as a compact glucokinase molecule locked by disulfide bonds.	Disulfides	216-225	glucokinase	Homo sapiens	185-196
9106167-1	1997	Thioredoxin is a highly conserved disulfide reducing protein whose structure and biochemical properties have been extensively studied.	Disulfides	34-43	uncharacterized protein	Drosophila melanogaster	0-11
9006939-8	1997	Trx2 possessed a dithiol-reducing enzymatic activity and, with mammalian thioredoxin reductase and NADPH, was able to reduce the interchain disulfide bridges of insulin.	Disulfides	140-149	2,4-dienoyl-CoA reductase 1	Homo sapiens	99-104
9030770-8	1997	This disulfide arrangement has been observed in other proteins, e.g. in human prostatic acid phosphatase, but the spacing between the cystines differs.	Disulfides	5-14	acid phosphatase 3	Homo sapiens	78-104
9685994-1	1997	The thyrotropin (TSH) receptor in human-thyroid glands is cleaved into an extracellular alpha subunit and a transmembrane beta subunit held together by disulfide bridges.	Disulfides	152-161	thyroid stimulating hormone receptor	Homo sapiens	4-30
9685994-7	1997	Shedding of the TSH receptor alpha domain is the consequence of two events: cleavage of the proreceptor into alpha and beta subunits and reduction of the disulfide bridge(s).	Disulfides	154-163	thyroid stimulating hormone receptor	Homo sapiens	16-28
9685994-8	1997	The use of different specific inhibitors including monoclonal antibodies allowed us to implicate the enzyme protein disulfide isomerase in the reduction of TSHR disulfide bounds.	Disulfides	116-125	thyroid stimulating hormone receptor	Homo sapiens	156-160
9035103-1	1997	Interleukin-12 (IL-12) is unique amongst cytokines in being a disulfide-linked heterodimer of two separately encoded subunits (p35 and p40).	Disulfides	62-71	interleukin 12b	Mus musculus	135-138
9485507-5	1997	However, satisfactory predictions were achieved in one case, pig NK-lysin (target 42), a 78-residue protein with three disulfide bridges.	Disulfides	119-128	granulysin	Sus scrofa	65-73
8955184-1	1996	The CD94 NK cell receptor is assembled as a disulfide-linked dimer and appears to be encoded by a single-copy gene of the C-type lectin superfamily.	Disulfides	44-53	killer cell lectin like receptor D1	Homo sapiens	4-8
8997239-4	1996	Chemical reduction of disulfide linkages disaggregated GC-C in fed but not fasted rat samples, causing it to migrate as smaller forms (approximately 220 and 240 kDa).	Disulfides	22-31	guanylate cyclase 2C	Rattus norvegicus	55-59
8943374-0	1996	Human natural killer cell receptors involved in MHC class I recognition are disulfide-linked heterodimers of CD94 and NKG2 subunits.	Disulfides	76-85	killer cell lectin like receptor D1	Homo sapiens	109-113
8943374-2	1996	We now demonstrate that CD94 glycoproteins form disulfide-bonded heterodimers with the NKG2A/B, NKG2C, and NKG2E glycoproteins.	Disulfides	48-57	killer cell lectin like receptor D1	Homo sapiens	24-28
8955366-4	1996	Increases of 3- to 4-fold in the oxidation constants for both S-adenosylmethionine synthetase isoenzymes in the presence of protein disulfide isomerase suggested the possibility of a thiol-disulfide exchange regulatory mechanism for this enzyme in vivo.	Disulfides	132-141	methionine adenosyltransferase 1A	Rattus norvegicus	62-93
8917542-1	1996	Biochemical studies have shown that the periplasmic protein disulfide oxidoreductase DsbC can isomerize aberrant disulfide bonds.	Disulfides	60-69	oxidoreductase	Escherichia coli	70-84
8849679-0	1996	Determination of the disulfide array of the first inducible antifungal peptide from insects: drosomycin from Drosophila melanogaster.	Disulfides	21-30	Drosomycin	Drosophila melanogaster	93-103
8849679-1	1996	Drosomycin is a 44-residue antifungal peptide with four intramolecular disulfide bridges which have been isolated from immune-challenged Drosophila.	Disulfides	71-80	Drosomycin	Drosophila melanogaster	0-10
8849679-4	1996	Using a combination of Edman degradation and mass spectrometry, we show that drosomycin shares the same array of intramolecular disulfide bridges than plant defensins, in addition to their sequence similarities.	Disulfides	128-137	Drosomycin	Drosophila melanogaster	77-87
8814226-3	1996	In contrast to other tissues, the main molecular form of endometrial GRP is larger (6-8 kDa versus 1-3 kDa), and based on the increased hydrophobicity of its circulating form after reduction, contains at least one disulfide bond.	Disulfides	214-223	gastrin releasing peptide	Homo sapiens	69-72
9181070-4	1996	The different states of fibromodulin aggregation due to disulfide bonding demonstrable in different regions of the same joint suggest that the presence of different biomechanical forces results in the differential expression of small proteoglycans.	Disulfides	56-65	fibromodulin	Bos taurus	24-36
8812865-7	1996	Peptide mapping analysis derived from pepsin digestion of recombinant kallikrein assigned five disulfide bonds which match those of porcine kallikrein predicted from X-ray structure.	Disulfides	95-104	kallikrein related peptidase 4	Homo sapiens	70-80
8702885-2	1996	TNF-R p75 belongs to the TNF receptor superfamily characterized by cysteine-rich extracellular regions composed of three to six disulfide-linked domains.	Disulfides	128-137	TNF receptor superfamily member 1B	Homo sapiens	6-9
8781545-3	1996	Subsequent exposure to increasing levels of oxidative stress induced by tert-butylhydroperoxide resulted in decreased levels of ([3-13C]cysteinyl)-glutathione and a loss of 13C NMR resonance intensity, a reflection of protein-glutathione mixed disulfide formation.	Disulfides	244-253	telomerase reverse transcriptase	Bos taurus	72-76
9076635-5	1996	The result of this modeling study showed that the structure of cathepsin E is similar to that of porcine pepsin and has three disulfide bonds that are conserved in both enzymes.	Disulfides	126-135	cathepsin E	Homo sapiens	63-74
8703947-2	1996	The insect developmental factor bombyxin, the relaxin-like factor from Leydig cells, and the insulin-like factor 4 (INSL4) all are made of two disulfide-linked chains and have one disulfide bond within the A-chain.	Disulfides	143-152	insulin like 4	Homo sapiens	93-114
8703947-2	1996	The insect developmental factor bombyxin, the relaxin-like factor from Leydig cells, and the insulin-like factor 4 (INSL4) all are made of two disulfide-linked chains and have one disulfide bond within the A-chain.	Disulfides	143-152	insulin like 4	Homo sapiens	116-121
8703947-2	1996	The insect developmental factor bombyxin, the relaxin-like factor from Leydig cells, and the insulin-like factor 4 (INSL4) all are made of two disulfide-linked chains and have one disulfide bond within the A-chain.	Disulfides	180-189	insulin like 4	Homo sapiens	93-114
8703947-2	1996	The insect developmental factor bombyxin, the relaxin-like factor from Leydig cells, and the insulin-like factor 4 (INSL4) all are made of two disulfide-linked chains and have one disulfide bond within the A-chain.	Disulfides	180-189	insulin like 4	Homo sapiens	116-121
8670797-4	1996	If HA"s binding to CNX and CRT was inhibited using a glucosidase inhibitor, castanospermine (CST), the rate of disulfide formation and oligomerization was doubled but the overall efficiency of maturation of HA decreased due to aggregation and degradation.	Disulfides	111-120	calnexin	Canis lupus familiaris	19-22
8695913-0	1996	Biological activity of brain-derived neurotrophic factor with mismatched disulfide linkages produced by Escherichia coli.	Disulfides	73-82	brain-derived neurotrophic factor	Rattus norvegicus	23-56
8695913-2	1996	Ten different proteins of BDNF were purified from the precipitate and the three disulfide linkages of six proteins were identified.	Disulfides	80-89	brain-derived neurotrophic factor	Rattus norvegicus	26-30
8695913-3	1996	Those disulfide structures were different from that of authentic BDNF and the biological activities of BDNF with mismatched disulfide linkages (EC50 of 2 to 15 ng/ml) were much lower than that of authentic BDNF (EC50 of 30 pg/ml).	Disulfides	6-15	brain-derived neurotrophic factor	Rattus norvegicus	103-107
8695913-3	1996	Those disulfide structures were different from that of authentic BDNF and the biological activities of BDNF with mismatched disulfide linkages (EC50 of 2 to 15 ng/ml) were much lower than that of authentic BDNF (EC50 of 30 pg/ml).	Disulfides	6-15	brain-derived neurotrophic factor	Rattus norvegicus	103-107
8695913-3	1996	Those disulfide structures were different from that of authentic BDNF and the biological activities of BDNF with mismatched disulfide linkages (EC50 of 2 to 15 ng/ml) were much lower than that of authentic BDNF (EC50 of 30 pg/ml).	Disulfides	124-133	brain-derived neurotrophic factor	Rattus norvegicus	103-107
8695913-3	1996	Those disulfide structures were different from that of authentic BDNF and the biological activities of BDNF with mismatched disulfide linkages (EC50 of 2 to 15 ng/ml) were much lower than that of authentic BDNF (EC50 of 30 pg/ml).	Disulfides	124-133	brain-derived neurotrophic factor	Rattus norvegicus	103-107
8695913-4	1996	The BDNF with mismatched disulfide linkages inhibited the biological activity of authentic BDNF.	Disulfides	25-34	brain-derived neurotrophic factor	Rattus norvegicus	4-8
8695913-4	1996	The BDNF with mismatched disulfide linkages inhibited the biological activity of authentic BDNF.	Disulfides	25-34	brain-derived neurotrophic factor	Rattus norvegicus	91-95
8827452-5	1996	Thus, PHBP was a heterodimer composed of 50-kDa and 17-kDa subunits, bridged by a disulfide linkage.	Disulfides	82-91	hyaluronan binding protein 2	Homo sapiens	6-10
8647179-4	1996	The F4/80 molecule is synthesized as a single polypeptide chain which acquires numerous intramolecular disulfide bonds and requires an extended time period (T1/2 = 60 min) for transport to an endoglycosidase H-resistant form.	Disulfides	103-112	adhesion G protein-coupled receptor E1	Mus musculus	4-9
9026359-7	1996	Granulocytic protein p25 was found to be a product of oxidative cleavage of disulfide bridges in the p50 dimer.	Disulfides	76-85	tubulin polymerization promoting protein	Homo sapiens	21-24
8637916-3	1996	VEGF-B formed cell-surface-associated disulfide-linked homodimers and heterodimerized with VEGF when coexpressed.	Disulfides	38-47	vascular endothelial growth factor B	Homo sapiens	0-6
8626810-2	1996	The thyrotropin (TSH) receptor in human thyroid glands has been shown to be cleaved into an extracellular alpha subunit and a transmembrane beta subunit held together by disulfide bridges.	Disulfides	170-179	thyroid stimulating hormone receptor	Homo sapiens	4-30
8621699-7	1996	This region is located in an area encompassing a predicted disulfide bond between linearly distant cysteines in beta1 (Cys415-Cys671).	Disulfides	59-68	UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2	Homo sapiens	112-117
8635547-7	1996	These findings suggest that endogenous FGFR-1 in the LHA plays an important role in FGF-induced feeding suppression, while, in addition, the dissolving disulfide bond formation in aFGF fragments enhances their inhibitory effects on feeding.	Disulfides	152-161	fibroblast growth factor 1	Rattus norvegicus	180-184
8547274-0	1996	Preparation and characterization of a disulfide-linked bioconjugate of annexin V with the B-chain of urokinase: an improved fibrinolytic agent targeted to phospholipid-containing thrombi.	Disulfides	38-47	annexin A5	Rattus norvegicus	71-80
8555268-4	1996	(4) cPLA2 is insensitive to reduction; sPLA2 is inactivated by agents that reduce disulfide bonds.	Disulfides	82-91	phospholipase A2 group IIA	Homo sapiens	39-44
8907186-1	1996	Cathepsin E (CE) is the only known aspartic proteinase that exists as a homodimer consisting of two fully catalytically active monomers, which are covalently bound by a disulfide bond between two cysteine residues at the NH2-terminal region (Cys43 in human pro-CE).	Disulfides	169-178	cathepsin E	Homo sapiens	0-11
8907186-1	1996	Cathepsin E (CE) is the only known aspartic proteinase that exists as a homodimer consisting of two fully catalytically active monomers, which are covalently bound by a disulfide bond between two cysteine residues at the NH2-terminal region (Cys43 in human pro-CE).	Disulfides	169-178	cathepsin E	Homo sapiens	13-15
8907186-1	1996	Cathepsin E (CE) is the only known aspartic proteinase that exists as a homodimer consisting of two fully catalytically active monomers, which are covalently bound by a disulfide bond between two cysteine residues at the NH2-terminal region (Cys43 in human pro-CE).	Disulfides	169-178	cathepsin E	Homo sapiens	261-263
7499282-1	1995	Protein-disulfide isomerase (PDI) is an abundant protein of the endoplasmic reticulum that catalyzes dithiol oxidation and disulfide bond reduction and isomerization using the active site CGHC.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	29-32
7499282-6	1995	These results indicate that in vivo protein folding pathways contain intermediates with non-native disulfide bonds, and that the essential role of PDI is to unscramble these intermediates.	Disulfides	99-108	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	147-150
7498463-1	1995	The avian parvalbumin called CPV3 readily forms disulfide-linked oligomers.	Disulfides	48-57	parvalbumin	Homo sapiens	10-21
7578020-3	1995	Western blot analysis of COS-1 cells transiently transfected with full-length cDNA coding for either peripherin/rds or rom-1 indicates that each protein is expressed primarily as a disulfide-linked homodimer; recombinant peripherin/rds is glycosylated while recombinant rom-1 is not--akin to their counterparts in rod photoreceptor disk membranes.	Disulfides	181-190	retinal outer segment membrane protein 1	Homo sapiens	119-124
8570096-3	1995	We found that reductive alkylation of disulfide linkages eliminated the ability of secreted beta-APP to activate MAP kinase.	Disulfides	38-47	amyloid beta precursor protein	Rattus norvegicus	92-100
8570096-7	1995	These results suggest that the amino-terminal region of beta-APP is responsible for activation of MAP kinase and that it requires structural loops created by disulfide linkages for activity.	Disulfides	158-167	amyloid beta precursor protein	Rattus norvegicus	56-64
7574684-0	1995	Extracellular domain of neurotrophin receptor trkB: disulfide structure, N-glycosylation sites, and ligand binding.	Disulfides	52-61	brain derived neurotrophic factor	Homo sapiens	24-36
7650011-4	1995	Whereas GroEL did not bind to the immobilized native LA, it associated with the immobilized Ca(2+)-depleted, disulfide bond-reduced form of LA (rLA) rapidly (kon = 1.96 x 10(5) M-1 S-1) and dissociated extremely slowly (koff = 2.08 x 10(-4) S-1), giving a low dissociation constant (KD = 1.06 nM).	Disulfides	109-118	heat shock protein family D (Hsp60) member 1	Homo sapiens	8-13
7636210-3	1995	LTBP is disulfide-linked to the amino-terminal propeptide of latent TGF-beta.	Disulfides	8-17	latent transforming growth factor beta binding protein 1	Mus musculus	0-4
7636210-3	1995	LTBP is disulfide-linked to the amino-terminal propeptide of latent TGF-beta.	Disulfides	8-17	latent transforming growth factor beta binding protein 1	Mus musculus	68-76
7629114-5	1995	We demonstrate that the properties of the purified calnexin delta TMC correspond to those of full-length calnexin in canine microsomes with at least one intramolecular disulfide bond and binding to 45Ca2+.	Disulfides	168-177	calnexin	Canis lupus familiaris	51-59
7629114-5	1995	We demonstrate that the properties of the purified calnexin delta TMC correspond to those of full-length calnexin in canine microsomes with at least one intramolecular disulfide bond and binding to 45Ca2+.	Disulfides	168-177	calnexin	Canis lupus familiaris	105-113
7627335-1	1995	Calcitonin, calcitonin gene-related peptide, adrenomedullin and amylin are structurally related peptides with N-terminal 6-7 amino acid ring structures linked by a disulfide bridge and with amidated C-termini.	Disulfides	164-173	adrenomedullin	Homo sapiens	45-59
7538125-0	1995	The asparagine-linked oligosaccharides of the human chorionic gonadotropin beta subunit facilitate correct disulfide bond pairing.	Disulfides	107-116	chorionic gonadotropin subunit beta 3	Homo sapiens	52-87
7538125-4	1995	The inefficient folding of hCG-beta lacking both N-linked glycans correlated with the slow formation of the last three disulfide bonds (i.e. disulfides 23-72, 93-100, and 26-110) to form in the hCG-beta-folding pathway.	Disulfides	119-128	chorionic gonadotropin subunit beta 3	Homo sapiens	27-35
7538125-4	1995	The inefficient folding of hCG-beta lacking both N-linked glycans correlated with the slow formation of the last three disulfide bonds (i.e. disulfides 23-72, 93-100, and 26-110) to form in the hCG-beta-folding pathway.	Disulfides	141-151	chorionic gonadotropin subunit beta 3	Homo sapiens	27-35
7538125-6	1995	However, coexpression of the hCG-alpha gene enhanced folding and formation of disulfide bonds 23-72, 93-100, and 26-110 of hCG-beta lacking N-linked glycans.	Disulfides	78-87	chorionic gonadotropin subunit beta 3	Homo sapiens	123-131
7538125-8	1995	These data indicate that N-linked oligosaccharides assist hCG-beta subunit folding by facilitating disulfide bond formation.	Disulfides	99-108	chorionic gonadotropin subunit beta 3	Homo sapiens	58-66
7766677-1	1995	Tick anticoagulant peptide (TAP) is a disulfide rich potent inhibitor of factor Xa.	Disulfides	38-47	coagulation factor X	Homo sapiens	73-82
7648447-6	1995	The IL-2/IL-2R gamma c, but not the IL-2/IL-2R beta, complex exhibited enhanced mobility after SDS-polyacrylamide gel electrophoresis under nonreducing conditions, suggesting a more compact structure for gamma c as a result of intrachain disulfide bonds.	Disulfides	238-247	interleukin 2 receptor, alpha chain	Mus musculus	9-14
7707501-0	1995	Constitutive activation of a variant of the env-mpl oncogene product by disulfide-linked homodimerization.	Disulfides	72-81	endogenous retrovirus group K member 20	Homo sapiens	44-47
7719935-2	1995	IL-12 is a disulfide-linked heterodimeric cytokine composed of a 35-kDa light chain (p35) and a 40-kDa heavy chain (p40).	Disulfides	11-20	interleukin 12A	Homo sapiens	85-88
7876306-6	1995	We demonstrate that the difference between ISC and control beta-actin is the inaccessibility of two cysteine residues in ISC beta-actin to labeling by thiol reactive reagents; due to the formation of a disulfide bridge between cysteine284 and cysteine373 in ISC beta-actin, or alternatively another modification of cysteine284 and cysteine373 which is reversible with DTT and adds less than 100 D to the molecular weight of beta-actin.	Disulfides	202-211	POTE ankyrin domain family member F	Homo sapiens	59-69
7876306-6	1995	We demonstrate that the difference between ISC and control beta-actin is the inaccessibility of two cysteine residues in ISC beta-actin to labeling by thiol reactive reagents; due to the formation of a disulfide bridge between cysteine284 and cysteine373 in ISC beta-actin, or alternatively another modification of cysteine284 and cysteine373 which is reversible with DTT and adds less than 100 D to the molecular weight of beta-actin.	Disulfides	202-211	POTE ankyrin domain family member F	Homo sapiens	125-135
7876306-6	1995	We demonstrate that the difference between ISC and control beta-actin is the inaccessibility of two cysteine residues in ISC beta-actin to labeling by thiol reactive reagents; due to the formation of a disulfide bridge between cysteine284 and cysteine373 in ISC beta-actin, or alternatively another modification of cysteine284 and cysteine373 which is reversible with DTT and adds less than 100 D to the molecular weight of beta-actin.	Disulfides	202-211	POTE ankyrin domain family member F	Homo sapiens	125-135
7876306-6	1995	We demonstrate that the difference between ISC and control beta-actin is the inaccessibility of two cysteine residues in ISC beta-actin to labeling by thiol reactive reagents; due to the formation of a disulfide bridge between cysteine284 and cysteine373 in ISC beta-actin, or alternatively another modification of cysteine284 and cysteine373 which is reversible with DTT and adds less than 100 D to the molecular weight of beta-actin.	Disulfides	202-211	POTE ankyrin domain family member F	Homo sapiens	125-135
7533087-3	1995	Here, we show that a disulfide-bonded dimer of CD44, formed by substituting the transmembrane region of CD3 zeta chain for that of CD44, binds Fl-HA, even when the cytoplasmic domain of the CD44 dimer is absent.	Disulfides	21-30	CD44 molecule (Indian blood group)	Homo sapiens	47-51
7533087-3	1995	Here, we show that a disulfide-bonded dimer of CD44, formed by substituting the transmembrane region of CD3 zeta chain for that of CD44, binds Fl-HA, even when the cytoplasmic domain of the CD44 dimer is absent.	Disulfides	21-30	CD44 molecule (Indian blood group)	Homo sapiens	131-135
7533087-3	1995	Here, we show that a disulfide-bonded dimer of CD44, formed by substituting the transmembrane region of CD3 zeta chain for that of CD44, binds Fl-HA, even when the cytoplasmic domain of the CD44 dimer is absent.	Disulfides	21-30	CD44 molecule (Indian blood group)	Homo sapiens	131-135
7597727-2	1995	The purified peptides covered 75.9% of the whole sequence of human alpha 1BG (359/474 residues) and showed 46.4% identity (167/360 amino acids) with the sequence of human alpha 1BG including cysteine residues forming disulfide linkages.	Disulfides	217-226	alpha-1-B glycoprotein	Homo sapiens	171-180
7851394-1	1995	Glutaredoxin is generally a glutathione-dependent hydrogen donor for ribonucleotide reductase and also catalyses general glutathione (GSH)-disulfide-oxidoreduction reactions in the presence of NADPH and glutathione reductase.	Disulfides	139-148	2,4-dienoyl-CoA reductase 1	Homo sapiens	193-198
7527811-1	1995	IL-12, a heterodimeric cytokine, consists of two disulfide-linked subunits, p40 and p35.	Disulfides	49-58	interleukin 12A	Homo sapiens	84-87
7714031-7	1994	Recombinant rp24 consists of about 40% alpha-helix and 10% beta-sheet from circular dichroism measurements and the two cysteine residues, within the rp24 sequence, are bridged by a disulfide bond.	Disulfides	181-190	RP24	Homo sapiens	12-16
7714031-7	1994	Recombinant rp24 consists of about 40% alpha-helix and 10% beta-sheet from circular dichroism measurements and the two cysteine residues, within the rp24 sequence, are bridged by a disulfide bond.	Disulfides	181-190	RP24	Homo sapiens	149-153
7538845-5	1994	However, the most highly protected amide protons in each variant differ, and are contained within the sequences of previously studied peptide models of related BPTI folding intermediates containing either the 5-55 or the 30-51 disulfide bond.	Disulfides	227-236	spleen trypsin inhibitor I	Bos taurus	160-164
7531529-1	1994	In the folding of bovine pancreatic trypsin inhibitor (BPTI), the single-disulfide intermediate [30-51] plays a key role.	Disulfides	73-82	spleen trypsin inhibitor I	Bos taurus	18-53
7531529-1	1994	In the folding of bovine pancreatic trypsin inhibitor (BPTI), the single-disulfide intermediate [30-51] plays a key role.	Disulfides	73-82	spleen trypsin inhibitor I	Bos taurus	55-59
8062245-3	1994	We have engineered a disulfide bond in the alpha 1 domain of a murine class I molecule, Kb.	Disulfides	21-30	ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1	Mus musculus	70-77
8062829-3	1994	The major RON transcript is translated into a glycosylated single chain precursor, cleaved into a 185 kDa heterodimer (p185RON) of 35 (alpha) and 150 kDa (beta) disulfide-linked chains, before exposure at the cell surface.	Disulfides	161-170	macrophage stimulating 1 receptor	Homo sapiens	10-13
8062829-3	1994	The major RON transcript is translated into a glycosylated single chain precursor, cleaved into a 185 kDa heterodimer (p185RON) of 35 (alpha) and 150 kDa (beta) disulfide-linked chains, before exposure at the cell surface.	Disulfides	161-170	macrophage stimulating 1 receptor	Homo sapiens	119-126
7913682-4	1994	The conformers of alpha LA with high affinity for GroEL are compact, containing up to three disulfide bonds, and have significant secondary structure, but lack stable tertiary structure and expose hydrophobic surfaces.	Disulfides	92-101	heat shock protein family D (Hsp60) member 1	Homo sapiens	50-55
7913682-7	1994	Interestingly, GroEL interacts only with a specific subset of the many partially folded disulfide intermediates of alpha LA and thus may influence in vitro the kinetics of the folding pathways that lead to disulfide bonds with native combinations.	Disulfides	88-97	heat shock protein family D (Hsp60) member 1	Homo sapiens	15-20
7913682-7	1994	Interestingly, GroEL interacts only with a specific subset of the many partially folded disulfide intermediates of alpha LA and thus may influence in vitro the kinetics of the folding pathways that lead to disulfide bonds with native combinations.	Disulfides	206-215	heat shock protein family D (Hsp60) member 1	Homo sapiens	15-20
8202491-0	1994	Disulfide cross-linking in crude embryonic lysates reveals three complexes of the Drosophila morphogen dorsal and its inhibitor cactus.	Disulfides	0-9	dorsal	Drosophila melanogaster	103-109
8200976-1	1994	Glycoprotein Ib beta (GPIb beta) exists in platelets disulfide-linked to glycoprotein Ib alpha (GPIb alpha), a major receptor for von Willebrand factor.	Disulfides	53-62	glycoprotein Ib platelet subunit beta	Homo sapiens	22-31
8200976-1	1994	Glycoprotein Ib beta (GPIb beta) exists in platelets disulfide-linked to glycoprotein Ib alpha (GPIb alpha), a major receptor for von Willebrand factor.	Disulfides	53-62	glycoprotein Ib platelet subunit alpha	Homo sapiens	96-106
8138569-8	1994	The larger loop connecting TMD3 and TMD4 of both UPIa and UPIb contains six highly conserved cysteine residues; at least one centrally located cysteine doublet in UPIa is involved in forming intramolecular disulfide bridges.	Disulfides	206-215	uroplakin 1A	Bos taurus	49-53
8138569-8	1994	The larger loop connecting TMD3 and TMD4 of both UPIa and UPIb contains six highly conserved cysteine residues; at least one centrally located cysteine doublet in UPIa is involved in forming intramolecular disulfide bridges.	Disulfides	206-215	uroplakin 1A	Bos taurus	163-167
7517603-1	1994	Our studies have shown that the administration of antibodies to chicken riboflavin carrier protein (cRCP) or disulfide-reduced carboxymethylated cRCP (RCM-RCP) leads to termination of pregnancy in mice.	Disulfides	109-118	CGRP receptor component	Gallus gallus	145-149
7508914-1	1994	Human serum macrophage stimulating protein (MSP) is a disulfide-linked heterodimer that induces motile and phagocytic activity of mouse resident peritoneal macrophages.	Disulfides	54-63	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	12-42
7508914-1	1994	Human serum macrophage stimulating protein (MSP) is a disulfide-linked heterodimer that induces motile and phagocytic activity of mouse resident peritoneal macrophages.	Disulfides	54-63	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	44-47
7509189-1	1994	In order to characterize the major transition states in the disulfide-coupled folding pathway of bovine pancreatic trypsin inhibitor (BPTI), the reductive unfolding kinetics of wild-type BPTI and 18 variants with single amino acid replacements were measured in the presence of varying concentrations of dithiothreitol (DTTSHSH).	Disulfides	60-69	spleen trypsin inhibitor I	Bos taurus	97-132
8170929-1	1994	The thermal stability of bovine beta-lactoglobulin (BLG) has been enhanced by the introduction of an additional disulfide bond.	Disulfides	112-121	beta-lactoglobulin	Bos taurus	32-50
8170929-1	1994	The thermal stability of bovine beta-lactoglobulin (BLG) has been enhanced by the introduction of an additional disulfide bond.	Disulfides	112-121	beta-lactoglobulin	Bos taurus	52-55
8170929-2	1994	Wild-type BLG has two disulfide bonds, C106-C119 and C66-C160, with a free cysteine at position 121.	Disulfides	22-31	beta-lactoglobulin	Bos taurus	10-13
8276843-1	1994	The presence of intramolecular disulfides in different functional states of the native glucocorticoid receptor in the absence of added oxidants has been examined on nonreducing SDS-polyacrylamide gels.	Disulfides	31-41	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	87-110
7734147-4	1994	Gel permeation chromatography of secreted hOP-1 in physiological buffers yields an apparent molecular weight of 110-120 k, indicating that after proteolytic processing the two pro-domains remain non-covalently associated with the disulfide linked mature dimer in a complex termed soluble hOP-1.	Disulfides	230-239	bone morphogenetic protein 7	Homo sapiens	42-47
7505111-1	1993	The disulfide-coupled folding pathway of a bovine pancreatic trypsin inhibitor (BPTI) variant, in which Tyr 35 is replaced by Leu, was determined and compared with that of the wild-type protein.	Disulfides	4-13	spleen trypsin inhibitor I	Bos taurus	43-78
7505111-1	1993	The disulfide-coupled folding pathway of a bovine pancreatic trypsin inhibitor (BPTI) variant, in which Tyr 35 is replaced by Leu, was determined and compared with that of the wild-type protein.	Disulfides	4-13	spleen trypsin inhibitor I	Bos taurus	80-84
8260495-5	1993	We report a new method for the purification and renaturation of rTIMP-1 from E. coli inclusion bodies to an active inhibitor of matrix metalloproteinases (80% yield), presumably containing the correct assignment of the six disulfide bonds.	Disulfides	223-232	TIMP metallopeptidase inhibitor 1	Rattus norvegicus	64-71
8267575-1	1993	The role of intermolecular disulfide linkages in transthyretin (TTR) amyloid fibril formation was investigated by comparing wild type TTR to Cys-10-Ala TTR which is incapable of disulfide formation.	Disulfides	27-36	transthyretin	Homo sapiens	49-62
8267575-1	1993	The role of intermolecular disulfide linkages in transthyretin (TTR) amyloid fibril formation was investigated by comparing wild type TTR to Cys-10-Ala TTR which is incapable of disulfide formation.	Disulfides	27-36	transthyretin	Homo sapiens	64-67
7693706-8	1993	After treatment with N-ethylmaleimide to prevent formation of disulfide-linked multimers, purification in 8 M urea, and dialysis against physiological saline, vitronectin was largely oligomeric (approximately 800 kDa) as assessed by gel filtration and polyacrylamide gel electrophoresis in the absence of sodium dodecyl sulfate.	Disulfides	62-71	vitronectin	Homo sapiens	159-170
7693706-10	1993	After incubation with urea at 25 degrees C, native vitronectin, treated during purification with dithionitrobenzoic acid to force free sulfhydryls to intramolecular disulfides, exhibited increased reactivity with antibody 8E6, increased binding to heparin, and oligomerization.	Disulfides	165-175	vitronectin	Homo sapiens	51-62
7693706-11	1993	In addition, incubation in urea caused rearrangement of disulfides as assessed by loss of the light chain of two-chain vitronectin.	Disulfides	56-66	vitronectin	Homo sapiens	119-130
7504753-1	1993	Tenascin is an extracellular matrix glycoprotein consisting of six disulfide-linked subunits with molecular masses of 190-250 kDa.	Disulfides	67-76	tenascin C	Homo sapiens	0-8
8514775-0	1993	Assignment of intrachain disulfide bonds in platelet-derived growth factor B-chain.	Disulfides	25-34	platelet derived growth factor subunit B	Homo sapiens	44-82
8514775-5	1993	Based on whether the mutated proteins remained in one piece or fell apart after CNBr cleavage, it was possible to deduce the disulfide bond arrangement in the PDGF B-chain; one bond involves the 1st and 6th cysteine residues, another the 3rd and 7th, and the last the 5th and 8th.	Disulfides	125-134	platelet derived growth factor subunit B	Homo sapiens	159-165
8385607-4	1993	When translations were carried out under conditions which prevent disulfide bond formation, the product synthesized formed aggregates which were associated with the immunoglobulin heavy chain binding protein (BiP).	Disulfides	66-75	heat shock protein family A (Hsp70) member 5	Rattus norvegicus	209-212
7681323-1	1993	The effects of single amino acid replacements on the stability of the 14-38 disulfide bond in the native form of bovine pancreatic trypsin inhibitor (BPTI) were measured.	Disulfides	76-85	spleen trypsin inhibitor I	Bos taurus	113-148
7681323-7	1993	The stability of the disulfide in a peptide corresponding to the segments that are linked together by the 14-38 disulfide in native BPTI was found to be about 5 kcal/mol less than that of the disulfide in the intact wild-type protein.	Disulfides	21-30	spleen trypsin inhibitor I	Bos taurus	132-136
7681323-7	1993	The stability of the disulfide in a peptide corresponding to the segments that are linked together by the 14-38 disulfide in native BPTI was found to be about 5 kcal/mol less than that of the disulfide in the intact wild-type protein.	Disulfides	112-121	spleen trypsin inhibitor I	Bos taurus	132-136
8468534-1	1993	The glycoprotein apolipoprotein[a] (apo[a]) is present in plasma at highly variable concentrations and appears as a number of genetically determined size isoforms (400-800 kDa), disulfide linked to apoB-100 in low density lipoprotein to produce lipoprotein [a](Lp[a]).	Disulfides	178-187	apolipoprotein(a)	Papio anubis	17-33
8095018-7	1993	This cysteine seemed to be involved in an interchain disulfide bridge both between intact TTR molecules and between small fragments.	Disulfides	53-62	transthyretin	Homo sapiens	90-93
8422244-0	1993	The disulfide bond arrangement of leukemia inhibitory factor: homology to oncostatin M and structural implications.	Disulfides	4-13	oncostatin M	Mus musculus	74-86
8422244-4	1993	The three disulfide bonds are CYS13-CYS135, CYS19-CYS132 and CYS61-164 and the first and third of these are clearly homologous to the two disulfide bonds in oncostatin M.	Disulfides	10-19	oncostatin M	Mus musculus	157-169
8422244-4	1993	The three disulfide bonds are CYS13-CYS135, CYS19-CYS132 and CYS61-164 and the first and third of these are clearly homologous to the two disulfide bonds in oncostatin M.	Disulfides	138-147	oncostatin M	Mus musculus	157-169
7678252-8	1993	The amino-terminal region of VN and the thrombin moiety of the TAT complex were found to be responsible for their interaction, which was stabilized by disulfide bridges.	Disulfides	151-160	vitronectin	Homo sapiens	29-31
8374001-7	1993	Second, single cysteine substitutions in PRPs (Pa from PRH1 and G1 8 from PRB3) may lead to disulfide bonded homodimers as well as heterodimers with salivary peroxidase.	Disulfides	92-101	proline rich protein HaeIII subfamily 1	Homo sapiens	55-59
7678222-6	1993	All of these epitopes are shown to be sensitive to reduction, thus indicating the importance of disulfide bonding in the correct folding of the CD53 hydrophilic domain.	Disulfides	96-105	CD53 antigen	Mus musculus	144-148
7510792-1	1993	3 alpha-Hydroxysteroid dehydrogenase (EC 1.1.1.50), purified to homogeneity from rat liver, was strongly inactivated by incubation with a disulfide such as GSSG, L-cystine or L-cystamine, as well as an SH-reagent such as DTNB (5,5"-dithiobis(2-nitrobenzoic acid)), NEM (N-ethylmaleimide) or iodoacetic acid.	Disulfides	138-147	aldo-keto reductase family 1, member C14	Rattus norvegicus	0-36
7684341-2	1993	Results on the human choriogonadotropin beta (hCG beta) subunit, obtained using synthetic peptides, chemically modified derivatives, and mutant forms prepared via site-directed mutagenesis, have suggested that amino acid residues enclosed by the purported disulfide loop between Cys-93 and Cys-100 may contribute to receptor binding and perhaps specificity.	Disulfides	256-265	chorionic gonadotropin subunit beta 3	Homo sapiens	46-54
1463721-7	1992	In plasma, C4BP alpha exists as disulfide-linked multimers consisting of seven C4BP alpha chains and a single C4BP beta chain.	Disulfides	32-41	apolipoprotein R	Sus scrofa	11-21
1463721-7	1992	In plasma, C4BP alpha exists as disulfide-linked multimers consisting of seven C4BP alpha chains and a single C4BP beta chain.	Disulfides	32-41	apolipoprotein R	Sus scrofa	79-89
1463721-8	1992	Like C4BP, apoR forms high molecular weight disulfide-linked complexes in plasma.	Disulfides	44-53	apolipoprotein R	Sus scrofa	11-15
1384990-1	1992	The in vitro folding pathway of bovine pancreatic trypsin inhibitor (BPTI) has been described previously in terms of the disulfide-bonded intermediates that accumulate during folding of the protein.	Disulfides	121-130	spleen trypsin inhibitor I	Bos taurus	32-67
1384990-1	1992	The in vitro folding pathway of bovine pancreatic trypsin inhibitor (BPTI) has been described previously in terms of the disulfide-bonded intermediates that accumulate during folding of the protein.	Disulfides	121-130	spleen trypsin inhibitor I	Bos taurus	69-73
1384990-7	1992	Moreover, a single cysteine residue, tethered to the carboxy-terminal end of BPTI with a flexible linker of repeating Ser-Gly-Gly residues, is sufficient to assist in disulfide formation.	Disulfides	167-176	spleen trypsin inhibitor I	Bos taurus	77-81
1472481-1	1992	Natural killer cells express an Fc receptor for IgG (CD16) in association with disulfide-linked dimers composed of two homologous subunits: the zeta chain of the T cell antigen receptor complex and the gamma chain of the mast cell/basophil Fc receptor for IgE.	Disulfides	79-88	Fc gamma receptor IIIa	Homo sapiens	53-57
1328685-0	1992	Disulfide bond structure of glycoprotein D of herpes simplex virus types 1 and 2.	Disulfides	0-9	atypical chemokine receptor 1 (Duffy blood group)	Homo sapiens	28-42
1400452-0	1992	Domain-dependent protein folding is indicated by the intracellular kinetics of disulfide bond formation of human chorionic gonadotropin beta subunit.	Disulfides	79-88	chorionic gonadotropin subunit beta 3	Homo sapiens	113-148
1400452-3	1992	The individual rates of disulfide bridging were determined by identifying the extent of disulfide bond formation in hCG-beta intermediates purified from choriocarcinoma cells that had been metabolically labeled for 40 to 120 s and chased for 0 to 25 min.	Disulfides	24-33	chorionic gonadotropin subunit beta 3	Homo sapiens	116-124
1400452-3	1992	The individual rates of disulfide bridging were determined by identifying the extent of disulfide bond formation in hCG-beta intermediates purified from choriocarcinoma cells that had been metabolically labeled for 40 to 120 s and chased for 0 to 25 min.	Disulfides	88-97	chorionic gonadotropin subunit beta 3	Homo sapiens	116-124
1400452-4	1992	The results of these kinetic studies describe a folding pathway in which the disulfide bonds between cysteines 34-88, 38-57, 9-90 and 23-72 stabilize, in a discrete order, the putative domain(s) involving amino acids 1-90 of hCG-beta.	Disulfides	77-86	chorionic gonadotropin subunit beta 3	Homo sapiens	225-233
1400452-6	1992	The order of completion of each of the six disulfide bonds of hCG-beta is: 34-88 (t1/2 = 1-2 min), 38-57 (t1/2 = 2-3 min), 9-90 and 23-72, 93-100, and 26-110.	Disulfides	43-52	chorionic gonadotropin subunit beta 3	Homo sapiens	62-70
1384932-1	1992	Two extracellular matrix proteins of brain tissue, neuronectin (NEC1) and cytotactin (CT), are disulfide-bonded multimers of M(r) 180,000-250,000 subunits.	Disulfides	95-104	tenascin C	Homo sapiens	51-62
1384932-1	1992	Two extracellular matrix proteins of brain tissue, neuronectin (NEC1) and cytotactin (CT), are disulfide-bonded multimers of M(r) 180,000-250,000 subunits.	Disulfides	95-104	tenascin C	Homo sapiens	74-84
1384932-1	1992	Two extracellular matrix proteins of brain tissue, neuronectin (NEC1) and cytotactin (CT), are disulfide-bonded multimers of M(r) 180,000-250,000 subunits.	Disulfides	95-104	tenascin C	Homo sapiens	86-88
1358798-1	1992	IL12 (formerly NKSF or CLMF) is a unique cytokine composed of two unrelated disulfide-linked subunits.	Disulfides	76-85	interleukin 12B	Homo sapiens	15-19
1358798-1	1992	IL12 (formerly NKSF or CLMF) is a unique cytokine composed of two unrelated disulfide-linked subunits.	Disulfides	76-85	interleukin 12B	Homo sapiens	23-27
1282503-6	1992	The BPTI analogue with one disulfide bridge was obtained following treatment with dimethyl sulfoxide (DMSO)-pH 6 buffer (1:9).	Disulfides	27-36	spleen trypsin inhibitor I	Bos taurus	4-8
16652969-0	1992	Bilevel disulfide group reduction in the activation of c(4) leaf nicotinamide adenine dinucleotide phosphate-malate dehydrogenase.	Disulfides	8-17	LOC100856934	Zea mays	109-129
16652969-6	1992	We suggest that reduction of one particular higher redox potential disulfide group in unactivated nicotinamide adenine dinucleotide phosphate-malate dehydrogenase facilitates the subsequent reduction of the critical S-S group (regulatory S-S) necessary to generate the active form of the enzyme.	Disulfides	67-76	LOC100856934	Zea mays	142-162
1404081-0	1992	Release of two-cell block by reduction of protein disulfide with thioredoxin from Escherichia coli in mice.	Disulfides	50-59	thioredoxin 1	Mus musculus	65-76
1404081-7	1992	These results indicate that the effect of thioredoxin on the two-cell block is due to the thioredoxin molecule itself, and suggest that disulfide formation within or between proteins resulting from oxidative stress is one of the major causes of the two-cell block.	Disulfides	136-145	thioredoxin 1	Mus musculus	42-53
1404081-7	1992	These results indicate that the effect of thioredoxin on the two-cell block is due to the thioredoxin molecule itself, and suggest that disulfide formation within or between proteins resulting from oxidative stress is one of the major causes of the two-cell block.	Disulfides	136-145	thioredoxin 1	Mus musculus	90-101
1304387-1	1992	Human and bovine alpha-thrombin cleaved at the B-chain by chymotrypsin generates catalytically competent zeta-thrombins, which are comprised of two noncovalently linked fragments: a 36-(human) or 49-(bovine) residue A-chain linked by a disulfide to B-chain residues B1-148 (zeta 1-thrombin) and B-chain residues B149-259 (zeta 2-thrombin).	Disulfides	236-245	coagulation factor II, thrombin	Bos taurus	23-31
1304387-1	1992	Human and bovine alpha-thrombin cleaved at the B-chain by chymotrypsin generates catalytically competent zeta-thrombins, which are comprised of two noncovalently linked fragments: a 36-(human) or 49-(bovine) residue A-chain linked by a disulfide to B-chain residues B1-148 (zeta 1-thrombin) and B-chain residues B149-259 (zeta 2-thrombin).	Disulfides	236-245	coagulation factor II, thrombin	Bos taurus	110-118
1304387-1	1992	Human and bovine alpha-thrombin cleaved at the B-chain by chymotrypsin generates catalytically competent zeta-thrombins, which are comprised of two noncovalently linked fragments: a 36-(human) or 49-(bovine) residue A-chain linked by a disulfide to B-chain residues B1-148 (zeta 1-thrombin) and B-chain residues B149-259 (zeta 2-thrombin).	Disulfides	236-245	coagulation factor II, thrombin	Bos taurus	110-118
1330111-0	1992	Disulfide bond as peptide-resin linkage in Boc-Bzl SPPS, for potential biochemical applications.	Disulfides	0-9	BOC cell adhesion associated, oncogene regulated	Homo sapiens	43-46
1350784-9	1992	The data strongly suggest that hemin regulates eIF-2 alpha kinase activity by promoting formation of the inactive dimer HCI.p87 via disulfide bonds and direct binding of hemin.	Disulfides	132-141	inner membrane mitochondrial protein	Homo sapiens	124-127
1610568-5	1992	Although both rom-1 and peripherin form disulfide-linked dimers, they do not form heterodimers with each other, but appear to associate noncovalently.	Disulfides	40-49	retinal outer segment membrane protein 1	Homo sapiens	14-19
1547731-1	1992	Previous in vivo cross-linking studies of TSH to the recombinant TSH receptor revealed that the receptor exists at least in part as a single chain glycoprotein of approximately about 100 kilodaltons (kDa), with intramolecular disulfide bonds.	Disulfides	226-235	thyroid stimulating hormone receptor	Homo sapiens	65-77
1314580-3	1992	Our results indicate that only the ring portion of CNP with a disulfide bond (CNP(6-22)) participates in stimulation of cGMP accumulation, especially the sequence Leu9-Lys10-Leu11 in the ring portion executes essential roles for both elevation of cGMP and selectivity of the ligand for NPR-B.	Disulfides	62-71	natriuretic peptide C	Rattus norvegicus	51-54
1314580-3	1992	Our results indicate that only the ring portion of CNP with a disulfide bond (CNP(6-22)) participates in stimulation of cGMP accumulation, especially the sequence Leu9-Lys10-Leu11 in the ring portion executes essential roles for both elevation of cGMP and selectivity of the ligand for NPR-B.	Disulfides	62-71	natriuretic peptide C	Rattus norvegicus	78-81
1371999-4	1992	The latter has been called a putative "link" component because it is assumed to be important for disulfide bond-mediated mucin polymerization.	Disulfides	97-106	solute carrier family 13 member 2	Rattus norvegicus	121-126
1735425-0	1992	Localization of two interchain disulfide bridges in dimers of bovine alpha s2-casein.	Disulfides	31-40	alpha-S2-casein	Bos taurus	69-84
1735425-2	1992	Carboxymethylation of bovine skimmed milk with 14C-labelled iodoacetic acid followed by purification of the alpha s2-casein dimer showed that all four cysteine residues in the protein are engaged in disulfide linkages.	Disulfides	199-208	alpha-S2-casein	Bos taurus	108-123
1304906-4	1992	However, refolding of denatured beta-NGF is dependent on the three disulfide bonds present in the native protein and does not readily occur when the disulfide bonds are reduced.	Disulfides	67-76	nerve growth factor	Mus musculus	32-40
1304906-4	1992	However, refolding of denatured beta-NGF is dependent on the three disulfide bonds present in the native protein and does not readily occur when the disulfide bonds are reduced.	Disulfides	149-158	nerve growth factor	Mus musculus	32-40
1582526-2	1992	o-Iodosobenzoic acid (IOB) caused the formation of a disulfide bridge between SH1 and SH2 groups of myosin SF1 rendering inactive its ATPase activity.	Disulfides	53-62	splicing factor 1	Homo sapiens	107-110
1885591-8	1991	Our data indicate that the disulfide between Cys48 and Cys82 stabilizes the structure of the N-terminal domain of TnC and blocks its ability to interact with TnI.	Disulfides	27-36	tenascin	Oryctolagus cuniculus	114-117
1885591-9	1991	The effects of the disulfide appear to be restricted to the N-terminal domain of TnC.	Disulfides	19-28	tenascin	Oryctolagus cuniculus	81-84
1891462-0	1991	Intersubunit disulfide-bonded lambda-Cro protein.	Disulfides	13-22	cro	Escherichia virus Lambda	37-40
1891462-2	1991	It has been found that the Cys55 Cro protein (Cro VC55) spontaneously forms a stable disulfide-bonded dimer in the absence of a reducing agent.	Disulfides	85-94	cro	Escherichia virus Lambda	33-36
1674604-1	1991	Cytotoxic lymphocyte maturation factor (CLMF) is a disulfide-bonded heterodimeric lymphokine that (i) acts as a growth factor for activated T cells independent of interleukin 2 and (ii) synergizes with suboptimal concentrations of interleukin 2 to induce lymphokine-activated killer cells.	Disulfides	51-60	interleukin 12A	Homo sapiens	0-38
1674604-1	1991	Cytotoxic lymphocyte maturation factor (CLMF) is a disulfide-bonded heterodimeric lymphokine that (i) acts as a growth factor for activated T cells independent of interleukin 2 and (ii) synergizes with suboptimal concentrations of interleukin 2 to induce lymphokine-activated killer cells.	Disulfides	51-60	interleukin 12A	Homo sapiens	40-44
1827141-3	1991	The disulfide-linked two-chain structure of MSP was confirmed by separation of reduced and alkylated MSP chains.	Disulfides	4-13	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	44-47
1827141-3	1991	The disulfide-linked two-chain structure of MSP was confirmed by separation of reduced and alkylated MSP chains.	Disulfides	4-13	macrophage stimulating 1 (hepatocyte growth factor-like)	Mus musculus	101-104
2019579-0	1991	Bovine brain acetylcholinesterase primary sequence involved in intersubunit disulfide linkages.	Disulfides	76-85	acetylcholinesterase	Bos taurus	13-33
2019579-2	1991	A12 AChE is composed of 12 catalytic subunits that are linked to noncatalytic collagen-like subunits through intersubunit disulfide bonds.	Disulfides	122-131	acetylcholinesterase	Bos taurus	4-8
2019579-4	1991	Brain G4 AChE involves two catalytic subunits linked by a direct intersubunit disulfide bond while the other two are disulfide-linked to a membrane-binding 20-kDa noncatalytic subunit.	Disulfides	78-87	acetylcholinesterase	Bos taurus	9-13
2019579-9	1991	Cysteines involved in intersubunit disulfide linkages in brain AChE were reduced selectively with dithiothreitol in the absence of denaturants and radioalkylated with iodoacetamide.	Disulfides	35-44	acetylcholinesterase	Bos taurus	63-67
1830446-2	1991	SDS-polyacrylamide gel electrophoresis in combination with immunoblot analysis showed that the bone TrATPase has a molecular weight of 33,000 D and is composed of disulfide-linked polypeptides of 20,000 and 16,000 D. The enzyme contains 1.7 mol Fe per mol enzyme.	Disulfides	163-172	acid phosphatase 5, tartrate resistant	Rattus norvegicus	100-108
2005383-7	1991	component was completely dissociated into equimolar quantities of two kinds of 28 kDa polypeptides, P28a and P28b, under reducing conditions, indicating that the association of these polypeptides was stabilized by disulfide bonds.	Disulfides	214-223	mediator complex subunit 18	Homo sapiens	109-113
1704365-2	1991	Hexabrachion (Tenascin) is a large glycoprotein that appears in extracellular matrices as a disulfide-linked multimer.	Disulfides	92-101	tenascin C	Homo sapiens	14-22
1703368-5	1991	Interestingly, the HBs-specific MAbs directed to disulfide-bond-dependent epitopes were found to be the best inhibitors of the preS1-HepG2 cell interaction (greater than 50%, at the final concentration of 0.5 micrograms/ml).	Disulfides	49-58	large envelope protein;middle envelope protein;small envelope protein	Hepatitis B virus	127-132
1824927-3	1991	An isolated CCP module, the 16th repeat from human complement factor H, has been expressed in a yeast vector and shown to fold with the same pattern of disulfide bond formation as is seen in the native protein.	Disulfides	152-161	complement factor H	Homo sapiens	51-70
1826679-5	1991	The purified HGF-like factor had a molecular weight of 82-85 kDa, as estimated by SDS-PAGE, and was a heterodimer composed of a large subunit of about 69 kDa and a small subunit of 34 kDa linked by disulfide bridges.	Disulfides	198-207	hepatocyte growth factor	Rattus norvegicus	13-16
1711921-1	1990	Tenascin is a large disulfide-linked hexameric extracellular matrix glycoprotein.	Disulfides	20-29	avian tenascin X	Gallus gallus	0-8
1710077-4	1990	We also demonstrate that the CDw50 antigen is expressed on thymocytes and T lymphocytes as an N-glycosylated glycoprotein monomer with a relative molecular weight (Mr) of 130,000 daltons with intrachain disulfide bonds, and that this molecule is resistant to treatment with phosphatidylinositol (PI) phospholipase C and therefore probably not PI-anchored to the membrane.	Disulfides	203-212	intercellular adhesion molecule 3	Homo sapiens	29-34
2271592-4	1990	A mutation is also described whereby cysteine links the two Cro monomers by a disulfide bond.	Disulfides	78-87	cro	Escherichia virus Lambda	60-63
2204066-4	1990	Analysis of the purified protein by sodium dodecyl sulfate/polyacrylamide gel electrophoresis demonstrated that CLMF is a 75-kDa heterodimer composed of disulfide-bonded 40-kDa and 35-kDa subunits.	Disulfides	153-162	interleukin 12A	Homo sapiens	112-116
2251783-1	1990	Heating of cow milk beta-lactoglobulin at 96 degrees, pH 8.0 led to the protein aggregation because of intermolecular disulfide exchange as shown by agarose gel immunoelectrophoresis, where additional precipitation strips were detected.	Disulfides	118-127	beta-lactoglobulin	Bos taurus	20-38
2385828-2	1990	With purified GPIIb:IIIa as an antigen, we have produced monoclonal antibody CS-1, which immunoblotting demonstrates to be specific for native GPIIIa; disulfide bond reduction of GPIIIa resulted in loss of immunoreactivity.	Disulfides	151-160	integrin subunit alpha 2b	Homo sapiens	14-19
2385828-2	1990	With purified GPIIb:IIIa as an antigen, we have produced monoclonal antibody CS-1, which immunoblotting demonstrates to be specific for native GPIIIa; disulfide bond reduction of GPIIIa resulted in loss of immunoreactivity.	Disulfides	151-160	chorionic somatomammotropin hormone 1	Homo sapiens	77-81
1969395-13	1990	In addition, release of the link component from the rest of the mucin by disulfide bond reduction causes greater exposure of specific bacterium-binding sites.	Disulfides	73-82	solute carrier family 13 member 2	Rattus norvegicus	64-69
2201313-1	1990	We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51-found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin.	Disulfides	66-75	LOC105613195	Ovis aries	84-91
2154392-4	1990	This suggests that hZP1, like mouse ZP1, is composed of two polypeptides held together by intermolecular disulfides.	Disulfides	105-115	zona pellucida glycoprotein 1	Homo sapiens	19-23
2154392-4	1990	This suggests that hZP1, like mouse ZP1, is composed of two polypeptides held together by intermolecular disulfides.	Disulfides	105-115	zona pellucida glycoprotein 1	Mus musculus	20-23
2138084-5	1990	Radioimmunoprecipitation from digitonin lysates of surface-labeled cells with an anti-CD3 antiserum showed that the CD5+, but not the CD5- population of TcR alpha/beta- cells expresses a CD3-associated disulfide-linked cell surface molecule of about 100 kDa apparent mol.	Disulfides	202-211	Cd5 molecule	Rattus norvegicus	116-119
2118298-2	1990	Stable fragments can be obtained in good yield from the purified IgG 1, first by cleavage with pepsin and then by reducing the disulfide bonds with cysteine and subsequent alkylation with iodoacetamide.	Disulfides	127-136	LOC105243590	Mus musculus	65-70
33767592-7	2021	Physical interactions of AGR2 and FABP1 depended on the PDI motif in AGR2 and the formation of a disulfide bond between these two proteins.	Disulfides	97-106	fatty acid binding protein 1, liver	Mus musculus	34-39
28470603-0	2017	A Generic Protocol for Purifying Disulfide-Bonded Domains and Random Protein Fragments Using Fusion Proteins with SUMO3 and Cleavage by SenP2 Protease.	Disulfides	33-42	small ubiquitin like modifier 3	Homo sapiens	114-119
15967461-11	2005	Furthermore, we show that the exchange of subunits between Hsp26 oligomers is significantly slower than substrate aggregation and even inhibited in the presence of disulfide bonds.	Disulfides	164-173	chaperone protein HSP26	Saccharomyces cerevisiae S288C	59-64
8535165-1	1995	Protein disulfide isomerase (PDI) is an abundant protein of the endoplasmic reticulum that catalyzes the oxidation of protein sulfhydryl groups and the isomerization and reduction of protein disulfide bonds.	Disulfides	8-17	prolyl 4-hydroxylase subunit beta	Rattus norvegicus	29-32
34923639-4	2022	The specificities of gamma-EC and its disulfide form to GGT were comparable to GSH and its oxidized form, GSSG, respectively.	Disulfides	38-47	gamma-glutamyltransferase 1	Homo sapiens	56-59
34565182-5	2021	Fluorescence resonance energy transfer screening employing blocking peptides determined that cycteine129/131 residues in the extracellular domain of CaSR formed intermolecular disulfide bonds to promote CaSR polymerization.	Disulfides	176-185	calcium-sensing receptor	Rattus norvegicus	149-153
34565182-5	2021	Fluorescence resonance energy transfer screening employing blocking peptides determined that cycteine129/131 residues in the extracellular domain of CaSR formed intermolecular disulfide bonds to promote CaSR polymerization.	Disulfides	176-185	calcium-sensing receptor	Rattus norvegicus	203-207
34565182-7	2021	In contrast, the blockade of disulfide bonds formation using a peptide decreased both CaSR and hypoxia-induced mitogenic factor expression as well as other hypoxic-related genes in vitro and in vivo and attenuated pulmonary hypertension development in rats.	Disulfides	29-38	calcium-sensing receptor	Rattus norvegicus	86-90
34428184-6	2021	It is plausible that, with the absence of J-chain, the cysteine residue of mono-IgA1 might aberrantly form disulfide bond in poly-IgA formation.	Disulfides	107-116	immunoglobulin heavy constant alpha 1	Homo sapiens	80-84
34461091-7	2021	Deletion of Aim32 or mutation of conserved cysteine residues that coordinate the Fe-S center in Aim32 resulted in an increased accumulation of proteins with aberrant disulfide linkages.	Disulfides	166-175	Aim32p	Saccharomyces cerevisiae S288C	12-17
34461091-7	2021	Deletion of Aim32 or mutation of conserved cysteine residues that coordinate the Fe-S center in Aim32 resulted in an increased accumulation of proteins with aberrant disulfide linkages.	Disulfides	166-175	Aim32p	Saccharomyces cerevisiae S288C	96-101
34325342-1	2021	Protein Disulfide Isomerase Family A Member 6 (PDIA6) is an endoplasmic reticulum protein that is capable of catalyzing protein folding and disulfide bond formation.	Disulfides	140-149	protein disulfide isomerase family A member 6	Homo sapiens	0-45
34325342-1	2021	Protein Disulfide Isomerase Family A Member 6 (PDIA6) is an endoplasmic reticulum protein that is capable of catalyzing protein folding and disulfide bond formation.	Disulfides	140-149	protein disulfide isomerase family A member 6	Homo sapiens	47-52
34440055-9	2021	Then, we used two different linkers, one of molecular disulfide bonds and another of a maleimide group, to couple LLC2B to the toxin DM1.	Disulfides	54-63	DM1 protein kinase	Homo sapiens	133-136
34360542-6	2021	Cys-mutants of HspB6 and HspB8 containing a single-Cys residue in the central part of the beta7 strand in a position homologous to that of Cys137 in HspB1 can be crosslinked to the wild-type HspB7 through a disulfide bond.	Disulfides	207-216	heat shock protein family B (small) member 7	Homo sapiens	191-196
34136078-2	2021	We have previously shown that disulfide trapping successfully yielded covalent stabilizers for the PPI of 14-3-3 with the estrogen receptor ERalpha.	Disulfides	30-39	tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein theta	Homo sapiens	106-112
35597280-0	2022	O-Fucosylation stabilizes the TSR3 motif in Thrombospondin-1 by interacting with nearby amino acids and protecting a disulfide bond.	Disulfides	117-126	thrombospondin 1	Mus musculus	44-60
35597280-8	2022	Here we conducted molecular dynamics simulations and provide crystallographic and NMR evidence that the Glucose-Fucose disaccharide interacts with specific amino acids in the TSR3 domain in thrombospondin-1 that are within proximity to the O-fucosylation modification site resulting in protection of a nearby disulfide bond.	Disulfides	309-318	thrombospondin 1	Mus musculus	190-206
35458529-13	2022	The relevant motifs for each protein were highly conserved, with fewer polymorphisms in the fusion peptide, immunosuppression domain, and disulfide bonds on the surface (SU) and transmembrane (TM) of env.	Disulfides	138-147	endogenous retrovirus group K member 20	Homo sapiens	200-203
35077997-1	2022	Protein disulfide isomerase (PDI), an oxidoreductase, possesses two vicinal cysteines in the -Cys-Gly-His-Cys-motif that either form a disulfide bridge (S-S) or exist in a sulfhydryl form (-SH), forming oxidized or reduced PDI, respectively.	Disulfides	135-144	thioredoxin reductase 1	Homo sapiens	38-52
35358180-7	2022	Cysteine depalmitoylation sites in transmembrane PPT1 substrates frequently participate in disulfide bonds in the mature protein.	Disulfides	91-100	palmitoyl-protein thioesterase 1	Mus musculus	49-53
34870817-4	2022	Group B SRCR domains, found in WC1, CD163, CD5, CD6, Spalpha and DMBT1, are approximately 100-110 amino acids long and contain 6-8 cysteines predicted to form 3-4 disulfide bonds.	Disulfides	163-172	deleted in malignant brain tumors 1	Homo sapiens	65-70
34870817-16	2022	Thus, bacterial binding studies with WC1 SRCR domains must be done with native, correctly disulfide bonded, protein, ideally posttranslationally modified in mammalian cells.WC1 is found in the genomes of most mammals, reptiles, and birds and is expressed exclusively on gammadelta T cells in ruminants.	Disulfides	90-99	ATPase copper transporting beta	Homo sapiens	173-176